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Conserved domains on  [gi|767943404|ref|XP_011534355|]
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proto-oncogene tyrosine-protein kinase ROS isoform X7 [Homo sapiens]

Protein Classification

proto-oncogene tyrosine-protein kinase ROS( domain architecture ID 10046102)

proto-oncogene tyrosine-protein kinase ROS is an orphan receptor tyrosine-protein kinase containing an extracellular ligand-binding domain, a transmembrane segment, and an intracellular kinase domain that catalyzes the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates

EC:  2.7.10.1
Gene Symbol:  ROS1
PubMed:  10966463

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
1902-2168 0e+00

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 554.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd05044     2 FLGSGAFGEVFEGTAKDILGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtSPRIVKIGDFGLARDI 2061
Cdd:cd05044    82 EGGDLLSYLRAARPTAFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDY-RERVVKIGDFGLARDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDD 2141
Cdd:cd05044   161 YKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPDD 240
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2142 LWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05044   241 LYELMLRCWSTDPEERPSFARILEQLQ 267
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
211-290 2.23e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.83  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  211 NIESSSPDTVEVSWDPPQFPGGPILGYNLRLISKNQK-----LDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGEGPEAE 285
Cdd:cd00063     8 RVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGdwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSE 87

                  ....*
gi 767943404  286 SSITT 290
Cdd:cd00063    88 SVTVT 92
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
103-297 1.20e-10

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 66.95  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  103 EVLENADLPTAP---FASSIGSHNMTLRWKSANFSGVK-YIIQWKYAQLlGSWTYTKTVSRPSYVVKPLHPFTEYIFRVV 178
Cdd:COG3401   225 SVTTPTTPPSAPtglTATADTPGSVTLSWDPVTESDATgYRVYRSNSGD-GPFTKVATVTTTSYTDTGLTNGTTYYYRVT 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  179 WIFTAQLQlySPPSPSYRTHPHGVPETAPLIRNIESSSPDTVEVSWDPPqfPGGPILGYNL-RLISKN---QKLDAGTQR 254
Cdd:COG3401   304 AVDAAGNE--SAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS--SDADVTGYNVyRSTSGGgtyTKIAETVTT 379
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767943404  255 TSFQFYSTLPNTIYRFSIAAVNEVGEGPEAESSITTSSSAVQQ 297
Cdd:COG3401   380 TSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAAS 422
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
993-1099 6.35e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.11  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  993 PSAPENPRIfilpsgKCCNKNEVVVefRWNKPKHENGVLTKFEIFYNISNQsitnktcEDWIAVNVTP-SVMSFQLEGMS 1071
Cdd:cd00063     1 PSPPTNLRV------TDVTSTSVTL--SWTPPEDDGGPITGYVVEYREKGS-------GDWKEVEVTPgSETSYTLTGLK 65
                          90       100
                  ....*....|....*....|....*...
gi 767943404 1072 PRCFIAFQVRAFTSKGPGPYADVVKSTT 1099
Cdd:cd00063    66 PGTEYEFRVRAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1611-1700 7.57e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.11  E-value: 7.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1611 PEKPYSLVPEN---TSLQFNWKAPL--NVNLIRFWVELQKWKYNEFYHVKTSCSQGPAYVcnITNLQPYTSYNVRVVVVY 1685
Cdd:cd00063     1 PSPPTNLRVTDvtsTSVTLSWTPPEddGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT--LTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 767943404 1686 KTGENSTSLPESFKT 1700
Cdd:cd00063    79 GGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1705-1794 1.64e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.26  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1705 PNKPGIPKLLEGSKNSI--QWEKAEDNGCRITYYILEIRKSTSNnlqnqnlRWKmTFNGSCSSVCTWKSKNLK--GIFQF 1780
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVtlSWTPPEDDGGPITGYVVEYREKGSG-------DWK-EVEVTPGSETSYTLTGLKpgTEYEF 72
                          90
                  ....*....|....
gi 767943404 1781 RVVAANNLGFGEYS 1794
Cdd:cd00063    73 RVRAVNGGGESPPS 86
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
1383-1711 4.50e-05

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 48.85  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1383 AYSSVMQPFPDKAFLSLASDTVEPTILNATNTSLTIRLPLAKTNLTWYGITSPTPTYLVYYAEVNDRKNSSDLKYRILEF 1462
Cdd:COG3401   110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1463 QDSIALIEDLQPFSTYMIQIAVKNYYSDPlehlPPGKEIWGKTKNGVPEAVQLINTTVRSDTSLIISWReshkPNGPKES 1542
Cdd:COG3401   190 TTLVDGGGDIEPGTTYYYRVAATDTGGES----APSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD----PVTESDA 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1543 VRYQLaishlalipetplRQSEFPNGRLTLL---------VTRLSGGNIYVLKVLACHSEEMWCTESHPVTVEMFNT-PE 1612
Cdd:COG3401   262 TGYRV-------------YRSNSGDGPFTKVatvtttsytDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTpPA 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1613 KPYSL---VPENTSLQFNWKAPLNVNLIRFWVELQKWKYNEFYHVKTSCSqGPAYVcnITNLQPYTSYNVRVVVVYKTGE 1689
Cdd:COG3401   329 APSGLtatAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAETVT-TTSYT--DTGLTPGTTYYYKVTAVDAAGN 405
                         330       340
                  ....*....|....*....|..
gi 767943404 1690 NSTSLPESFKTKAGVPNKPGIP 1711
Cdd:COG3401   406 ESAPSEEVSATTASAASGESLT 427
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
561-619 6.24e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.94  E-value: 6.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  561 YEVKVSTQDPPEVTHI-FLNISGTMLNVPELQSAMKYKVSVRASSPKRPGPWSEPSVGTT 619
Cdd:cd00063    34 YVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
1902-2168 0e+00

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 554.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd05044     2 FLGSGAFGEVFEGTAKDILGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtSPRIVKIGDFGLARDI 2061
Cdd:cd05044    82 EGGDLLSYLRAARPTAFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDY-RERVVKIGDFGLARDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDD 2141
Cdd:cd05044   161 YKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPDD 240
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2142 LWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05044   241 LYELMLRCWSTDPEERPSFARILEQLQ 267
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
1897-2167 2.70e-127

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 400.33  E-value: 2.70e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  1897 LTLRLLLGSGAFGEVYEGTAVDilGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKG--EGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  1977 ILELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFG 2056
Cdd:pfam07714   79 VTEYMPGGDLLDFLRKHK------RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLV-----SENLVVKISDFG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  2057 LARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPR 2136
Cdd:pfam07714  148 LSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPE 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 767943404  2137 NCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:pfam07714  228 NCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
1897-2167 2.26e-125

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 394.98  E-value: 2.26e-125
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   1897 LTLRLLLGSGAFGEVYEGTAVDILGvgSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLKGKGG--KKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   1977 ILELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFG 2056
Cdd:smart00219   79 VMEYMEGGDLLSYLRKNR------PKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG-----ENLVVKISDFG 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   2057 LARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPR 2136
Cdd:smart00219  148 LSRDLYDDDYYRKRG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPP 226
                           250       260       270
                    ....*....|....*....|....*....|.
gi 767943404   2137 NCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:smart00219  227 NCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1902-2158 2.72e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 127.44  E-value: 2.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDIlgvgsgEIKVAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:COG0515    14 LLGRGGMGVVYLARDLRL------GRPVALKVLRPELAADPEARerFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRK---------ARMAtfygplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIV 2050
Cdd:COG0515    88 YVEGESLADLLRRrgplppaeaLRIL----------------AQLAEALAAAHAAGIVHRDIKPANILL-----TPDGRV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLARDIYKNDYYRkRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGG 2130
Cdd:COG0515   147 KLIDFGIARALGGATLTQ-TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREP 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2131 RLEPPR---NCPDDLWNLMTQCWAQEPDQRP 2158
Cdd:COG0515   225 PPPPSElrpDLPPALDAIVLRALAKDPEERY 255
PHA02988 PHA02988
hypothetical protein; Provisional
1928-2174 9.79e-14

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 74.01  E-value: 9.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1928 KVAVKTLKKGSTDQEKI--EFLKEAHLMSKFNHPNILKQLG--VCLLNEPQY--IILELMEGGDLLTYLRKARMATFYgp 2001
Cdd:PHA02988   45 EVIIRTFKKFHKGHKVLidITENEIKNLRRIDSNNILKIYGfiIDIVDDLPRlsLILEYCTRGYLREVLDKEKDLSFK-- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2002 lltlvDLVDLCVDISKGcvyLERMHFI----HRDLAARNCLVSvKDYTspriVKIGDFGLARdIYKNDYYRKrgegllpV 2077
Cdd:PHA02988  123 -----TKLDMAIDCCKG---LYNLYKYtnkpYKNLTSVSFLVT-ENYK----LKIICHGLEK-ILSSPPFKN-------V 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2078 RWMA--PESLMDGIF---TTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLN-YVQTGGRLEPPRNCPDDLWNLMTQCWA 2151
Cdd:PHA02988  182 NFMVyfSYKMLNDIFseyTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDlIINKNNSLKLPLDCPLEIKCIVEACTS 260
                         250       260
                  ....*....|....*....|...
gi 767943404 2152 QEPDQRPTFHRIQDQLQLFRNFF 2174
Cdd:PHA02988  261 HDSIKRPNIKEILYNLSLYKFYI 283
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
1902-2158 1.51e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.91  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVD-ILGvgsgeIKVAVKTLKKG-STDQEKIE-FLKEAHLMSKFNHPNIlkqlgVCLL-----NEP 1973
Cdd:NF033483   14 RIGRGGMAEVYL--AKDtRLD-----RDVAVKVLRPDlARDPEFVArFRREAQSAASLSHPNI-----VSVYdvgedGGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKarmatfYGPlltlvDLVDLCVDISKG-CVYLE---RMHFIHRDLAARNCLVSvKDytspRI 2049
Cdd:NF033483   82 PYIVMEYVDGRTLKDYIRE------HGP-----LSPEEAVEIMIQiLSALEhahRNGIVHRDIKPQNILIT-KD----GR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDI------YKND-----YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHS 2118
Cdd:NF033483  146 VKVTDFGIARALssttmtQTNSvlgtvHY------------LSPEQARGGTVDARSDIYSLGIVLYEMLT-GRPPFDGDS 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767943404 2119 NLDV-LNYVQtggrlEPPR-------NCPDDLWNLMTQCWAQEPDQRP 2158
Cdd:NF033483  213 PVSVaYKHVQ-----EDPPppselnpGIPQSLDAVVLKATAKDPDDRY 255
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
211-290 2.23e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.83  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  211 NIESSSPDTVEVSWDPPQFPGGPILGYNLRLISKNQK-----LDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGEGPEAE 285
Cdd:cd00063     8 RVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGdwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSE 87

                  ....*
gi 767943404  286 SSITT 290
Cdd:cd00063    88 SVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
103-297 1.20e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 66.95  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  103 EVLENADLPTAP---FASSIGSHNMTLRWKSANFSGVK-YIIQWKYAQLlGSWTYTKTVSRPSYVVKPLHPFTEYIFRVV 178
Cdd:COG3401   225 SVTTPTTPPSAPtglTATADTPGSVTLSWDPVTESDATgYRVYRSNSGD-GPFTKVATVTTTSYTDTGLTNGTTYYYRVT 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  179 WIFTAQLQlySPPSPSYRTHPHGVPETAPLIRNIESSSPDTVEVSWDPPqfPGGPILGYNL-RLISKN---QKLDAGTQR 254
Cdd:COG3401   304 AVDAAGNE--SAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS--SDADVTGYNVyRSTSGGgtyTKIAETVTT 379
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767943404  255 TSFQFYSTLPNTIYRFSIAAVNEVGEGPEAESSITTSSSAVQQ 297
Cdd:COG3401   380 TSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAAS 422
fn3 pfam00041
Fibronectin type III domain;
206-283 1.64e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 1.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   206 APLIRNIESSSPDTVEVSWDPPQFPGGPILGYNLRLISKN-----QKLDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGE 280
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsgepwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                   ...
gi 767943404   281 GPE 283
Cdd:pfam00041   82 GPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
206-281 1.48e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.47  E-value: 1.48e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404    206 APLIRNIESSSPDTVEVSWDPPQFPG--GPILGYNLRLISKN---QKLDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGE 280
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82

                    .
gi 767943404    281 G 281
Cdd:smart00060   83 G 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
993-1099 6.35e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.11  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  993 PSAPENPRIfilpsgKCCNKNEVVVefRWNKPKHENGVLTKFEIFYNISNQsitnktcEDWIAVNVTP-SVMSFQLEGMS 1071
Cdd:cd00063     1 PSPPTNLRV------TDVTSTSVTL--SWTPPEDDGGPITGYVVEYREKGS-------GDWKEVEVTPgSETSYTLTGLK 65
                          90       100
                  ....*....|....*....|....*...
gi 767943404 1072 PRCFIAFQVRAFTSKGPGPYADVVKSTT 1099
Cdd:cd00063    66 PGTEYEFRVRAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1611-1700 7.57e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.11  E-value: 7.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1611 PEKPYSLVPEN---TSLQFNWKAPL--NVNLIRFWVELQKWKYNEFYHVKTSCSQGPAYVcnITNLQPYTSYNVRVVVVY 1685
Cdd:cd00063     1 PSPPTNLRVTDvtsTSVTLSWTPPEddGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT--LTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 767943404 1686 KTGENSTSLPESFKT 1700
Cdd:cd00063    79 GGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
111-194 1.03e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.73  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  111 PTAPFASSIGSHNMTLRWKSANFSG---VKYIIQWKYAQLLGSWTYTKT-VSRPSYVVKPLHPFTEYIFRVVWIFTAQlq 186
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGgpiTGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNGGG-- 81

                  ....*...
gi 767943404  187 lYSPPSPS 194
Cdd:cd00063    82 -ESPPSES 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
111-178 1.26e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 1.26e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404    111 PTAPFASSIGSHNMTLRWKSANFSG-VKYIIQWK--YAQLLGSW-TYTKTVSRPSYVVKPLHPFTEYIFRVV 178
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGiTGYIVGYRveYREEGSEWkEVNVTPSSTSYTLTGLKPGTEYEFRVR 75
fn3 pfam00041
Fibronectin type III domain;
994-1091 4.27e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 49.72  E-value: 4.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   994 SAPENPRIfilpsgkcCNKNEVVVEFRWNKPKHENGVLTKFEIFYNISNQSitnktcEDWIAVNVTPSVMSFQLEGMSPR 1073
Cdd:pfam00041    1 SAPSNLTV--------TDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSG------EPWNEITVPGTTTSVTLTGLKPG 66
                           90
                   ....*....|....*...
gi 767943404  1074 CFIAFQVRAFTSKGPGPY 1091
Cdd:pfam00041   67 TEYEVRVQAVNGGGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
993-1089 1.41e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.99  E-value: 1.41e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404    993 PSAPENPRIfilpsgKCCNKNEVVVefRWNKPKHENGvlTKFEIFYNISNQSitnkTCEDWIAVNVTPSVMSFQLEGMSP 1072
Cdd:smart00060    1 PSPPSNLRV------TDVTSTSVTL--SWEPPPDDGI--TGYIVGYRVEYRE----EGSEWKEVNVTPSSTSYTLTGLKP 66
                            90
                    ....*....|....*..
gi 767943404   1073 RCFIAFQVRAFTSKGPG 1089
Cdd:smart00060   67 GTEYEFRVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1705-1794 1.64e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.26  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1705 PNKPGIPKLLEGSKNSI--QWEKAEDNGCRITYYILEIRKSTSNnlqnqnlRWKmTFNGSCSSVCTWKSKNLK--GIFQF 1780
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVtlSWTPPEDDGGPITGYVVEYREKGSG-------DWK-EVEVTPGSETSYTLTGLKpgTEYEF 72
                          90
                  ....*....|....
gi 767943404 1781 RVVAANNLGFGEYS 1794
Cdd:cd00063    73 RVRAVNGGGESPPS 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1621-1689 2.51e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 2.51e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404   1621 NTSLQFNWKAPLNVNLIRFWVELQKWKYNEFYHVKTSCSQGPAYVCNITNLQPYTSYNVRVVVVYKTGE 1689
Cdd:smart00060   14 STSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82
fn3 pfam00041
Fibronectin type III domain;
111-178 1.28e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 1.28e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404   111 PTAPFASSIGSHNMTLRWKSANFSG---VKYIIQWKYAQLLGSWTyTKTVSRP--SYVVKPLHPFTEYIFRVV 178
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNSGEPWN-EITVPGTttSVTLTGLKPGTEYEVRVQ 74
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1383-1711 4.50e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 48.85  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1383 AYSSVMQPFPDKAFLSLASDTVEPTILNATNTSLTIRLPLAKTNLTWYGITSPTPTYLVYYAEVNDRKNSSDLKYRILEF 1462
Cdd:COG3401   110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1463 QDSIALIEDLQPFSTYMIQIAVKNYYSDPlehlPPGKEIWGKTKNGVPEAVQLINTTVRSDTSLIISWReshkPNGPKES 1542
Cdd:COG3401   190 TTLVDGGGDIEPGTTYYYRVAATDTGGES----APSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD----PVTESDA 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1543 VRYQLaishlalipetplRQSEFPNGRLTLL---------VTRLSGGNIYVLKVLACHSEEMWCTESHPVTVEMFNT-PE 1612
Cdd:COG3401   262 TGYRV-------------YRSNSGDGPFTKVatvtttsytDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTpPA 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1613 KPYSL---VPENTSLQFNWKAPLNVNLIRFWVELQKWKYNEFYHVKTSCSqGPAYVcnITNLQPYTSYNVRVVVVYKTGE 1689
Cdd:COG3401   329 APSGLtatAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAETVT-TTSYT--DTGLTPGTTYYYKVTAVDAAGN 405
                         330       340
                  ....*....|....*....|..
gi 767943404 1690 NSTSLPESFKTKAGVPNKPGIP 1711
Cdd:COG3401   406 ESAPSEEVSATTASAASGESLT 427
fn3 pfam00041
Fibronectin type III domain;
1621-1693 2.04e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.02  E-value: 2.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404  1621 NTSLQFNWKAPLNVNLIRFWVELQKWKYNEFYHVKTSCSQGPAYVCNITNLQPYTSYNVRVVVVYKTGENSTS 1693
Cdd:pfam00041   13 STSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
561-619 6.24e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.94  E-value: 6.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  561 YEVKVSTQDPPEVTHI-FLNISGTMLNVPELQSAMKYKVSVRASSPKRPGPWSEPSVGTT 619
Cdd:cd00063    34 YVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
1902-2168 0e+00

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 554.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd05044     2 FLGSGAFGEVFEGTAKDILGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtSPRIVKIGDFGLARDI 2061
Cdd:cd05044    82 EGGDLLSYLRAARPTAFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDY-RERVVKIGDFGLARDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDD 2141
Cdd:cd05044   161 YKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPDD 240
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2142 LWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05044   241 LYELMLRCWSTDPEERPSFARILEQLQ 267
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
1897-2167 2.70e-127

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 400.33  E-value: 2.70e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  1897 LTLRLLLGSGAFGEVYEGTAVDilGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKG--EGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  1977 ILELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFG 2056
Cdd:pfam07714   79 VTEYMPGGDLLDFLRKHK------RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLV-----SENLVVKISDFG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  2057 LARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPR 2136
Cdd:pfam07714  148 LSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPE 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 767943404  2137 NCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:pfam07714  228 NCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1903-2168 1.68e-125

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 395.75  E-value: 1.68e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGvgsGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd00192     3 LGEGAFGEVYKGKLKGGDG---KTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKAR--MATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARD 2060
Cdd:cd00192    80 GGDLLDFLRKSRpvFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLV-----GEDLVVKISDFGLSRD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPD 2140
Cdd:cd00192   155 IYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPD 234
                         250       260
                  ....*....|....*....|....*...
gi 767943404 2141 DLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd00192   235 ELYELMLSCWQLDPEDRPTFSELVERLE 262
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
1897-2167 2.26e-125

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 394.98  E-value: 2.26e-125
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   1897 LTLRLLLGSGAFGEVYEGTAVDILGvgSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLKGKGG--KKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   1977 ILELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFG 2056
Cdd:smart00219   79 VMEYMEGGDLLSYLRKNR------PKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG-----ENLVVKISDFG 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   2057 LARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPR 2136
Cdd:smart00219  148 LSRDLYDDDYYRKRG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPP 226
                           250       260       270
                    ....*....|....*....|....*....|.
gi 767943404   2137 NCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:smart00219  227 NCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1897-2167 8.53e-125

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 393.45  E-value: 8.53e-125
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   1897 LTLRLLLGSGAFGEVYEGTAVDILGvgSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGKGD--GKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   1977 ILELMEGGDLLTYLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFG 2056
Cdd:smart00221   79 VMEYMPGGDLLDYLRKNRPKEL-----SLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG-----ENLVVKISDFG 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   2057 LARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPR 2136
Cdd:smart00221  149 LSRDLYDDDYYKVKG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPP 227
                           250       260       270
                    ....*....|....*....|....*....|.
gi 767943404   2137 NCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:smart00221  228 NCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
1893-2168 1.56e-117

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 373.26  E-value: 1.56e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDILGvGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd05036     4 PRKNLTLIRALGQGAFGEVYEGTVSGMPG-DPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKdyTSPRIVKI 2052
Cdd:cd05036    83 PRFILLELMAGGDLKSFLRENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCK--GPGRVAKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05036   161 GDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRM 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05036   241 DPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLN 276
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1892-2163 5.08e-107

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 343.17  E-value: 5.08e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAVDILGvGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLN 1971
Cdd:cd05032     3 LPREKITLIRELGQGSFGMVYEGLAKGVVK-GEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1972 EPQYIILELMEGGDLLTYLR----KARMATFYGPLLTLVDLVDlCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTsp 2047
Cdd:cd05032    82 QPTLVVMELMAKGDLKSYLRsrrpEAENNPGLGPPTLQKFIQM-AAEIADGMAYLAAKKFVHRDLAARNCMVA-EDLT-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 riVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQ 2127
Cdd:cd05032   158 --VKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVI 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2128 TGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05032   236 DGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEI 271
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
1893-2168 8.74e-90

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 294.18  E-value: 8.74e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDILGvGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd05061     4 SREKITLLRELGQGSFGMVYEGNARDIIK-GEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARMATFYG---PLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspri 2049
Cdd:cd05061    83 PTLVVMELMAHGDLKSYLRSLRPEAENNpgrPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVA-HDFT---- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTG 2129
Cdd:cd05061   158 VKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDG 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2130 GRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05061   238 GYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLK 276
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
1892-2167 2.15e-85

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 282.00  E-value: 2.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLL 1970
Cdd:cd05053     9 LPRDRLTLGKPLGEGAFGQVVKAEAVGLDNKPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQYIILELMEGGDLLTYLRKAR-MATFYGPLLTLVDLVDL--------CVDISKGCVYLERMHFIHRDLAARNCLVsv 2041
Cdd:cd05053    89 DGPLYVVVEYASKGNLREFLRARRpPGEEASPDDPRVPEEQLtqkdlvsfAYQVARGMEYLASKKCIHRDLAARNVLV-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2042 kdyTSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLD 2121
Cdd:cd05053   167 ---TEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEE 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767943404 2122 VLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05053   244 LFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDL 289
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
1903-2167 1.51e-84

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 277.63  E-value: 1.51e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGtavdilgVGSGEIKVAVKTLKKGSTDQEkiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd05034     3 LGAGQFGEVWMG-------VWNGTTKVAVKTLKPGTMSPE--AFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLARDIy 2062
Cdd:cd05034    74 KGSLLDYLRTGE-----GRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENN-----VCKVADFGLARLI- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDDL 2142
Cdd:cd05034   143 EDDEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDEL 222
                         250       260
                  ....*....|....*....|....*
gi 767943404 2143 WNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05034   223 YDIMLQCWKKEPEERPTFEYLQSFL 247
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
1903-2168 3.70e-83

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 273.55  E-value: 3.70e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdilgVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd05041     3 IGRGNFGDVYRGV------LKPDNTEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKArmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLARDIY 2062
Cdd:cd05041    77 GGSLLTFLRKK------GARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENN-----VLKISDFGMSREEE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDDL 2142
Cdd:cd05041   146 DGEYTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPEAV 225
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2143 WNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05041   226 YRLMLQCWAYDPENRPSFSEIYNELQ 251
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
1892-2168 7.15e-83

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 274.98  E-value: 7.15e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGEIK----------VAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNI 1961
Cdd:cd05051     2 FPREKLEFVEKLGEGQFGEVHLCEANGLSDLTSDDFIgndnkdepvlVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1962 LKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMAT-----FYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARN 2036
Cdd:cd05051    82 VRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETqgasaTNSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATRN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2037 CLVSvKDYTspriVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLG-HQPYP 2115
Cdd:cd05051   162 CLVG-PNYT----IKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCkEQPYE 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2116 AHSNLDVLN-----YVQTGGR--LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05051   237 HLTDEQVIEnagefFRDDGMEvyLSRPPNCPKEIYELMLECWRRDEEDRPTFREIHLFLQ 296
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
1893-2168 1.60e-82

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 273.19  E-value: 1.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDiLGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd05049     3 KRDTIVLKRELGEGAFGKVFLGECYN-LEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDL-------------CVDISKGCVYLERMHFIHRDLAARNCLV 2039
Cdd:cd05049    82 PLLMVFEYMEHGDLNKFLRS------HGPDAAFLASEDSapgeltlsqllhiAVQIASGMVYLASQHFVHRDLATRNCLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2040 SVKdytspRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSN 2119
Cdd:cd05049   156 GTN-----LVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSN 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767943404 2120 LDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05049   231 TEVIECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQ 279
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1893-2170 1.39e-81

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 270.05  E-value: 1.39e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGtavdilgVGSGEIKVAVKTLKKGSTDQEkiEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd05068     6 DRKSLKLLRKLGSGQFGEVWEG-------LWNNTTPVAVKTLKPGTMDPE--DFLREAQIMKKLRHPKLIQLYAVCTLEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKArmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKI 2052
Cdd:cd05068    77 PIYIITELMKHGSLLEYLQGK------GRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENN-----ICKV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05068   146 ADFGLARVIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGYRM 225
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLF 2170
Cdd:cd05068   226 PCPPNCPPQLYDIMLECWKADPMERPTFETLQWKLEDF 263
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
1893-2163 4.12e-80

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 266.13  E-value: 4.12e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDILGvGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd05062     4 AREKITMSRELGQGSFGMVYEGIAKGVVK-DEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARMATFYGPLLTL---VDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspri 2049
Cdd:cd05062    83 PTLVIMELMTRGDLKSYLRSLRPEMENNPVQAPpslKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVA-EDFT---- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTG 2129
Cdd:cd05062   158 VKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEG 237
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767943404 2130 GRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05062   238 GLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 271
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
1896-2168 5.44e-79

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 263.36  E-value: 5.44e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1896 KLTLRLLLGSGAFGEVYEGTAVDILGVgSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd05045     1 NLVLGKTLGEGEFGKVVKATAFRLKGR-AGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMA--TFYGPLLTLVDLVDLCVD---------------ISKGCVYLERMHFIHRDLAARNCL 2038
Cdd:cd05045    80 LIVEYAKYGSLRSFLRESRKVgpSYLGSDGNRNSSYLDNPDeraltmgdlisfawqISRGMQYLAEMKLVHRDLAARNVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2039 VSvkdytSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHS 2118
Cdd:cd05045   160 VA-----EGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIA 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767943404 2119 NLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05045   235 PERLFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELE 284
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
1899-2168 6.19e-79

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 263.08  E-value: 6.19e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1899 LRLL--LGSGAFGEVYEGtavDILGVGSGE--IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ 1974
Cdd:cd05048     7 VRFLeeLGEGAFGKVYKG---ELLGPSSEEsaISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYL--RKARMATFYGPLLTLVDLVDLCVD-------ISKGCVYLERMHFIHRDLAARNCLVSVKdyt 2045
Cdd:cd05048    84 CMLFEYMAHGDLHEFLvrHSPHSDVGVSSDDDGTASSLDQSDflhiaiqIAAGMEYLSSHHYVHRDLAARNCLVGDG--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2046 spRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNY 2125
Cdd:cd05048   161 --LTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIEM 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2126 VQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05048   239 IRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLR 281
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
1894-2167 4.90e-78

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 259.66  E-value: 4.90e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYEGTAVDILGVgsgEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLlNEP 1973
Cdd:cd05056     5 REDITLGRCIGEGQFGDVYQGVYMSPENE---KIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVIT-ENP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKARMATfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIG 2053
Cdd:cd05056    81 VWIVMELAPLGELRSYLQVNKYSL------DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS-----SPDCVKLG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDYYrKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLE 2133
Cdd:cd05056   150 DFGLSRYMEDESYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLP 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767943404 2134 PPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05056   229 MPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQL 262
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
1892-2168 1.73e-77

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 258.99  E-value: 1.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAvdiLGVGSGE--IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCL 1969
Cdd:cd05050     2 YPRNNIEYVRDIGQGAFGRVFQARA---PGLLPYEpfTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 LNEPQYIILELMEGGDLLTYLR-------------KARMATFYGPLLTLVDLVDLCV--DISKGCVYLERMHFIHRDLAA 2034
Cdd:cd05050    79 VGKPMCLLFEYMAYGDLNEFLRhrspraqcslshsTSSARKCGLNPLPLSCTEQLCIakQVAAGMAYLSERKFVHRDLAT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2035 RNCLVSvkdytSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPY 2114
Cdd:cd05050   159 RNCLVG-----ENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPY 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2115 PAHSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05050   234 YGMAHEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQ 287
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
1891-2163 2.93e-76

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 255.08  E-value: 2.93e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1891 AFPREKLTLRLLLGSGAFGEVYEGTAVDILgVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLL 1970
Cdd:cd05046     1 AFPRSNLQEITTLGRGEFGEVFLAKAKGIE-EEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQYIILELMEGGDLLTYLR--KARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPR 2048
Cdd:cd05046    80 AEPHYMILEYTDLGDLKQFLRatKSKDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVS-----SQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDIYKNDYYRKRgEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQT 2128
Cdd:cd05046   155 EVKVSLLSLSKDVYNSEYYKLR-NALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQA 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2129 GG-RLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05046   234 GKlELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSEL 269
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1897-2167 4.23e-75

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 250.83  E-value: 4.23e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYegtavdiLGVGSGEIKVAVKTLKKGSTDQEkiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd05059     6 LTFLKELGSGQFGVVH-------LGKWRGKIDVAIKMIKEGSMSED--DFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLR----KARMATFYGplltlvdlvdLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd05059    77 VTEYMANGCLLNYLRerrgKFQTEQLLE----------MCKDVCEAMEYLESNGFIHRDLAARNCLVG-----EQNVVKV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGLlPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05059   142 SDFGLARYVLDDEYTSSVGTKF-PVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRL 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05059   221 YRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1891-2170 8.73e-75

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 249.96  E-value: 8.73e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1891 AFPREKLTLRLLLGSGAFGEVYEGTAvdilgvgSGEiKVAVKTLKKGSTDQEKieFLKEAHLMSKFNHPNILKQLGVCLL 1970
Cdd:cd05039     2 AINKKDLKLGELIGKGEFGDVMLGDY-------RGQ-KVAVKCLKDDSTAAQA--FLAEASVMTTLRHPNLVQLLGVVLE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQYIILELMEGGDLLTYLR-KARMAtfygplLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprI 2049
Cdd:cd05039    72 GNGLYIVTEYMAKGSLVDYLRsRGRAV------ITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDN-----V 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKNdyyrkRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTG 2129
Cdd:cd05039   141 AKVSDFGLAKEASSN-----QDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKG 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767943404 2130 GRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLF 2170
Cdd:cd05039   216 YRMEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
1897-2168 1.92e-74

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 249.21  E-value: 1.92e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTavdILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd05033     6 VTIEKVIGGGEFGEVCSGS---LKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKAR--------MATFYGplltlvdlvdlcvdISKGCVYLERMHFIHRDLAARNCLVSvkdytSPR 2048
Cdd:cd05033    83 VTEYMENGSLDKFLRENDgkftvtqlVGMLRG--------------IASGMKYLSEMNYVHRDLAARNILVN-----SDL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDI-YKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQ 2127
Cdd:cd05033   144 VCKVSDFGLSRRLeDSEATYTTKG-GKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVE 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767943404 2128 TGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05033   223 DGYRLPPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLD 263
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1897-2168 2.45e-73

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 246.29  E-value: 2.45e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTAVDILGVgsgEIKVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ- 1974
Cdd:cd05035     1 LKLGKILGEGEFGSVMEAQLKQDDGS---QLKVAVKTMKvDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLn 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 -----YIILELMEGGDLLTYLRKARMAT--FYGPLLTLVDLVdlcVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTsp 2047
Cdd:cd05035    78 kppspMVILPFMKHGDLHSYLLYSRLGGlpEKLPLQTLLKFM---VDIAKGMEYLSNRNFIHRDLAARNCMLD-ENMT-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 riVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQ 2127
Cdd:cd05035   152 --VCVADFGLSRKIYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLR 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767943404 2128 TGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05035   230 NGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLE 270
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1903-2167 8.36e-73

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 244.18  E-value: 8.36e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLlNEPQYIILELME 1982
Cdd:cd05060     3 LGHGNFGSVRKGV---YLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCK-GEPLMLVMELAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARDI- 2061
Cdd:cd05060    79 LGPLLKYLKKRREIP-------VSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ-----AKISDFGMSRALg 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDD 2141
Cdd:cd05060   147 AGSDYYRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECPQE 226
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2142 LWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05060   227 IYSIMLSCWKYRPEDRPTFSELESTF 252
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
1903-2168 2.45e-72

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 242.91  E-value: 2.45e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdilgVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd05084     4 IGRGNFGEVFSGR------LRADNTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKArmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLARDIY 2062
Cdd:cd05084    78 GGDFLTFLRTE------GPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKN-----VLKISDFGMSREEE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDDL 2142
Cdd:cd05084   147 DGVYAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEV 226
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2143 WNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05084   227 YRLMEQCWEYDPRKRPSFSTVHQDLQ 252
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
1893-2171 1.35e-71

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 241.75  E-value: 1.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEgtAVDILGVGSGEiKVAVKTLKK---GSTDQEkiEFLKEAHLMSKFNHPNILKQLGVCL 1969
Cdd:cd05074     7 QEQQFTLGRMLGKGEFGSVRE--AQLKSEDGSFQ-KVAVKMLKAdifSSSDIE--EFLREAACMKEFDHPNVIKLIGVSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 LNEPQ------YIILELMEGGDLLTYLRKARMAT--FYGPLLTLVDLVdlcVDISKGCVYLERMHFIHRDLAARNCLVSv 2041
Cdd:cd05074    82 RSRAKgrlpipMVILPFMKHGDLHTFLLMSRIGEepFTLPLQTLVRFM---IDIASGMEYLSSKNFIHRDLAARNCMLN- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2042 KDYTspriVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLD 2121
Cdd:cd05074   158 ENMT----VCVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSE 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767943404 2122 VLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFR 2171
Cdd:cd05074   234 IYNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELIW 283
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
1903-2167 4.31e-71

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 238.98  E-value: 4.31e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDIlgvgsgeiKVAVKTLKKGSTDQEKI-EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd13999     1 IGSGSFGEVYKGKWRGT--------DVAIKKLKVEDDNDELLkEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARdi 2061
Cdd:cd13999    73 PGGSLYDLLHKKK------IPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILL-----DENFTVKIADFGLSR-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV-QTGGRLEPPRNCPD 2140
Cdd:cd13999   140 IKNSTTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPIQIAAAVvQKGLRPPIPPDCPP 218
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2141 DLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd13999   219 ELSKLIKRCWNEDPEKRPSFSEIVKRL 245
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
1892-2167 8.11e-71

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 241.02  E-value: 8.11e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGE-IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFN-HPNILKQLGVCL 1969
Cdd:cd05099     9 FPRDRLVLGKPLGEGCFGQVVRAEAYGIDKSRPDQtVTVAVKMLKDNATDKDLADLISEMELMKLIGkHKNIINLLGVCT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 LNEPQYIILELMEGGDLLTYLRKARMA----TFYGPLLTLVDLV----DLCV-DISKGCVYLERMHFIHRDLAARNCLVS 2040
Cdd:cd05099    89 QEGPLYVIVEYAAKGNLREFLRARRPPgpdyTFDITKVPEEQLSfkdlVSCAyQVARGMEYLESRRCIHRDLAARNVLVT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2041 VKDytsprIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNL 2120
Cdd:cd05099   169 EDN-----VMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPVE 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767943404 2121 DVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05099   244 ELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEAL 290
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
1881-2168 1.14e-70

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 240.08  E-value: 1.14e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1881 PTQEEIENLPAFPREKLTLRLLLGSGAFGEVYEGTAVDiLGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHP 1959
Cdd:cd05055    21 PTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYG-LSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLgNHE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1960 NILKQLGVCLLNEPQYIILELMEGGDLLTYLRKAR--MATFygplltlVDLVDLCVDISKGCVYLERMHFIHRDLAARNC 2037
Cdd:cd05055   100 NIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKResFLTL-------EDLLSFSYQVAKGMAFLASKNCIHRDLAARNV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2038 LVsvkdyTSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAH 2117
Cdd:cd05055   173 LL-----THGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGM 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2118 S-NLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05055   248 PvDSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIG 299
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
1902-2167 1.23e-70

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 237.98  E-value: 1.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgsgEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd05085     3 LLGKGNFGEVYKGTLKD-------KTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLARDi 2061
Cdd:cd05085    76 PGGDFLSFLRKKK------DELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENN-----ALKISDFGMSRQ- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDD 2141
Cdd:cd05085   144 EDDGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPED 223
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2142 LWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05085   224 IYKIMQRCWDYNPENRPKFSELQKEL 249
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
1894-2168 3.52e-70

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 237.56  E-value: 3.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYEGTAVDILGvGSGEIKVAVKTLKKgSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEP 1973
Cdd:cd05092     4 RRDIVLKWELGEGAFGKVFLAECHNLLP-EQDKMLVAVKALKE-ATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLR----------KARMATfYGPLLTLVDLVDlCVDISKGCVYLERMHFIHRDLAARNCLVSvkd 2043
Cdd:cd05092    82 LIMVFEYMRHGDLNRFLRshgpdakildGGEGQA-PGQLTLGQMLQI-ASQIASGMVYLASLHFVHRDLATRNCLVG--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2044 ytSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVL 2123
Cdd:cd05092   157 --QGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAI 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767943404 2124 NYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05092   235 ECITQGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQ 279
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
1902-2160 3.91e-70

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 236.99  E-value: 3.91e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDILGVgsgEIKVAVKTLKKgSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLLNE-PQYIILE 1979
Cdd:cd05058     2 VIGKGHFGCVYHGTLIDSDGQ---KIHCAVKSLNR-ITDIEEVEqFLKEGIIMKDFSHPNVLSLLGICLPSEgSPLVVLP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRK-ARMATF-----YGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIG 2053
Cdd:cd05058    78 YMKHGDLRNFIRSeTHNPTVkdligFG------------LQVAKGMEYLASKKFVHRDLAARNCMLD-ESFT----VKVA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDYY---RKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGG 2130
Cdd:cd05058   141 DFGLARDIYDKEYYsvhNHTG-AKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGR 219
                         250       260       270
                  ....*....|....*....|....*....|
gi 767943404 2131 RLEPPRNCPDDLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd05058   220 RLLQPEYCPDPLYEVMLSCWHPKPEMRPTF 249
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
1894-2168 6.62e-70

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 237.14  E-value: 6.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYEGTAVDILGVgsgEIKVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd14204     6 RNLLSLGKVLGEGEFGSVMEGELQQPDGT---NHKVAVKTMKLDNFSQREIEeFLSEAACMKDFNHPNVIRLLGVCLEVG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYI-----ILELMEGGDLLTYLRKAR--MATFYGPLLTLVDLVdlcVDISKGCVYLERMHFIHRDLAARNCLVSvKDYT 2045
Cdd:cd14204    83 SQRIpkpmvILPFMKYGDLHSFLLRSRlgSGPQHVPLQTLLKFM---IDIALGMEYLSSRNFLHRDLAARNCMLR-DDMT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2046 spriVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNY 2125
Cdd:cd14204   159 ----VCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDY 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2126 VQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14204   235 LLHGHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLE 277
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
1893-2167 2.29e-68

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 231.55  E-value: 2.29e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGtavdilgVGSGEIKVAVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd05148     4 PREEFTLERKLGSGYFGEVWEG-------LWKNRVRVAIKILKSDDLLKQQ-DFQKEVQALKRLRHKHLISLFAVCSVGE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKI 2052
Cdd:cd05148    76 PVYIITELMEKGSLLAFLRSPE-----GQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVG-EDLV----CKV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARdIYKNDYYRKRGEGLlPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05148   146 ADFGLAR-LIKEDVYLSSDKKI-PYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRM 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05148   224 PCPAKCPQEIYKIMLECWAAEPEDRPSFKALREEL 258
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
1903-2167 3.04e-68

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 231.08  E-value: 3.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGtavDILGVGSGEIKVAVKTLKKGSTDQEKI--EFLKEAHLMSKFNHPNILKQLGVcLLNEPQYIILEL 1980
Cdd:cd05040     3 LGDGSFGVVRRG---EWTTPSGKVIQVAVKCLKSDVLSQPNAmdDFLKEVNAMHSLDHPNLIRLYGV-VLSSPLMMVTEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKArmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARD 2060
Cdd:cd05040    79 APLGSLLDRLRKD------QGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLA-----SKDKVKIGDFGLMRA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYKN-DYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYV-QTGGRLEPPRNC 2138
Cdd:cd05040   148 LPQNeDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIdKEGERLERPDDC 227
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2139 PDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05040   228 PQDIYNVMLQCWAHKPADRPTFVALRDFL 256
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
1892-2167 7.11e-68

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 231.79  E-value: 7.11e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVY----EGTAvDILGVGSGE-----IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNIL 1962
Cdd:cd05097     2 FPRQQLRLKEKLGEGQFGEVHlceaEGLA-EFLGEGAPEfdgqpVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1963 KQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATFYG-----PLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNC 2037
Cdd:cd05097    81 RLLGVCVSDDPLCMITEYMENGDLNQFLSQREIESTFThanniPSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2038 LVSvKDYTspriVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTL-GHQPYPA 2116
Cdd:cd05097   161 LVG-NHYT----IKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2117 HSNLDVL----NYVQTGGR---LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05097   236 LSDEQVIentgEFFRNQGRqiyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFL 293
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
1896-2168 6.26e-67

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 228.35  E-value: 6.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1896 KLTLRLLLGSGAFGEVYEGTavdiLGVGSGEIKVAVKTLKKG-STDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ 1974
Cdd:cd05075     1 KLALGKTLGEGEFGSVMEGQ----LNQDDSVLKVAVKTMKIAiCTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTES 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 ------YIILELMEGGDLLTYLRKARMAT--FYGPLLTLVDLVdlcVDISKGCVYLERMHFIHRDLAARNCLVSvkdytS 2046
Cdd:cd05075    77 egypspVVILPFMKHGDLHSFLLYSRLGDcpVYLPTQMLVKFM---TDIASGMEYLSSKNFIHRDLAARNCMLN-----E 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2047 PRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYV 2126
Cdd:cd05075   149 NMNVCVADFGLSKKIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYL 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2127 QTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05075   229 RQGNRLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELE 270
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
1894-2168 7.50e-67

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 227.30  E-value: 7.50e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYEGTAvdilgvGSGEIKVAVKTLKKGSTDQEkiEFLKEAHLMSKFNHPNILKQLGVCLLNEP 1973
Cdd:cd05052     5 RTDITMKHKLGGGQYGEVYEGVW------KKYNLTVAVKTLKEDTMEVE--EFLKEAAVMKEIKHPNLVQLLGVCTREPP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIG 2053
Cdd:cd05052    77 FYIITEFMPYGNLLDYLRECNREEL-----NAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVG-----ENHLVKVA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARdIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLE 2133
Cdd:cd05052   147 DFGLSR-LMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGYRME 225
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2134 PPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05052   226 RPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALE 260
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
1893-2170 1.79e-66

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 226.85  E-value: 1.79e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYegtavdiLGVGSGEIKVAVKTLKKGSTDQEKieFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd05072     5 PRESIKLVKKLGAGQFGEVW-------MGYYNNSTKVAVKTLKPGTMSVQA--FLEEANLMKTLQHDKLVRLYAVVTKEE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARMATFYGPLLTLVDlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd05072    76 PIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFS-----AQIAEGMAYIERKNYIHRDLRAANVLVS-----ESLMCKI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05072   146 ADFGLARVIEDNEYTAREG-AKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRM 224
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLF 2170
Cdd:cd05072   225 PRMENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDDF 262
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
1892-2170 5.08e-66

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 225.76  E-value: 5.08e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGtavdiLGVGSGE---IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVC 1968
Cdd:cd05057     4 VKETELEKGKVLGSGAFGTVYKG-----VWIPEGEkvkIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGIC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1969 LLNEPQyIILELMEGGDLLTYLRKARMAtfygplLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPR 2048
Cdd:cd05057    79 LSSQVQ-LITQLMPLGCLLDYVRNHRDN------IGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVK-----TPN 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDI-YKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQ 2127
Cdd:cd05057   147 HVKITDFGLAKLLdVDEKEYHAEG-GKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLE 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2128 TGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLF 2170
Cdd:cd05057   226 KGERLPQPPICTIDVYMVLVKCWMIDAESRPTFKELANEFSKM 268
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
1893-2170 9.30e-66

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 224.38  E-value: 9.30e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYegtavdiLGVGSGEIKVAVKTLKKGSTDQEKieFLKEAHLMSKFNHPNILKqLGVCLLNE 1972
Cdd:cd05067     5 PRETLKLVERLGAGQFGEVW-------MGYYNGHTKVAIKSLKQGSMSPDA--FLAEANLMKQLQHQRLVR-LYAVVTQE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRkarmaTFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd05067    75 PIYIITEYMENGSLVDFLK-----TPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVS-----DTLSCKI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05067   145 ADFGLARLIEDNEYTAREG-AKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRM 223
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLF 2170
Cdd:cd05067   224 PRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVLEDF 261
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
1893-2167 1.17e-65

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 225.66  E-value: 1.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGEI-KVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLL 1970
Cdd:cd05098    11 PRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVtKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQYIILELMEGGDLLTYLRKAR---MATFYGPLLTLVDLVDL-----CV-DISKGCVYLERMHFIHRDLAARNCLVsv 2041
Cdd:cd05098    91 DGPLYVIVEYASKGNLREYLQARRppgMEYCYNPSHNPEEQLSSkdlvsCAyQVARGMEYLASKKCIHRDLAARNVLV-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2042 kdyTSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLD 2121
Cdd:cd05098   169 ---TEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEE 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767943404 2122 VLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05098   246 LFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDL 291
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
1892-2167 2.20e-65

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 224.68  E-value: 2.20e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLL 1970
Cdd:cd05054     4 FPRDRLKLGKPLGRGAFGKVIQASAFGIDKSATCR-TVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACTK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NE-PQYIILELMEGGDLLTYLRKARMATFYGPLLTLVDL--VDLCVDISKGCVYLER-----------MHF------IHR 2030
Cdd:cd05054    83 PGgPLMVIVEFCKFGNLSNYLRSKREEFVPYRDKGARDVeeEEDDDELYKEPLTLEDlicysfqvargMEFlasrkcIHR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2031 DLAARNCLVSVKDytsprIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLG 2110
Cdd:cd05054   163 DLAARNILLSENN-----VVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLG 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2111 HQPYPA-HSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05054   238 ASPYPGvQMDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
1892-2167 2.67e-64

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 222.20  E-value: 2.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGE-IKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCL 1969
Cdd:cd05101    21 FPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEaVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 LNEPQYIILELMEGGDLLTYLRKAR---MATFYGPLLTLVDLVD-----LCV-DISKGCVYLERMHFIHRDLAARNCLVs 2040
Cdd:cd05101   101 QDGPLYVIVEYASKGNLREYLRARRppgMEYSYDINRVPEEQMTfkdlvSCTyQLARGMEYLASQKCIHRDLAARNVLV- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2041 vkdyTSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNL 2120
Cdd:cd05101   180 ----TENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVE 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767943404 2121 DVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05101   256 ELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDL 302
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
1893-2167 3.36e-64

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 219.44  E-value: 3.36e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREkLTLRLLLGSGAFGEVYegtavdiLGVGSGEIKVAVKTLKKGSTDQEkiEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd05112     3 PSE-LTFVQEIGSGQFGLVH-------LGYWLNKDKVAIKTIREGAMSEE--DFIEEAEVMMKLSHPKLVQLYGVCLEQA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd05112    73 PICLVFEFMEHGCLSDYLRTQR------GLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVG-----ENQVVKV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGLlPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05112   142 SDFGMTRFVLDDQYTSSTGTKF-PVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRL 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05112   221 YKPRLASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
1892-2171 3.80e-64

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 220.33  E-value: 3.80e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTaVDILGVGSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVClln 1971
Cdd:cd05038     1 FEERHLKFIKQLGEGHFGSVELCR-YDPLGDNTGE-QVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVC--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1972 EPQY-----IILELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytS 2046
Cdd:cd05038    76 ESPGrrslrLIMEYLPSGSLRDYLQRHR------DQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVE-----S 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2047 PRIVKIGDFGLARDI-YKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLG--------------- 2110
Cdd:cd05038   145 EDLVKISDFGLAKVLpEDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGdpsqsppalflrmig 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2111 -HQPYPAHsnLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFR 2171
Cdd:cd05038   225 iAQGQMIV--TRLLELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
1892-2168 1.37e-63

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 219.48  E-value: 1.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVY--EGTAVD-------ILGVGSGE-IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNI 1961
Cdd:cd05095     2 FPRKLLTFKEKLGEGQFGEVHlcEAEGMEkfmdkdfALEVSENQpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1962 LKQLGVCLLNEPQYIILELMEGGDLLTYLrkARMATFYGPLLTLVDLVDLCVD-------ISKGCVYLERMHFIHRDLAA 2034
Cdd:cd05095    82 IRLLAVCITDDPLCMITEYMENGDLNQFL--SRQQPEGQLALPSNALTVSYSDlrfmaaqIASGMKYLSSLNFVHRDLAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2035 RNCLVSvKDYTspriVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTL-GHQP 2113
Cdd:cd05095   160 RNCLVG-KNYT----IKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFcREQP 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2114 YPAHSNLDVL----NYVQTGGR---LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05095   235 YSQLSDEQVIentgEFFRDQGRqtyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQ 296
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1903-2168 5.26e-63

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 215.94  E-value: 5.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdilgvGSGEIKVAVKTLKKGSTDQEKieFLKEAHLMSKFNHpNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14203     3 LGQGCFGEVWMGT-------WNGTTKVAIKTLKPGTMSPEA--FLEEAQIMKKLRH-DKLVQLYAVVSEEPIYIVTEFMS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDIY 2062
Cdd:cd14203    73 KGSLLDFLKDGE-----GKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVG-----DNLVCKIADFGLARLIE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLlPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDDL 2142
Cdd:cd14203   143 DNEYTARQGAKF-PIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESL 221
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2143 WNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14203   222 HELMCQCWRKDPEERPTFEYLQSFLE 247
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
1889-2167 5.40e-62

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 216.04  E-value: 5.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1889 LPAFP-----REKLTLRLLLGSGAFGEVYEGTAVDILGVGSGE-IKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNI 1961
Cdd:cd05100     1 LPADPkwelsRTRLTLGKPLGEGCFGQVVMAEAIGIDKDKPNKpVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1962 LKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMA--TFYGPLLTLVDLVDLCVD-------ISKGCVYLERMHFIHRDL 2032
Cdd:cd05100    81 INLLGACTQDGPLYVLVEYASKGNLREYLRARRPPgmDYSFDTCKLPEEQLTFKDlvscayqVARGMEYLASQKCIHRDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2033 AARNCLVsvkdyTSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQ 2112
Cdd:cd05100   161 AARNVLV-----TEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGS 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2113 PYPAHSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05100   236 PYPGIPVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDL 290
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
1894-2168 9.54e-62

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 213.75  E-value: 9.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYEGTAVDiLGVGSGEIKVAVKTLKKGStDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEP 1973
Cdd:cd05093     4 RHNIVLKRELGEGAFGKVFLAECYN-LCPEQDKILVAVKTLKDAS-DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLCVD------------ISKGCVYLERMHFIHRDLAARNCLVSv 2041
Cdd:cd05093    82 LIMVFEYMKHGDLNKFLRA------HGPDAVLMAEGNRPAEltqsqmlhiaqqIAAGMVYLASQHFVHRDLATRNCLVG- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2042 kdytSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLD 2121
Cdd:cd05093   155 ----ENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNE 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767943404 2122 VLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05093   231 VIECITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQ 277
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
1893-2168 2.43e-61

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 212.24  E-value: 2.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTavdilgvGSGEIKVAVKTLKKGSTDQEKieFLKEAHLMSKFNHPNILKQLGVcLLNE 1972
Cdd:cd05069    10 PRESLRLDVKLGQGCFGEVWMGT-------WNGTTKVAIKTLKPGTMMPEA--FLQEAQIMKKLRHDKLVPLYAV-VSEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd05069    80 PIYIVTEFMGKGSLLDFLKEGD-----GKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVG-----DNLVCKI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05069   150 ADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRM 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05069   229 PCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLE 264
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
1894-2170 1.49e-60

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 210.00  E-value: 1.49e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYEGTAVDILGVgsgEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCL-LNE 1972
Cdd:cd05043     5 RERVTLSDLLQEGTFGRIFHGILRDEKGK---EEEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIeDGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARMATFYGPLLTLVDLV-DLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVK 2051
Cdd:cd05043    82 KPMVLYPYMNWGNLKLFLQQCRLSEANNPQALSTQQLvHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQ-----VK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLARDIYKNDY-------YRkrgegllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLN 2124
Cdd:cd05043   157 ITDNALSRDLFPMDYhclgdneNR-------PIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAA 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767943404 2125 YVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLF 2170
Cdd:cd05043   230 YLKDGYRLAQPINCPDELFAVMACCWALDPEERPSFQQLVQCLTDF 275
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
1895-2168 1.89e-60

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 208.57  E-value: 1.89e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEGtavDILGVgsgeiKVAVKTLKKGSTDQEkieFLKEAHLMSKFNHPNILKQLGVcLLNEPQ 1974
Cdd:cd05083     6 QKLTLGEIIGEGEFGAVLQG---EYMGQ-----KVAVKNIKCDVTAQA---FLEETAVMTKLQHKNLVRLLGV-ILHNGL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLR-KARMATfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIG 2053
Cdd:cd05083    74 YIVMELMSKGNLVNFLRsRGRALV------PVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDG-----VAKIS 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDyyrkrGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLE 2133
Cdd:cd05083   143 DFGLAKVGSMGV-----DNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRME 217
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2134 PPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05083   218 PPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
1894-2167 3.71e-60

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 209.10  E-value: 3.71e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYEGTAVDiLGVGSGEIKVAVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCLLNEP 1973
Cdd:cd05094     4 RRDIVLKRELGEGAFGKVFLAECYN-LSPTKDKMLVAVKTLKDPTLAARK-DFQREAELLTNLQHDHIVKFYGVCGDGDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKarmatfYGPLLT---------------LVDLVDLCVDISKGCVYLERMHFIHRDLAARNCL 2038
Cdd:cd05094    82 LIMVFEYMKHGDLNKFLRA------HGPDAMilvdgqprqakgelgLSQMLHIATQIASGMVYLASQHFVHRDLATRNCL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2039 VSvkdytSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHS 2118
Cdd:cd05094   156 VG-----ANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLS 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767943404 2119 NLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05094   231 NTEVIECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKIL 279
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
1892-2164 4.95e-60

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 209.41  E-value: 4.95e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVY--------EGTAVDI-LGVGSGE-IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNI 1961
Cdd:cd05096     2 FPRGHLLFKEKLGEGQFGEVHlcevvnpqDLPTLQFpFNVRKGRpLLVAVKILRPDANKNARNDFLKEVKILSRLKDPNI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1962 LKQLGVCLLNEPQYIILELMEGGDLLTYL------------RKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIH 2029
Cdd:cd05096    82 IRLLGVCVDEDPLCMITEYMENGDLNQFLsshhlddkeengNDAVPPAHCLPAISYSSLLHVALQIASGMKYLSSLNFVH 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2030 RDLAARNCLVSvkdytSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTL 2109
Cdd:cd05096   162 RDLATRNCLVG-----ENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILML 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2110 -GHQPYPAHSNLDVLN----YVQTGGR---LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQ 2164
Cdd:cd05096   237 cKEQPYGELTDEQVIEnageFFRDQGRqvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIH 299
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
1902-2167 7.44e-60

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 207.41  E-value: 7.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTavdILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd05065    11 VIGAGEFGEVCRGR---LKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARmATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLAR-- 2059
Cdd:cd05065    88 ENGALDSFLRQND-GQF-----TVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVN-----SNLVCKVSDFGLSRfl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 -DIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNC 2138
Cdd:cd05065   157 eDDTSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLPPPMDC 236
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2139 PDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05065   237 PTALHQLMLDCWQKDRNLRPKFGQIVNTL 265
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
1894-2160 8.44e-60

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 207.04  E-value: 8.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYegtavdiLGVGSGEIKVAVKTLKKGSTDQEkiEFLKEAHLMSKFNHPNILKQLGVCLLNEP 1973
Cdd:cd05113     3 PKDLTFLKELGTGQFGVVK-------YGKWRGQYDVAIKMIKEGSMSED--EFIEEAKVMMNLSHEKLVQLYGVCTKQRP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIG 2053
Cdd:cd05113    74 IFIITEYMANGCLLNYLRE------MRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVN-----DQGVVKVS 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDYYRKRGEGLlPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLE 2133
Cdd:cd05113   143 DFGLSRYVLDDEYTSSVGSKF-PVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLY 221
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2134 PPRNCPDDLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd05113   222 RPHLASEKVYTIMYSCWHEKADERPTF 248
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
1893-2170 9.82e-60

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 207.19  E-value: 9.82e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAvdilgvgSGEIKVAVKTLKKGSTDQEKieFLKEAHLMSKFNHPNILKqLGVCLLNE 1972
Cdd:cd05073     9 PRESLKLEKKLGAGQFGEVWMATY-------NKHTKVAVKTMKPGSMSVEA--FLAEANVMKTLQHDKLVK-LHAVVTKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd05073    79 PIYIITEFMAKGSLLDFLKSDE-----GSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVS-----ASLVCKI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05073   149 ADFGLARVIEDNEYTAREG-AKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRM 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLF 2170
Cdd:cd05073   228 PRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDF 265
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
1896-2163 1.21e-59

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 207.03  E-value: 1.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1896 KLTLRLLLGSGAFGEVYEGTavdiLGV-GSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ 1974
Cdd:cd05066     5 CIKIEKVIGAGEFGEVCSGR----LKLpGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGD 2054
Cdd:cd05066    81 MIVTEYMENGSLDAFLRK------HDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVN-----SNLVCKVSD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARdIYKND---YYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGR 2131
Cdd:cd05066   150 FGLSR-VLEDDpeaAYTTRG-GKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYR 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767943404 2132 LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05066   228 LPAPMDCPAALHQLMLDCWQKDRNERPKFEQI 259
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
1893-2168 5.53e-59

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 205.31  E-value: 5.53e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTavdilgvGSGEIKVAVKTLKKGSTDQEKieFLKEAHLMSKFNHPNILkQLGVCLLNE 1972
Cdd:cd05071     7 PRESLRLEVKLGQGCFGEVWMGT-------WNGTTRVAIKTLKPGTMSPEA--FLQEAQVMKKLRHEKLV-QLYAVVSEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKArmatfYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd05071    77 PIYIVTEYMSKGSLLDFLKGE-----MGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVG-----ENLVCKV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05071   147 ADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRM 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05071   226 PCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLE 261
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
1893-2168 1.77e-58

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 203.76  E-value: 1.77e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTavdilgvGSGEIKVAVKTLKKGSTDQEkiEFLKEAHLMSKFNHPNILkQLGVCLLNE 1972
Cdd:cd05070     7 PRESLQLIKRLGNGQFGEVWMGT-------WNGNTKVAIKTLKPGTMSPE--SFLEEAQIMKKLKHDKLV-QLYAVVSEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd05070    77 PIYIVTEYMSKGSLLDFLKDGE-----GRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVG-----NGLICKI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05070   147 ADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRM 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05070   226 PCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLE 261
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
1897-2163 1.85e-58

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 203.67  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGtavdILGV-GSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd05063     7 ITKQKVIGAGEFGEVFRG----ILKMpGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDF 2055
Cdd:cd05063    83 IITEYMENGALDKYLRD------HDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVN-----SNLECKVSDF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARdIYKND---YYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05063   152 GLSR-VLEDDpegTYTTSG-GKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRL 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05063   230 PAPMDCPSAVYQLMLQCWQQDRARRPRFVDI 260
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
1893-2160 7.15e-58

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 201.63  E-value: 7.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREkLTLRLLLGSGAFGEVYegtavdiLGVGSGEIKVAVKTLKKGSTDQEkiEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd05114     3 PSE-LTFMKELGSGLFGVVR-------LGKWRAQYKVAIKAIREGAMSEE--DFIEEAKVMMKLTHPKLVQLYGVCTQQK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd05114    73 PIYIVTEFMENGCLLNYLRQRR------GKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVN-----DTGVVKV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGeGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05114   142 SDFGMTRYVLDDQYTSSSG-AKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRL 220
                         250       260
                  ....*....|....*....|....*...
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd05114   221 YRPKLASKSVYEVMYSCWHEKPEGRPTF 248
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
1903-2168 1.66e-57

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 201.39  E-value: 1.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGtAVDILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd05090    13 LGECAFGKIYKG-HLYLPGMDHAQL-VAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMATFYGPLLTLVDLVDLCVD----------ISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd05090    91 QGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDhgdflhiaiqIAAGMEYLSSHFFVHKDLAARNILVGEQLH-----VKI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05090   166 SDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLL 245
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05090   246 PCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARLR 281
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
1891-2168 2.22e-57

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 199.82  E-value: 2.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1891 AFPREKLTLRLLLGSGAFGEVYEGtavDILGVgsgeiKVAVKTLKKGSTDQEkieFLKEAHLMSKFNHPNILKQLGVCLL 1970
Cdd:cd05082     2 ALNMKELKLLQTIGKGEFGDVMLG---DYRGN-----KVAVKCIKNDATAQA---FLAEASVMTQLRHSNLVQLLGVIVE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQ-YIILELMEGGDLLTYLRKARMATFYGPLLTLVDlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprI 2049
Cdd:cd05082    71 EKGGlYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFS-----LDVCEAMEYLEGNNFVHRDLAARNVLVSEDN-----V 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKNdyyrkRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTG 2129
Cdd:cd05082   141 AKVSDFGLTKEASST-----QDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKG 215
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2130 GRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05082   216 YKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLE 254
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
1902-2167 1.03e-56

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 199.10  E-value: 1.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdiLGVGSGE---IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQyIIL 1978
Cdd:cd05109    14 VLGSGAFGTVYKG-----IWIPDGEnvkIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTSTVQ-LVT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLR--KARMATFYgplltlvdLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFG 2056
Cdd:cd05109    88 QLMPYGCLLDYVRenKDRIGSQD--------LLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVK-----SPNHVKITDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LAR--DIYKNDYYRKRGEglLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEP 2134
Cdd:cd05109   155 LARllDIDETEYHADGGK--VPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQ 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767943404 2135 PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05109   233 PPICTIDVYMIMVKCWMIDSECRPRFRELVDEF 265
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
1880-2168 2.15e-56

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 201.61  E-value: 2.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1880 LPTQEEIEnlpaFPREKLTLRLLLGSGAFGEVYEGTAVDiLGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NH 1958
Cdd:cd05106    27 LPYNEKWE----FPRDNLQFGKTLGAGAFGKVVEATAFG-LGKEDNVLRVAVKMLKASAHTDEREALMSELKILSHLgQH 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1959 PNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKaRMATFYGPLLTLVDLVDLCVD----------------ISKGCV-- 2020
Cdd:cd05106   102 KNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRK-KAETFLNFVMALPEISETSSDyknitlekkyirsdsgFSSQGSdt 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2021 YLER------------------------------MHF----------------IHRDLAARNCLVsvkdyTSPRIVKIGD 2054
Cdd:cd05106   181 YVEMrpvsssssqssdskdeedtedswpldlddlLRFssqvaqgmdflaskncIHRDVAARNVLL-----TDGRVAKICD 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHS-NLDVLNYVQTGGRLE 2133
Cdd:cd05106   256 FGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILvNSKFYKMVKRGYQMS 335
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 767943404 2134 PPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05106   336 RPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQ 370
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
1902-2163 2.08e-55

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 196.40  E-value: 2.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdiLGVGSGE---IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQyIIL 1978
Cdd:cd05108    14 VLGSGAFGTVYKG-----LWIPEGEkvkIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQ-LIT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLR--KARMATFYgplltlvdLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFG 2056
Cdd:cd05108    88 QLMPFGCLLDYVRehKDNIGSQY--------LLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVK-----TPQHVKITDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPR 2136
Cdd:cd05108   155 LAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPP 234
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2137 NCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05108   235 ICTIDVYMIMVKCWMIDADSRPKFREL 261
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
1892-2160 2.77e-55

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 196.74  E-value: 2.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLL 1970
Cdd:cd05102     4 FPRDRLRLGKVLGHGAFGKVVEASAFGIDKSSSCE-TVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGACTK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 -NEPQYIILELMEGGDLLTYLRKAR------------------------------------MATFYGPLLTLVDLVDLCV 2013
Cdd:cd05102    83 pNGPLMVIVEFCKYGNLSNFLRAKRegfspyrersprtrsqvrsmveavradrrsrqgsdrVASFTESTSSTNQPRQEVD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2014 D-----------------ISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLARDIYKNDYYRKRGEGLLP 2076
Cdd:cd05102   163 DlwqspltmedlicysfqVARGMEFLASRKCIHRDLAARNILLSENN-----VVKICDFGLARDIYKDPDYVRKGSARLP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2077 VRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPA-HSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPD 2155
Cdd:cd05102   238 LKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGvQINEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPK 317

                  ....*
gi 767943404 2156 QRPTF 2160
Cdd:cd05102   318 ERPTF 322
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
1903-2174 3.14e-55

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 193.64  E-value: 3.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGtavdILGVGSGEIKVAVKTLKKGSTDQE-KIEFLKEAHLMSKFNHPNILKQLGVCLlNEPQYIILELM 1981
Cdd:cd05116     3 LGSGNFGTVKKG----YYQMKKVVKTVAVKILKNEANDPAlKDELLREANVMQQLDNPYIVRMIGICE-AESWMLVMEMA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTsprivKIGDFGLARDI 2061
Cdd:cd05116    78 ELGPLNKFLQKNRHVT-------EKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYA-----KISDFGLSKAL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKND-YYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPD 2140
Cdd:cd05116   146 RADEnYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCPP 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767943404 2141 DLWNLMTQCWAQEPDQRPTFHRIQDQLqlfRNFF 2174
Cdd:cd05116   226 EMYDLMKLCWTYDVDERPGFAAVELRL---RNYY 256
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1902-2163 5.18e-55

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 193.13  E-value: 5.18e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   1902 LLGSGAFGEVYEgtAVDIlgvGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:smart00220    6 KLGEGSFGKVYL--ARDK---KTGKL-VAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   1982 EGGDLLTYLRKAR-----MATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFG 2056
Cdd:smart00220   80 EGGDLFDLLKKRGrlsedEARFY------------LRQILSALEYLHSKGIVHRDLKPENILL-----DEDGHVKLADFG 142
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   2057 LARDIYKNDYYRKR-GegllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGRLEPP 2135
Cdd:smart00220  143 LARQLDPGEKLTTFvG----TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQLLELFKKIGKPKPPFP 217
                           250       260       270
                    ....*....|....*....|....*....|.
gi 767943404   2136 R---NCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:smart00220  218 PpewDISPEAKDLIRKLLVKDPEKRLTAEEA 248
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
1877-2165 7.26e-55

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 197.94  E-value: 7.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1877 IHTLPTQEEIENLPAFPREKLTLRLLLGSGAFGEVYEGTAVDiLGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKF 1956
Cdd:cd05105    19 IYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYG-LSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1957 N-HPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKAR----------------------------------------- 1994
Cdd:cd05105    98 GpHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRdnflsrhpekpkkdldifginpadestrsyvilsfenkgdy 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1995 --------------------------MATFYGPLLTLVDLVDLCVD----------------------ISKGCVYLERMH 2026
Cdd:cd05105   178 mdmkqadttqyvpmleikeaskysdiQRSNYDRPASYKGSNDSEVKnllsddgseglttldllsftyqVARGMEFLASKN 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2027 FIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEI 2106
Cdd:cd05105   258 CVHRDLAARNVLLA-----QGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEI 332
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2107 LTLGHQPYPAH-SNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd05105   333 FSLGGTPYPGMiVDSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSD 392
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
1892-2167 1.33e-54

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 195.20  E-value: 1.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLL 1970
Cdd:cd05103     4 FPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCR-TVAVKMLKEGATHSEHRALMSELKILIHIgHHLNVVNLLGACTK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 -NEPQYIILELMEGGDLLTYLRKAR--MATFYGPLLTLVDLVDLCVDIS------------------------------- 2016
Cdd:cd05103    83 pGGPLMVIVEFCKFGNLSAYLRSKRseFVPYKTKGARFRQGKDYVGDISvdlkrrldsitssqssassgfveekslsdve 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2017 ---------------------------KGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLARDIYKNDYYRK 2069
Cdd:cd05103   163 eeeagqedlykdfltledlicysfqvaKGMEFLASRKCIHRDLAARNILLSENN-----VVKICDFGLARDIYKDPDYVR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2070 RGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPA-HSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQ 2148
Cdd:cd05103   238 KGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGvKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLD 317
                         330
                  ....*....|....*....
gi 767943404 2149 CWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05103   318 CWHGEPSQRPTFSELVEHL 336
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
1898-2168 1.98e-54

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 192.54  E-value: 1.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1898 TLRLL--LGSGAFGEVYEGtavDILGVGSGEIK--VAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEP 1973
Cdd:cd05091     7 AVRFMeeLGEDRFGKVYKG---HLFGTAPGEQTqaVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKARMATFYGPLLTLVDLVDL---------CVDISKGCVYLERMHFIHRDLAARNCLVSVKdy 2044
Cdd:cd05091    84 MSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDKTVKSTlepadflhiVTQIAAGMEYLSSHHVVHKDLATRNVLVFDK-- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2045 tspRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLN 2124
Cdd:cd05091   162 ---LNVKISDLGLFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIE 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767943404 2125 YVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd05091   239 MIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDIHSRLR 282
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
1892-2167 1.13e-53

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 192.53  E-value: 1.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLL 1970
Cdd:cd14207     4 FARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRV-VAVKMLKEGATASEYKALMTELKILIHIgHHLNVVNLLGACTK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NE-PQYIILELMEGGDLLTYL-------------------------------RKARMAT--------------------- 1997
Cdd:cd14207    83 SGgPLMVIVEYCKYGNLSNYLkskrdffvtnkdtslqeelikekkeaeptggKKKRLESvtssesfassgfqedkslsdv 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1998 ---------FYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLARDIYKNDYYR 2068
Cdd:cd14207   163 eeeeedsgdFYKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENN-----VVKICDFGLARDIYKNPDYV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2069 KRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPA-HSNLDVLNYVQTGGRLEPPRNCPDDLWNLMT 2147
Cdd:cd14207   238 RKGDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGvQIDEDFCSKLKEGIRMRAPEFATSEIYQIML 317
                         330       340
                  ....*....|....*....|
gi 767943404 2148 QCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14207   318 DCWQGDPNERPRFSELVERL 337
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1902-2167 1.11e-52

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 187.17  E-value: 1.11e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd05047     2 VIGEGNFGQVLKA----RIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARM---------ATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYtsprIVK 2051
Cdd:cd05047    78 APHGNLLDFLRKSRVletdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVG-ENY----VAK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLARDiykNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGR 2131
Cdd:cd05047   153 IADFGLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2132 LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05047   230 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 265
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
1895-2167 1.14e-52

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 187.90  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEGtavdILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLLNEP 1973
Cdd:cd05089     2 EDIKFEDVIGEGNFGQVIKA----MIKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKARM-------ATFYGPLLTLVDLV--DLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdy 2044
Cdd:cd05089    78 LYIAIEYAPYGNLLDFLRKSRVletdpafAKEHGTASTLTSQQllQFASDVAKGMQYLSEKQFIHRDLAARNVLVG---- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2045 tSPRIVKIGDFGLARDiykNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLN 2124
Cdd:cd05089   154 -ENLVSKIADFGLSRG---EEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYE 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2125 YVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05089   230 KLPQGYRMEKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQL 272
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
1881-2163 1.16e-51

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 187.80  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1881 PTQEEIENLPAFPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSgEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKF-NHP 1959
Cdd:cd05104    21 PTQLPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYGLAKADS-AMTVAVKMLKPSAHSTEREALMSELKVLSYLgNHI 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1960 NILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATFYG--------------------------------------- 2000
Cdd:cd05104   100 NIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFICPkfedlaeaalyrnllhqremacdslneymdmkpsvsyvv 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2001 PLLTLVDLVDLC-----------------------------VDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVK 2051
Cdd:cd05104   180 PTKADKRRGVRSgsyvdqdvtseileedelaldtedllsfsYQVAKGMEFLASKNCIHRDLAARNILL-----THGRITK 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSnLDVLNY--VQTG 2129
Cdd:cd05104   255 ICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMP-VDSKFYkmIKEG 333
                         330       340       350
                  ....*....|....*....|....*....|....
gi 767943404 2130 GRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05104   334 YRMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQI 367
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
1903-2167 1.61e-51

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 181.31  E-value: 1.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgsGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd00180     1 LGKGSFGKVYKARDKE------TGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKarmatfYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDIY 2062
Cdd:cd00180    75 GGSLKDLLKE------NKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLD-----SDGTVKLADFGLAKDLD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEIltlghqpypahsnldvlnyvqtggrlepprncpDDL 2142
Cdd:cd00180   144 SDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EEL 190
                         250       260
                  ....*....|....*....|....*
gi 767943404 2143 WNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd00180   191 KDLIRRMLQYDPKKRPSAKELLEHL 215
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
1897-2167 9.15e-51

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 181.28  E-value: 9.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTavdILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd05064     7 IKIERILGTGRFGELCRGC---LKLPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFG 2056
Cdd:cd05064    84 VTEYMSNGALDSFLRK------HEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVN-----SDLVCKISGFR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 -LARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPP 2135
Cdd:cd05064   153 rLQEDKSEAIYTTMSGKS--PVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRLPAP 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767943404 2136 RNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05064   231 RNCPNLLHQLMLDCWQKERGERPRFSQIHSIL 262
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
1894-2170 1.35e-50

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 180.91  E-value: 1.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTL-RLLLGSGAFGEVYEGtavdILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLnE 1972
Cdd:cd05115     2 RDNLLIdEVELGSGNFGCVKKG----VYKMRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEA-E 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTsprivKI 2052
Cdd:cd05115    77 ALMLVMEMASGGPLNKFLSGKK------DEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYA-----KI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKND-YYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGR 2131
Cdd:cd05115   146 SDFGLSKALGADDsYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKR 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2132 LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLF 2170
Cdd:cd05115   226 MDCPAECPPEMYALMSDCWIYKWEDRPNFLTVEQRMRTY 264
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
1902-2163 6.09e-50

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 180.26  E-value: 6.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdiLGVGSGE---IKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQyIIL 1978
Cdd:cd05110    14 VLGSGAFGTVYKG-----IWVPEGEtvkIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQ-LVT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLA 2058
Cdd:cd05110    88 QLMPHGCLLDYVHEHK------DNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVK-----SPNHVKITDFGLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNC 2138
Cdd:cd05110   157 RLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPIC 236
                         250       260
                  ....*....|....*....|....*
gi 767943404 2139 PDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05110   237 TIDVYMVMVKCWMIDADSRPKFKEL 261
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
1903-2167 9.07e-50

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 178.55  E-value: 9.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdiLGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd05042     3 IGNGWFGKVLLGE----IYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMATFyGPLLTLVDLVDLCvDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARDIY 2062
Cdd:cd05042    79 LGDLKAYLRSEREHER-GDSDTRTLQRMAC-EVAAGLAHLHKLNFVHSDLALRNCLL-----TSDLTVKIGDYGLAHSRY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPVRWMAPE-------SLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYV--QTGGRLE 2133
Cdd:cd05042   152 KEDYIETDDKLWFPLRWTAPElvtefhdRLLVVDQTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLAQVvrEQDTKLP 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767943404 2134 PPR---NCPDDLWNLMTQCWAQePDQRPTFHRIQDQL 2167
Cdd:cd05042   232 KPQlelPYSDRWYEVLQFCWLS-PEQRPAAEDVHLLL 267
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
1877-2163 4.41e-49

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 180.98  E-value: 4.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1877 IHTLPTQEEIENLPAFPREKLTLRLLLGSGAFGEVYEGTAVDiLGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKF 1956
Cdd:cd05107    19 IYVDPMQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHG-LSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1957 N-HPNILKQLGVCLLNEPQYIILELMEGGDLLTYL--------------RKARMATFYGPLLTLVDLVD----------- 2010
Cdd:cd05107    98 GpHLNIVNLLGACTKGGPIYIITEYCRYGDLVDYLhrnkhtflqyyldkNRDDGSLISGGSTPLSQRKShvslgsesdgg 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2011 ----------------------------------------------LCVD--------------------ISKGCVYLER 2024
Cdd:cd05107   178 ymdmskdesadyvpmqdmkgtvkyadiessnyespydqylpsaperTRRDtlinespalsymdlvgfsyqVANGMEFLAS 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2025 MHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIW 2104
Cdd:cd05107   258 KNCVHRDLAARNVLI-----CEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLW 332
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2105 EILTLGHQPYPAHS-NLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05107   333 EIFTLGGTPYPELPmNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQL 392
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
1903-2159 2.12e-48

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 174.79  E-value: 2.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdiLGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd05087     5 IGHGWFGKVFLGE----VNSGLSSTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMATFYGPLLTLVDLVDlCvDISKGCVYLERMHFIHRDLAARNCLVSVkDYTspriVKIGDFGLARDIY 2062
Cdd:cd05087    81 LGDLKGYLRSCRAAESMAPDPLTLQRMA-C-EVACGLLHLHRNNFVHSDLALRNCLLTA-DLT----VKIGDYGLSHCKY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPVRWMAPEsLMDGIF--------TTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEP 2134
Cdd:cd05087   154 KEDYFVTADQLWVPLRWIAPE-LVDEVHgnllvvdqTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTYTVREQQLKL 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 767943404 2135 PR-----NCPDDLWNLMTQCWAQePDQRPT 2159
Cdd:cd05087   233 PKpqlklSLAERWYEVMQFCWLQ-PEQRPT 261
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
1902-2167 3.85e-47

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 171.29  E-value: 3.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtaVDILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQyIILELM 1981
Cdd:cd05111    14 VLGSGVFGTVHKG--IWIPEGDSIKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGASLQ-LVTQLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATfyGPLLTLVDlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDI 2061
Cdd:cd05111    91 PLGSLLDHVRQHRGSL--GPQLLLNW----CVQIAKGMYYLEEHRMVHRNLAARNVLLK-----SPSQVQVADFGVADLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDD 2141
Cdd:cd05111   160 YPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERLAQPQICTID 239
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2142 LWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd05111   240 VYMVMVKCWMIDENIRPTFKELANEF 265
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
1890-2163 1.80e-46

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 170.18  E-value: 1.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1890 PAFPREKLTLRLLLGSGAFGEVYEGTavdiLGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFN-HPNILKQLGVC 1968
Cdd:cd05088     2 PVLEWNDIKFQDVIGEGNFGQVLKAR----IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGhHPNIINLLGAC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1969 LLNEPQYIILELMEGGDLLTYLRKAR---------MATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLV 2039
Cdd:cd05088    78 EHRGYLYLAIEYAPHGNLLDFLRKSRvletdpafaIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2040 SvKDYtsprIVKIGDFGLARDiykNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSN 2119
Cdd:cd05088   158 G-ENY----VAKIADFGLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTC 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767943404 2120 LDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05088   230 AELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 273
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
1903-2163 4.81e-45

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 165.49  E-value: 4.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVyEGTAVDILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI--ILEL 1980
Cdd:cd05079    12 LGEGHFGKV-ELCRYDPEGDNTGEQ-VAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIklIMEF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARMATfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARD 2060
Cdd:cd05079    90 LPSGSLKEYLPRNKNKI------NLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVE-----SEHQVKIGDFGLTKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYKN-DYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPY-----------PAHSNLDV---LNY 2125
Cdd:cd05079   159 IETDkEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESspmtlflkmigPTHGQMTVtrlVRV 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2126 VQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05079   239 LEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNL 276
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
1902-2159 4.93e-45

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 164.62  E-value: 4.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd06606     7 LLGKGSFGSVYLALNLD-----TGEL-MAVKEVELSGDSEEELEALErEIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRK--------ARMATFygplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKI 2052
Cdd:cd06606    81 VPGGSLASLLKKfgklpepvVRKYTR---------------QILEGLEYLHSNGIVHRDIKGANILVDSDG-----VVKL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYyrkrGEGLLPVR----WMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSN-LDVLNYVQ 2127
Cdd:cd06606   141 ADFGCAKRLAEIAT----GEGTKSLRgtpyWMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELGNpVAALFKIG 215
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767943404 2128 TGGRLEP-PRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06606   216 SSGEPPPiPEHLSEEAKDFLRKCLQRDPKKRPT 248
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
1902-2171 1.08e-44

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 164.30  E-value: 1.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyEGTAVDILGVGSGEIkVAVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCL-LNEPQY-IILE 1979
Cdd:cd05081    11 QLGKGNFGSV-ELCRYDPLGDNTGAL-VAVKQLQHSGPDQQR-DFQREIQILKALHSDFIVKYRGVSYgPGRRSLrLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMAtfYGPLLTLVDLVDLCvdisKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLAR 2059
Cdd:cd05081    88 YLPSGCLRDFLQRHRAR--LDASRLLLYSSQIC----KGMEYLGSRRCVHRDLAARNILVESEAH-----VKIADFGLAK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIYKN-DYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILT---------------LG-HQPYPAHSNLdv 2122
Cdd:cd05081   157 LLPLDkDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTycdkscspsaeflrmMGcERDVPALCRL-- 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767943404 2123 LNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFR 2171
Cdd:cd05081   235 LELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLW 283
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
1892-2172 6.69e-44

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 161.99  E-value: 6.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEV--YegtAVDILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCL 1969
Cdd:cd05080     1 FHKRYLKKIRDLGEGHFGKVslY---CYDPTNDGTGEM-VAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 LNEPQ--YIILELMEGGDLLTYLRKARMAtfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSP 2047
Cdd:cd05080    77 EQGGKslQLIMEYVPLGSLRDYLPKHSIG--------LAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLD-----ND 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 RIVKIGDFGLARDIYK-NDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTL--GHQPYPAH------- 2117
Cdd:cd05080   144 RLVKIGDFGLAKAVPEgHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHcdSSQSPPTKflemigi 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2118 -----SNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFRN 2172
Cdd:cd05080   224 aqgqmTVVRLIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTVHE 283
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
1903-2163 1.08e-43

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 160.30  E-value: 1.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILgvgsgeikVAVKTLKkgsTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14058     1 VGRGSFGVVCKARWRNQI--------VAVKIIE---SESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMATFYgpllTLVDLVDLCVDISKGCVYLERMH---FIHRDLAARNCLVsvkdYTSPRIVKIGDFGLAR 2059
Cdd:cd14058    70 GGSLYNVLHGKEPKPIY----TAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLL----TNGGTVLKICDFGTAC 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIyKNDYYRKRGEgllpVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLgHQPYP--AHSNLDVLNYVQTGGRLEPPRN 2137
Cdd:cd14058   142 DI-STHMTNNKGS----AAWMAPEVFEGSKYSEKCDVFSWGIILWEVITR-RKPFDhiGGPAFRIMWAVHNGERPPLIKN 215
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2138 CPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14058   216 CPKPIESLMTRCWSKDPEKRPSMKEI 241
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
1903-2167 3.01e-43

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 160.12  E-value: 3.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVyegtavdILGvgsgEI-------KVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd14206     5 IGNGWFGKV-------ILG----EIfsdytpaQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMATFYGPLLTL---VDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKI 2052
Cdd:cd14206    74 LIMEFCQLGDLKRYLRAQRKADGMTPDLPTrdlRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLL-----TSDLTVRI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGLLPVRWMAPESL--MDGIF-----TTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNY 2125
Cdd:cd14206   149 GDYGLSHNNYKEDYYLTPDRLWIPLRWVAPELLdeLHGNLivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTF 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767943404 2126 V--QTGGRLEPPR-NCP-DDLW-NLMTQCWaQEPDQRPTFHRIQDQL 2167
Cdd:cd14206   229 VvrEQQMKLAKPRlKLPyADYWyEIMQSCW-LPPSQRPSVEELHLQL 274
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
1892-2168 1.53e-41

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 155.17  E-value: 1.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVyEGTAVDILGVGSGEIkVAVKTLKKgSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLL- 1970
Cdd:cd14205     1 FEERHLKFLQQLGKGNFGSV-EMCRYDPLQDNTGEV-VAVKKLQH-STEEHLRDFEREIEILKSLQHDNIVKYKGVCYSa 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 -NEPQYIILELMEGGDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRI 2049
Cdd:cd14205    78 gRRNLRLIMEYLPYGSLRDYLQKHK------ERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVE-----NENR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKN-DYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILT---------------LGHQP 2113
Cdd:cd14205   147 VKIGDFGLTKVLPQDkEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTyieksksppaefmrmIGNDK 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2114 YPAHSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14205   227 QGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVD 281
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
1902-2168 1.19e-40

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 151.78  E-value: 1.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAvdilgvgSGEiKVAVKTLKK-GSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLlNEPQY-II 1977
Cdd:cd14061     1 VIGVGGFGKVYRGIW-------RGE-EVAVKAARQdPDEDISVTLenVRQEARLFWMLRHPNIIALRGVCL-QPPNLcLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKARMAtfygplltLVDLVDLCVDISKGCVYLER---MHFIHRDLAARNCLVSVK---DYTSPRIVK 2051
Cdd:cd14061    72 MEYARGGALNRVLAGRKIP--------PHVLVDWAIQIARGMNYLHNeapVPIIHRDLKSSNILILEAienEDLENKTLK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLARDIYKNDYYRKRGEgllpVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGR 2131
Cdd:cd14061   144 ITDFGLAREWHKTTRMSAAGT----YAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVAYGVAVNKL 218
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2132 LEP-PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14061   219 TLPiPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLE 256
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
1903-2163 5.06e-39

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 147.71  E-value: 5.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdiLGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd05086     5 IGNGWFGKVLLGE----IYTGTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMATFyGPLLTLVDLVDLCvDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARDIY 2062
Cdd:cd05086    81 LGDLKTYLANQQEKLR-GDSQIMLLQRMAC-EIAAGLAHMHKHNFLHSDLALRNCYL-----TSDLTVKVGDYGIGFSRY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPVRWMAPE---SLMDGIF----TTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYV----QT--- 2128
Cdd:cd05086   154 KEDYIETDDKKYAPLRWTAPElvtSFQDGLLaaeqTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLNHVikerQVklf 233
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2129 GGRLEPPRNcpdDLWNLMTQ-CWAQePDQRPT---FHRI 2163
Cdd:cd05086   234 KPHLEQPYS---DRWYEVLQfCWLS-PEKRPTaeeVHRL 268
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
1902-2159 1.55e-38

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 145.81  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVDIlgvgSGEIKVAVKTLKKGSTDQEKI--EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd14014     7 LLGRGGMGEVYR--ARDT----LLGRPVAIKVLRPELAEDEEFreRFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKarmatfYGPlLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLAR 2059
Cdd:cd14014    81 YVEGGSLADLLRE------RGP-LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG-----RVKLTDFGIAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIYKNDYYRkRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGRLEPPR--- 2136
Cdd:cd14014   149 ALGDSGLTQ-TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHLQEAPPPPSPlnp 226
                         250       260
                  ....*....|....*....|...
gi 767943404 2137 NCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14014   227 DVPPALDAIILRALAKDPEERPQ 249
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
1902-2167 4.18e-38

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 144.80  E-value: 4.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTavdilgvGSGEiKVAVKTLKKGSTDQEKI---EFLKEAHLMSKFNHPNILKQLGVCLlNEPQY-II 1977
Cdd:cd14146     1 IIGVGGFGKVYRAT-------WKGQ-EVAVKAARQDPDEDIKAtaeSVRQEAKLFSMLRHPNIIKLEGVCL-EEPNLcLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKARMATfyGPLLTLVDLVDLCVD----ISKGCVYLERMHF---IHRDLAARNCLVSVK---DYTSP 2047
Cdd:cd14146    72 MEFARGGTLNRALAAANAAP--GPRRARRIPPHILVNwavqIARGMLYLHEEAVvpiLHRDLKSSNILLLEKiehDDICN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 RIVKIGDFGLARDIYKNDYYRKRGEgllpVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQ 2127
Cdd:cd14146   150 KTLKITDFGLAREWHRTTKMSAAGT----YAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAYGVA 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767943404 2128 TGGRLEP-PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14146   225 VNKLTLPiPSTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
1895-2168 1.81e-37

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 142.86  E-value: 1.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEGTavdilgvGSGEIkVAVKTLKKG-----STDQEKIEflKEAHLMSKFNHPNILKQLGVCL 1969
Cdd:cd14147     3 QELRLEEVIGIGGFGKVYRGS-------WRGEL-VAVKAARQDpdediSVTAESVR--QEARLFAMLAHPNIIALKAVCL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 lNEPQY-IILELMEGGDLLTYLRKARMATfygplltlVDLVDLCVDISKGCVYLER---MHFIHRDLAARNCLVS---VK 2042
Cdd:cd14147    73 -EEPNLcLVMEYAAGGPLSRALAGRRVPP--------HVLVNWAVQIARGMHYLHCealVPVIHRDLKSNNILLLqpiEN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2043 DYTSPRIVKIGDFGLARDIYKNDYYRKRGEgllpVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDV 2122
Cdd:cd14147   144 DDMEHKTLKITDFGLAREWHKTTQMSAAGT----YAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCLAV 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767943404 2123 LNYVQTGGRLEP-PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14147   219 AYGVAVNKLTLPiPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLE 265
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
1903-2160 3.13e-37

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 142.21  E-value: 3.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGvgsgeiKVAVKTLKKG-STDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFG------MVAIKCLHSSpNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATfygPLLTLVDLVDlcvDISKGCVYLERMH--FIHRDLAARNCLVSvKDYTspriVKIGDFGLAR 2059
Cdd:cd13978    75 ENGSLKSLLEREIQDV---PWSLRFRIIH---EIALGMNFLHNMDppLLHHDLKPENILLD-NHFH----VKISDFGLSK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 ---DIYKNDYYRKRGEGLLPVRWMAPESLMDGI--FTTQSDVWSFGILIWEILTlGHQPYP-AHSNLDVLNYVQTG---- 2129
Cdd:cd13978   144 lgmKSISANRRRGTENLGGTPIYMAPEAFDDFNkkPTSKSDVYSFAIVIWAVLT-RKEPFEnAINPLLIMQIVSKGdrps 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2130 ----GRLEPPRNCPdDLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd13978   223 lddiGRLKQIENVQ-ELISLMIRCWDGNPDARPTF 256
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
1896-2167 4.51e-36

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 139.02  E-value: 4.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1896 KLTLRLLLGSGAFGEVYEGtavdilgVGSGEiKVAVKTLKKGSTD--QEKIEFLK-EAHLMSKFNHPNILKQLGVCLlNE 1972
Cdd:cd14145     7 ELVLEEIIGIGGFGKVYRA-------IWIGD-EVAVKAARHDPDEdiSQTIENVRqEAKLFAMLKHPNIIALRGVCL-KE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQY-IILELMEGGDLLTYLRKARMATfygplltlVDLVDLCVDISKGCVYLER---MHFIHRDLAARNCLVSVK---DYT 2045
Cdd:cd14145    78 PNLcLVMEFARGGPLNRVLSGKRIPP--------DILVNWAVQIARGMNYLHCeaiVPVIHRDLKSSNILILEKvenGDL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2046 SPRIVKIGDFGLARDIYKNDYYRKRGEgllpVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNY 2125
Cdd:cd14145   150 SNKILKITDFGLAREWHRTTKMSAAGT----YAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDGLAVAYG 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2126 VQTGGRLEP-PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14145   225 VAMNKLSLPiPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQL 267
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
1902-2168 1.24e-34

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 134.34  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdilgVGSGEiKVAVKTLKKGSTDQEKI---EFLKEAHLMSKFNHPNILKQLGVCLlNEPQY-II 1977
Cdd:cd14148     1 IIGVGGFGKVYKG-------LWRGE-EVAVKAARQDPDEDIAVtaeNVRQEARLFWMLQHPNIIALRGVCL-NPPHLcLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRkarmatfyGPLLTLVDLVDLCVDISKGCVYLERMHF---IHRDLAARNCLVSVK---DYTSPRIVK 2051
Cdd:cd14148    72 MEYARGGALNRALA--------GKKVPPHVLVNWAVQIARGMNYLHNEAIvpiIHRDLKSSNILILEPienDDLSGKTLK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLARDIYKNDYYRKRGEgllpVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGR 2131
Cdd:cd14148   144 ITDFGLAREWHKTTKMSAAGT----YAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDALAVAYGVAMNKL 218
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2132 LEP-PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14148   219 TLPiPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLE 256
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
1903-2159 4.53e-34

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 132.71  E-value: 4.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLK-KGSTDQEKIefLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd05122     8 IGKGGFGVVYKARHKK-----TGQI-VAIKKINlESKEKKESI--LNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLrKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARDI 2061
Cdd:cd05122    80 SGGSLKDLL-KNTNKTL-----TEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILL-----TSDGEVKLIDFGLSAQL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 yKNDYYRKRGEGLLPvrWMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYPAHSNLDVLNYVQTGG--RLEPPRNCP 2139
Cdd:cd05122   149 -SDGKTRNTFVGTPY--WMAPEVIQGKPYGFKADIWSLGITAIE-MAEGKPPYSELPPMKALFLIATNGppGLRNPKKWS 224
                         250       260
                  ....*....|....*....|
gi 767943404 2140 DDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd05122   225 KEFKDFLKKCLQKDPEKRPT 244
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
1902-2159 1.10e-32

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 128.50  E-value: 1.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdiLGVGSGEIkVAVKTLKKGSTDQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd06627     7 LIGRGAFGSVYKG-----LNLNTGEF-VAIKQISLEKIPKSDLKSVMgEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKarmatfYGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARD 2060
Cdd:cd06627    81 VENGSLASIIKK------FGKFPESLVAVYI-YQVLEGLAYLHEQGVIHRDIKGANILT-----TKDGLVKLADFGVATK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYKNDyyrkrGEGLLPV---RWMAPESL-MDGIfTTQSDVWSFGILIWEILTlGHQPYpahSNLD----VLNYVQTGgrl 2132
Cdd:cd06627   149 LNEVE-----KDENSVVgtpYWMAPEVIeMSGV-TTASDIWSVGCTVIELLT-GNPPY---YDLQpmaaLFRIVQDD--- 215
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2133 EP--PRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06627   216 HPplPENISPELRDFLLQCFQKDPTLRPS 244
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
1903-2167 1.19e-32

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 128.38  E-value: 1.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIKVavktLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14065     1 LGKGFFGEVYKVTHRE-----TGKVMV----MKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMatfygPLLTLVDLVDLCvDISKGCVYLERMHFIHRDLAARNCLVSVKDytSPRIVKIGDFGLARDIy 2062
Cdd:cd14065    72 GGTLEELLKSMDE-----QLPWSQRVSLAK-DIASGMAYLHSKNIIHRDLNSKNCLVREAN--RGRNAVVADFGLAREM- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 kNDYYRKRGEGLLPVR------WMAPESLMDGIFTTQSDVWSFGILIWEILTL-----GHQPYPAHSNLDVLNYvqtggR 2131
Cdd:cd14065   143 -PDEKTKKPDRKKRLTvvgspyWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRvpadpDYLPRTMDFGLDVRAF-----R 216
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2132 LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14065   217 TLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
1903-2163 2.37e-32

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 127.23  E-value: 2.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdiLGVGSGEiKVAVKTLKkgstDQEKIEFlkeAHLmSKFNHPNILKQLGVCLLnEPQY-IILELM 1981
Cdd:cd14059     1 LGSGAQGAVF-------LGKFRGE-EVAVKKVR----DEKETDI---KHL-RKLNHPNIIKFKGVCTQ-APCYcILMEYC 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATfygPLLTLVDLVdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLARDI 2061
Cdd:cd14059    64 PYGQLYEVLRAGREIT---PSLLVDWSK----QIASGMNYLHLHKIIHRDLKSPNVLVTYND-----VLKISDFGTSKEL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 ykNDYYRKRG-EGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGG-RLEPPRNCP 2139
Cdd:cd14059   132 --SEKSTKMSfAG--TVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIWGVGSNSlQLPVPSTCP 206
                         250       260
                  ....*....|....*....|....
gi 767943404 2140 DDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14059   207 DGFKLLMKQCWNSKPRNRPSFRQI 230
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
1897-2163 2.49e-31

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 124.90  E-value: 2.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKKGSTDQEkIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQyI 1976
Cdd:cd05037     1 ITFHEHLGQGTFTNIYDGILREVGDGRVQEVEVLLKVLDSDHRDIS-ESFFETASLMSQISHKHLVKLYGVCVADENI-M 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKARmatfygplltlvdlvdLCVDIS----------KGCVYLERMHFIHRDLAARNCLVSVKDYTS 2046
Cdd:cd05037    79 VQEYVRYGPLDKYLRRMG----------------NNVPLSwklqvakqlaSALHYLEDKKLIHGNVRGRNILLAREGLDG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2047 PR-IVKIGDFGLARDIYKndyyrkRGEGLLPVRWMAPESLMDGI-FTTQ-SDVWSFGILIWEILTLGHQPYPAHSNLDVL 2123
Cdd:cd05037   143 YPpFIKLSDPGVPITVLS------REERVDRIPWIAPECLRNLQaNLTIaADKWSFGTTLWEICSGGEEPLSALSSQEKL 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767943404 2124 NYVQTGGRLEPPrNCPDdLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05037   217 QFYEDQHQLPAP-DCAE-LAELIMQCWTYEPTKRPSFRAI 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
1903-2164 2.53e-31

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 124.55  E-value: 2.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEiKVAVKTLKKGSTDQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14003     8 LGEGSFGKVKL--ARHKL---TGE-KVAIKIIDKSKLKEEIEEKIKrEIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMAT-------FYgplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGD 2054
Cdd:cd14003    82 SGGELFDYIVNNGRLSedearrfFQ--------------QLISAVDYCHSNGIVHRDLKLENILLD-KNGN----LKIID 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIYKNDYYRKRGeGLLPvrWMAPESLM----DGiftTQSDVWSFGILIWEILTlGHQPYPAHsNLDVLNYVQTGG 2130
Cdd:cd14003   143 FGLSNEFRGGSLLKTFC-GTPA--YAAPEVLLgrkyDG---PKADVWSLGVILYAMLT-GYLPFDDD-NDSKLFRKILKG 214
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767943404 2131 RLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQ 2164
Cdd:cd14003   215 KYPIPSHLSPDARDLIRRMLVVDPSKRITIEEIL 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1902-2158 2.72e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 127.44  E-value: 2.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDIlgvgsgEIKVAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:COG0515    14 LLGRGGMGVVYLARDLRL------GRPVALKVLRPELAADPEARerFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRK---------ARMAtfygplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIV 2050
Cdd:COG0515    88 YVEGESLADLLRRrgplppaeaLRIL----------------AQLAEALAAAHAAGIVHRDIKPANILL-----TPDGRV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLARDIYKNDYYRkRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGG 2130
Cdd:COG0515   147 KLIDFGIARALGGATLTQ-TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREP 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2131 RLEPPR---NCPDDLWNLMTQCWAQEPDQRP 2158
Cdd:COG0515   225 PPPPSElrpDLPPALDAIVLRALAKDPEERY 255
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
1903-2171 2.79e-30

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 121.86  E-value: 2.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilGVGSgeiKVAVKTLKKGSTDQEKIefLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14156     1 IGSGFFSKVYKVTH----GATG---KVMVVKIYKNDVDQHKI--VREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMatfygPLLTLVDLVDLCvDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIVKigDFGLAR--- 2059
Cdd:cd14156    72 GGCLEELLAREEL-----PLSWREKVELAC-DISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVT--DFGLARevg 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIYKNDYYRKR---GEGLlpvrWMAPESLMDGIFTTQSDVWSFGILIWEIltLGHQPypahSNLDVLNYVQTGGR----- 2131
Cdd:cd14156   144 EMPANDPERKLslvGSAF----WMAPEMLRGEPYDRKVDVFSFGIVLCEI--LARIP----ADPEVLPRTGDFGLdvqaf 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767943404 2132 LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFR 2171
Cdd:cd14156   214 KEMVPGCPEPFLDLAASCCRMDAFKRPSFAELLDELEDIA 253
Pkinase pfam00069
Protein kinase domain;
1902-2163 3.73e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 120.04  E-value: 3.73e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:pfam00069    6 KLGSGSFGTVYKAKHRD-----TGKI-VAIKKIKKEKIKKKKDKnILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  1981 MEGGDLLTYLRkarmatfygplltlvdlvdlcvdiskgcvylERMHFIHRDlaarnclvsVKDYTSpRIVKigdfGLARD 2060
Cdd:pfam00069   80 VEGGSLFDLLS-------------------------------EKGAFSERE---------AKFIMK-QILE----GLESG 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  2061 IYKNDYyrkrgEGLLpvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDV--LNYVQTGGRLEPPRNC 2138
Cdd:pfam00069  115 SSLTTF-----VGTP--WYMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIyeLIIDQPYAFPELPSNL 186
                          250       260
                   ....*....|....*....|....*
gi 767943404  2139 PDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:pfam00069  187 SEEAKDLLKKLLKKDPSKRLTATQA 211
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
1903-2175 7.34e-30

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 121.07  E-value: 7.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdiLGVGSGEIKVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14027     1 LDSGGFGKVS-------LCFHRTQGLVVLKTVYTGPNCIEHNEaLLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMAtfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGDFGLA--- 2058
Cdd:cd14027    74 EKGNLMHVLKKVSVP--------LSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVD-NDFH----IKIADLGLAsfk 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 ----------RDIYKNDYYRKRGEGLLpvRWMAPESLMD--GIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNY- 2125
Cdd:cd14027   141 mwskltkeehNEQREVDGTAKKNAGTL--YYMAPEHLNDvnAKPTEKSDVYSFAIVLWAIFA-NKEPYENAINEDQIIMc 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2126 VQTGGR---LEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQlqlFRNFFL 2175
Cdd:cd14027   218 IKSGNRpdvDDITEYCPREIIDLMKLCWEANPEARPTFPGIEEK---FRPFYL 267
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
1902-2159 7.64e-30

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 120.59  E-value: 7.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEFLKEAH----LMSKFNHPNILKQLGVCLLNEPQYII 1977
Cdd:cd06632     7 LLGSGSFGSVYEGFNGD-----TGDF-FAVKEVSLVDDDKKSRESVKQLEqeiaLLSKLRHPNIVQYYGTEREEDNLYIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLVSvkdyTSPRiVKIGDFGL 2057
Cdd:cd06632    81 LEYVPGGSIHKLLQR------YGAFEEPVIRLYT-RQILSGLAYLHSRNTVHRDIKGANILVD----TNGV-VKLADFGM 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2058 ARDIYKNDYYRK-RGEGLlpvrWMAPESLM--DGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGRLEP 2134
Cdd:cd06632   149 AKHVEAFSFAKSfKGSPY----WMAPEVIMqkNSGYGLAVDIWSLGCTVLEMAT-GKPPWSQYEGVAAIFKIGNSGELPP 223
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2135 -PRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06632   224 iPDHLSPDAKDFIRLCLQRDPEDRPT 249
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
1903-2168 1.82e-29

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 119.42  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGtavDILGVgsgeikVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCllNEPQY-IILEL 1980
Cdd:cd14062     1 IGSGSFGTVYKG---RWHGD------VAVKKLNvTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYM--TKPQLaIVTQW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYL----RKARMATFygplltlvdlVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGDFG 2056
Cdd:cd14062    70 CEGSSLYKHLhvleTKFEMLQL----------IDIARQTAQGMDYLHAKNIIHRDLKSNNIFLH-EDLT----VKIGDFG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARdiykndyYRKRGEGLLPVR-------WMAPESL-MDGI--FTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd14062   135 LAT-------VKTRWSGSQQFEqptgsilWMAPEVIrMQDEnpYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDQILFM 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767943404 2127 QTGGRLEPPR-----NCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14062   207 VGRGYLRPDLskvrsDTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
1903-2169 2.19e-29

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 119.12  E-value: 2.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVdilgvGSGEIKVavktLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14155     1 IGSGFFSEVYKVRHR-----TSGQVMA----LKMNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYIN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDL---------LTYLRKARMAtfygplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIVkiG 2053
Cdd:cd14155    72 GGNLeqlldsnepLSWTVRVKLA----------------LDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVV--G 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDYYRKRgeglLPV----RWMAPESLMDGIFTTQSDVWSFGILIWEILTL-----GHQPYPAHSNLDVLN 2124
Cdd:cd14155   134 DFGLAEKIPDYSDGKEK----LAVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEIIARiqadpDYLPRTEDFGLDYDA 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767943404 2125 YVQTGGrlepprNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQL 2169
Cdd:cd14155   210 FQHMVG------DCPPDFLQLAFNCCNMDPKSRPSFHDIVKTLEE 248
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
1903-2176 9.86e-29

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 117.31  E-value: 9.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDilgVGSGEiKVAVKTLKKGSTDQEKIefLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd06614     8 IGEGASGEVY--KATD---RATGK-EVAIKKMRLRKQNKELI--INEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GG---DLLTY----LRKARMATfygplltlvdlvdLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGDF 2055
Cdd:cd06614    80 GGsltDIITQnpvrMNESQIAY-------------VCREVLQGLEYLHSQNVIHRDIKSDNILLS-KDGS----VKLADF 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDIYKNDYYRKRGEGlLPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGG--RLE 2133
Cdd:cd06614   142 GFAAQLTKEKSKRNSVVG-TPY-WMAPEVIKRKDYGPKVDIWSLGIMCIEMAE-GEPPYLEEPPLRALFLITTKGipPLK 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2134 PPRNCPDDLWNLMTQCWAQEPDQRPTFHriqdqlQLFRNFFLN 2176
Cdd:cd06614   219 NPEKWSPEFKDFLNKCLVKDPEKRPSAE------ELLQHPFLK 255
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
1904-2168 1.71e-28

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 116.21  E-value: 1.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1904 GSGAFGEVYEGTAVdilgvgSGEIKVAVKTLKKgstdqekIEflKEAHLMSKFNHPNILKQLGVCLlNEPQY-IILELME 1982
Cdd:cd14060     2 GGGSFGSVYRAIWV------SQDKEVAVKKLLK-------IE--KEAEILSVLSHRNIIQFYGAIL-EAPNYgIVTEYAS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLER---MHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLAR 2059
Cdd:cd14060    66 YGSLFDYLNSNE-----SEEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVI-----AADGVLKICDFGASR 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 diYKNDYYRKRGEGLLPvrWMAPEsLMDGIFTTQS-DVWSFGILIWEILTLgHQPYPAHSNLDVL-NYVQTGGRLEPPRN 2137
Cdd:cd14060   136 --FHSHTTHMSLVGTFP--WMAPE-VIQSLPVSETcDTYSYGVVLWEMLTR-EVPFKGLEGLQVAwLVVEKNERPTIPSS 209
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2138 CPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14060   210 CPRSFAELMRRCWEADVKERPSFKQIIGILE 240
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
1903-2168 3.01e-28

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 116.22  E-value: 3.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdiLGVGSgeiKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14066     1 IGSGGFGTVYKGV----LENGT---VVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMatfyGPLLTLVDLVDLCVDISKGCVYL---ERMHFIHRDLAARNCLVsVKDYTSprivKIGDFGLAR 2059
Cdd:cd14066    74 NGSLEDRLHCHKG----SPPLPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILL-DEDFEP----KLTDFGLAR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DI-YKNDYYRKRG-EGLLPvrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQP-YPAHSNLDVLNYVQTGGRLEPPR 2136
Cdd:cd14066   145 LIpPSESVSKTSAvKGTIG--YLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAvDENRENASRKDLVEWVESKGKEE 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767943404 2137 N---CPDDLWNLMTQ--------------CWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14066   222 LediLDKRLVDDDGVeeeeveallrlallCTRSDPSLRPSMKEVVQMLE 270
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
1902-2159 1.44e-27

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 114.10  E-value: 1.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegTAVDIlgvgSGEIKVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd08215     7 VIGKGSFGSAY--LVRRK----SDGKLYVLKEIDlSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKAR-----------MATFygplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRI 2049
Cdd:cd08215    81 ADGGDLAQKIKKQKkkgqpfpeeqiLDWF--------------VQICLALKYLHSRKILHRDLKTQNIFL-----TKDGV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARdIYKND-----------YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTLGHqPYPAHS 2118
Cdd:cd08215   142 VKLGDFGISK-VLESTtdlaktvvgtpYY------------LSPELCENKPYNYKSDIWALGCVLYELCTLKH-PFEANN 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767943404 2119 NLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd08215   208 LPALVYKIVKGQYPPIPSQYSSELRDLVNSMLQKDPEKRPS 248
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
1903-2168 5.13e-27

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 112.73  E-value: 5.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEvyegtAVDILGVGSGEIKVaVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14222     1 LGKGFFGQ-----AIKVTHKATGKVMV-MKELIRCDEETQK-TFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRkarmATFYGPLLTLVDLVDlcvDISKGCVYLERMHFIHRDLAARNCLVSVkDYTspriVKIGDFGLARDIY 2062
Cdd:cd14222    74 GGTLKDFLR----ADDPFPWQQKVSFAK---GIASGMAYLHSMSIIHRDLNSHNCLIKL-DKT----VVVADFGLSRLIV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 -------------------KNDyYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEIL-TLGHQPYPAHSNLDV 2122
Cdd:cd14222   142 eekkkpppdkpttkkrtlrKND-RKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIgQVYADPDCLPRTLDF 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767943404 2123 LNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14222   221 GLNVRLFWEKFVPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFE 266
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
1902-2157 1.42e-26

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 111.80  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdiLGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNH---PNILKQLGvCLLNEPQ-YII 1977
Cdd:cd06917     8 LVGRGSYGAVYRG-----YHVKTGRV-VALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYG-SYLKGPSlWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKARMATFYgplltlvdlvdLCVDISKGCVYLERMH---FIHRDLAARNCLVsvkdyTSPRIVKIGD 2054
Cdd:cd06917    81 MDYCEGGSIRTLMRAGPIAERY-----------IAVIMREVLVALKFIHkdgIIHRDIKAANILV-----TNTGNVKLCD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIYKNDyyRKRGEGLLPVRWMAPESLMDGI-FTTQSDVWSFGILIWEILTlGHQPYpahSNLDVLNYVQTGGRLE 2133
Cdd:cd06917   145 FGVAASLNQNS--SKRSTFVGTPYWMAPEVITEGKyYDTKADIWSLGITTYEMAT-GNPPY---SDVDALRAVMLIPKSK 218
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2134 PPRnCPDDLWNLMTQ-----CWAQEPDQR 2157
Cdd:cd06917   219 PPR-LEGNGYSPLLKefvaaCLDEEPKDR 246
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
1903-2159 1.53e-26

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 111.11  E-value: 1.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEiKVAVKTLKK--------GSTDQEKIE-----FLKEAHLMSKFNHPNILKQLGVcl 1969
Cdd:cd14008     1 LGRGSFGKVKL--ALDTE---TGQ-LYAIKIFNKsrlrkrreGKNDRGKIKnalddVRREIAIMKKLDHPNIVRLYEV-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 LNEPQ----YIILELMEGGDLLTYLRKARMATFygpllTLVDLVDLCVDISKGcvyLERMHF---IHRDLAARNCLVsvk 2042
Cdd:cd14008    73 IDDPEsdklYLVLEYCEGGPVMELDSGDRVPPL-----PEETARKYFRDLVLG---LEYLHEngiVHRDIKPENLLL--- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2043 dyTSPRIVKIGDFGLARDIYKNDYYRKRGEGlLPVrWMAPEsLMDGIFTTQS----DVWSFGILIWeILTLGHQPYPAHS 2118
Cdd:cd14008   142 --TADGTVKISDFGVSEMFEDGNDTLQKTAG-TPA-FLAPE-LCDGDSKTYSgkaaDIWALGVTLY-CLVFGRLPFNGDN 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2119 NLDVLNYVQTGG-RLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14008   216 ILELYEAIQNQNdEFPIPPELSPELKDLLRRMLEKDPEKRIT 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
1903-2163 2.61e-26

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 110.26  E-value: 2.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDIlgvGSGEIkVAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd14007     8 LGKGKFGNVY--LAREK---KSGFI-VALKVISKSQLQKSGLEhqLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKAR-----MATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDF 2055
Cdd:cd14007    82 APNGELYKELKKQKrfdekEAAKY------------IYQLALALDYLHSKNIIHRDIKPENILLGSNG-----ELKLADF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDIYKN---------DYyrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd14007   145 GWSVHAPSNrrktfcgtlDY-------------LPPEMVEGKEYDYKVDIWSLGVLCYELLV-GKPPFESKSHQETYKRI 210
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767943404 2127 QTgGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14007   211 QN-VDIKFPSSVSPEAKDLISKLLQKDPSKRLSLEQV 246
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
1903-2159 2.27e-24

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 104.87  E-value: 2.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDIlgvGSGEiKVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVclLNEPQ--YIILE 1979
Cdd:cd05117     8 LGRGSFGVVRL--AVHK---KTGE-EYAVKIIDKKKLKSEDEEmLRREIEILKRLDHPNIVKLYEV--FEDDKnlYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKA-----RMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPriVKIGD 2054
Cdd:cd05117    80 LCTGGELFDRIVKKgsfseREAAKI------------MKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSP--IKIID 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIYKND---------YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNY 2125
Cdd:cd05117   146 FGLAKIFEEGEklktvcgtpYY------------VAPEVLKGKGYGKKCDIWSLGVILYILLC-GYPPFYGETEQELFEK 212
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767943404 2126 VQTGG-RLEPPR--NCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd05117   213 ILKGKySFDSPEwkNVSEEAKDLIKRLLVVDPKKRLT 249
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
1902-2159 2.55e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 104.82  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVDilgVGSGEIkVAVKTLK---KGSTDQEKI--EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd06630     7 LLGTGAFSSCYQ--ARD---VKTGTL-MAVKQVSfcrNSSSEQEEVveAIREEIRMMARLNHPNIVRMLGATQHKSHFNI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKarmatfYGPlLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkDYTSpRIVKIGDFG 2056
Cdd:cd06630    81 FVEWMAGGSVASLLSK------YGA-FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLV---DSTG-QRLRIADFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 ----LARDIYKNDYYrkRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPA--HSN-LDVLNYVQTG 2129
Cdd:cd06630   150 aaarLASKGTGAGEF--QGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT-AKPPWNAekISNhLALIFKIASA 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2130 GRLEP-PRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06630   227 TTPPPiPEHLSPGLRDVTLRCLELQPEDRPP 257
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
1902-2167 5.38e-24

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 104.23  E-value: 5.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVY------EGTAVDILGV--GSGEIKVAVKTLKKGSTDQEKI----EFLKEAHLMSKFNHPNILKQLGVCL 1969
Cdd:cd14000     1 LLGDGGFGSVYrasykgEPVAVKIFNKhtSSNFANVPADTMLRHLRATDAMknfrLLRQELTVLSHLHHPSIVYLLGIGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 lnEPQYIILELMEGGDLLTYLRK-ARMATFYGPLLTLVDLvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPR 2048
Cdd:cd14000    81 --HPLMLVLELAPLGSLDHLLQQdSRSFASLGRTLQQRIA----LQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSAI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDIYKndyyrkrgEGLLPVR----WMAPESL-MDGIFTTQSDVWSFGILIWEILTLGhQPYPAHSNLDvl 2123
Cdd:cd14000   155 IIKIADYGISRQCCR--------MGAKGSEgtpgFRAPEIArGNVIYNEKVDVFSFGMLLYEILSGG-APMVGHLKFP-- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767943404 2124 NYVQTGGRLEPP---RNC--PDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14000   224 NEFDIHGGLRPPlkqYECapWPEVEVLMKKCWKENPQQRPTAVTVVSIL 272
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
1903-2171 6.26e-24

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 103.88  E-value: 6.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEvyegtAVDILGVGSGEIKVaVKTLKKGSTDQEKIeFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14221     1 LGKGCFGQ-----AIKVTHRETGEVMV-MKELIRFDEETQRT-FLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKarMATFYgPLLTLVDLVDlcvDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDIY 2062
Cdd:cd14221    74 GGTLRGIIKS--MDSHY-PWSQRVSFAK---DIASGMAYLHSMNIIHRDLNSHNCLVR-----ENKSVVVADFGLARLMV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNdyyRKRGEGLLPVR---------------WMAPESLMDGIFTTQSDVWSFGILIWEILTL-----GHQPYPAHSNLDV 2122
Cdd:cd14221   143 DE---KTQPEGLRSLKkpdrkkrytvvgnpyWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRvnadpDYLPRTMDFGLNV 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767943404 2123 LNYVQtggRLEPPrNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFR 2171
Cdd:cd14221   220 RGFLD---RYCPP-NCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLR 264
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
1903-2168 7.63e-24

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 102.99  E-value: 7.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilgvgSGEIkVAVKTLK------KGSTDQekieFLKEAHLMSKFNHPNILKQLGVCLLNEPQY- 1975
Cdd:cd14064     1 IGSGSFGKVYKGRC-------RNKI-VAIKRYRantycsKSDVDM----FCREVSILCRLNHPCVIQFVGACLDDPSQFa 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMatfygpLLTLVDLVDLCVDISKGCVYLERMH--FIHRDLAARNCLVsvkdYTSPRIVkIG 2053
Cdd:cd14064    69 IVTQYVSGGSLFSLLHEQKR------VIDLQSKLIIAVDVAKGMEYLHNLTqpIIHRDLNSHNILL----YEDGHAV-VA 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDI--YKNDYYRKRGEGLlpvRWMAPESL-MDGIFTTQSDVWSFGILIWEILTlGHQPY----PAHSNLDVlnyv 2126
Cdd:cd14064   138 DFGESRFLqsLDEDNMTKQPGNL---RWMAPEVFtQCTRYSIKADVFSYALCLWELLT-GEIPFahlkPAAAAADM---- 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767943404 2127 qTGGRLEPP--RNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14064   210 -AYHHIRPPigYSIPKPISSLLMRGWNAEPESRPSFVEIVALLE 252
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
1902-2159 9.01e-24

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 103.38  E-value: 9.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdiLGVGSGEIkVAVKTLKKGSTDQEK-------IEFLK-EAHLMSKFNHPNILKQLGVCLLNEP 1973
Cdd:cd06628     7 LIGSGSFGSVYLG-----MNASSGEL-MAVKQVELPSVSAENkdrkksmLDALQrEIALLRELQHENIVQYLGSSSDANH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLrkarmaTFYGpLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIG 2053
Cdd:cd06628    81 LNIFLEYVPGGSVATLL------NNYG-AFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKG-----GIKIS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDYYRKRGeGLLP-----VRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQT 2128
Cdd:cd06628   149 DFGISKKLEANSLSTKNN-GARPslqgsVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAIFKIGE 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2129 GGRLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06628   227 NASPTIPSNISSEARDFLEKTFEIDHNKRPT 257
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
1902-2168 2.94e-23

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 101.31  E-value: 2.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtaVDILgvgSGEIKVAVKTLKKGS-TDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd08530     7 KLGKGSYGSVYK---VKRL---SDNQVYALKEVNLGSlSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARMATFYGPLLTLVDLVdlcVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARD 2060
Cdd:cd08530    81 APFGDLSKLISKRKKKRRLFPEDDIWRIF---IQMLRGLKALHDQKILHRDLKSANILLS-----AGDLVKIGDLGISKV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYKNDYYRKRGEGLlpvrWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHqPYPAHSNLDVLNYVQTGGRLEPPRNCPD 2140
Cdd:cd08530   153 LKKNLAKTQIGTPL----YAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRP-PFEARTMQELRYKVCRGKFPPIPPVYSQ 227
                         250       260
                  ....*....|....*....|....*...
gi 767943404 2141 DLWNLMTQCWAQEPDQRPTfhrIQDQLQ 2168
Cdd:cd08530   228 DLQQIIRSLLQVNPKKRPS---CDKLLQ 252
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
1893-2170 8.95e-23

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 100.52  E-value: 8.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTavdilgvGSGEikVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCllN 1971
Cdd:cd14151     6 PDGQITVGQRIGSGSFGTVYKGK-------WHGD--VAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS--T 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1972 EPQY-IILELMEGGDLLTYLRKARmatfygplltLVDLVDLCVDISK----GCVYLERMHFIHRDLAARNCLVSvKDYTs 2046
Cdd:cd14151    75 KPQLaIVTQWCEGSSLYHHLHIIE----------TKFEMIKLIDIARqtaqGMDYLHAKSIIHRDLKSNNIFLH-EDLT- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2047 priVKIGDFGLA--RDIYKNDYYRKRGEGllPVRWMAPESLM---DGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLD 2121
Cdd:cd14151   143 ---VKIGDFGLAtvKSRWSGSHQFEQLSG--SILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRD 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2122 VLNYVQTGGRLEPP-----RNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLF 2170
Cdd:cd14151   217 QIIFMVGRGYLSPDlskvrSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 270
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
1903-2171 1.13e-22

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 100.09  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdilgvGSGEikVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGvcLLNEPQY-IILEL 1980
Cdd:cd14150     8 IGTGSFGTVFRGK-------WHGD--VAVKILKVTEPTPEQLQaFKNEMQVLRKTRHVNILLFMG--FMTRPNFaIITQW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLR--KARMATFygplltlvdlvdLCVDISK----GCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGD 2054
Cdd:cd14150    77 CEGSSLYRHLHvtETRFDTM------------QLIDVARqtaqGMDYLHAKNIIHRDLKSNNIFLH-EGLT----VKIGD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARdiykndyYRKRGEGLLPVR-------WMAPESLM---DGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLN 2124
Cdd:cd14150   140 FGLAT-------VKTRWSGSQQVEqpsgsilWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNRDQII 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2125 YVQTGGRLEP-----PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFR 2171
Cdd:cd14150   212 FMVGRGYLSPdlsklSSNCPKAMKRLLIDCLKFKREERPLFPQILVSIELLQ 263
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
1903-2168 1.29e-22

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 99.89  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIKVaVKTLKKgSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14154     1 LGKGFFGQAIKVTHRE-----TGEVMV-MKELIR-FDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDL----------LTYLRKARMATfygplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKI 2052
Cdd:cd14154    74 GGTLkdvlkdmarpLPWAQRVRFAK----------------DIASGMAYLHSMNIIHRDLNSHNCLVR-----EDKTVVV 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIY---KNDYYRKRGEGLLPVR---------------WMAPESLMDGIFTTQSDVWSFGILIWEIL-TLGHQP 2113
Cdd:cd14154   133 ADFGLARLIVeerLPSGNMSPSETLRHLKspdrkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIgRVEADP 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2114 YPAHSNLDV-LNyvQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14154   213 DYLPRTKDFgLN--VDSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLE 266
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1903-2165 1.32e-22

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 99.13  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGS-TDQEKIEFLK-EAHLMSKFNHPNIlkqlgVCLL-----NEPQY 1975
Cdd:cd05123     1 LGKGSFGKVLLVRKKD-----TGKL-YAMKVLRKKEiIKRKEVEHTLnERNILERVNHPFI-----VKLHyafqtEEKLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriV 2050
Cdd:cd05123    70 LVLDYVPGGELFSHLSKEGRfpeerARFYA------------AEIVLALEYLHSLGIIYRDLKPENILLDSDGH-----I 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLARDIYKNDYYRKRGEGLLPvrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGG 2130
Cdd:cd05123   133 KLTDFGLAKELSSDGDRTYTFCGTPE--YLAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYEKILKSP 209
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2131 rLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd05123   210 -LKFPEYVSPEAKSLISGLLQKDPTKRLGSGGAEE 243
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1903-2159 5.88e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 97.88  E-value: 5.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDILGVGSGEIKV----AVKTLKKgstdQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd08222     8 LGSGNFGTVY--LVSDLKATADEELKVlkeiSVGELQP----DETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRKARMAtfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNclVSVKDytspRIVKIGDFGLA 2058
Cdd:cd08222    82 EYCEGGDLDDKISEYKKS---GTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKN--IFLKN----NVIKVGDFGIS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIYKND----------YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTLGHqPYPAHSNLDVLNYVQT 2128
Cdd:cd08222   153 RILMGTSdlattftgtpYY------------MSPEVLKHEGYNSKSDIWSLGCILYEMCCLKH-AFDGQNLLSVMYKIVE 219
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2129 GGRLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd08222   220 GETPSLPDKYSKELNAIYSRMLNKDPALRPS 250
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
1902-2168 1.29e-21

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 97.03  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAvdilgvgSGEikVAVKTLKKGSTDQEKIEFLK-EAHLMSKFNHPNILKQLGVCLlNEPQY-IILE 1979
Cdd:cd14063     7 VIGKGRFGRVHRGRW-------HGD--VAIKLLNIDYLNEEQLEAFKeEVAAYKNTRHDNLVLFMGACM-DPPHLaIVTS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARmATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPRIVkIGDFGLAR 2059
Cdd:cd14063    77 LCKGRTLYSLIHERK-EKF-----DFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIF-----LENGRVV-ITDFGLFS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIYKNDYYRKRGEGLLPVRW---MAPE---SLMDGI-------FTTQSDVWSFGIlIWEILTLGHQPY---PAHSNLdvl 2123
Cdd:cd14063   145 LSGLLQPGRREDTLVIPNGWlcyLAPEiirALSPDLdfeeslpFTKASDVYAFGT-VWYELLAGRWPFkeqPAESII--- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2124 nyVQTGGRLEPPRN---CPDDLWNLMTQCWAQEPDQRPTFH---RIQDQLQ 2168
Cdd:cd14063   221 --WQVGCGKKQSLSqldIGREVKDILMQCWAYDPEKRPTFSdllRMLERLP 269
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
1902-2137 2.34e-21

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 96.01  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIKvAVKTLKKG---STDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd14098     7 RLGSGTFAEVKKAVEVE-----TGKMR-AIKQIVKRkvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLrkarMATFYGPLLTLVDLVdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsPRIVKIGDFGLA 2058
Cdd:cd14098    81 EYVEGGDLMDFI----MAWGAIPEQHARELT---KQILEAMAYTHSMGITHRDLKPENILITQDD---PVIVKISDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIYkNDYYRKRGEGLLpvRWMAPESLM------DGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd14098   151 KVIH-TGTFLVTFCGTM--AYLAPEILMskeqnlQGGYSNLVDMWSVGCLVYVMLT-GALPFDGSSQLPVEKRIRKGRYT 226

                  ....*
gi 767943404 2133 EPPRN 2137
Cdd:cd14098   227 QPPLV 231
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
1903-2159 3.86e-21

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 95.50  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEiKVAVKT--LKKGSTDQEkiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd06610     9 IGSGATAVVYAAYCLP-----KKE-KVAIKRidLEKCQTSMD--ELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARmatfygPLLTLVDLVDLCV--DISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGDFGLA 2058
Cdd:cd06610    81 LSGGSLLDIMKSSY------PRGGLDEAIIATVlkEVLKGLEYLHSNGQIHRDVKAGNILLG-EDGS----VKIADFGVS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIYKNDYYRKRgegllpVR--------WMAPESLMDGI-FTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVL-NYVQT 2128
Cdd:cd06610   150 ASLATGGDRTRK------VRktfvgtpcWMAPEVMEQVRgYDFKADIWSFGITAIELAT-GAAPYSKYPPMKVLmLTLQN 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2129 ggrlEPPR--------NCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06610   223 ----DPPSletgadykKYSKSFRKMISLCLQKDPSKRPT 257
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
1895-2159 4.26e-21

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 95.39  E-value: 4.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEGtaVDilgVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ 1974
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKG--ID---KRTNQV-VAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRKARMATFYgplltlvdLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGD 2054
Cdd:cd06609    75 WIIMEYCGGGSVLDLLKPGPLDETY--------IAFILREVLLGLEYLHSEGKIHRDIKAANILLS-EEGD----VKLAD 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIYKNDYYRKRGEGLlPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLnyvqtggRLEP 2134
Cdd:cd06609   142 FGVSGQLTSTMSKRNTFVGT-PF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLHPMRVL-------FLIP 211
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767943404 2135 PRNCP--------DDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06609   212 KNNPPslegnkfsKPFKDFVELCLNKDPKERPS 244
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
1903-2160 5.28e-21

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 94.60  E-value: 5.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVK---TLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd14009     1 IGRGSFATVWKGRHKQ-----TGEV-VAIKeisRKKLNKKLQENLE--SEIAILKSIKHPNIVRLYDVQKTEDFIYLVLE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRK--------AR--MAtfygplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSvKDYTSPRI 2049
Cdd:cd14009    73 YCAGGDLSQYIRKrgrlpeavARhfMQ-----------------QLASGLKFLRSKNIIHRDLKPQNLLLS-TSGDDPVL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 vKIGDFGLARDIYKNDYYRK-RGEGLlpvrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQT 2128
Cdd:cd14009   135 -KIADFGFARSLQPASMAETlCGSPL----YMAPEILQFQKYDAKADLWSVGAILFEMLV-GKPPFRGSNHVQLLRNIER 208
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2129 GGRLEPPRNCPD---DLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd14009   209 SDAVIPFPIAAQlspDCKDLLRRLLRRDPAERISF 243
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
1903-2159 6.72e-21

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 94.58  E-value: 6.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDIlgvGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd06623     9 LGQGSSGVVYK--VRHK---PTGKI-YALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GG---DLLTYLRK------ARMATfygplltlvdlvdlcvDISKGCVYLERM-HFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd06623    83 GGslaDLLKKVGKipepvlAYIAR----------------QILKGLDYLHTKrHIIHRDIKPSNLLINSKGE-----VKI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYPAHSNLDV---LNYVQTG 2129
Cdd:cd06623   142 ADFGISKVLENTLDQCNTFVG--TVTYMSPERIQGESYSYAADIWSLGLTLLE-CALGKFPFLPPGQPSFfelMQAICDG 218
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2130 GRLE-PPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06623   219 PPPSlPAEEFSPEFRDFISACLQKDPKKRPS 249
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
1903-2159 6.98e-21

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 95.29  E-value: 6.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFN-HPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd07830     7 LGDGTFGSVYLARNKE-----TGEL-VAIKKMKKKFYSWEECMNLREVKSLRKLNeHPNIVKLKEVFRENDELYFVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGgDLLTYLRKARMATFYGPLLtlvdlvdlcvdisKGCVY-----LERMH---FIHRDLAARNCLVSvkdytSPRIVKIG 2053
Cdd:cd07830    81 EG-NLYQLMKDRKGKPFSESVI-------------RSIIYqilqgLAHIHkhgFFHRDLKPENLLVS-----GPEVVKIA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKN----DY-----YRkrgegllpvrwmAPESLM-DGIFTTQSDVWSFGILIWEILTLghQP-YPAHSNLDV 2122
Cdd:cd07830   142 DFGLAREIRSRppytDYvstrwYR------------APEILLrSTSYSSPVDIWALGCIMAELYTL--RPlFPGSSEIDQ 207
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2123 LNYVQT------------GGRL-----------EPPR------NCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd07830   208 LYKICSvlgtptkqdwpeGYKLasklgfrfpqfAPTSlhqlipNASPEAIDLIKDMLRWDPKKRPT 273
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
1903-2160 8.28e-21

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 94.98  E-value: 8.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgsGEIKVAVKTLKKGS--TDQEKIEFLKEAHLMSK--FNHpnILKQLGVCllNEPQY--I 1976
Cdd:cd14026     5 LSRGAFGTVSRARHAD------WRVTVAIKCLKLDSpvGDSERNCLLKEAEILHKarFSY--ILPILGIC--NEPEFlgI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKARMAtfygPLLTLVDLVDLCVDISKGCVYLERMH--FIHRDLAARNCLVSVKDYtspriVKIGD 2054
Cdd:cd14026    75 VTEYMTNGSLNELLHEKDIY----PDVAWPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFH-----VKIAD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLA--RDIyknDYYRKRGEGLLP----VRWMAPESLMDGIFTTQS---DVWSFGILIWEILTLGHqPYPAHSN-LDVLN 2124
Cdd:cd14026   146 FGLSkwRQL---SISQSRSSKSAPeggtIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKI-PFEEVTNpLQIMY 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2125 YVQTGGRLEP-----PRNCP--DDLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd14026   222 SVSQGHRPDTgedslPVDIPhrATLINLIESGWAQNPDERPSF 264
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
1902-2163 8.97e-21

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 94.48  E-value: 8.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVdilgvgSGEIKVAVKTLKK-GSTDQEKIEFLKEAHLMS--KFNHpnILKQLGVCllNEPQYIIL 1978
Cdd:cd14025     3 KVGSGGFGQVYKVRHK------HWKTWLAIKCPPSlHVDDSERMELLEEAKKMEmaKFRH--ILPVYGIC--SEPVGLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLR------KARMATFYgplltlvdlvdlcvDISKGCVYLERMH--FIHRDLAARNCLVSVKDYtspriV 2050
Cdd:cd14025    73 EYMETGSLEKLLAseplpwELRFRIIH--------------ETAVGMNFLHCMKppLLHLDLKPANILLDAHYH-----V 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLAR---DIYKNDYYRKRGEGLLPvrWMAPESLM--DGIFTTQSDVWSFGILIWEILTlGHQPYPAHSN-LDVLN 2124
Cdd:cd14025   134 KISDFGLAKwngLSHSHDLSRDGLRGTIA--YLPPERFKekNRCPDTKHDVYSFAIVIWGILT-QKKPFAGENNiLHIMV 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767943404 2125 YVQTGGR--LEP-----PRNCpDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14025   211 KVVKGHRpsLSPiprqrPSEC-QQMICLMKRCWDQDPRKRPTFQDI 255
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
1903-2159 1.19e-20

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 93.95  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd06605     9 LGEGNGGVVSK-----VRHRPSGQI-MAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKA---------RMAtfygplltlvdlvdlcVDISKGCVYL-ERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd06605    83 GGSLDKILKEVgriperilgKIA----------------VAVVKGLIYLhEKHKIIHRDVKPSNILVNSRGQ-----VKL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFG----LARDIYKND----YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYP------AHS 2118
Cdd:cd06605   142 CDFGvsgqLVDSLAKTFvgtrSY------------MAPERISGGKYTVKSDIWSLGLSLVE-LATGRFPYPppnakpSMM 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767943404 2119 NLDVLNYVQTGgrlEPPR----NCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06605   209 IFELLSYIVDE---PPPLlpsgKFSPDFQDFVSQCLQKDPTERPS 250
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1903-2163 1.36e-20

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 93.45  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLKKGSTDQEK----IEFLKeaHLMSKFNHPNILKQLGVCLLNEPQ--YI 1976
Cdd:cd05118     7 IGEGAFGTVWLARDKV-----TGE-KVAIKKIKNDFRHPKAalreIKLLK--HLNDVEGHPNIVKLLDVFEHRGGNhlCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMeGGDLLTYLRKarmatfYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdyTSPRIVKIGDFG 2056
Cdd:cd05118    79 VFELM-GMNLYELIKD------YPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILIN----LELGQLKLADFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARDIYKNDYYrkrgeGLLPVRW-MAPESLMDGIFTTQS-DVWSFGILIWEILTLGHQpYPAHSNLDVLNYV--QTGgrl 2132
Cdd:cd05118   148 LARSFTSPPYT-----PYVATRWyRAPEVLLGAKPYGSSiDIWSLGCILAELLTGRPL-FPGDSEVDQLAKIvrLLG--- 218
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2133 epprncPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05118   219 ------TPEALDLLSKMLKYDPAKRITASQA 243
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1903-2169 1.50e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 93.76  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdILGVGSGEIkVAVKTLKKGS-TDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ--YIILE 1979
Cdd:cd08217     8 IGKGSFGTVRK-----VRRKSDGKI-LVWKEIDYGKmSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANTtlYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDISKGCVYLE--RMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGL 2057
Cdd:cd08217    82 YCEGGDLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgGGKILHRDLKPANIFLD-----SDNNVKLGDFGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2058 ARDIYKND----------YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTLgHQPYPAHSNLDVLNYVQ 2127
Cdd:cd08217   157 ARVLSHDSsfaktyvgtpYY------------MSPELLNEQSYDEKSDIWSLGCLIYELCAL-HPPFQAANQLELAKKIK 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2128 TGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTfhrIQDQLQL 2169
Cdd:cd08217   224 EGKFPRIPSRYSSELNEVIKSMLNVDPDKRPS---VEELLQL 262
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
1902-2168 1.87e-20

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 94.10  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAvdilgvgsGEIKVAVKTL---KKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGvCLLNEPQY-II 1977
Cdd:cd14158    22 KLGEGGFGVVFKGYI--------NDKNVAVKKLaamVDISTEDLTKQFEQEIQVMAKCQHENLVELLG-YSCDGPQLcLV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTylrkaRMATFYG-PLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFG 2056
Cdd:cd14158    93 YTYMPNGSLLD-----RLACLNDtPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILL-----DETFVPKISDFG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARDIYK--NDYYRKRGEGllPVRWMAPESLMdGIFTTQSDVWSFGILIWEILT--------------LGHQPYPAHSNL 2120
Cdd:cd14158   163 LARASEKfsQTIMTERIVG--TTAYMAPEALR-GEITPKSDIFSFGVVLLEIITglppvdenrdpqllLDIKEEIEDEEK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767943404 2121 DVLNYVQTGGRLEPPrNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14158   240 TIEDYVDKKMGDWDS-TSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQ 286
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
1902-2174 2.06e-20

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 93.19  E-value: 2.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLKKGSTDQE---KIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYII 1977
Cdd:cd06625     7 LLGQGAFGQVYLCYDAD-----TGR-ELAVKQVEIDPINTEaskEVKALEcEIQLLKNLQHERIVQYYGCLQDEKSLSIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKarmatfYGPlLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLvsvKDytSPRIVKIGDFGL 2057
Cdd:cd06625    81 MEYMPGGSVKDEIKA------YGA-LTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL---RD--SNGNVKLGDFGA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2058 ArdiykndyyrKR------GEGLLPVR----WMAPESLMDGIFTTQSDVWSFGILIWEILTlghqPYPAHSNLD----VL 2123
Cdd:cd06625   149 S----------KRlqticsSTGMKSVTgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLT----TKPPWAEFEpmaaIF 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2124 NYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTfhriqdQLQLFRNFF 2174
Cdd:cd06625   215 KIATQPTNPQLPPHVSEDARDFLSLIFVRNKKQRPS------AEELLSHSF 259
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1902-2159 2.11e-20

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 93.51  E-value: 2.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVDILGvgsgEIKVAVKT--LKKGSTDQEKIefLKEAHLMSKFNHPNILKQLGvCLLNEPQ-YIIL 1978
Cdd:cd13996    13 LLGSGGFGSVYK--VRNKVD----GVTYAIKKirLTEKSSASEKV--LREVKALAKLNHPNIVRYYT-AWVEEPPlYIQM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRKARmatfygplLTLVDLVDLCVD----ISKGCVYLERMHFIHRDLAARNCLVSVKDYtsprIVKIGD 2054
Cdd:cd13996    84 ELCEGGTLRDWIDRRN--------SSSKNDRKLALElfkqILKGVSYIHSKGIVHRDLKPSNIFLDNDDL----QVKIGD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDI--------------YKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILtlgHQPYPAHSNL 2120
Cdd:cd13996   152 FGLATSIgnqkrelnnlnnnnNGNTSNNSVGIG--TPLYASPEQLDGENYNEKADIYSLGIILFEML---HPFKTAMERS 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2121 DVLNYVQTGgrLEPP---RNCPDDLwNLMTQCWAQEPDQRPT 2159
Cdd:cd13996   227 TILTDLRNG--ILPEsfkAKHPKEA-DLIQSLLSKNPEERPS 265
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
1903-2163 5.76e-20

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 91.93  E-value: 5.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGVGS-GEIKVAVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd05078     7 LGQGTFTKIFKGIRREVGDYGQlHETEVLLKVLDKAHRNYSE-SFFEAASMMSQLSHKHLVLNYGVCVCGDENILVQEYV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATfygplltlvdLVDLCVDISKGCV----YLERMHFIHRDLAARNCLVSVKD---YTSPRIVKIGD 2054
Cdd:cd05078    86 KFGSLDTYLKKNKNCI----------NILWKLEVAKQLAwamhFLEEKTLVHGNVCAKNILLIREEdrkTGNPPFIKLSD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIYKNDYYRKRgegllpVRWMAPESLMDGI-FTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLE 2133
Cdd:cd05078   156 PGISITVLPKDILLER------IPWVPPECIENPKnLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLP 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 767943404 2134 PPRNCpdDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05078   230 APKWT--ELANLINNCMDYEPDHRPSFRAI 257
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
1902-2175 9.02e-20

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 91.34  E-value: 9.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTavdilgVGSGEIkVAVKTLKKGSTDQEKI--EFLK---EAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd06631     8 VLGKGAYGTVYCGL------TSTGQL-IAVKQVELDTSDKEKAekEYEKlqeEVDLLKTLKHVNIVGYLGTCLEDNVVSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFG 2056
Cdd:cd06631    81 FMEFVPGGSIASILAR------FGALEEPVFCRYT-KQILEGVAYLHNNNVIHRDIKGNNIML-----MPNGVIKLIDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARDIYKNDYYRKRGEGLLPVR----WMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd06631   149 CAKRLCINLSSGSQSQLLKSMRgtpyWMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWADMNPMAAIFAIGSGRKP 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767943404 2133 EP--PRNCPDDLWNLMTQCWAQEPDQRPTfhriqdQLQLFRNFFL 2175
Cdd:cd06631   228 VPrlPDKFSPEARDFVHACLTRDQDERPS------AEQLLKHPFI 266
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1903-2170 1.33e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 91.24  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVdilgvgSGEIKVAVKTLK--KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd08228    10 IGRGQFSEVYRATCL------LDRKPVALKKVQifEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLltylrkARMATFYGPLLTLVDLVDLCVDISKGCVYLERMH---FIHRDLAARNCLVsvkdyTSPRIVKIGDFGL 2057
Cdd:cd08228    84 ADAGDL------SQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHsrrVMHRDIKPANVFI-----TATGVVKLGDLGL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2058 ARdIYKNDYYRKRGEGLLPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTLgHQPYPAhsnlDVLNYVQTGGRLE---- 2133
Cdd:cd08228   153 GR-FFSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYG----DKMNLFSLCQKIEqcdy 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2134 ---PPRNCPDDLWNLMTQCWAQEPDQRPTF---HRIQDQLQLF 2170
Cdd:cd08228   226 pplPTEHYSEKLRELVSMCIYPDPDQRPDIgyvHQIAKQMHVW 268
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
1897-2159 2.15e-19

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 90.52  E-value: 2.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLL--LGSGAFGEVYEGTAvdilgvgSGEiKVAVKTLKKGSTDQEKIE-FLKEAHLmSKFNHPNILKQLG---VCLL 1970
Cdd:cd13979     3 EPLRLQepLGSGGFGSVYKATY-------KGE-TVAVKIVRRRRKNRASRQsFWAELNA-ARLRHENIVRVLAaetGTDF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQYIILELMEGGDLLTYLrkarmatfYGPLLTLVDLVDLCV--DISKGCVYLERMHFIHRDLAARNCLVSVKDytspr 2048
Cdd:cd13979    74 ASLGLIIMEYCGNGTLQQLI--------YEGSEPLPLAHRILIslDIARALRFCHSHGIVHLDVKPANILISEQG----- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDIYKndyYRKRGEGLLPVR----WMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLN 2124
Cdd:cd13979   141 VCKLCDFGCSVKLGE---GNEVGTPRSHIGgtytYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAGLRQHVLYA 216
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2125 YVQTGGRLEPPRNCPDD----LWNLMTQCWAQEPDQRPT 2159
Cdd:cd13979   217 VVAKDLRPDLSGLEDSEfgqrLRSLISRCWSAQPAERPN 255
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1903-2163 2.17e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 90.19  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdILGVGSGEIKVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILK-----QLGVCLLnepqYI 1976
Cdd:cd08223     8 IGKGSYGEVW------LVRHKRDRKQYVIKKLNlKNASKRERKAAEQEAKLLSKLKHPNIVSykesfEGEDGFL----YI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFG 2056
Cdd:cd08223    78 VMGFCEGGDLYTRLKEQK-----GVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFL-----TKSNIIKVGDLG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARDI-YKND---------YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTLGHqPYPAhSNLDVLNYV 2126
Cdd:cd08223   148 IARVLeSSSDmattligtpYY------------MSPELFSNKPYNHKSDVWALGCCVYEMATLKH-AFNA-KDMNSLVYK 213
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2127 QTGGRLEP-PRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd08223   214 ILEGKLPPmPKQYSPELGELIKAMLHQDPEKRPSVKRI 251
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
1929-2171 2.24e-19

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 90.73  E-value: 2.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCLlNEPQYIIL----------ELMEGGDL-LTYLRKARMAT 1997
Cdd:cd14042    33 VAIKKVNKKRIDLTR-EVLKELKHMRDLQHDNLTRFIGACV-DPPNICILteycpkgslqDILENEDIkLDWMFRYSLIH 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1998 fygplltlvdlvdlcvDISKGCVYLERMHFI-HRDLAARNCLVsvkdyTSPRIVKIGDFGLAR----DIYKND---YYRK 2069
Cdd:cd14042   111 ----------------DIVKGMHYLHDSEIKsHGNLKSSNCVV-----DSRFVLKITDFGLHSfrsgQEPPDDshaYYAK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2070 rgegLLpvrWMAPESLMDGIF----TTQSDVWSFGILIWEILTLG---HQPYPAHSNLDVLNYVQTGGRLEPPR------ 2136
Cdd:cd14042   170 ----LL---WTAPELLRDPNPpppgTQKGDVYSFGIILQEIATRQgpfYEEGPDLSPKEIIKKKVRNGEKPPFRpsldel 242
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2137 NCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFR 2171
Cdd:cd14042   243 ECPDEVLSLMQRCWAEDPEERPDFSTLRNKLKKLN 277
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
1902-2159 3.33e-19

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 89.75  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdiLGVGSGEIkVAVKT--LKKGSTDQEK------IEFLK-EAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd06629     8 LIGKGTYGRVYLA-----MNATTGEM-LAVKQveLPKTSSDRADsrqktvVDALKsEIDTLKDLDHPNIVQYLGFEETED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLVsvkDYTSprIVKI 2052
Cdd:cd06629    82 YFSIFLEYVPGGSIGSCLRK------YGKFEEDLVRFFT-RQILDGLAYLHSKGILHRDLKADNILV---DLEG--ICKI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLAR---DIYKNDyyrkrgEGLL---PVRWMAPESLM---DGiFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVL 2123
Cdd:cd06629   150 SDFGISKksdDIYGNN------GATSmqgSVFWMAPEVIHsqgQG-YSAKVDIWSLGCVVLEMLA-GRRPWSDDEAIAAM 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2124 nYVQTGGRLEPPrnCPDDL------WNLMTQCWAQEPDQRPT 2159
Cdd:cd06629   222 -FKLGNKRSAPP--VPEDVnlspeaLDFLNACFAIDPRDRPT 260
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
1903-2174 3.90e-19

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 89.97  E-value: 3.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKK------GSTDQEKIEflKEAhlMSKFNHPNILK-----QLGVCLln 1971
Cdd:cd05581     9 LGEGSYSTVVLAKEKE-----TGKE-YAIKVLDKrhiikeKKVKYVTIE--KEV--LSRLAHPGIVKlyytfQDESKL-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1972 epqYIILELMEGGDLLTYLRKA-----RMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTs 2046
Cdd:cd05581    77 ---YFVLEYAPNGDLLEYIRKYgsldeKCTRFY------------TAEIVLALEYLHSKGIIHRDLKPENILLD-EDMH- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2047 priVKIGDFGLArDIYKND----------------YYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlG 2110
Cdd:cd05581   140 ---IKITDFGTA-KVLGPDsspestkgdadsqiayNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLT-G 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2111 HQPYPAHSNLDVLNYVQTGGrLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFRN-FF 2174
Cdd:cd05581   215 KPPFRGSNEYLTFQKIVKLE-YEFPENFPPDAKDLIQKLLVLDPSKRLGVNENGGYDELKAHpFF 278
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
1893-2159 4.02e-19

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 89.25  E-value: 4.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLkkgSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd06612     1 PEEVFDILEKLGEGSYGSVYKAIHKE-----TGQV-VAIKVV---PVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTyLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKI 2052
Cdd:cd06612    72 DLWIVMEYCGAGSVSD-IMKITNKTL-----TEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEG-----QAKL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIykNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYpahSNLDVLNYVQTGGRL 2132
Cdd:cd06612   141 ADFGVSGQL--TDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIE-MAEGKPPY---SDIHPMRAIFMIPNK 214
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767943404 2133 EPP--RNcPDDlW-----NLMTQCWAQEPDQRPT 2159
Cdd:cd06612   215 PPPtlSD-PEK-WspefnDFVKKCLVKDPEERPS 246
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
1903-2172 4.72e-19

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 89.71  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdilgvGSGEikVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVcLLNEPQYIILELM 1981
Cdd:cd14149    20 IGSGSFGTVYKGK-------WHGD--VAVKILKVVDPTPEQFQaFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLR--KARMATFygplltlvdlvdLCVDISK----GCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDF 2055
Cdd:cd14149    90 EGSSLYKHLHvqETKFQMF------------QLIDIARqtaqGMDYLHAKNIIHRDMKSNNIFLH-----EGLTVKIGDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDIYKNDYYRKRGEGLLPVRWMAPESLM---DGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd14149   153 GLATVKSRWSGSQQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMT-GELPYSHINNRDQIIFMVGRGYA 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767943404 2133 EPP-----RNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFRN 2172
Cdd:cd14149   232 SPDlsklyKNCPKAMKRLVADCIKKVKEERPLFPQILSSIELLQH 276
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
1929-2163 5.77e-19

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 89.37  E-value: 5.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVK--TLKKGSTDQEKIEFLKeahlMSKFNHPNILKQLGVCLlNEPQYIIL-ELMEGGDLLTYLRKARMA---TFYGPL 2002
Cdd:cd13992    28 VAIKhiTFSRTEKRTILQELNQ----LKELVHDNLNKFIGICI-NPPNIAVVtEYCTRGSLQDVLLNREIKmdwMFKSSF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2003 LTlvdlvdlcvDISKGCVYLERMHFI-HRDLAARNCLVSvkdytSPRIVKIGDFGLAR------DIYKNDYYRKrgEGLL 2075
Cdd:cd13992   103 IK---------DIVKGMNYLHSSSIGyHGRLKSSNCLVD-----SRWVVKLTDFGLRNlleeqtNHQLDEDAQH--KKLL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2076 pvrWMAPESL---MDGIFTTQ-SDVWSFGILIWEILTLgHQPYPAHSNLDVLNYVQTGGRlEPPR--------NCPDDLW 2143
Cdd:cd13992   167 ---WTAPELLrgsLLEVRGTQkGDVYSFAIILYEILFR-SDPFALEREVAIVEKVISGGN-KPFRpelavlldEFPPRLV 241
                         250       260
                  ....*....|....*....|
gi 767943404 2144 NLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd13992   242 LLVKQCWAENPEKRPSFKQI 261
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
1904-2159 8.36e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 88.51  E-value: 8.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1904 GSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd06626     9 GEGTFGKVYTAVNLD-----TGEL-MAMKEIRFQDNDPKTIKEIAdEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRkarmatfYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARDIY 2062
Cdd:cd06626    83 EGTLEELLR-------HGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFL-----DSNGLIKLGDFGSAVKLK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPV---RWMAPESLMDGIFTTQ---SDVWSFGILIWEILTlGHQPYPAH-SNLDVLNYVQTGGRlePP 2135
Cdd:cd06626   151 NNTTTMAPGEVNSLVgtpAYMAPEVITGNKGEGHgraADIWSLGCVVLEMAT-GKRPWSELdNEWAIMYHVGMGHK--PP 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 767943404 2136 rnCPDDLW------NLMTQCWAQEPDQRPT 2159
Cdd:cd06626   228 --IPDSLQlspegkDFLSRCLESDPKKRPT 255
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
1894-2159 2.35e-18

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 87.45  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEV---YEGTAVDilgvgsgeiKVAVKTLKK-------GSTDQEKIEFLKEAHLMSKFNHPNILK 1963
Cdd:cd14084     5 RKKYIMSRTLGSGACGEVklaYDKSTCK---------KVAIKIINKrkftigsRREINKPRNIETEIEILKKLSHPCIIK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1964 QLGVCLLNEPQYIILELMEGGDLLTYLRKARMAT-------FYgplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARN 2036
Cdd:cd14084    76 IEDFFDAEDDYYIVLELMEGGELFDRVVSNKRLKeaicklyFY--------------QMLLAVKYLHSNGIIHRDLKPEN 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2037 CLVSVKDYTSprIVKIGDFGLARdIYKNDYYRKRGEGllPVRWMAPESLMDGI---FTTQSDVWSFGILIWEILTlGHQP 2113
Cdd:cd14084   142 VLLSSQEEEC--LIKITDFGLSK-ILGETSLMKTLCG--TPTYLAPEVLRSFGtegYTRAVDCWSLGVILFICLS-GYPP 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767943404 2114 YPAH-SNLDVLNYVQTGG-RLEPP--RNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14084   216 FSEEyTQMSLKEQILSGKyTFIPKawKNVSEEAKDLVKKMLVVDPSRRPS 265
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
1890-2159 2.56e-18

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 87.11  E-value: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1890 PAFPREKLTLRLLLGSGAFGEVYegTAVDIlgvgSGEIKVAVKtlKKGSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVC 1968
Cdd:cd06648     2 PGDPRSDLDNFVKIGEGSTGIVC--IATDK----STGRQVAVK--KMDLRKQQRRELLfNEVVIMRDYQHPNIVEMYSSY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1969 LLNEPQYIILELMEGGDLLTYLRKARMatfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPR 2048
Cdd:cd06648    74 LVGDELWVVMEFLEGGALTDIVTHTRM--------NEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILL-----TSDG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDIYKNDYYRKRGEGLlPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQT 2128
Cdd:cd06648   141 RVKLSDFGFCAQVSKEVPRRKSLVGT-PY-WMAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPYFNEPPLQAMKRIRD 217
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2129 ggrLEPPR-----NCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06648   218 ---NEPPKlknlhKVSPRLRSFLDRMLVRDPAQRAT 250
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
1903-2159 2.86e-18

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 86.98  E-value: 2.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEIkVAVKTLKkgSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd06613     8 IGSGTYGDVYK--ARNIA---TGEL-AAVKVIK--LEPGDDFEIIqQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGG---DLLTYLRkarmatfygpLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLA 2058
Cdd:cd06613    80 GGGslqDIYQVTG----------PLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILL-----TEDGDVKLADFGVS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIYKNDYYRKRGEGLLpvRWMAPESL---MDGIFTTQSDVWSFGILIWEILTLghqpYPAHSNLD---VLnYVQTGGRL 2132
Cdd:cd06613   145 AQLTATIAKRKSFIGTP--YWMAPEVAaveRKGGYDGKCDIWALGITAIELAEL----QPPMFDLHpmrAL-FLIPKSNF 217
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767943404 2133 EPPRNCPDDLW-----NLMTQCWAQEPDQRPT 2159
Cdd:cd06613   218 DPPKLKDKEKWspdfhDFIKKCLTKNPKKRPT 249
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
1903-2159 3.27e-18

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 86.70  E-value: 3.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTD-QEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd08529     8 LGKGSFGVVYKVVRKV-----DGRV-YALKQIDISRMSrKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARDI 2061
Cdd:cd08529    82 ENGDLHSLIKSQR-----GRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN-----VKIGDLGVAKIL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGLlPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLD-VLNYVQtgGRLEP-PRNCP 2139
Cdd:cd08529   152 SDTTNFAQTIVGT-PY-YLSPELCEDKPYNEKSDVWALGCVLYELCT-GKHPFEAQNQGAlILKIVR--GKYPPiSASYS 226
                         250       260
                  ....*....|....*....|
gi 767943404 2140 DDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd08529   227 QDLSQLIDSCLTKDYRQRPD 246
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
1903-2159 5.25e-18

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 86.72  E-value: 5.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdilgVGSGEIKV--AVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd06611    13 LGDGAFGKVYK--------AQHKETGLfaAAKIIQIESEEELE-DFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKArmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARD 2060
Cdd:cd06611    84 CDGGALDSIMLEL------ERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILL-----TLDGDVKLADFGVSAK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYKNDyyRKRGEGLLPVRWMAPESLM-----DGIFTTQSDVWSFGILIWEILtlghQPYPAHSNLD---VLNYVQTGG-- 2130
Cdd:cd06611   153 NKSTL--QKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELA----QMEPPHHELNpmrVLLKILKSEpp 226
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2131 RLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06611   227 TLDQPSKWSSSFNDFLKSCLVKDPDDRPT 255
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
1903-2123 6.50e-18

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 86.38  E-value: 6.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEIkVAVKTLKKgstDQEKIEF----LKEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd07829     7 LGEGTYGVVYK--AKDKK---TGEI-VALKKIRL---DNEEEGIpstaLREISLLKELKHPNIVKLLDVIHTENKLYLVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGgDLLTYLRKARmatfygplltlvdlvdlcVDIS------------KGCVYLERMHFIHRDLAARNCLVSVKdyts 2046
Cdd:cd07829    78 EYCDQ-DLKKYLDKRP------------------GPLPpnliksimyqllRGLAYCHSHRILHRDLKPQNLLINRD---- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2047 pRIVKIGDFGLARDI------YKND----YYRkrgegllpvrwmAPESLM-DGIFTTQSDVWSFGILIWEILTlGHQPYP 2115
Cdd:cd07829   135 -GVLKLADFGLARAFgiplrtYTHEvvtlWYR------------APEILLgSKHYSTAVDIWSVGCIFAELIT-GKPLFP 200

                  ....*...
gi 767943404 2116 AHSNLDVL 2123
Cdd:cd07829   201 GDSEIDQL 208
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
1893-2159 1.12e-17

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 85.49  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGtavdiLGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd06642     2 PEELFTKLERIGKGSFGEVYKG-----IDNRTKEV-VAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARMATFYgplltlvdLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd06642    76 KLWIIMEYLGGGSALDLLKPGPLEETY--------IATILREILKGLDYLHSERKIHRDIKAANVLLSEQGD-----VKL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIykNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYPAHSNLDVLNYVqtggrl 2132
Cdd:cd06642   143 ADFGVAGQL--TDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIE-LAKGEPPNSDLHPMRVLFLI------ 213
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2133 epPRNCPDDLW--------NLMTQCWAQEPDQRPT 2159
Cdd:cd06642   214 --PKNSPPTLEgqhskpfkEFVEACLNKDPRFRPT 246
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
1902-2163 1.14e-17

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 85.35  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAfGEVYEGTAVDILGVGSGEIKVAVKTLKKGSTDQeKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd05076    20 LLVEGS-GEPEEDKELVPGRDRGQELRVVLKVLDPSHHDI-ALAFFETASLMSQVSHTHLVFVHGVCVRGSENIMVEEFV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVS---VKDYTSPrIVKIGDFGLA 2058
Cdd:cd05076    98 EHGPLDVWLRKEKGHV------PMAWKFVVARQLASALSYLENKNLVHGNVCAKNILLArlgLEEGTSP-FIKLSDPGVG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIYkndyyrKRGEGLLPVRWMAPESLMDGI-FTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPrN 2137
Cdd:cd05076   171 LGVL------SREERVERIPWIAPECVPGGNsLSTAADKWGFGATLLEICFNGEAPLQSRTPSEKERFYQRQHRLPEP-S 243
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2138 CPdDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05076   244 CP-ELATLISQCLTYEPTQRPSFRTI 268
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
2013-2168 1.15e-17

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 85.23  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2013 VDISKGCVYLERMHFIHRDLAARNCLVSVKDYTsprivKIGDFGLARDiykndyyrkrgEGLL-------PVRwMAPEsL 2085
Cdd:cd13975   109 LDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRA-----KITDLGFCKP-----------EAMMsgsivgtPIH-MAPE-L 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2086 MDGIFTTQSDVWSFGILIWEILTlGHQPYP-----AHSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd13975   171 FSGKYDNSVDVYAFGILFWYLCA-GHVKLPeafeqCASKDHLWNNVRKGVRPERLPVFDEECWNLMEACWSGDPSQRPLL 249

                  ....*...
gi 767943404 2161 HRIQDQLQ 2168
Cdd:cd13975   250 GIVQPKLQ 257
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
1903-2163 1.75e-17

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 84.57  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKkgSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLLNEpQYIILELM 1981
Cdd:cd14208     7 LGKGSFTKIYRGLRTDEEDDERCETEVLLKVMD--PTHGNCQEsFLEAASIMSQISHKHLVLLHGVCVGKD-SIMVQEFV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRK----ARMATFYGPLLTLVDLVDLCvdiskgcvYLERMHFIHRDLAARNCLVSVK-DYTSPRIVKIGDFG 2056
Cdd:cd14208    84 CHGALDLYLKKqqqkGPVAISWKLQVVKQLAYALN--------YLEDKQLVHGNVSAKKVLLSREgDKGSPPFIKLSDPG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARDIYKNDYYRKRgegllpVRWMAPESLMDG-IFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPP 2135
Cdd:cd14208   156 VSIKVLDEELLAER------IPWVAPECLSDPqNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQLPAP 229
                         250       260
                  ....*....|....*....|....*...
gi 767943404 2136 RNCpdDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14208   230 HWI--ELASLIQQCMSYNPLLRPSFRAI 255
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1903-2163 2.13e-17

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 84.24  E-value: 2.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilGVGSGEIKVAVKTLKKGSTdQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd08225     8 IGEGSFGKIYLAKA----KSDSEHCVIKEIDLTKMPV-KEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdyTSPRIVKIGDFGLARDIy 2062
Cdd:cd08225    83 GGDLMKRINRQRGVLF-----SEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLS----KNGMVAKLGDFGIARQL- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 kNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHqPYPAhSNLDVLNYVQTGGRLEP-PRNCPDD 2141
Cdd:cd08225   153 -NDSMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKH-PFEG-NNLHQLVLKICQGYFAPiSPNFSRD 229
                         250       260
                  ....*....|....*....|..
gi 767943404 2142 LWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd08225   230 LRSLISQLFKVSPRDRPSITSI 251
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
1893-2157 2.60e-17

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 84.21  E-value: 2.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYegTAVDIlgvgSGEIKVAVKTLKkgSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVCLLN 1971
Cdd:cd06647     5 PKKKYTRFEKIGQGASGTVY--TAIDV----ATGQEVAIKQMN--LQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1972 EPQYIILELMEGGDLLTYLRKARMatfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVK 2051
Cdd:cd06647    77 DELWVVMEYLAGGSLTDVVTETCM--------DEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGS-----VK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLARDIYKNDyyRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGR 2131
Cdd:cd06647   144 LTDFGFCAQITPEQ--SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGT 220
                         250       260       270
                  ....*....|....*....|....*....|
gi 767943404 2132 LEPPRncPDDL----WNLMTQCWAQEPDQR 2157
Cdd:cd06647   221 PELQN--PEKLsaifRDFLNRCLEMDVEKR 248
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
1902-2165 3.06e-17

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 83.92  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegTAVDIlgvgSGEIKVAVKTLKKGSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd14069     8 TLGEGAFGEVF--LAVNR----NTEEAVAVKFVDMKRAPGDCPENIkKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTylrkaRMATFYG-PLLTLVDLVDLCVdisKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLAr 2059
Cdd:cd14069    82 ASGGELFD-----KIEPDVGmPEDVAQFYFQQLM---AGLKYLHSCGITHRDIKPENLLLDEND-----NLKISDFGLA- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 diyknDYYRKRGE--------GLLPvrWMAPESLMDGIFTTQ-SDVWSFGILIWEILTlGHQPY--PAHSNLDVLNYVqT 2128
Cdd:cd14069   148 -----TVFRYKGKerllnkmcGTLP--YVAPELLAKKKYRAEpVDVWSCGIVLFAMLA-GELPWdqPSDSCQEYSDWK-E 218
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2129 GGRLE--PPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd14069   219 NKKTYltPWKKIDTAALSLLRKILTENPNKRITIEDIKK 257
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
1903-2182 4.59e-17

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 84.31  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGeIKVAVKTLKKGStDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd06644    20 LGDGAFGKVYKAKNKE-----TG-ALAAAKVIETKS-EEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDL-LTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARDI 2061
Cdd:cd06644    93 GGAVdAIMLELDRGLT-------EPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD-----IKLADFGVSAKN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNdyYRKRGEGLLPVRWMAPESLM-----DGIFTTQSDVWSFGILIWEILtlghQPYPAHSNLDVLNYVQTGGRLEPPR 2136
Cdd:cd06644   161 VKT--LQRRDSFIGTPYWMAPEVVMcetmkDTPYDYKADIWSLGITLIEMA----QIEPPHHELNPMRVLLKIAKSEPPT 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2137 -NCPD----DLWNLMTQCWAQEPDQRPTfhriqdQLQLFRNFFLNSIYKSR 2182
Cdd:cd06644   235 lSQPSkwsmEFRDFLKTALDKHPETRPS------AAQLLEHPFVSSVTSNR 279
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
1903-2165 5.06e-17

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 84.03  E-value: 5.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAfgevyEGTAVDILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYII-LELM 1981
Cdd:cd06620    13 LGAGN-----GGSVSKVLHIPTGTI-MAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENNNIIIcMEYM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKarmatfYGPLLTLVDLVDLcVDISKGCVYLERMH-FIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARD 2060
Cdd:cd06620    87 DCGSLDKILKK------KGPFPEEVLGKIA-VAVLEGLTYLYNVHrIIHRDIKPSNILV-----NSKGQIKLCDFGVSGE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYKNDYYRKRGEGLlpvrWMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYPAHsNLDVLNYVQTGGRL-------- 2132
Cdd:cd06620   155 LINSIADTFVGTST----YMSPERIQGGKYSVKSDVWSLGLSIIE-LALGEFPFAGS-NDDDDGYNGPMGILdllqrivn 228
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2133 EPP------RNCPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd06620   229 EPPprlpkdRIFPKDLRDFVDRCLLKDPRERPSPQLLLD 267
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
1903-2157 5.64e-17

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 83.04  E-value: 5.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdILGVGSGEIKVAVKTLKKGS---TDQEKIEFLkEAHLMSKFNHPNILKQlgVCLLNEPQYI--I 1977
Cdd:cd05572     1 LGVGGFGRVE------LVQLKSKGRTFALKCVKKRHivqTRQQEHIFS-EKEILEECNSPFIVKL--YRTFKDKKYLymL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKA-----RMATFYgplltlvdlvdlcvdisKGCV-----YLERMHFIHRDLAARNCLVSVKDYtsp 2047
Cdd:cd05572    72 MEYCLGGELWTILRDRglfdeYTARFY-----------------TACVvlafeYLHSRGIIYRDLKPENLLLDSNGY--- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 riVKIGDFGLARDIYKndyYRKRgegllpvrW--------MAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY--PAH 2117
Cdd:cd05572   132 --VKLVDFGFAKKLGS---GRKT--------WtfcgtpeyVAPEIILNKGYDFSVDYWSLGILLYELLT-GRPPFggDDE 197
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767943404 2118 SNLDVLNYVQTG-GRLEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05572   198 DPMKIYNIILKGiDKIEFPKYIDKNAKNLIKQLLRRNPEER 238
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
1903-2159 6.36e-17

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 83.58  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGVgsgeikVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd06641    12 IGKGSFGEVFKGIDNRTQKV------VAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKarmatfyGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARDIy 2062
Cdd:cd06641    86 GGSALDLLEP-------GPLDETQIATIL-REILKGLDYLHSEKKIHRDIKAANVLLSEHGE-----VKLADFGVAGQL- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 kNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILtlghQPYPAHSNLDVLNYVQTGGRLEPPR---NCP 2139
Cdd:cd06641   152 -TDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELA----RGEPPHSELHPMKVLFLIPKNNPPTlegNYS 226
                         250       260
                  ....*....|....*....|
gi 767943404 2140 DDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06641   227 KPLKEFVEACLNKEPSFRPT 246
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
1902-2146 6.97e-17

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 83.14  E-value: 6.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14202     9 LIGHGAFAVVFKGRHKE-----KHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdYTSPR-------IVKIGD 2054
Cdd:cd14202    84 NGGDLADYLHTMRTLS-------EDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLS---YSGGRksnpnniRIKIAD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIYKNDYYRKR-GEGLlpvrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGGRLE 2133
Cdd:cd14202   154 FGFARYLQNNMMAATLcGSPM----YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEKNKSLS 228
                         250
                  ....*....|....*
gi 767943404 2134 P--PRNCPDDLWNLM 2146
Cdd:cd14202   229 PniPRETSSHLRQLL 243
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
1902-2163 7.56e-17

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 82.60  E-value: 7.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd14099     8 FLGKGGFAKCYEVTDMS-----TGKV-YAGKVVPKSSLTKPKQRekLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMAT-----FYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGD 2054
Cdd:cd14099    82 LCSNGSLMELLKRRKALTepevrYF------------MRQILSGVKYLHSNRIIHRDLKLGNLFL-----DENMNVKIGD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIyKNDYYRKR---GEgllPvRWMAPESLMDGI-FTTQSDVWSFGILIWEILTlGHQPYPAhSNLDVL------- 2123
Cdd:cd14099   145 FGLAARL-EYDGERKKtlcGT---P-NYIAPEVLEKKKgHSFEVDIWSLGVILYTLLV-GKPPFET-SDVKETykrikkn 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2124 NYvqtggrlEPPRNC--PDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14099   218 EY-------SFPSHLsiSDEAKDLIRSMLQPDPTKRPSLDEI 252
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
1893-2159 7.64e-17

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 83.18  E-value: 7.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDILGVgsgeikVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd06640     2 PEELFTKLERIGKGSFGEVFKGIDNRTQQV------VAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARMATFygplltlvDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd06640    76 KLWIIMEYLGGGSALDLLRAGPFDEF--------QIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGD-----VKL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIykNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYPAHSNLDVLNYVqtggrl 2132
Cdd:cd06640   143 ADFGVAGQL--TDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIE-LAKGEPPNSDMHPMRVLFLI------ 213
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2133 epPRNCPDDLWNLMTQ--------CWAQEPDQRPT 2159
Cdd:cd06640   214 --PKNNPPTLVGDFSKpfkefidaCLNKDPSFRPT 246
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
1903-2160 8.89e-17

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 82.34  E-value: 8.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVdilgVGSGEIkVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14121     3 LGSGTYATVYKAYRK----SGAREV-VAVKCVSKSSLNKASTEnLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMAtfygPLLTLVDLVDlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYTsprIVKIGDFGLARDI 2061
Cdd:cd14121    78 SGGDLSRFIRSRRTL----PESTVRRFLQ---QLASALQFLREHNISHMDLKPQNLLLSSRYNP---VLKLADFGFAQHL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRK-RGEGLlpvrWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAHSNLDVLNYVQTGGRLEPP----- 2135
Cdd:cd14121   148 KPNDEAHSlRGSPL----YMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRSFEELEEKIRSSKPIEIPtrpel 222
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2136 -RNCPDDLWNLMtqcwAQEPDQRPTF 2160
Cdd:cd14121   223 sADCRDLLLRLL----QRDPDRRISF 244
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
1903-2163 9.83e-17

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 82.62  E-value: 9.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGVGsgeiKVAVKTL--KKGSTD-QEKieFL-KEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd14080     8 IGEGSYSKVKLAEYTKSGLKE----KVACKIIdkKKAPKDfLEK--FLpRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLR--------KARmATFYgplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriV 2050
Cdd:cd14080    82 EYAEHGDLLEYIQkrgalsesQAR-IWFR--------------QLALAVQYLHSLDIAHRDLKCENILLDSNNN-----V 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLARDIYKNDY------------YrkrgegllpvrwMAPESLMdGI--FTTQSDVWSFGILIWeILTLGHQPYpA 2116
Cdd:cd14080   142 KLSDFGFARLCPDDDGdvlsktfcgsaaY------------AAPEILQ-GIpyDPKKYDIWSLGVILY-IMLCGSMPF-D 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767943404 2117 HSNLDVLNYVQTGGRLEPPR---NCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14080   207 DSNIKKMLKDQQNRKVRFPSsvkKLSPECKDLIDQLLEPDPTKRATIEEI 256
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
1893-2159 2.18e-16

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 81.58  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKkgSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLLN 1971
Cdd:cd06608     4 PAGIFELVEVIGEGTYGKVYKARHKK-----TGQL-AAIKIMD--IIEDEEEEIKLEINILRKFsNHPNIATFYGAFIKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1972 EPQ------YIILELMEGG---DLLTYLRKArmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvk 2042
Cdd:cd06608    76 DPPggddqlWLVMEYCGGGsvtDLVKGLRKK------GKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILL--- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2043 dyTSPRIVKIGDFGLARDIYKNdyYRKRGEGLLPVRWMAPESLM-----DGIFTTQSDVWSFGILIWEiLTLGHQP---- 2113
Cdd:cd06608   147 --TEEAEVKLVDFGVSAQLDST--LGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIE-LADGKPPlcdm 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767943404 2114 YPAHSNLDVLNYVQTggRLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06608   222 HPMRALFKIPRNPPP--TLKSPEKWSKEFNDFISECLIKNYEQRPF 265
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
1900-2146 2.56e-16

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 81.59  E-value: 2.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1900 RLLLGSGAFGEVYEGTAVDilgvgSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd14201    11 KDLVGHGAFAVVFKGRHRK-----KTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRI----VKIGDF 2055
Cdd:cd14201    86 YCNGGDLADYLQAKGTLS-------EDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSSVsgirIKIADF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDIYKNDYYRKRGEGLLpvrWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAHSNLDVLNYVQTGGRLEP- 2134
Cdd:cd14201   159 GFARYLQSNMMAATLCGSPM---YMAPEVIMSQHYDAKADLWSIGTVIYQCL-VGKPPFQANSPQDLRMFYEKNKNLQPs 234
                         250
                  ....*....|...
gi 767943404 2135 -PRNCPDDLWNLM 2146
Cdd:cd14201   235 iPRETSPYLADLL 247
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
1902-2157 2.73e-16

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 81.86  E-value: 2.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegTAVDILGvgSGEIkVAVKTLKKgstdqEKIEFLK-------EAHLMSKFNHPNILKQLGV-----CL 1969
Cdd:cd05580     8 TLGTGSFGRV---RLVKHKD--SGKY-YALKILKK-----AKIIKLKqvehvlnEKRILSEVRHPFIVNLLGSfqddrNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 lnepqYIILELMEGGDLLTYLRKAR-----MATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDY 2044
Cdd:cd05580    77 -----YMVMEYVPGGELFSLLRRSGrfpndVAKFYA------------AEVVLALEYLHSLDIVYRDLKPENLLLDSDGH 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2045 tspriVKIGDFGLARDIYKNDY-------YrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAH 2117
Cdd:cd05580   140 -----IKITDFGFAKRVKDRTYtlcgtpeY------------LAPEIILSKGHGKAVDWWALGILIYEMLA-GYPPFFDE 201
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767943404 2118 SNLDVlnYVQT-GGRLEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05580   202 NPMKI--YEKIlEGKIRFPSFFDPDAKDLIKRLLVVDLTKR 240
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
1903-2114 3.19e-16

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 80.73  E-value: 3.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEG----TAVDilgVGSGEIKVavktlkKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd13983     9 LGRGSFKTVYRAfdteEGIE---VAWNEIKL------RKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 --ELMEGGDLLTYLRKArmatfygPLLTLVDLVDLCVDISKGCVYLermH-----FIHRDLAARNCLVSvkdyTSPRIVK 2051
Cdd:cd13983    80 itELMTSGTLKQYLKRF-------KRLKLKVIKSWCRQILEGLNYL---HtrdppIIHRDLKCDNIFIN----GNTGEVK 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2052 IGDFGLArdIYKNDYYRKRGEGLLpvRWMAPEsLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd13983   146 IGDLGLA--TLLRQSFAKSVIGTP--EFMAPE-MYEEHYDEKVDIYAFGMCLLEMAT-GEYPY 202
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
1903-2178 3.95e-16

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 81.23  E-value: 3.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDIlgvgsgEIKVAVKTLKKgSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd06643    13 LGDGAFGKVYKAQNKET------GILAAAKVIDT-KSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLltylrKARMATFYGPLLTLVDLVDlCVDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPRIVKIGDFGLARdiy 2062
Cdd:cd06643    86 GGAV-----DAVMLELERPLTEPQIRVV-CKQTLEALVYLHENKIIHRDLKAGNIL-----FTLDGDIKLADFGVSA--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPV-RWMAPESLM-----DGIFTTQSDVWSFGILIWEILtlghQPYPAHSNLDVLNYVQTGGRLEPPR 2136
Cdd:cd06643   152 KNTRTLQRRDSFIGTpYWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMA----QIEPPHHELNPMRVLLKIAKSEPPT 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767943404 2137 NCPDDLW-----NLMTQCWAQEPDQRPTfhriqdQLQLFRNFFLNSI 2178
Cdd:cd06643   228 LAQPSRWspefkDFLRKCLEKNVDARWT------TSQLLQHPFVSVL 268
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
1898-2159 4.25e-16

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 80.78  E-value: 4.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1898 TLRLLLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKI--EFLKEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd08224     3 EIEKKIGKGQFSVVYRARCLL-----DGRL-VALKKVQIFEMMDAKArqDCLKEIDLLQQLNHPNIIKYLASFIENNELN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMATFYGPLLTLVDLvdlcvdISKGCVYLERMH---FIHRDLAARNCLVsvkdyTSPRIVKI 2052
Cdd:cd08224    77 IVLELADAGDLSRLIKHFKKQKRLIPERTIWKY------FVQLCSALEHMHskrIMHRDIKPANVFI-----TANGVVKL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKND----------YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDV 2122
Cdd:cd08224   146 GDLGLGRFFSSKTtaahslvgtpYY------------MSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNLYS 213
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2123 LNYVQTGGRLEP-PRNC-PDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd08224   214 LCKKIEKCEYPPlPADLySQELRDLVAACIQPDPEKRPD 252
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
1903-2160 4.99e-16

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 80.11  E-value: 4.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14120     1 IGHGAFAVVFKGRHRK-----KPDLPVAIKCITKKNLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKAR------MATFYgplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSP---RI-VKI 2052
Cdd:cd14120    76 GGDLADYLQAKGtlsedtIRVFL-------------QQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPspnDIrLKI 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARdiYKNDyyrkrgeGLLPVR------WMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd14120   143 ADFGFAR--FLQD-------GMMAATlcgspmYMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELKAFY 212
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767943404 2127 QTGGRLEP--PRNCPDDLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd14120   213 EKNANLRPniPSGTSPALKDLLLGLLKRNPKDRIDF 248
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
1903-2163 5.53e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 80.37  E-value: 5.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDI------LGVGSGEIKVAVKTLKKGSTDQEkIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd05077     7 LGRGTRTQIYAGILNYKdddedeGYSYEKEIKVILKVLDPSHRDIS-LAFFETASMMRQVSHKHIVLLYGVCVRDVENIM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYL-RKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVK--DYTSPRIVKIG 2053
Cdd:cd05077    86 VEEFVEFGPLDLFMhRKSDVLT-------TPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLAREgiDGECGPFIKLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKndyyrkRGEGLLPVRWMAPESLMDG-IFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd05077   159 DPGIPITVLS------RQECVERIPWIAPECVEDSkNLSIAADKWSFGTTLWEICYNGEIPLKDKTLAEKERFYEGQCML 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2133 EPPrNCpDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd05077   233 VTP-SC-KELADLMTHCMNYDPNQRPFFRAI 261
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
1890-2175 6.27e-16

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 80.85  E-value: 6.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1890 PAFPREKLTLRLLLGSGAFGEVYEGTAVDilgvgSGEiKVAVKtlKKGSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVC 1968
Cdd:cd06658    17 PGDPREYLDSFIKIGEGSTGIVCIATEKH-----TGK-QVAVK--KMDLRKQQRRELLfNEVVIMRDYHHENVVDMYNSY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1969 LLNEPQYIILELMEGGDLLTYLRKARMatfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPR 2048
Cdd:cd06658    89 LVGDELWVVMEFLEGGALTDIVTHTRM--------NEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILL-----TSDG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQT 2128
Cdd:cd06658   156 RIKLSDFGFCAQVSKEVPKRKSLVG--TPYWMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPYFNEPPLQAMRRIRD 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767943404 2129 G--GRLEPPRNCPDDLWNLMTQCWAQEPDQRPTfhriqdQLQLFRNFFL 2175
Cdd:cd06658   233 NlpPRVKDSHKVSSVLRGFLDLMLVREPSQRAT------AQELLQHPFL 275
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
1902-2124 8.25e-16

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 80.40  E-value: 8.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVdilgvGSGEIkVAVKTLKKgSTDQEKI--EFLKEAHLMSK---FNHPNILKQLGVCLLNEPQ-- 1974
Cdd:cd07838     6 EIGEGAYGTVYKARDL-----QDGRF-VALKKVRV-PLSEEGIplSTIREIALLKQlesFEHPNVVRLLDVCHGPRTDre 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 ---YIILELMEGgDLLTYLRKARMATFyGPLLTLvdlvdlcvDIS----KGCVYLERMHFIHRDLAARNCLVsvkdyTSP 2047
Cdd:cd07838    79 lklTLVFEHVDQ-DLATYLDKCPKPGL-PPETIK--------DLMrqllRGLDFLHSHRIVHRDLKPQNILV-----TSD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 RIVKIGDFGLARdIYKND----------YYRkrgegllpvrwmAPESLMDGIFTTQSDVWSFGILIWEILTLghQP-YPA 2116
Cdd:cd07838   144 GQVKLADFGLAR-IYSFEmaltsvvvtlWYR------------APEVLLQSSYATPVDMWSVGCIFAELFNR--RPlFRG 208

                  ....*...
gi 767943404 2117 HSNLDVLN 2124
Cdd:cd07838   209 SSEADQLG 216
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
1903-2165 8.89e-16

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 79.61  E-value: 8.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILgvgsgeIKVAVKTLKKgsTDQEKI-----EFLKEAHLMSKFNHPNILKQLGVCLLNEPQ--Y 1975
Cdd:cd14119     1 LGEGSYGKVKEVLDTETL------CRRAVKILKK--RKLRRIpngeaNVKREIQILRRLNHRNVIKLVDVLYNEEKQklY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGdLLTYLRKARMATFygPLLTLVDLVDLCVDiskGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDF 2055
Cdd:cd14119    73 MVMEYCVGG-LQEMLDSAPDKRL--PIWQAHGYFVQLID---GLEYLHSQGIIHKDIKPGNLLLTTDG-----TLKISDF 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLAR--DIYKNDYYRKRGEGlLPVrWMAPE-----SLMDGIfttQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQT 2128
Cdd:cd14119   142 GVAEalDLFAEDDTCTTSQG-SPA-FQPPEiangqDSFSGF---KVDIWSAGVTLYNMTT-GKYPFEGDNIYKLFENIGK 215
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767943404 2129 gGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd14119   216 -GEYTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQ 251
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
1908-2172 9.77e-16

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 80.44  E-value: 9.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1908 FGEVYEgTAVDIlGVGSGEI-----------KVAVKTLKKGSTD-QEKIEFLkeahlMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd14177     2 FTDVYE-LKEDI-GVGSYSVckrcihratnmEFAVKIIDKSKRDpSEEIEIL-----MRYGQHPNIITLKDVYDDGRYVY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsVKDYTSPRIVKIGDF 2055
Cdd:cd14177    75 LVTELMKGGELLDRILRQKFFS-------EREASAVLYTITKTVDYLHCQGVVHRDLKPSNILY-MDDSANADSIRICDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDIykndyyrkRGE-GLL-----PVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY---PAHSNLDVL--- 2123
Cdd:cd14177   147 GFAKQL--------RGEnGLLltpcyTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLA-GYTPFangPNDTPEEILlri 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2124 ---NYVQTGGRLEpprNCPDDLWNLMTQCWAQEPDQRPTFHRI--------QDQL---QLFRN 2172
Cdd:cd14177   218 gsgKFSLSGGNWD---TVSDAAKDLLSHMLHVDPHQRYTAEQVlkhswiacRDQLphyQLNRQ 277
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
2014-2172 1.42e-15

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 78.99  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2014 DISKGCVYLERMHFIHRDLAARNCLVSvkdytsPRIV-KIGDFGLardiykNDYYR--------KRGEGLLpvrWMAPES 2084
Cdd:cd14043   105 DLIKGMRYLHHRGIVHGRLKSRNCVVD------GRFVlKITDYGY------NEILEaqnlplpePAPEELL---WTAPEL 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2085 LMDGIF----TTQSDVWSFGILIWEILTLGhQPY-----PAHsnlDVLNYVQtggrlEPPRNC---------PDDLWNLM 2146
Cdd:cd14043   170 LRDPRLerrgTFPGDVFSFAIIMQEVIVRG-APYcmlglSPE---EIIEKVR-----SPPPLCrpsvsmdqaPLECIQLM 240
                         170       180
                  ....*....|....*....|....*.
gi 767943404 2147 TQCWAQEPDQRPTFHRIQDQlqlFRN 2172
Cdd:cd14043   241 KQCWSEAPERRPTFDQIFDQ---FKS 263
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
1903-2164 1.47e-15

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 78.83  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdiLGVG--SGEiKVAVKTLKKGSTDQE----KIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd14081     9 LGKGQTGLVK-------LAKHcvTGQ-KVAIKIVNKEKLSKEsvlmKVE--REIAIMKLIEHPNVLKLYDVYENKKYLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYL-RKARM-----ATFYGplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKdytspRIV 2050
Cdd:cd14081    79 VLEYVSGGELFDYLvKKGRLtekeaRKFFR-------------QIISALDYCHSHSICHRDLKPENLLLDEK-----NNI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLARdIYKNDYYRKRGEGLLpvRWMAPESLM----DGIfttQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd14081   141 KIADFGMAS-LQPEGSLLETSCGSP--HYACPEVIKgekyDGR---KADIWSCGVILYALLV-GALPFDDDNLRQLLEKV 213
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2127 QTgGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQ 2164
Cdd:cd14081   214 KR-GVFHIPHFISPDAQDLLRRMLEVNPEKRITIEEIK 250
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
1928-2175 1.61e-15

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 79.64  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1928 KVAVKT--LKKgstdQEKIEFL-KEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATFYgpllt 2004
Cdd:cd06659    48 QVAVKMmdLRK----QQRRELLfNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQ----- 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2005 lvdLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARDIYKNDYYRKRGEGLlPVrWMAPES 2084
Cdd:cd06659   119 ---IATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGR-----VKLSDFGFCAQISKDVPKRKSLVGT-PY-WMAPEV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2085 LMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVqtggRLEPPRNCPDD------LWNLMTQCWAQEPDQRP 2158
Cdd:cd06659   189 ISRCPYGTEVDIWSLGIMVIEMVD-GEPPYFSDSPVQAMKRL----RDSPPPKLKNShkaspvLRDFLERMLVRDPQERA 263
                         250
                  ....*....|....*..
gi 767943404 2159 TFHriqdqlQLFRNFFL 2175
Cdd:cd06659   264 TAQ------ELLDHPFL 274
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
1893-2157 1.71e-15

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 79.77  E-value: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYegTAVDIlgvGSGEiKVAVKTLKKGSTDQEKIeFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd06656    17 PKKKYTRFEKIGQGASGTVY--TAIDI---ATGQ-EVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARMatfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd06656    90 ELWVVMEYLAGGSLTDVVTETCM--------DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS-----VKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDyyRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGG-- 2130
Cdd:cd06656   157 TDFGFCAQITPEQ--SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGtp 233
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2131 RLEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd06656   234 ELQNPERLSAVFRDFLNRCLEMDVDRR 260
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
1903-2159 1.75e-15

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 78.89  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGvgsgEIKVAVKTLKK--GSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQY-II 1977
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRS----GVLYAVKEYRRrdDESKRKDYVkrLTSEYIISSKLHHPNIVKVLDLCQDLHGKWcLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKARMATFygplltlvdLVDLCV--DISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDF 2055
Cdd:cd13994    77 MEYCPGGDLFTLIEKADSLSL---------EEKDCFfkQILRGVAYLHSHGIAHRDLKPENILLDEDG-----VLKLTDF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLArDIYKN--DYYRKRGEGL---LPvrWMAPESLMDGIFT-TQSDVWSFGILIWEILTlGHQP-----------YPAHS 2118
Cdd:cd13994   143 GTA-EVFGMpaEKESPMSAGLcgsEP--YMAPEVFTSGSYDgRAVDVWSCGIVLFALFT-GRFPwrsakksdsayKAYEK 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767943404 2119 NLDVLNYVQTGGRLEPPRNCPDDLWNLMTqcwaQEPDQRPT 2159
Cdd:cd13994   219 SGDFTNGPYEPIENLLPSECRRLIYRMLH----PDPEKRIT 255
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1902-2158 1.80e-15

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 79.08  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVY----EGTAVDILGVGsgEIKVAVKTLKKGSTDQEKI--EFLKEAHLM-SKFNHPNILKQLGVCLLNEPQ 1974
Cdd:cd08528     7 LLGSGAFGCVYkvrkKSNGQTLLALK--EINMTNPAFGRTEQERDKSvgDIISEVNIIkEQLRHPNIVRYYKTFLENDRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEG---GDLLTYLRKARMatfygpLLTLVDLVDLCVDISKGCVYLERMHFI-HRDLAARNCLVSVKDYtspriV 2050
Cdd:cd08528    85 YIVMELIEGaplGEHFSSLKEKNE------HFTEDRIWNIFVQMVLALRYLHKEKQIvHRDLKPNNIMLGEDDK-----V 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLARDIYKNDYYRKRGEGLLpvRWMAPESLMDGIFTTQSDVWSFGILIWEILTLghQPyPAHS-NLDVLNYVQTG 2129
Cdd:cd08528   154 TITDFGLAKQKGPESSKMTSVVGTI--LYSCPEIVQNEPYGEKADIWALGCILYQMCTL--QP-PFYStNMLTLATKIVE 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767943404 2130 GRLEPprnCPDDLW-----NLMTQCWAQEPDQRP 2158
Cdd:cd08528   229 AEYEP---LPEGMYsdditFVIRSCLTPDPEARP 259
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
1900-2168 2.24e-15

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 78.60  E-value: 2.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1900 RLLLGSGAFGEVYegTAVDIlgvgSGEIKVAVKTLKKgsTDQEKIEFL-KEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd06624    13 RVVLGKGTFGVVY--AARDL----STQVRIAIKEIPE--RDSREVQPLhEEIALHSRLSHKNIVQYLGSVSEDGFFKIFM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRkarmaTFYGPLLTLVDLVDLCV-DISKGCVYLERMHFIHRDLAARNCLVSvkdyTSPRIVKIGDFGL 2057
Cdd:cd06624    85 EQVPGGSLSALLR-----SKWGPLKDNENTIGYYTkQILEGLKYLHDNKIVHRDIKGDNVLVN----TYSGVVKISDFGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2058 ArdiykndyyrKRGEGLLPV--------RWMAPESLMDGI--FTTQSDVWSFGILIWEILTlGHQPY----PAHSNLDVL 2123
Cdd:cd06624   156 S----------KRLAGINPCtetftgtlQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMAT-GKPPFielgEPQAAMFKV 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767943404 2124 NYVQTggRLEPPRNCPDDLWNLMTQCWAQEPDQRPTfhrIQDQLQ 2168
Cdd:cd06624   225 GMFKI--HPEIPESLSEEAKSFILRCFEPDPDKRAT---ASDLLQ 264
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1902-2159 3.88e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 77.71  E-value: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEvyegtAVDILGVGSGEiKVAVKTLK--KGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd08219     7 VVGEGSFGR-----ALLVQHVNSDQ-KYAMKEIRlpKSSSAVEDSR--KEAVLLAKMKHPNIVAFKESFEADGHLYIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLAR 2059
Cdd:cd08219    79 YCDGGDLMQKIKLQR-----GKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFL-----TQNGKVKLGDFGSAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIYKNDYYRKRGEGLlPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHqPYPAHSNLDVLNYVQTGGRLEPPRNCP 2139
Cdd:cd08219   149 LLTSPGAYACTYVGT-PY-YVPPEIWENMPYNNKSDIWSLGCILYELCTLKH-PFQANSWKNLILKVCQGSYKPLPSHYS 225
                         250       260
                  ....*....|....*....|
gi 767943404 2140 DDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd08219   226 YELRSLIKQMFKRNPRSRPS 245
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
1903-2158 5.27e-15

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 77.70  E-value: 5.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEV-----YEGTAVDI--------LGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCL 1969
Cdd:cd14067     1 LGQGGSGTViyrarYQGQPVAVkrfhikkcKKRTDGSADTMLKHLRAADAMKNFSEFRQEASMLHSLQHPCIVYLIGISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 lnEPQYIILELMEGGDLLTYLRKARMATFYGPLLTLVDLVDlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRI 2049
Cdd:cd14067    81 --HPLCFALELAPLGSLNTVLEENHKGSSFMPLGHMLTFKI-AYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDVQEHIN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKndyyrkrgEGLLPVR----WMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNY 2125
Cdd:cd14067   158 IKLSDYGISRQSFH--------EGALGVEgtpgYQAPEIRPRIVYDEKVDMFSYGMVLYELLS-GQRPSLGHHQLQIAKK 228
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2126 VQTGGRlePPRNCPDD-----LWNLMTQCWAQEPDQRP 2158
Cdd:cd14067   229 LSKGIR--PVLGQPEEvqffrLQALMMECWDTKPEKRP 264
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
1903-2108 6.03e-15

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 77.60  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAvktLKKGSTDQEKIEF----LKEAHLMSKFNHPNILKQLGVCLLNEPQ---- 1974
Cdd:cd07840     7 IGEGTYGQVYKARNKK-----TGEL-VA---LKKIRMENEKEGFpitaIREIKLLQKLDHPNVVRLKEIVTSKGSAkykg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 --YIILELMEGgDLLTYLRKarmatfygPLLTLVDLVDLCV--DISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriV 2050
Cdd:cd07840    78 siYMVFEYMDH-DLTGLLDN--------PEVKFTESQIKCYmkQLLEGLQYLHSNGILHRDIKGSNILINNDGV-----L 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2051 KIGDFGLARdiykndYYRKRGEGLLPVR----WM-APESLM-DGIFTTQSDVWSFGILIWEILT 2108
Cdd:cd07840   144 KLADFGLAR------PYTKENNADYTNRvitlWYrPPELLLgATRYGPEVDMWSVGCILAELFT 201
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
1903-2159 6.35e-15

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 77.39  E-value: 6.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDIlgvgSGEIKVAVKTLKK------GSTDQEKIEFLKEAHLMSKF-NHPNILKQLGVCLLNEPQY 1975
Cdd:cd13993     8 IGEGAYGVVY--LAVDL----RTGRKYAIKCLYKsgpnskDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMAtfygpLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTspriVKIGDF 2055
Cdd:cd13993    82 IVLEYCPNGDLFEAITENRIY-----VGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT----VKLCDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDiykNDYYRKRGEGLLpvRWMAPESLMD------GIFTTQSDVWSFGILIWEiLTLGHQPY-PAHSNLDVLNYVQT 2128
Cdd:cd13993   153 GLATT---EKISMDFGVGSE--FYMAPECFDEvgrslkGYPCAAGDIWSLGIILLN-LTFGRNPWkIASESDPIFYDYYL 226
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2129 GG----RLEPPRNcpDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd13993   227 NSpnlfDVILPMS--DDFYNLLRQIFTVNPNNRIL 259
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
1903-2168 8.88e-15

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 77.31  E-value: 8.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdiLGVGSGEiKVAVKTLKkgSTDQEkiEFLKEAHLMSK--FNHPNILKQLG---VCLLNEPQYI- 1976
Cdd:cd14056     3 IGKGRYGEVW-------LGKYRGE-KVAVKIFS--SRDED--SWFRETEIYQTvmLRHENILGFIAadiKSTGSWTQLWl 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKA--------RMATfygplltlvdlvdlcvdisKGCVYLERMH-----------FIHRDLAARNC 2037
Cdd:cd14056    71 ITEYHEHGSLYDYLQRNtldteealRLAY-------------------SAASGLAHLHteivgtqgkpaIAHRDLKSKNI 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2038 LVSvKDYTSPrivkIGDFGLARDiykndYYRKRGEGLLPV-------RWMAPESLMDGIFTT------QSDVWSFGILIW 2104
Cdd:cd14056   132 LVK-RDGTCC----IADLGLAVR-----YDSDTNTIDIPPnprvgtkRYMAPEVLDDSINPKsfesfkMADIYSFGLVLW 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2105 EILTLG---------HQPY----PAHSNLDVLNYVQTGGRLEPPrncPDDLWN----------LMTQCWAQEPDQRPTFH 2161
Cdd:cd14056   202 EIARRCeiggiaeeyQLPYfgmvPSDPSFEEMRKVVCVEKLRPP---IPNRWKsdpvlrsmvkLMQECWSENPHARLTAL 278

                  ....*..
gi 767943404 2162 RIQDQLQ 2168
Cdd:cd14056   279 RVKKTLA 285
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
1898-2165 9.07e-15

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 76.61  E-value: 9.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1898 TLRLLLGSGAFGEVYegtavdiLGVGS-GEIKVAVKTLKKGSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd14075     5 RIRGELGSGNFSQVK-------LGIHQlTKEKVAIKILDKTKLDQKTQRLLsREISSMEKLHHPNIIRLYEVVETLSKLH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKArmatfyGPLLTLVDLVDlcvdISKGCVYLERMH---FIHRDLAARNCLvsvkdYTSPRIVKI 2052
Cdd:cd14075    78 LVMEYASGGELYTKISTE------GKLSESEAKPL----FAQIVSAVKHMHennIIHRDLKAENVF-----YASNNCVKV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARdiykndyYRKRGE------GLLPvrWMAPESLMD----GIFTtqsDVWSFGILIWEILTlGHQPYPAhSNLDV 2122
Cdd:cd14075   143 GDFGFST-------HAKRGEtlntfcGSPP--YAAPELFKDehyiGIYV---DIWALGVLLYFMVT-GVMPFRA-ETVAK 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2123 LNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd14075   209 LKKCILEGTYTIPSYVSEPCQELIRGILQPVPSDRYSIDEIKN 251
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
1902-2168 9.72e-15

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 77.40  E-value: 9.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAvdilgvgsGEIKVAVKTLKKGSTDQekieFLKEAHLMSKF--NHPNILKQLGVC------LLNEP 1973
Cdd:cd14054     2 LIGQGRYGTVWKGSL--------DERPVAVKVFPARHRQN----FQNEKDIYELPlmEHSNILRFIGADerptadGRMEY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QyIILELMEGGDLLTYLRK--------ARMatfygplltlvdlvdlCVDISKGCVYL-ERMH--------FIHRDLAARN 2036
Cdd:cd14054    70 L-LVLEYAPKGSLCSYLREntldwmssCRM----------------ALSLTRGLAYLhTDLRrgdqykpaIAHRDLNSRN 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2037 CLVSVkDYTspriVKIGDFGLARDIYKNDYYRKR---GEGLLP-----VRWMAPEsLMDGI--------FTTQSDVWSFG 2100
Cdd:cd14054   133 VLVKA-DGS----CVICDFGLAMVLRGSSLVRGRpgaAENASIsevgtLRYMAPE-VLEGAvnlrdcesALKQVDVYALG 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2101 ILIWEILTL-----------GHQ-PYPA----HSNLDVLNYVQTGGRLEP------PRNCP--DDLWNLMTQCWAQEPDQ 2156
Cdd:cd14054   207 LVLWEIAMRcsdlypgesvpPYQmPYEAelgnHPTFEDMQLLVSREKARPkfpdawKENSLavRSLKETIEDCWDQDAEA 286
                         330
                  ....*....|..
gi 767943404 2157 RPTFHRIQDQLQ 2168
Cdd:cd14054   287 RLTALCVEERLA 298
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
1893-2157 9.99e-15

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 77.46  E-value: 9.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYegTAVDIlGVGSgeiKVAVKTLKKGSTDQEKIeFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd06655    17 PKKKYTRYEKIGQGASGTVF--TAIDV-ATGQ---EVAIKQINLQKQPKKEL-IINEILVMKELKNPNIVNFLDSFLVGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLL-----TYLRKARMATFygplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtsp 2047
Cdd:cd06655    90 ELFVVMEYLAGGSLTdvvteTCMDEAQIAAV-------------CRECLQALEFLHANQVIHRDIKSDNVLLGMDGS--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 riVKIGDFGLARDIYKNDyyRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQ 2127
Cdd:cd06655   154 --VKLTDFGFCAQITPEQ--SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIA 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767943404 2128 TGG--RLEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd06655   229 TNGtpELQNPEKLSPIFRDFLNRCLEMDVEKR 260
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
1902-2168 1.05e-14

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 76.69  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegTAVDILGVGSgeiKVAVKTLKK---GSTDQEK----IEFLKEahlMSKFNHPNILKQLGVCLLNEPQ 1974
Cdd:cd14052     7 LIGSGEFSQVY--KVSERVPTGK---VYAVKKLKPnyaGAKDRLRrleeVSILRE---LTLDGHDNIVQLIDSWEYHGHL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYL----RKARMATFygplltlvDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIV 2050
Cdd:cd14052    79 YIQTELCENGSLDVFLselgLLGRLDEF--------RVWKILVELSLGLRFIHDHHFVHLDLKPANVLI-----TFEGTL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLA------RDIykndyyrkRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILT---LGHQPYPAH---- 2117
Cdd:cd14052   146 KIGDFGMAtvwpliRGI--------EREG--DREYIAPEILSEHMYDKPADIFSLGLILLEAAAnvvLPDNGDAWQklrs 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2118 ---SNLDVLNYVQTGGRLEPPRNCPDDLWNL-------------MTQCwaqEPDQRPTfhrIQDQLQ 2168
Cdd:cd14052   216 gdlSDAPRLSSTDLHSASSPSSNPPPDPPNMpilsgsldrvvrwMLSP---EPDRRPT---ADDVLA 276
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
1893-2157 1.06e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 77.07  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYegTAVDilgVGSGEiKVAVKTLKKGSTDQEKIeFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd06654    18 PKKKYTRFEKIGQGASGTVY--TAMD---VATGQ-EVAIRQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKARMatfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd06654    91 ELWVVMEYLAGGSLTDVVTETCM--------DEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGS-----VKL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDyyRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGG-- 2130
Cdd:cd06654   158 TDFGFCAQITPEQ--SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNGtp 234
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2131 RLEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd06654   235 ELQNPEKLSAIFRDFLNRCLEMDVEKR 261
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
1902-2167 1.28e-14

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 76.14  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdilgVGSGEiKVAVKTLKKGSTDQEkieFLKEAHLMSKFNHPNILKQLGVCLlnEPQYIILELM 1981
Cdd:cd14068     1 LLGDGGFGSVYRA-------VYRGE-DVAVKIFNKHTSFRL---LRQELVVLSHLHHPSLVALLAAGT--APRMLVMELA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMAtfygplLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIVKIGDFGLARdi 2061
Cdd:cd14068    68 PKGSLDALLQQDNAS------LTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIAKIADYGIAQ-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGLLPVRwmAPE-SLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPP---RN 2137
Cdd:cd14068   140 YCCRMGIKTSEGTPGFR--APEvARGNVIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQGKLPDPvkeYG 217
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767943404 2138 CP--DDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14068   218 CApwPGVEALIKDCLKENPQCRPTSAQVFDIL 249
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
1902-2159 1.36e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 76.84  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVDILgvgSGEIkVAVKTLKKG--STDQEKIEF--LKEAHLMSKFNHPNILKQLGVCLLNEPQYII 1977
Cdd:cd07841     7 KLGEGTYAVVYK--ARDKE---TGRI-VAIKKIKLGerKEAKDGINFtaLREIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGgDLLTYLRkaRMATFYGPLltlvdlvdlcvDIS-------KGCVYLERMHFIHRDLAARNCLVSVKDytsprIV 2050
Cdd:cd07841    81 FEFMET-DLEKVIK--DKSIVLTPA-----------DIKsymlmtlRGLEYLHSNWILHRDLKPNNLLIASDG-----VL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLARDI-YKNDYYRKRgeglLPVRWM-APESLMdG--IFTTQSDVWSFGILIWEILTlgHQPY-PAHSNLDVL-- 2123
Cdd:cd07841   142 KLADFGLARSFgSPNRKMTHQ----VVTRWYrAPELLF-GarHYGVGVDMWSVGCIFAELLL--RVPFlPGDSDIDQLgk 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2124 --------------------NYVQTGGRLEPPR-----NCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd07841   215 ifealgtpteenwpgvtslpDYVEFKPFPPTPLkqifpAASDDALDLLQRLLTLNPNKRIT 275
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
1903-2127 1.73e-14

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 75.99  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgsGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14664     1 IGRGGAGTVYKGVMPN------GTL-VAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMAtfyGPLLTLVDLVDLCVDISKGCVYLER---MHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLAR 2059
Cdd:cd14664    74 NGSLGELLHSRPES---QPPLDWETRQRIALGSARGLAYLHHdcsPLIIHRDVKSNNILLD-----EEFEAHVADFGLAK 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2060 DIykNDyyrKRGEGLLPVR----WMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQ 2127
Cdd:cd14664   146 LM--DD---KDSHVMSSVAgsygYIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFDEAFLDDGVDIVD 211
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1941-2163 1.93e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 75.62  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1941 QEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATFygpllTLVDLVDLCVDIskgCV 2020
Cdd:cd08218    41 KEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLYKRINAQRGVLF-----PEDQILDWFVQL---CL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2021 YLERMH---FIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARdIYKNDYYRKRGEGLLPVrWMAPESLMDGIFTTQSDVW 2097
Cdd:cd08218   113 ALKHVHdrkILHRDIKSQNIFL-----TKDGIIKLGDFGIAR-VLNSTVELARTCIGTPY-YLSPEICENKPYNNKSDIW 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2098 SFGILIWEILTLGHqPYPAHS--NLdVLNYVQtgGRLEP-PRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd08218   186 ALGCVLYEMCTLKH-AFEAGNmkNL-VLKIIR--GSYPPvPSRYSYDLRSLVSQLFKRNPRDRPSINSI 250
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
1921-2167 4.30e-14

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 74.89  E-value: 4.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1921 GVGSGEIkVAVKTLKKGSTDQEKIeFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATFYG 2000
Cdd:cd14045    26 GIYDGRT-VAIKKIAKKSFTLSKR-IRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDIPLNWG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2001 plltlvDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKdytspRIVKIGDFGLArdIYKND-------YYRKRgeg 2073
Cdd:cd14045   104 ------FRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDR-----WVCKIADYGLT--TYRKEdgsenasGYQQR--- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2074 LLPVrWMAPE--SLMDGIFTTQSDVWSFGILIWEILTLgHQPYPAHSN---------LDVLnyvqTGGRLEPPRNCPDDL 2142
Cdd:cd14045   168 LMQV-YLPPEnhSNTDTEPTQATDVYSYAIILLEIATR-NDPVPEDDYsldeawcppLPEL----ISGKTENSCPCPADY 241
                         250       260
                  ....*....|....*....|....*
gi 767943404 2143 WNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14045   242 VELIRRCRKNNPAQRPTFEQIKKTL 266
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
1903-2126 4.40e-14

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 74.23  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVdilgvGSGeIKVAVKTLKKGSTDQEKIefLKEAHLMSKFNHPNILkQLGVCLLNEPQYI-ILELM 1981
Cdd:cd14006     1 LGRGRFGVVKRCIEK-----ATG-REFAAKFIPKRDKKKEAV--LREISILNQLQHPRII-QLHEAYESPTELVlILELC 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRK-----ARMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSvkDYTSPRIvKIGDFG 2056
Cdd:cd14006    72 SGGELLDRLAErgslsEEEVRTY------------MRQLLEGLQYLHNHHILHLDLKPENILLA--DRPSPQI-KIIDFG 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARDIYKNDYYRKRGEGLlpvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd14006   137 LARKLNPGEELKEIFGTP---EFVAPEIVNGEPVSLATDMWSIGVLTYVLLS-GLSPFLGEDDQETLANI 202
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
1926-2159 6.27e-14

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 74.67  E-value: 6.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1926 EIKVAVKTLKKGSTD-QEKIEFLkeahlMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTylRKARMATFygplLT 2004
Cdd:cd14178    28 STEYAVKIIDKSKRDpSEEIEIL-----LRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELLD--RILRQKCF----SE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2005 LVDLVDLCVdISKGCVYLERMHFIHRDLAARNCLVsVKDYTSPRIVKIGDFGLARDIykndyyrKRGEGLL-----PVRW 2079
Cdd:cd14178    97 REASAVLCT-ITKTVEYLHSQGVVHRDLKPSNILY-MDESGNPESIRICDFGFAKQL-------RAENGLLmtpcyTANF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2080 MAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY---PAHSNLDVL------NYVQTGGRLEPPRNCPDDLWNLMTQCw 2150
Cdd:cd14178   168 VAPEVLKRQGYDAACDIWSLGILLYTMLA-GFTPFangPDDTPEEILarigsgKYALSGGNWDSISDAAKDIVSKMLHV- 245

                  ....*....
gi 767943404 2151 aqEPDQRPT 2159
Cdd:cd14178   246 --DPHQRLT 252
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
1902-2169 7.33e-14

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 74.25  E-value: 7.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtavdILGVGSGEIkVAVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ-----YI 1976
Cdd:cd13986     7 LLGEGGFSFVYL-----VEDLSTGRL-YALKKILCHSKEDVK-EAMREIENYRLFNHPNILRLLDSQIVKEAGgkkevYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKARMATFYGPlltlvdlVDLCVDISKG-CVYLERMH------FIHRDLAARNCLVSvkdyTSPRI 2049
Cdd:cd13986    80 LLPYYKRGSLQDEIERRLVKGTFFP-------EDRILHIFLGiCRGLKAMHepelvpYAHRDIKPGNVLLS----EDDEP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VkIGDFGLARDIYKNDYYRKRGEGL---------LPVRwmAPE---SLMDGIFTTQSDVWSFGILIWEILtLGHQPY-PA 2116
Cdd:cd13986   149 I-LMDLGSMNPARIEIEGRREALALqdwaaehctMPYR--APElfdVKSHCTIDEKTDIWSLGCTLYALM-YGESPFeRI 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2117 HSNLDVLNYVQTGGRLEPPRNC--PDDLWNLMTQCWAQEPDQRPTFHRIQDQLQL 2169
Cdd:cd13986   225 FQKGDSLALAVLSGNYSFPDNSrySEELHQLVKSMLVVNPAERPSIDDLLSRVHD 279
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1895-2166 8.17e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 74.14  E-value: 8.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEGtavdiLGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ 1974
Cdd:cd06619     1 QDIQYQEILGHGNGGTVYKA-----YHLLTRRI-LAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRK-----ARMAtfygplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspri 2049
Cdd:cd06619    75 SICTEFMDGGSLDVYRKIpehvlGRIA----------------VAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQ----- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKNDYYRKRGEGllpvRWMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYPA----HSNLDVLNY 2125
Cdd:cd06619   134 VKLCDFGVSTQLVNSIAKTYVGTN----AYMAPERISGEQYGIHSDVWSLGISFME-LALGRFPYPQiqknQGSLMPLQL 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767943404 2126 VQTGGRLEPPRnCPDDLW-----NLMTQCWAQEPDQRPTFHRIQDQ 2166
Cdd:cd06619   209 LQCIVDEDPPV-LPVGQFsekfvHFITQCMRKQPKERPAPENLMDH 253
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
1930-2163 8.30e-14

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 74.21  E-value: 8.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1930 AVKTLKKGSTD-QEKIEFLkeahlMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTY-LRK---------ARMATf 1998
Cdd:cd14091    29 AVKIIDKSKRDpSEEIEIL-----LRYGQHPNIITLRDVYDDGNSVYLVTELLRGGELLDRiLRQkffsereasAVMKT- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1999 ygplltlvdlvdlcvdISKGCVYLERMHFIHRDLAARNCLVSvKDYTSPRIVKIGDFGLARDIykndyyrkRGE-GLL-- 2075
Cdd:cd14091   103 ----------------LTKTVEYLHSQGVVHRDLKPSNILYA-DESGDPESLRICDFGFAKQL--------RAEnGLLmt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2076 P---VRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY---PAHSNLDVL------NYVQTGGRLEpprNCPDDLW 2143
Cdd:cd14091   158 PcytANFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPFasgPNDTPEVILarigsgKIDLSGGNWD---HVSDSAK 233
                         250       260
                  ....*....|....*....|
gi 767943404 2144 NLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14091   234 DLVRKMLHVDPSQRPTAAQV 253
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1903-2165 8.77e-14

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 74.30  E-value: 8.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVdILGVGSGEIKVAVKTLKKGSTDQEKIeflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd08229    32 IGRGQFSEVYRATCL-LDGVPVALKKVQIFDLMDAKARADCI---KEIDLLKQLNHPNVIKYYASFIEDNELNIVLELAD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLltylrkARMATFYGPLLTLVDLVDLCVDISKGCVYLERMH---FIHRDLAARNCLVsvkdyTSPRIVKIGDFGLAR 2059
Cdd:cd08229   108 AGDL------SRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHsrrVMHRDIKPANVFI-----TATGVVKLGDLGLGR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 dIYKNDYYRKRGEGLLPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVL--NYVQTGGRLEPPRN 2137
Cdd:cd08229   177 -FFSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLckKIEQCDYPPLPSDH 254
                         250       260
                  ....*....|....*....|....*...
gi 767943404 2138 CPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd08229   255 YSEELRQLVNMCINPDPEKRPDITYVYD 282
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
1906-2172 9.07e-14

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 74.29  E-value: 9.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1906 GAFGEVYEGTAVDILgvgsgeikVAVKTLKKgstdQEKIEFLKEAHLMS--KFNHPNILKQLG---VCLLNEPQY-IILE 1979
Cdd:cd14053     6 GRFGAVWKAQYLNRL--------VAVKIFPL----QEKQSWLTEREIYSlpGMKHENILQFIGaekHGESLEAEYwLITE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLrKARMATFygplltlVDLVDLCVDISKGCVYL--ERMHF--------IHRDLAARNCLVSvKDYTspri 2049
Cdd:cd14053    74 FHERGSLCDYL-KGNVISW-------NELCKIAESMARGLAYLheDIPATngghkpsiAHRDFKSKNVLLK-SDLT---- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARdiyKNDYYRKRGEGLLPV---RWMAPESLMDGI-FTTQS----DVWSFGILIWEILT--LGHQ------- 2112
Cdd:cd14053   141 ACIADFGLAL---KFEPGKSCGDTHGQVgtrRYMAPEVLEGAInFTRDAflriDMYAMGLVLWELLSrcSVHDgpvdeyq 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2113 -PYPA----HSNL-DVLNYVQTggRLEPPRNCPD--------DLWNLMTQCWAQEPDQRPTFHRIQDQLQLFRN 2172
Cdd:cd14053   218 lPFEEevgqHPTLeDMQECVVH--KKLRPQIRDEwrkhpglaQLCETIEECWDHDAEARLSAGCVEERLSQLSR 289
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
1903-2118 9.35e-14

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 74.36  E-value: 9.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdILGVGSGEIKVAVKTLkkgstDQEKIEFLKE-AHLMskfNHPNILKQLGVCLL---------NE 1972
Cdd:cd14209     9 LGTGSFGRVM------LVRHKETGNYYAMKIL-----DKQKVVKLKQvEHTL---NEKRILQAINFPFLvkleysfkdNS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKAR-----MATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtsp 2047
Cdd:cd14209    75 NLYMVMEYVPGGEMFSHLRRIGrfsepHARFYA------------AQIVLAFEYLHSLDLIYRDLKPENLLIDQQGY--- 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2048 riVKIGDFGLARDIykndyyRKRGEGLLPV-RWMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYPAHS 2118
Cdd:cd14209   140 --IKVTDFGFAKRV------KGRTWTLCGTpEYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQ 202
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
1903-2163 9.53e-14

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 74.00  E-value: 9.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVyegTAVDILGvgSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ--YIILEL 1980
Cdd:cd06621     9 LGEGAGGSV---TKCRLRN--TKTI-FALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEQDSsiGIAMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARMAtfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFG---- 2056
Cdd:cd06621    83 CEGGSLDSIYKKVKKK---GGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ-----VKLCDFGvsge 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 ----LARDIYKNDYYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEIlTLGHQPYPAHSN-----LDVLNYVQ 2127
Cdd:cd06621   155 lvnsLAGTFTGTSYY------------MAPERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFPPEGEpplgpIELLSYIV 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2128 TGGRLEPPrNCPDD--LWN-----LMTQCWAQEPDQRPTFHRI 2163
Cdd:cd06621   222 NMPNPELK-DEPENgiKWSesfkdFIEKCLEKDGTRRPGPWQM 263
PHA02988 PHA02988
hypothetical protein; Provisional
1928-2174 9.79e-14

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 74.01  E-value: 9.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1928 KVAVKTLKKGSTDQEKI--EFLKEAHLMSKFNHPNILKQLG--VCLLNEPQY--IILELMEGGDLLTYLRKARMATFYgp 2001
Cdd:PHA02988   45 EVIIRTFKKFHKGHKVLidITENEIKNLRRIDSNNILKIYGfiIDIVDDLPRlsLILEYCTRGYLREVLDKEKDLSFK-- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2002 lltlvDLVDLCVDISKGcvyLERMHFI----HRDLAARNCLVSvKDYTspriVKIGDFGLARdIYKNDYYRKrgegllpV 2077
Cdd:PHA02988  123 -----TKLDMAIDCCKG---LYNLYKYtnkpYKNLTSVSFLVT-ENYK----LKIICHGLEK-ILSSPPFKN-------V 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2078 RWMA--PESLMDGIF---TTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLN-YVQTGGRLEPPRNCPDDLWNLMTQCWA 2151
Cdd:PHA02988  182 NFMVyfSYKMLNDIFseyTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDlIINKNNSLKLPLDCPLEIKCIVEACTS 260
                         250       260
                  ....*....|....*....|...
gi 767943404 2152 QEPDQRPTFHRIQDQLQLFRNFF 2174
Cdd:PHA02988  261 HDSIKRPNIKEILYNLSLYKFYI 283
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
1903-2123 1.14e-13

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 74.80  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEIkVAVKTLK--KGSTDQEK---------IEF--LKEAHLMSKFNHPNILKQLGVCL 1969
Cdd:PTZ00024   17 LGEGTYGKVEK--AYDTL---TGKI-VAIKKVKiiEISNDVTKdrqlvgmcgIHFttLRELKIMNEIKHENIMGLVDVYV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 LNEPQYIILELMEGgDLLTYL-RKARMATFYgplltlvdlvDLCV--DISKGCVYLERMHFIHRDLAARNCLVSVKDyts 2046
Cdd:PTZ00024   91 EGDFINLVMDIMAS-DLKKVVdRKIRLTESQ----------VKCIllQILNGLNVLHKWYFMHRDLSPANIFINSKG--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2047 prIVKIGDFGLAR--------DIYKNDYYRKRGEGLLP----VRWMAPESLMDGIFTTQS-DVWSFGILIWEILTlGHQP 2113
Cdd:PTZ00024  157 --ICKIADFGLARrygyppysDTLSKDETMQRREEMTSkvvtLWYRAPELLMGAEKYHFAvDMWSVGCIFAELLT-GKPL 233
                         250
                  ....*....|
gi 767943404 2114 YPAHSNLDVL 2123
Cdd:PTZ00024  234 FPGENEIDQL 243
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
1902-2168 1.26e-13

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 73.50  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTavdilgvGSGEIKVAVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14153     7 LIGKGRFGQVYHGR-------WHGEVAIRLIDIERDNEEQLK-AFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMAtfygplLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPRIVkIGDFGL---- 2057
Cdd:cd14153    79 KGRTLYSVVRDAKVV------LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-----YDNGKVV-ITDFGLftis 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2058 --ARDIYKNDYYRKRGEGLLP-----VRWMAPESLMDGI-FTTQSDVWSFGIlIWEILTLGHQPYPAHSNLDVLnyVQTG 2129
Cdd:cd14153   147 gvLQAGRREDKLRIQSGWLCHlapeiIRQLSPETEEDKLpFSKHSDVFAFGT-IWYELHAREWPFKTQPAEAII--WQVG 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2130 GRLEPPRN---CPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14153   224 SGMKPNLSqigMGKEISDILLFCWAYEQEERPTFSKLMEMLE 265
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
1903-2124 1.27e-13

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 74.36  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDILGVGSGEIkVAVKTLKKGSTD-QEKIEFLKEAHLMSKFNHPNILKqLGVCLLNEPQ-YIILEL 1980
Cdd:cd05582     3 LGQGSFGKVF--LVRKITGPDAGTL-YAMKVLKKATLKvRDRVRTKMERDILADVNHPFIVK-LHYAFQTEGKlYLILDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARMAT-----FYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDF 2055
Cdd:cd05582    79 LRGGDLFTRLSKEVMFTeedvkFY------------LAELALALDHLHSLGIIYRDLKPENILLDEDGH-----IKLTDF 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDIYKNDyyrKRGEGLL-PVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLN 2124
Cdd:cd05582   142 GLSKESIDHE---KKAYSFCgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMT 207
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
1902-2124 1.86e-13

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 74.10  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVDILgvgSGEiKVAVKtlKKGSTDQEKIE---FLKEAHLMSKFNHPNILKqlgvcLLN--EPQ-- 1974
Cdd:cd07834     7 PIGSGAYGVVCS--AYDKR---TGR-KVAIK--KISNVFDDLIDakrILREIKILRHLKHENIIG-----LLDilRPPsp 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 ------YIILELMEGgDLLT------YLRKARMATF-YgplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSv 2041
Cdd:cd07834    74 eefndvYIVTELMET-DLHKvikspqPLTDDHIQYFlY--------------QILRGLKYLHSAGVIHRDLKPSNILVN- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2042 KDYTspriVKIGDFGLARDIYKND------------YYRkrgegllpvrwmAPESLMDGI-FTTQSDVWSFGILIWEILT 2108
Cdd:cd07834   138 SNCD----LKICDFGLARGVDPDEdkgflteyvvtrWYR------------APELLLSSKkYTKAIDIWSVGCIFAELLT 201
                         250
                  ....*....|....*..
gi 767943404 2109 lgHQP-YPAHSNLDVLN 2124
Cdd:cd07834   202 --RKPlFPGRDYIDQLN 216
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1903-2107 1.90e-13

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 73.24  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILGVGSgeiKVAVKTLKKGSTDQ------EKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd14096     9 IGEGAFSNVYK--AVPLRNTGK---PVAIKVVRKADLSSdnlkgsSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDL------LTYLRKArmatfygplltlvDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPR-- 2048
Cdd:cd14096    84 VLELADGGEIfhqivrLTYFSED-------------LSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPIPFIPSIvk 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 --------------------------IVKIGDFGLARDIYKNDYYRKRGEgllpVRWMAPESLMDGIFTTQSDVWSFGIL 2102
Cdd:cd14096   151 lrkadddetkvdegefipgvggggigIVKLADFGLSKQVWDSNTKTPCGT----VGYTAPEVVKDERYSKKVDMWALGCV 226

                  ....*
gi 767943404 2103 IWEIL 2107
Cdd:cd14096   227 LYTLL 231
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
1902-2123 2.33e-13

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 72.92  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKtlkkgSTDQEKiEFL-KEAHLMSKFNHPNILKQLGVCLLNEP------Q 1974
Cdd:cd14137    11 VIGSGSFGVVYQAKLLE-----TGEV-VAIK-----KVLQDK-RYKnRELQIMRRLKHPNIVKLKYFFYSSGEkkdevyL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGgDLLTYLR-----KARMATFYgplltlvdlvdlcV-----DISKGCVYLERMHFIHRDLAARNCLVSVKDY 2044
Cdd:cd14137    79 NLVMEYMPE-TLYRVIRhysknKQTIPIIY-------------VklysyQLFRGLAYLHSLGICHRDIKPQNLLVDPETG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2045 tsprIVKIGDFGLARDIYKND---------YYRkrgegllpvrwmAPEsLMDGI--FTTQSDVWSFGILIWEILtLGHQP 2113
Cdd:cd14137   145 ----VLKLCDFGSAKRLVPGEpnvsyicsrYYR------------APE-LIFGAtdYTTAIDIWSAGCVLAELL-LGQPL 206
                         250
                  ....*....|
gi 767943404 2114 YPAHSNLDVL 2123
Cdd:cd14137   207 FPGESSVDQL 216
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
1903-2163 2.51e-13

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 72.29  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDilgvGSGEIkVAVKTLKKGST--DQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd14161    11 LGKGTYGRVKK--ARD----SSGRL-VAIKSIRKDRIkdEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYL-RKARMAtfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLAr 2059
Cdd:cd14161    84 ASRGDLYDYIsERQRLS--------ELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN-----IKIADFGLS- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIYKNDYYRKRGEGlLPVrWMAPESLMDGIFT-TQSDVWSFGILIWeILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRnc 2138
Cdd:cd14161   150 NLYNQDKFLQTYCG-SPL-YASPEIVNGRPYIgPEVDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGAYREPTK-- 224
                         250       260
                  ....*....|....*....|....*
gi 767943404 2139 PDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14161   225 PSDACGLIRWLLMVNPERRATLEDV 249
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
1903-2158 2.97e-13

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 72.16  E-value: 2.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGtavdiLGVGSGEiKVAVKTLKKGSTDQEKI---EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd14070    10 LGEGSFAKVREG-----LHAVTGE-KVAIKVIDKKKAKKDSYvtkNLRREGRIQQMIRHPNITQLLDILETENSYYLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYL-RKARMAtfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLA 2058
Cdd:cd14070    84 LCPGGNLMHRIyDKKRLE--------EREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN-----IKLIDFGLS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDI----YKNDYYRKRGEgllPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHS-NLDVLNYVQTGGRLE 2133
Cdd:cd14070   151 NCAgilgYSDPFSTQCGS---PA-YAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTVEPfSLRALHQKMVDKEMN 225
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2134 P-PRNCPDDLWNLMTQCWAQEPDQRP 2158
Cdd:cd14070   226 PlPTDLSPGAISFLRSLLEPDPLKRP 251
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1903-2119 3.15e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 72.48  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVyegtaVDILGVGSGEiKVAVKTLKK--GSTDQEKIEFLKEAHLMSKFNHPNILK------QLGVCLLNEPQ 1974
Cdd:cd13989     1 LGSGGFGYV-----TLWKHQDTGE-YVAIKKCRQelSPSDKNRERWCLEVQIMKKLNHPNVVSardvppELEKLSPNDLP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRKARMATFYGPLLTLVDLVdlcvDISKGCVYLERMHFIHRDLAARNclVSVKDYTSPRIVKIGD 2054
Cdd:cd13989    75 LLAMEYCSGGDLRKVLNQPENCCGLKESEVRTLLS----DISSAISYLHENRIIHRDLKPEN--IVLQQGGGRVIYKLID 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2055 FGLARDIyknDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSN 2119
Cdd:cd13989   149 LGYAKEL---DQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPFLPNWQ 209
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
1929-2163 3.60e-13

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 71.94  E-value: 3.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGstdqEKIEFLKEAHLMSKFNHPNILK---------QLgvcllnepqYIILELMEGGDLLTYLRKAR----- 1994
Cdd:cd14010    28 VAIKCVDKS----KRPEVLNEVRLTHELKHPNVLKfyewyetsnHL---------WLVVEYCTGGDLETLLRQDGnlpes 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1995 -MATFygplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLAR-------------- 2059
Cdd:cd14010    95 sVRKF-------------GRDLVRGLHYIHSKGIIYCDLKPSNILLD-----GNGTLKLSDFGLARregeilkelfgqfs 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 --DIYKNDYYRKRGEGLlPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGgrlEPPR- 2136
Cdd:cd14010   157 deGNVNKVSKKQAKRGT-PY-YMAPELFQGGVHSFASDLWALGCVLYEMFT-GKPPFVAESFTELVEKILNE---DPPPp 230
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767943404 2137 ------NCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14010   231 ppkvssKPSPDFKSLLKGLLEKDPAKRLSWDEL 263
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
1903-2148 3.71e-13

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 71.97  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVyegtavdILGV--GSGEiKVAVKTLKKGSTDQEkiEFLKEAHL-MSKFNHPNILKQLGVCLLNEPQYIIL- 1978
Cdd:cd13987     1 LGEGTYGKV-------LLAVhkGSGT-KMALKFVPKPSTKLK--DFLREYNIsLELSVHPHIIKTYDVAFETEDYYVFAq 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLrkarmatfyGPLLTLVDlvdlcvDISKGCVY-----LERMH---FIHRDLAARNCLVSVKDYtspRIV 2050
Cdd:cd13987    71 EYAPYGDLFSII---------PPQVGLPE------ERVKRCAAqlasaLDFMHsknLVHRDIKPENVLLFDKDC---RRV 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLARdiyKNDYYRKRGEGLLPvrWMAPE----SLMDGIFTTQS-DVWSFGILIWEILTlGHQPYPAHSNLD--VL 2123
Cdd:cd13987   133 KLCDFGLTR---RVGSTVKRVSGTIP--YTAPEvceaKKNEGFVVDPSiDVWAFGVLLFCCLT-GNFPWEKADSDDqfYE 206
                         250       260
                  ....*....|....*....|....*
gi 767943404 2124 NYVQTGGRLEPprnCPDDLWNLMTQ 2148
Cdd:cd13987   207 EFVRWQKRKNT---AVPSQWRRFTP 228
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
1903-2162 4.38e-13

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 71.92  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFN-HPNILkQLGVCLLNEPQ---YIIL 1978
Cdd:cd07831     7 IGEGTFSEVLKAQSRK-----TGKY-YAIKCMKKHFKSLEQVNNLREIQALRRLSpHPNIL-RLIEVLFDRKTgrlALVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGG--DLL----TYLRKARMATFygplltlvdlvdlcvdISKGCVYLERMH---FIHRDLAARNCLVsvKDYtsprI 2049
Cdd:cd07831    80 ELMDMNlyELIkgrkRPLPEKRVKNY----------------MYQLLKSLDHMHrngIFHRDIKPENILI--KDD----I 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKNDYYRKrgegLLPVRWM-APESLM-DGIFTTQSDVWSFGILIWEILTLghQP-YPAHSNLD----- 2121
Cdd:cd07831   138 LKLADFGSCRGIYSKPPYTE----YISTRWYrAPECLLtDGYYGPKMDIWAVGCVFFEILSL--FPlFPGTNELDqiaki 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2122 ----------VLNYVQTGGRLE---PPR----------NCPDDLWNLMTQCWAQEPDQRPTFHR 2162
Cdd:cd07831   212 hdvlgtpdaeVLKKFRKSRHMNynfPSKkgtglrkllpNASAEGLDLLKKLLAYDPDERITAKQ 275
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
1927-2163 4.46e-13

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 71.52  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1927 IKVAVKTLKKGSTDQEKIEFLKEAHLmskfNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKArmATFYGPLLTLV 2006
Cdd:cd14185    30 MKIIDKSKLKGKEDMIESEILIIKSL----SHPNIVKLFEVYETEKEIYLILEYVRGGDLFDAIIES--VKFTEHDAALM 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2007 DlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTSPRIVKIGDFGLARDIYKndyyrkrgegllPV-------RW 2079
Cdd:cd14185   104 I-----IDLCEALVYIHSKHIVHRDLKPENLLVQ-HNPDKSTTLKLADFGLAKYVTG------------PIftvcgtpTY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2080 MAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPY--PAHSNLDVLNYVQTGG-RLEPP--RNCPDDLWNLMTQCWAQEP 2154
Cdd:cd14185   166 VAPEILSEKGYGLEVDMWAAGVILY-ILLCGFPPFrsPERDQEELFQIIQLGHyEFLPPywDNISEAAKDLISRLLVVDP 244

                  ....*....
gi 767943404 2155 DQRPTFHRI 2163
Cdd:cd14185   245 EKRYTAKQV 253
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
1930-2159 4.58e-13

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 72.37  E-value: 4.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1930 AVKTLKKGSTD-QEKIEFLkeahlMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARmatFYGPLLTLVDL 2008
Cdd:cd14175    30 AVKVIDKSKRDpSEEIEIL-----LRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQK---FFSEREASSVL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2009 VDLCvdisKGCVYLERMHFIHRDLAARNCLVsVKDYTSPRIVKIGDFGLARDIYKNDyyrkrgeGLL-----PVRWMAPE 2083
Cdd:cd14175   102 HTIC----KTVEYLHSQGVVHRDLKPSNILY-VDESGNPESLRICDFGFAKQLRAEN-------GLLmtpcyTANFVAPE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2084 SLMDGIFTTQSDVWSFGILIWEILTlGHQPY---PAHSNLDVLN------YVQTGGRLEPPRNCPDDLWNLMTQCwaqEP 2154
Cdd:cd14175   170 VLKRQGYDEGCDIWSLGILLYTMLA-GYTPFangPSDTPEEILTrigsgkFTLSGGNWNTVSDAAKDLVSKMLHV---DP 245

                  ....*
gi 767943404 2155 DQRPT 2159
Cdd:cd14175   246 HQRLT 250
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
1903-2159 4.85e-13

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 71.19  E-value: 4.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdilgVGSGE--IKVAVK-TLKKGSTDQEKIEFLKEAHLMSKFN-HPNILK------QLGVCllne 1972
Cdd:cd14050     9 LGEGSFGEVFK--------VRSREdgKLYAVKrSRSRFRGEKDRKRKLEEVERHEKLGeHPNCVRfikaweEKGIL---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 pqYIILELMeGGDLLTYLRKArmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDytspRIVKI 2052
Cdd:cd14050    77 --YIQTELC-DTSLQQYCEET-------HSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLS-KD----GVCKL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKND-YYRKRGEGllpvRWMAPEsLMDGIFTTQSDVWSFGILIWEILTlghqpypahsNLDVLNYvqtGGR 2131
Cdd:cd14050   142 GDFGLVVELDKEDiHDAQEGDP----RYMAPE-LLQGSFTKAADIFSLGITILELAC----------NLELPSG---GDG 203
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2132 LEPPRN----------CPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14050   204 WHQLRQgylpeeftagLSPELRSIIKLMMDPDPERRPT 241
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1903-2114 5.08e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 71.87  E-value: 5.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGV-----CLLNEPQYII 1977
Cdd:cd14039     1 LGTGGFGNVCLYQNQE-----TGE-KIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVpeemnFLVNDVPLLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKARMATfygpLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNclVSVKDYTSPRIVKIGDFGL 2057
Cdd:cd14039    75 MEYCSGGDLRKLLNKPENCC----GLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPEN--IVLQEINGKIVHKIIDLGY 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2058 ARDIykndyyrkrGEGLL------PVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd14039   149 AKDL---------DQGSLctsfvgTLQYLAPELFENKSYTVTVDYWSFGTMVFECIA-GFRPF 201
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
1903-2159 6.77e-13

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 71.98  E-value: 6.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDilgVGSGEIkVAVKTLK-KGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE- 1979
Cdd:cd06634    23 IGHGSFGAVY--FARD---VRNNEV-VAIKKMSySGKQSNEKWQdIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEy 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 -LMEGGDLLTYLRKARM-----ATFYGPLltlvdlvdlcvdisKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIG 2053
Cdd:cd06634    97 cLGSASDLLEVHKKPLQeveiaAITHGAL--------------QGLAYLHSHNMIHRDVKAGNILL-----TEPGLVKLG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDYYrkrgegLLPVRWMAPESLM---DGIFTTQSDVWSFGILIWEIltlgHQPYPAHSNLDVLNYVQTGG 2130
Cdd:cd06634   158 DFGSASIMAPANSF------VGTPYWMAPEVILamdEGQYDGKVDVWSLGITCIEL----AERKPPLFNMNAMSALYHIA 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767943404 2131 RLEPP----RNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06634   228 QNESPalqsGHWSEYFRNFVDSCLQKIPQDRPT 260
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1903-2159 6.83e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 71.53  E-value: 6.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGV------CLLNEPQYI 1976
Cdd:cd14038     2 LGTGGFGNVLRWINQE-----TGE-QVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVpeglqkLAPNDLPLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYL---------RKARMATFYGplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDytsP 2047
Cdd:cd14038    76 AMEYCQGGDLRKYLnqfenccglREGAILTLLS-------------DISSALRYLHENRIIHRDLKPENIVLQQGE---Q 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 RIV-KIGDFGLARDIyknDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY-----PAH---- 2117
Cdd:cd14038   140 RLIhKIIDLGYAKEL---DQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPFlpnwqPVQwhgk 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2118 ----SNLDVLNYVQTGG--RLEPPRNCPDDLWNLMT---QCWAQ-----EPDQRPT 2159
Cdd:cd14038   216 vrqkSNEDIVVYEDLTGavKFSSVLPTPNNLNGILAgklERWLQcmlmwHPRQRGT 271
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
1903-2123 8.27e-13

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 70.79  E-value: 8.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDIlgvgsgEIKVAVKTL-KKGSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd14162     8 LGHGSYAVVKKAYSTKH------KCKVAIKIVsKKKAPEDYLQKFLpREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARmatfYGPLLTLVDLVDLCVDiskGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGDFGLARD 2060
Cdd:cd14162    82 AENGDLLDYIRKNG----ALPEPQARRWFRQLVA---GVEYCHSKGVVHRDLKCENLLLD-KNNN----LKITDFGFARG 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2061 IYKNDYYRKRgegLLPV-----RWMAPESL----MDGIFttqSDVWSFGILIWEILtLGHQPYpAHSNLDVL 2123
Cdd:cd14162   150 VMKTKDGKPK---LSETycgsyAYASPEILrgipYDPFL---SDIWSMGVVLYTMV-YGRLPF-DDSNLKVL 213
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
1903-2130 8.81e-13

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 71.04  E-value: 8.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDIlgvgsgEIKVAVKTLKKGSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14097     9 LGQGSFGVVIEATHKET------QTKWAIKKINREKAGSSAVKLLeREVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKArmatfyGPLLTLVDLVDLCvDISKGCVYLERMHFIHRDLAARNCLV--SVKDYTSPRIVKIGDFGLAR 2059
Cdd:cd14097    83 EDGELKELLLRK------GFFSENETRHIIQ-SLASAVAYLHKNDIVHRDLKLENILVksSIIDNNDKLNIKVTDFGLSV 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2060 DIYKndyyrkRGEGLL------PVrWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPYPAHSNLDVLNYVQTGG 2130
Cdd:cd14097   156 QKYG------LGEDMLqetcgtPI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEKLFEEIRKGD 224
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
1895-2126 1.28e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 71.24  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLrllLGSGAFGEVYEGTAVDilgvgSGEIkVAvktLKKGSTDQEK----IEFLKEAHLMSKFNHPNILKQLGVCLL 1970
Cdd:cd07845    10 EKLNR---IGEGTYGIVYRARDTT-----SGEI-VA---LKKVRMDNERdgipISSLREITLLLNLRHPNIVELKEVVVG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQYIILeLMEGGDL-LTYLRKARMATFYGPLLTLVdlvdlCVDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPRI 2049
Cdd:cd07845    78 KHLDSIFL-VMEYCEQdLASLLDNMPTPFSESQVKCL-----MLQLLRGLQYLHENFIIHRDLKVSNLL-----LTDKGC 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2050 VKIGDFGLARDIykNDYYRKRGEGLLPVRWMAPESLM-DGIFTTQSDVWSFGILIWEILTlgHQP-YPAHSNLDVLNYV 2126
Cdd:cd07845   147 LKIADFGLARTY--GLPAKPMTPKVVTLWYRAPELLLgCTTYTTAIDMWAVGCILAELLA--HKPlLPGKSEIEQLDLI 221
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
1890-2159 1.33e-12

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 70.82  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1890 PAFPREKLTLRLLLGSGAFGevyegtAVDILGVGSGEIKVAVKtlKKGSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVC 1968
Cdd:cd06657    15 PGDPRTYLDNFIKIGEGSTG------IVCIATVKSSGKLVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1969 LLNEPQYIILELMEGGDLLTYLRKARMatfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPR 2048
Cdd:cd06657    87 LVGDELWVVMEFLEGGALTDIVTHTRM--------NEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILL-----THDG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQT 2128
Cdd:cd06657   154 RVKLSDFGFCAQVSKEVPRRKSLVG--TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMIRD 230
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767943404 2129 G--GRLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06657   231 NlpPKLKNLHKVSPSLKGFLDRLLVRDPAQRAT 263
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
1903-2157 1.39e-12

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 70.19  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDIlgvgsgEIKVAVKTLKKGSTDQEKIE-FL-KEAHLMSKFNHPNILKQLGVCLLNEPQ-YIILE 1979
Cdd:cd14165     9 LGEGSYAKVKSAYSERL------KCNVAIKIIDKKKAPDDFVEkFLpRELEILARLNHKSIIKTYEIFETSDGKvYIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKarmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGDFGLAR 2059
Cdd:cd14165    83 LGVQGDLLEFIKL-------RGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLD-KDFN----IKLTDFGFSK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIYKNDyyrkRGEGLL------PVRWMAPEsLMDGIF--TTQSDVWSFGILIWeILTLGHQPYPAhSNLDVLNYVQTGGR 2131
Cdd:cd14165   151 RCLRDE----NGRIVLsktfcgSAAYAAPE-VLQGIPydPRIYDIWSLGVILY-IMVCGSMPYDD-SNVKKMLKIQKEHR 223
                         250       260
                  ....*....|....*....|....*...
gi 767943404 2132 LEPPRNCPD--DLWNLMTQCWAQEPDQR 2157
Cdd:cd14165   224 VRFPRSKNLtsECKDLIYRLLQPDVSQR 251
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
1897-2129 1.39e-12

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 70.33  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTAVdilgvgSGEIKVAVKTLKK-GSTDQEKIefLKEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd14190     6 IHSKEVLGGGKFGKVHTCTEK------RTGLKLAAKVINKqNSKDKEMV--LLEIQVMNQLNHRNLIQLYEAIETPNEIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLL-------TYLRKARMATFYGplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVkdyTSPR 2048
Cdd:cd14190    78 LFMEYVEGGELFerivdedYHLTEVDAMVFVR-------------QICEGIQFMHQMRVLHLDLKPENILCVN---RTGH 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDiYKNDYYRKRGEGlLPvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQT 2128
Cdd:cd14190   142 QVKIIDFGLARR-YNPREKLKVNFG-TP-EFLSPEVVNYDQVSFPTDMWSMGVITYMLLS-GLSPFLGDDDTETLNNVLM 217

                  .
gi 767943404 2129 G 2129
Cdd:cd14190   218 G 218
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
1902-2158 1.51e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.91  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVD-ILGvgsgeIKVAVKTLKKG-STDQEKIE-FLKEAHLMSKFNHPNIlkqlgVCLL-----NEP 1973
Cdd:NF033483   14 RIGRGGMAEVYL--AKDtRLD-----RDVAVKVLRPDlARDPEFVArFRREAQSAASLSHPNI-----VSVYdvgedGGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKarmatfYGPlltlvDLVDLCVDISKG-CVYLE---RMHFIHRDLAARNCLVSvKDytspRI 2049
Cdd:NF033483   82 PYIVMEYVDGRTLKDYIRE------HGP-----LSPEEAVEIMIQiLSALEhahRNGIVHRDIKPQNILIT-KD----GR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDI------YKND-----YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHS 2118
Cdd:NF033483  146 VKVTDFGIARALssttmtQTNSvlgtvHY------------LSPEQARGGTVDARSDIYSLGIVLYEMLT-GRPPFDGDS 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767943404 2119 NLDV-LNYVQtggrlEPPR-------NCPDDLWNLMTQCWAQEPDQRP 2158
Cdd:NF033483  213 PVSVaYKHVQ-----EDPPppselnpGIPQSLDAVVLKATAKDPDDRY 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
1903-2163 1.68e-12

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 69.75  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFgevyegtAVDILG--VGSGEiKVAVKTLKKGSTDQE-KIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd14074    11 LGRGHF-------AVVKLArhVFTGE-KVAVKVIDKTKLDDVsKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKarmatfYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytspRIVKIGDFGLAr 2059
Cdd:cd14074    83 LGDGGDMYDYIMK------HENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQ----GLVKLTDFGFS- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 diykNDYyrKRGEGLL----PVRWMAPESLM-DGIFTTQSDVWSFGILIWeILTLGHQPYPAHSNLDVLNYVQTgGRLEP 2134
Cdd:cd14074   152 ----NKF--QPGEKLEtscgSLAYSAPEILLgDEYDAPAVDIWSLGVILY-MLVCGQPPFQEANDSETLTMIMD-CKYTV 223
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2135 PRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14074   224 PAHVSPECKDLIRRMLIRDPKKRASLEEI 252
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
1903-2159 1.72e-12

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 70.17  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdilGVGSGEiKVAVKTLKKGSTDQEKIEFLK--------------EAHLMSKFNHPNILKQLGVC 1968
Cdd:cd14077     9 IGAGSMGKVKLAK-----HIRTGE-KCAIKIIPRASNAGLKKEREKrlekeisrdirtirEAALSSLLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1969 LLNEPQYIILELMEGGDLLTY------LRKARMATFYgplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSvk 2042
Cdd:cd14077    83 RTPNHYYMLFEYVDGGQLLDYiishgkLKEKQARKFA-------------RQIASALDYLHRNSIVHRDLKIENILIS-- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2043 dytSPRIVKIGDFGLArDIYKNDYYRKRGEGLLpvRWMAPESLMDGIFT-TQSDVWSFGILIWeILTLGHQPYPaHSNLD 2121
Cdd:cd14077   148 ---KSGNIKIIDFGLS-NLYDPRRLLRTFCGSL--YFAAPELLQAQPYTgPEVDVWSFGVVLY-VLVCGKVPFD-DENMP 219
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767943404 2122 VLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14077   220 ALHAKIKKGKVEYPSYLSSECKSLISRMLVVDPKKRAT 257
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
1903-2163 1.86e-12

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 70.26  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd06622     9 LGKGNYGSVYK-----VLHRPTGVT-MAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLlTYLRKARMATFYGPLLTLVDLVDLCVdisKGCVYLERMH-FIHRDLAARNCLVSVKDYtspriVKIGDFGLARDI 2061
Cdd:cd06622    83 AGSL-DKLYAGGVATEGIPEDVLRRITYAVV---KGLKFLKEEHnIIHRDVKPTNVLVNGNGQ-----VKLCDFGVSGNL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNdyYRKRGEGLLpvRWMAPESLMDG------IFTTQSDVWSFGILIWEiLTLGHQPYPAHSNLDVLNYVQTGGRLEPP 2135
Cdd:cd06622   154 VAS--LAKTNIGCQ--SYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILE-MALGRYPYPPETYANIFAQLSAIVDGDPP 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2136 RNCPD---DLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd06622   229 TLPSGysdDAQDFVAKCLNKIPNRRPTYAQL 259
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
1947-2157 1.98e-12

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 69.59  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1947 LKEAHLMSKFNHPNIlkqlgVCLLNEPQ-----YIILELMEGGDLLTYL-RKARM----ATFYgplltlvdlvdlCVDIS 2016
Cdd:cd05578    48 LNELEILQELEHPFL-----VNLWYSFQdeedmYMVVDLLLGGDLRYHLqQKVKFseetVKFY------------ICEIV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2017 KGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARdIYKNDYYRKRGEGLLPvrWMAPESLMDGIFTTQSDV 2096
Cdd:cd05578   111 LALDYLHSKNIIHRDIKPDNILLDEQGH-----VHITDFNIAT-KLTDGTLATSTSGTKP--YMAPEVFMRAGYSFAVDW 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2097 WSFGILIWEILTlGHQPYPAHSNL---DVLNYVQTGGRLEPPRNCPD--DLWNLMTQcwaQEPDQR 2157
Cdd:cd05578   183 WSLGVTAYEMLR-GKRPYEIHSRTsieEIRAKFETASVLYPAGWSEEaiDLINKLLE---RDPQKR 244
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
211-290 2.23e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.83  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  211 NIESSSPDTVEVSWDPPQFPGGPILGYNLRLISKNQK-----LDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGEGPEAE 285
Cdd:cd00063     8 RVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGdwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSE 87

                  ....*
gi 767943404  286 SSITT 290
Cdd:cd00063    88 SVTVT 92
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
1895-2157 2.51e-12

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 70.72  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEGTAVdilgvGSGEIkVAVKTLKKGST---DQEKIEFLKEAHLMSKFNHPNILKQLGVCLLN 1971
Cdd:cd05619     5 EDFVLHKMLGKGSFGKVFLAELK-----GTNQF-FAIKALKKDVVlmdDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1972 EPQYIILELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYts 2046
Cdd:cd05619    79 ENLFFVMEYLNGGDLMFHIQSCHKfdlprATFYA------------AEIICGLQFLHSKGIVYRDLKLDNILLDKDGH-- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2047 priVKIGDFGLARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAHSNLDVLNYV 2126
Cdd:cd05619   145 ---IKIADFGMCKENMLGDAKTSTFCG--TPDYIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELFQSI 218
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2127 QTGGRLEpPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05619   219 RMDNPFY-PRWLEKEAKDILVKLFVREPERR 248
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
1903-2175 2.65e-12

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 70.07  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdilGVGSGEIkVAVKTLK-KGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE- 1979
Cdd:cd06633    29 IGHGSFGAVYFAT-----NSHTNEV-VAIKKMSySGKQTNEKWQdIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEy 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 -LMEGGDLLTYLRKARMAtfygplltlvdlvdlcVDIS-------KGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVK 2051
Cdd:cd06633   103 cLGSASDLLEVHKKPLQE----------------VEIAaithgalQGLAYLHSHNMIHRDIKAGNILL-----TEPGQVK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLARDIYKNDYYrkrgegLLPVRWMAPESLM---DGIFTTQSDVWSFGILIWEILtlghQPYPAHSNLDVLNYVQT 2128
Cdd:cd06633   162 LADFGSASIASPANSF------VGTPYWMAPEVILamdEGQYDGKVDIWSLGITCIELA----ERKPPLFNMNAMSALYH 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2129 GGRLEPP----RNCPDDLWNLMTQCWAQEPDQRPTfhriqdQLQLFRNFFL 2175
Cdd:cd06633   232 IAQNDSPtlqsNEWTDSFRGFVDYCLQKIPQERPS------SAELLRHDFV 276
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
1903-2156 2.66e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 70.06  E-value: 2.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKKG---STDQEkIEFLKEahlMSKFNHPNILKQLGVCLLN----EPQY 1975
Cdd:cd07862     9 IGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGmplSTIRE-VAVLRH---LETFEHPNVVRLFDVCTVSrtdrETKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDF 2055
Cdd:cd07862    85 TLVFEHVDQDLTTYLDKVP-----EPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV-----TSSGQIKLADF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARdIYKndYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlgHQP-YPAHSNLDVLNYVQTGGRLEP 2134
Cdd:cd07862   155 GLAR-IYS--FQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFR--RKPlFRGSSDVDQLGKILDVIGLPG 229
                         250       260
                  ....*....|....*....|..
gi 767943404 2135 PRNCPDDLwNLMTQCWAQEPDQ 2156
Cdd:cd07862   230 EEDWPRDV-ALPRQAFHSKSAQ 250
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
1897-2114 2.75e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 70.23  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTAVdilgvGSGEIkVAVKTLKKgstdQEKIEF------LKEAHLMSKFNHPNILKQLGVCLL 1970
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHK-----GTGEY-YAIKCLKK----REILKMkqvqhvAQEKSILMELSHPFIVNMMCSFQD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQYIILELMEGGDLLTYLRKA-----RMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYt 2045
Cdd:PTZ00263   90 ENRVYFLLEFVVGGELFTHLRKAgrfpnDVAKFY------------HAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH- 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2046 spriVKIGDFGLARDIykndyyRKRGEGLLPV-RWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:PTZ00263  157 ----VKVTDFGFAKKV------PDRTFTLCGTpEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA-GYPPF 215
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
1895-2135 3.42e-12

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 68.91  E-value: 3.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEgtavdILGVGSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ 1974
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKE-----CVERSTGK-EFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkDYTS-PRIVKIG 2053
Cdd:cd14184    75 YLVMELVKGGDLFDAITSSTKYT-------ERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVC--EYPDgTKSLKLG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLArDIYKNDYYRKRGEgllPVrWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPYPAHSNL--DVLNYVQTgGR 2131
Cdd:cd14184   146 DFGLA-TVVEGPLYTVCGT---PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRSENNLqeDLFDQILL-GK 218

                  ....
gi 767943404 2132 LEPP 2135
Cdd:cd14184   219 LEFP 222
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
1930-2129 3.92e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 70.05  E-value: 3.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1930 AVKTLKKGSTD-QEKIEFLkeahlMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARmatFYGPLLTLVDL 2008
Cdd:cd14176    48 AVKIIDKSKRDpTEEIEIL-----LRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQK---FFSEREASAVL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2009 VDlcvdISKGCVYLERMHFIHRDLAARNCLVsVKDYTSPRIVKIGDFGLARDIykndyyrkRGE-GLL-----PVRWMAP 2082
Cdd:cd14176   120 FT----ITKTVEYLHAQGVVHRDLKPSNILY-VDESGNPESIRICDFGFAKQL--------RAEnGLLmtpcyTANFVAP 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767943404 2083 ESLMDGIFTTQSDVWSFGILIWEILTlGHQPY---PAHSNLDVLNYVQTG 2129
Cdd:cd14176   187 EVLERQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSG 235
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
1903-2159 5.12e-12

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 69.85  E-value: 5.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:PLN00034   82 IGSGAGGTVYK-----VIHRPTGRL-YALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMD 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLltylRKARMAtfygplltlvdLVDLCVDISK----GCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLA 2058
Cdd:PLN00034  156 GGSL----EGTHIA-----------DEQFLADVARqilsGIAYLHRRHIVHRDIKPSNLLIN-----SAKNVKIADFGVS 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIykNDYYRKRGEGLLPVRWMAPE----SLMDGIFTTQS-DVWSFGILIWEiLTLGHQPYPAHSNLD------VLNYVQ 2127
Cdd:PLN00034  216 RIL--AQTMDPCNSSVGTIAYMSPErintDLNHGAYDGYAgDIWSLGVSILE-FYLGRFPFGVGRQGDwaslmcAICMSQ 292
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767943404 2128 TGgrlEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:PLN00034  293 PP---EAPATASREFRHFISCCLQREPAKRWS 321
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
1903-2107 5.80e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 68.84  E-value: 5.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKgSTDQE--KIEFLKEAHLMSK---FNHPNILKQLGVCLLNEPQY-- 1975
Cdd:cd07863     8 IGVGAYGTVYKARDPH-----SGHF-VALKSVRV-QTNEDglPLSTVREVALLKRleaFDHPNIVRLMDVCATSRTDRet 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 ---IILELMEGgDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKI 2052
Cdd:cd07863    81 kvtLVFEHVDQ-DLRTYLDKVP-----PPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILV-----TSGGQVKL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2053 GDFGLARdIYKndYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEIL 2107
Cdd:cd07863   150 ADFGLAR-IYS--CQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF 201
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
1903-2159 7.96e-12

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 67.86  E-value: 7.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdilGVGSGEIkVAVKTLK-KGSTDQEKI-EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE- 1979
Cdd:cd06607     9 IGHGSFGAVYYAR-----NKRTSEV-VAIKKMSySGKQSTEKWqDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEy 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 -LMEGGDLLTYLRKArmatfygplLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLA 2058
Cdd:cd06607    83 cLGSASDIVEVHKKP---------LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILL-----TEPGTVKLADFGSA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIYKNDYYRKRgegllPVrWMAPESL--MD-GIFTTQSDVWSFGILIWEILtlghQPYPAHSNLDVLNYVQTGGRLEPP 2135
Cdd:cd06607   149 SLVCPANSFVGT-----PY-WMAPEVIlaMDeGQYDGKVDVWSLGITCIELA----ERKPPLFNMNAMSALYHIAQNDSP 218
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2136 RNCPDDlW-----NLMTQCWAQEPDQRPT 2159
Cdd:cd06607   219 TLSSGE-WsddfrNFVDSCLQKIPQDRPS 246
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
1893-2163 8.03e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 68.15  E-value: 8.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTavdilGVGSGEIkVAVKTLK-KGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLN 1971
Cdd:cd06645     9 PQEDFELIQRIGSGTYGDVYKAR-----NVNTGEL-AAIKVIKlEPGEDFAVVQ--QEIIMMKDCKHSNIVAYFGSYLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1972 EPQYIILELMEGGDLltylrkARMATFYGPlLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVK 2051
Cdd:cd06645    81 DKLWICMEFCGGGSL------QDIYHVTGP-LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGH-----VK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLARDIYKNDYYRKRGEGllPVRWMAPESLM---DGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVlnYVQT 2128
Cdd:cd06645   149 LADFGVSAQITATIAKRKSFIG--TPYWMAPEVAAverKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRAL--FLMT 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767943404 2129 GGRLEPPR-----NCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd06645   225 KSNFQPPKlkdkmKWSNSFHHFVKMALTKNPKKRPTAEKL 264
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
1903-2108 1.30e-11

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 68.11  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAvktLKKGSTDQEK----IEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ---- 1974
Cdd:cd07866    16 LGEGTFGEVYKARQIK-----TGRV-VA---LKKILMHNEKdgfpITALREIKILKKLKHPNVVPLIDMAVERPDKskrk 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 ----YIILELMEGgDLLTYLRKarmatfygPLLTLVDLVDLCV--DISKGCVYLERMHFIHRDLAARNCLVSVKDytspr 2048
Cdd:cd07866    87 rgsvYMVTPYMDH-DLSGLLEN--------PSVKLTESQIKCYmlQLLEGINYLHENHILHRDIKAANILIDNQG----- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDIYKNDYYRKRGEG--------LLPVRWM-APESLM-DGIFTTQSDVWSFGILIWEILT 2108
Cdd:cd07866   153 ILKIADFGLARPYDGPPPNPKGGGGggtrkytnLVVTRWYrPPELLLgERRYTTAVDIWGIGCVFAEMFT 222
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
1903-2157 1.35e-11

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 68.01  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVY--EGTavdilgvGSGEIkVAVKTLKKGS-TDQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQ-YII 1977
Cdd:cd05570     3 LGKGSFGKVMlaERK-------KTDEL-YAIKVLKKEViIEDDDVECTMtEKRVLALANRHPFLTGLHACFQTEDRlYFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd05570    75 MEYVNGGDLMFHIQRARRfteerARFYA------------AEICLALQFLHERGIIYRDLKLDNVLLDAEGH-----IKI 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARdiykndyyrkrgEGLLPVR----------WMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAHSNLDV 2122
Cdd:cd05570   138 ADFGMCK------------EGIWGGNttstfcgtpdYIAPEILREQDYGFSVDWWALGVLLYEML-AGQSPFEGDDEDEL 204
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2123 LNYVQtGGRLEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05570   205 FEAIL-NDEVLYPRWLSREAVSILKGLLTKDPARR 238
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
1902-2107 1.44e-11

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 68.47  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKgsTDQEKIE----FLKEAHLMSKFNHPNIlkqlgVCLL-----NE 1972
Cdd:cd05573     8 VIGRGAFGEVWLVRDKD-----TGQV-YAMKILRK--SDMLKREqiahVRAERDILADADSPWI-----VRLHyafqdED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRK-----ARMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtsp 2047
Cdd:cd05573    75 HLYLVMEYMPGGDLMNLLIKydvfpEETARFY------------IAELVLALDSLHKLGFIHRDIKPDNILLDADGH--- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 riVKIGDFGLARDIYKND---YYRKRG------EGLLPVRW------------------MAPESLMDGIFTTQSDVWSFG 2100
Cdd:cd05573   140 --IKLADFGLCTKMNKSGdreSYLNDSvntlfqDNVLARRRphkqrrvraysavgtpdyIAPEVLRGTGYGPECDWWSLG 217

                  ....*..
gi 767943404 2101 ILIWEIL 2107
Cdd:cd05573   218 VILYEML 224
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
1906-2124 1.85e-11

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 67.25  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1906 GAFGEVYEgtAVDILgvgSGEIkVAVKTLKkgsTDQEKIEF----LKEAHLMSKFNHPNIL--KQLGVCLLNEPQYIILE 1979
Cdd:cd07843    16 GTYGVVYR--ARDKK---TGEI-VALKKLK---MEKEKEGFpitsLREINILLKLQHPNIVtvKEVVVGSNLDKIYMVME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGgDLltylrKARMATFYGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLAr 2059
Cdd:cd07843    87 YVEH-DL-----KSLMETMKQPFLQSEVKCLM-LQLLSGVAHLHDNWILHRDLKTSNLLLNNRG-----ILKICDFGLA- 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2060 diykndyyRKRGEGLLPVR------WM-APESLMD-GIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLN 2124
Cdd:cd07843   154 --------REYGSPLKPYTqlvvtlWYrAPELLLGaKEYSTAIDMWSVGCIFAELLT-KKPLFPGKSEIDQLN 217
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
1893-2163 1.89e-11

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 66.98  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIeFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd06646     7 PQHDYELIQRVGSGTYGDVYKARNLH-----TGEL-AAVKIIKLEPGDDFSL-IQQEIFMVKECKHCNIVAYFGSYLSRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLltylrkARMATFYGPlLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKI 2052
Cdd:cd06646    80 KLWICMEYCGGGSL------QDIYHVTGP-LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILL-----TDNGDVKL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGlLPVrWMAPESLM---DGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVlnYVQTG 2129
Cdd:cd06646   148 ADFGVAAKITATIAKRKSFIG-TPY-WMAPEVAAvekNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRAL--FLMSK 223
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2130 GRLEPPRNCPDDLW-----NLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd06646   224 SNFQPPKLKDKTKWsstfhNFVKISLTKNPKKRPTAERL 262
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
1903-2159 1.89e-11

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 66.91  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGE-VYEGTAvdilgvgsGEIKVAVKTLKK---GSTDQEkIEFLKEAHlmskfNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd13982     9 LGYGSEGTiVFRGTF--------DGRPVAVKRLLPeffDFADRE-VQLLRESD-----EHPNVIRYFCTEKDRQFLYIAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGgDLLTYLRKARmaTFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIVKIGDFGLA 2058
Cdd:cd13982    75 ELCAA-SLQDLVESPR--ESKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGNVRAMISDFGLC 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIYKNDY-YRKRGEGLLPVRWMAPESLMDGIFTTQS---DVWSFGILIWEILTLGHQPYPAH----SNLdVLNYVQTgG 2130
Cdd:cd13982   152 KKLDVGRSsFSRRSGVAGTSGWIAPEMLSGSTKRRQTravDIFSLGCVFYYVLSGGSHPFGDKlereANI-LKGKYSL-D 229
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2131 RLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd13982   230 KLLSLGEHGPEAQDLIERMIDFDPEKRPS 258
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
2014-2167 3.35e-11

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 66.06  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2014 DISKGCVYLERMHF-IHRDLAARNCLVSvkdytSPRIVKIGDFGlardiykndyyrkrGEGLLPVR---WMAPESLMDGI 2089
Cdd:cd14044   117 DIAKGMSYLHSSKTeVHGRLKSTNCVVD-----SRMVVKITDFG--------------CNSILPPSkdlWTAPEHLRQAG 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2090 FTTQSDVWSFGILIWEILTLGHQPYPAHSN--LDVLNYVQTGGRLEPPRncPD-----------DLWNLMTQCWAQEPDQ 2156
Cdd:cd14044   178 TSQKGDVYSYGIIAQEIILRKETFYTAACSdrKEKIYRVQNPKGMKPFR--PDlnlesagererEVYGLVKNCWEEDPEK 255
                         170
                  ....*....|.
gi 767943404 2157 RPTFHRIQDQL 2167
Cdd:cd14044   256 RPDFKKIENTL 266
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
1902-2114 4.45e-11

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 65.72  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDILGVGSGeiKVAVKTLKKGSTDQEKIEFlkEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14187    14 FLGKGGFAKCYEITDADTKEVFAG--KIVPKSLLLKPHQKEKMSM--EIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTyLRKARMATfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDI 2061
Cdd:cd14187    90 RRRSLLE-LHKRRKAL------TEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLN-----DDMEVKIGDFGLATKV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2062 yKNDYYRKRGEGLLPvRWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPY 2114
Cdd:cd14187   158 -EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLL-VGKPPF 207
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
1902-2159 4.56e-11

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 66.19  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQE-KIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd07833     8 VVGEGAYGVVLKCRNKA-----TGEI-VAIKKFKESEDDEDvKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGgDLLTYLRkaRMATFYGPLLTLVDLVDLCVDISkgcvYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARD 2060
Cdd:cd07833    82 VER-TLLELLE--ASPGGLPPDAVRSYIWQLLQAIA----YCHSHNIIHRDIKPENILVS-----ESGVLKLCDFGFARA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYKN------DYyrkrgeglLPVRWM-APESLM-DGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQ----- 2127
Cdd:cd07833   150 LTARpaspltDY--------VATRWYrAPELLVgDTNYGKPVDVWAIGCIMAELLD-GEPLFPGDSDIDQLYLIQkclgp 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2128 ---------------TGGRLEPP----------RNCPDDLW-NLMTQCWAQEPDQRPT 2159
Cdd:cd07833   221 lppshqelfssnprfAGVAFPEPsqpeslerryPGKVSSPAlDFLKACLRMDPKERLT 278
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1902-2107 5.07e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 65.59  E-value: 5.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAvdilgvgsgeiKVAVKT--LKKGSTDQEKIEflKEAHLMSKFNHPNILKQL----GVCLLNEPQY 1975
Cdd:cd14047    13 LIGSGGFGQVFKAKH-----------RIDGKTyaIKRVKLNNEKAE--REVKALAKLDHPNIVRYNgcwdGFDYDPETSS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 ------------IILELMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkd 2043
Cdd:cd14047    80 snssrsktkclfIQMEFCEKGTLESWIEKRN-----GEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLV--- 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2044 ytSPRIVKIGDFGLARDIyKNDYYRKRGEGLLpvRWMAPESLMDGIFTTQSDVWSFGILIWEIL 2107
Cdd:cd14047   152 --DTGKVKIGDFGLVTSL-KNDGKRTKSKGTL--SYMSPEQISSQDYGKEVDIYALGLILFELL 210
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
1902-2157 5.25e-11

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 65.35  E-value: 5.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVK-TLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGvCLLNEPQYIILEL 1980
Cdd:cd14002     8 LIGEGSFGKVYKGRRKY-----TGQV-VALKfIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLD-SFETKKEFVVVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARmatfygplltlvdlvDLCVD----ISKGCV----YLERMHFIHRDLAARNCLVsvkdyTSPRIVKI 2052
Cdd:cd14002    81 YAQGELFQILEDDG---------------TLPEEevrsIAKQLVsalhYLHSNRIIHRDMKPQNILI-----GKGGVVKL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGlLPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVqTGGRL 2132
Cdd:cd14002   141 CDFGFARAMSCNTLVLTSIKG-TPL-YMAPELVQEQPYDHTADLWSLGCILYELFV-GQPPFYTNSIYQLVQMI-VKDPV 216
                         250       260
                  ....*....|....*....|....*
gi 767943404 2133 EPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd14002   217 KWPSNMSPEFKSFLQGLLNKDPSKR 241
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
1902-2126 6.50e-11

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 65.37  E-value: 6.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVdilgvgSGEIKVAVKTLK-KGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd14192    11 VLGGGRFGQVHKCTEL------STGLTLAAKIIKvKGAKEREEVK--NEINIMNQLNHVNLIQLYDAFESKTNLTLIMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARMatfygpLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkDYTSPRIvKIGDFGLARD 2060
Cdd:cd14192    83 VDGGELFDRITDESY------QLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCV--NSTGNQI-KIIDFGLARR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2061 iykndyYRKRGEglLPV-----RWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd14192   154 ------YKPREK--LKVnfgtpEFLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLGETDAETMNNI 215
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
1903-2159 7.76e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 65.84  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDilgVGSGEIkVAVKTLK-KGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE- 1979
Cdd:cd06635    33 IGHGSFGAVY--FARD---VRTSEV-VAIKKMSySGKQSNEKWQdIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEy 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 -LMEGGDLLTYLRKARM-----ATFYGPLltlvdlvdlcvdisKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIG 2053
Cdd:cd06635   107 cLGSASDLLEVHKKPLQeieiaAITHGAL--------------QGLAYLHSHNMIHRDIKAGNILL-----TEPGQVKLA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDYYrkrgegLLPVRWMAPESLM---DGIFTTQSDVWSFGILIWEILtlghQPYPAHSNLDVLNYVQTGG 2130
Cdd:cd06635   168 DFGSASIASPANSF------VGTPYWMAPEVILamdEGQYDGKVDVWSLGITCIELA----ERKPPLFNMNAMSALYHIA 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767943404 2131 RLEPP----RNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd06635   238 QNESPtlqsNEWSDYFRNFVDSCLQKIPQDRPT 270
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
1902-2129 8.45e-11

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 64.65  E-value: 8.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVDILGVGSGEIKVAVKTLKKGstdQEK-IEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd14095     7 VIGDGNFAVVKE--CRDKATDKEYALKIIDKAKCKG---KEHmIE--NEVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsVKDYTSPRIVKIGDFGLARD 2060
Cdd:cd14095    80 VKGGDLFDAITSSTKFT-------ERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLV-VEHEDGSKSLKLADFGLATE 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2061 IyKNDYYRKRGEgllPVrWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPY--PAHSNLDVLNYVQTG 2129
Cdd:cd14095   152 V-KEPLFTVCGT---PT-YVAPEILAETGYGLKVDIWAAGVITY-ILLCGFPPFrsPDRDQEELFDLILAG 216
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
1901-2114 8.57e-11

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 65.79  E-value: 8.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1901 LLLGSGAFGEVY--EGTAVDILgvgsgeikVAVKTLKKGSTDQEK-IE-FLKEAHLMSKFNHPNILKQLGVCLLNEPQ-Y 1975
Cdd:cd05616     6 MVLGKGSFGKVMlaERKGTDEL--------YAVKILKKDVVIQDDdVEcTMVEKRVLALSGKPPFLTQLHSCFQTMDRlY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLR-----KARMATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriV 2050
Cdd:cd05616    78 FVMEYVNGGDLMYHIQqvgrfKEPHAVFYA------------AEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH-----I 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2051 KIGDFGLARDIYKNDYYRKRGEGLlPvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd05616   141 KIADFGMCKENIWDGVTTKTFCGT-P-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPF 201
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
1903-2157 1.02e-10

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 64.89  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdILGVGSGEIKVAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd14117    14 LGKGKFGNVY------LAREKQSKFIVALKVLFKSQIEKEGVEhqLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKA------RMATFYGplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGD 2054
Cdd:cd14117    88 APRGELYKELQKHgrfdeqRTATFME-------------ELADALHYCHEKKVIHRDIKPENLLMGYKGE-----LKIAD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLArdIYKNDYYRKRGEGLLPvrWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAHSNLDVLNYVqTGGRLEP 2134
Cdd:cd14117   150 FGWS--VHAPSLRRRTMCGTLD--YLPPEMIEGRTHDEKVDLWCIGVLCYELL-VGMPPFESASHTETYRRI-VKVDLKF 223
                         250       260
                  ....*....|....*....|...
gi 767943404 2135 PRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd14117   224 PPFLSDGSRDLISKLLRYHPSER 246
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
1903-2118 1.05e-10

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 65.23  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILgvgsgeikVAVKTLKKGST---DQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd14159     1 IGEGGFGCVYQAVMRNTE--------YAVKRLKEDSEldwSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRkaRMATFygPLLTLVDLVDLCVDISKGCVYLERMH--FIHRDLAARNCLVSvkDYTSPrivKIGDFGL 2057
Cdd:cd14159    73 YLPNGSLEDRLH--CQVSC--PCLSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLD--AALNP---KLGDFGL 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2058 ARdiykndYYRKRGEGLLP--------VR----WMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHS 2118
Cdd:cd14159   144 AR------FSRRPKQPGMSstlartqtVRgtlaYLPEEYVKTGTLSVEIDVYSFGVVLLELLT-GRRAMEVDS 209
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
1902-2106 1.19e-10

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 64.64  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKkgSTDQEKIEFLKEAHLMSKFNH-PNILKQLGVCLLNEPQ------ 1974
Cdd:cd06636    23 VVGNGTYGQVYKGRHVK-----TGQL-AAIKVMD--VTEDEEEEIKLEINMLKKYSHhRNIATYYGAFIKKSPPghddql 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGD 2054
Cdd:cd06636    95 WLVMEFCGAGSVTDLVKNTK-----GNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLL-----TENAEVKLVD 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2055 FGLARDIYKNdyYRKRGEGLLPVRWMAPESLM-----DGIFTTQSDVWSFGILIWEI 2106
Cdd:cd06636   165 FGVSAQLDRT--VGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 219
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
1902-2160 1.19e-10

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 64.66  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLKKGSTDQE---KIEFLK-EAHLMSKFNHPNILKQLGvCLLNEPQ--- 1974
Cdd:cd06653     9 LLGRGAFGEVYLCYDAD-----TGR-ELAVKQVPFDPDSQEtskEVNALEcEIQLLKNLRHDRIVQYYG-CLRDPEEkkl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLvsvKDytSPRIVKIGD 2054
Cdd:cd06653    82 SIFVEYMPGGSVKDQLKA------YGALTENVTRRYT-RQILQGVSYLHSNMIVHRDIKGANIL---RD--SAGNVKLGD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIykNDYYRKrGEGLLPVR----WMAPESLMDGIFTTQSDVWSFGILIWEILTlgHQP----YPAHSNLDVLNYV 2126
Cdd:cd06653   150 FGASKRI--QTICMS-GTGIKSVTgtpyWMSPEVISGEGYGRKADVWSVACTVVEMLT--EKPpwaeYEAMAAIFKIATQ 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767943404 2127 QTGGRLepPRNCPDDLWNLMTQCWAQEpDQRPTF 2160
Cdd:cd06653   225 PTKPQL--PDGVSDACRDFLRQIFVEE-KRRPTA 255
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
103-297 1.20e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 66.95  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  103 EVLENADLPTAP---FASSIGSHNMTLRWKSANFSGVK-YIIQWKYAQLlGSWTYTKTVSRPSYVVKPLHPFTEYIFRVV 178
Cdd:COG3401   225 SVTTPTTPPSAPtglTATADTPGSVTLSWDPVTESDATgYRVYRSNSGD-GPFTKVATVTTTSYTDTGLTNGTTYYYRVT 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  179 WIFTAQLQlySPPSPSYRTHPHGVPETAPLIRNIESSSPDTVEVSWDPPqfPGGPILGYNL-RLISKN---QKLDAGTQR 254
Cdd:COG3401   304 AVDAAGNE--SAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS--SDADVTGYNVyRSTSGGgtyTKIAETVTT 379
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 767943404  255 TSFQFYSTLPNTIYRFSIAAVNEVGEGPEAESSITTSSSAVQQ 297
Cdd:COG3401   380 TSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAAS 422
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
1906-2116 1.21e-10

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 64.42  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1906 GAFGEVYEGTAVdilgvGSGEIkVAVKTLKKGSTD-QEKIEFLK--EAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd05611     7 GAFGSVYLAKKR-----STGDY-FAIKVLKKSDMIaKNQVTNVKaeRAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKarmatfYGPLLTLVDlvdlCVDISKGCVYLERMH---FIHRDLAARNCLVSVKDYtspriVKIGDFGLAR 2059
Cdd:cd05611    81 GGDCASLIKT------LGGLPEDWA----KQYIAEVVLGVEDLHqrgIIHRDIKPENLLIDQTGH-----LKLTDFGLSR 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2060 DIYKNDYyRKRGEGLlPvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPA 2116
Cdd:cd05611   146 NGLEKRH-NKKFVGT-P-DYLAPETILGVGDDKMSDWWSLGCVIFEFLF-GYPPFHA 198
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1894-2114 1.28e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 64.28  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVyegtavdILGVGSGEIK-VAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd14167     2 RDIYDFREVLGTGAFSEV-------VLAEEKRTQKlVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLLTYLRKArmaTFYgpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPriVKI 2052
Cdd:cd14167    75 HLYLIMQLVSGGELFDRIVEK---GFY----TERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSK--IMI 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2053 GDFGLARdiykndyyrKRGEGLLPVR------WMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPY 2114
Cdd:cd14167   146 SDFGLSK---------IEGSGSVMSTacgtpgYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 203
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1892-2163 1.36e-10

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 64.69  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1892 FPREKLTLRLLLGSGAFGEVYEgtavdILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAH-LMSKFNHPNILKQLGVcLL 1970
Cdd:cd06616     3 FTAEDLKDLGEIGRGAFGTVNK-----MLHKPSGTI-MAVKRIRSTVDEKEQKRLLMDLDvVMRSSDCPYIVKFYGA-LF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQ-YIILELMEggdllTYLRKarmatFYGPLLTLVDLV-------DLCVDISKGCVYL-ERMHFIHRDLAARNCLVSV 2041
Cdd:cd06616    76 REGDcWICMELMD-----ISLDK-----FYKYVYEVLDSVipeeilgKIAVATVKALNYLkEELKIIHRDVKPSNILLDR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2042 KDYtspriVKIGDFGLARDIyKNDYYRKRGEGLLPvrWMAPESL-----MDGiFTTQSDVWSFGILIWEILTlGHQPYPA 2116
Cdd:cd06616   146 NGN-----IKLCDFGISGQL-VDSIAKTRDAGCRP--YMAPERIdpsasRDG-YDVRSDVWSLGITLYEVAT-GKFPYPK 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2117 -HSNLDVLNYVQTGgrlEPPRNCPDD-------LWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd06616   216 wNSVFDQLTQVVKG---DPPILSNSEerefspsFVNFVNLCLIKDESKRPKYKEL 267
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
1903-2125 1.39e-10

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 64.27  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilgvGSGEIKVAVKTLKKGSTD-------QEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd14194    13 LGSGQFAVVKKCRE------KSTGLQYAAKFIKKRRTKssrrgvsREDIE--REVSILKEIQHPNVITLHEVYENKTDVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIvKIGDF 2055
Cdd:cd14194    85 LILELVAGGELFDFLAEKESLT-------EEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRI-KIIDF 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2056 GLARDI-YKNDYYRKRGEgllPvRWMAPESLMDGIFTTQSDVWSFGILIWEILT-----LGHQPYPAHSNLDVLNY 2125
Cdd:cd14194   157 GLAHKIdFGNEFKNIFGT---P-EFVAPEIVNYEPLGLEADMWSIGVITYILLSgaspfLGDTKQETLANVSAVNY 228
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
1902-2117 1.45e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 64.63  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegTAVDILGVGSgeiKVAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd05631     7 VLGKGGFGEV---CACQVRATGK---MYACKKLEKKRIKKRKGEamALNEKRILEKVNSRFVVSLAYAYETKDALCLVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLltylrKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLAR 2059
Cdd:cd05631    81 IMNGGDL-----KFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGH-----IRISDLGLAV 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2060 DIYKNDYYRKRgegLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAH 2117
Cdd:cd05631   151 QIPEGETVRGR---VGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQ-GQSPFRKR 204
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
1902-2106 1.48e-10

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 64.74  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEflKEAHLMSKFN-HPNILKQLGVCLLNEPQ------ 1974
Cdd:cd06637    13 LVGNGTYGQVYKGRHVK-----TGQL-AAIKVMDVTGDEEEEIK--QEINMLKKYShHRNIATYYGAFIKKNPPgmddql 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGD 2054
Cdd:cd06637    85 WLVMEFCGAGSVTDLIKNTK-----GNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLL-----TENAEVKLVD 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2055 FGLARDIYKNdyYRKRGEGLLPVRWMAPESLM-----DGIFTTQSDVWSFGILIWEI 2106
Cdd:cd06637   155 FGVSAQLDRT--VGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEM 209
fn3 pfam00041
Fibronectin type III domain;
206-283 1.64e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 1.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   206 APLIRNIESSSPDTVEVSWDPPQFPGGPILGYNLRLISKN-----QKLDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGE 280
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsgepwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81

                   ...
gi 767943404   281 GPE 283
Cdd:pfam00041   82 GPP 84
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
1903-2126 1.87e-10

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 64.27  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDIlgvGSGEI----KVAVKTLKKGSTDQ--EKIEFLKEAHlmskfNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd07832     8 IGEGAHGIVFK--AKDR---ETGETvalkKVALRKLEGGIPNQalREIKALQACQ-----GHPYVVKLRDVFPHGTGFVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMeGGDLLTYLRKARMAtFYGPLLTLVDLVdlcvdISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFG 2056
Cdd:cd07832    78 VFEYM-LSSLSEVLRDEERP-LTEAQVKRYMRM-----LLKGVAYMHANRIMHRDLKPANLLISSTG-----VLKIADFG 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2057 LARdIYKND----YYRKRGegllpVRW-MAPESLMDGIFTTQS-DVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd07832   146 LAR-LFSEEdprlYSHQVA-----TRWyRAPELLYGSRKYDEGvDLWAVGCIFAELLN-GSPLFPGENDIEQLAIV 214
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
1929-2163 2.24e-10

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 63.28  E-value: 2.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGS-TDQEKIEFLKEAHLMSKFNHPNILKQLGVCllNEPQY--IILELMEGGDLLTYLRKARmatfyGPLLTL 2005
Cdd:cd14057    21 IVAKILKVRDvTTRISRDFNEEYPRLRIFSHPNVLPVLGAC--NSPPNlvVISQYMPYGSLYNVLHEGT-----GVVVDQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2006 VDLVDLCVDISKGCVYLERMH-FIHR-DLAARNclVSVKDYTSPRIvKIGDFGLArdiykndyYRKRGEGLLPVrWMAPE 2083
Cdd:cd14057    94 SQAVKFALDIARGMAFLHTLEpLIPRhHLNSKH--VMIDEDMTARI-NMADVKFS--------FQEPGKMYNPA-WMAPE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2084 SLM---DGIFTTQSDVWSFGILIWEILTLgHQPYPAHSNLDV-LNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14057   162 ALQkkpEDINRRSADMWSFAILLWELVTR-EVPFADLSNMEIgMKIALEGLRVTIPPGISPHMCKLMKICMNEDPGKRPK 240

                  ....
gi 767943404 2160 FHRI 2163
Cdd:cd14057   241 FDMI 244
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
1890-2159 2.47e-10

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 63.48  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1890 PAFPREKLTLRLLLGSGAFGEVYEGTAvdilgvGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCL 1969
Cdd:cd14183     1 PASISERYKVGRTIGDGNFAVVKECVE------RSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 LNEPQYIILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsVKDYTSPRI 2049
Cdd:cd14183    75 MPTELYLVMELVKGGDLFDAITSTNKYT-------ERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLV-YEHQDGSKS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLArDIYKNDYYRKRGEgllPVrWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPYPAHSNLDVLNYVQT- 2128
Cdd:cd14183   147 LKLGDFGLA-TVVDGPLYTVCGT---PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRGSGDDQEVLFDQIl 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2129 GGRLEPPR----NCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14183   221 MGQVDFPSpywdNVSDSAKELITMMLQVDVDQRYS 255
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
1902-2122 2.90e-10

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 64.16  E-value: 2.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEK-IE-FLKEAHLMS-KFNHPnILKQLGVCLLN-EPQYII 1977
Cdd:cd05590     2 VLGKGSFGKVMLARLKE-----SGRL-YAVKVLKKDVILQDDdVEcTMTEKRILSlARNHP-FLTQLYCCFQTpDRLFFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd05590    75 MEFVNGGDLMFHIQKSRRfdearARFYA------------AEITSALMFLHDKGIIYRDLKLDNVLLDHEGH-----CKL 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGLlPvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDV 2122
Cdd:cd05590   138 ADFGMCKEGIFNGKTTSTFCGT-P-DYIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDL 204
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
1902-2166 4.00e-10

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 62.57  E-value: 4.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDIlgvgsgEIKVAVKTLKKGSTDQEKI--EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd14186     8 LLGKGSFACVYRARSLHT------GLEVAIKMIDKKAMQKAGMvqRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLrKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLAR 2059
Cdd:cd14186    82 MCHNGEMSRYL-KNRKKPF-----TEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLL-----TRNMNIKIADFGLAT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIYKND--YYRKRGEGllpvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTgGRLEPPRN 2137
Cdd:cd14186   151 QLKMPHekHFTMCGTP----NYISPEIATRSAHGLESDVWSLGCMFYTLLV-GRPPFDTDTVKNTLNKVVL-ADYEMPAF 224
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2138 CPDDLWNLMTQCWAQEPDQRPTFHRIQDQ 2166
Cdd:cd14186   225 LSREAQDLIHQLLRKNPADRLSLSSVLDH 253
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1899-2114 4.57e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 63.21  E-value: 4.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1899 LRLLLGSGAFGEVYEGTAVdilgvgSGEIKVAVK---TLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd14086     5 LKEELGKGAFSVVRRCVQK------STGQEFAAKiinTKKLSARDHQKLE--REARICRLLKHPNIVRLHDSISEEGFHY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLrKARmaTFYgplltLVDLVDLCV-DISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPriVKIGD 2054
Cdd:cd14086    77 LVFDLVTGGELFEDI-VAR--EFY-----SEADASHCIqQILESVNHCHQNGIVHRDLKPENLLLASKSKGAA--VKLAD 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIyKNDYYRKRGEGLLPVrWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPY 2114
Cdd:cd14086   147 FGLAIEV-QGDQQAWFGFAGTPG-YLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPF 203
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
1902-2108 5.35e-10

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 62.37  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLK----KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGvCLLNEPQ--- 1974
Cdd:cd06652     9 LLGQGAFGRVYLCYDAD-----TGR-ELAVKQVQfdpeSPETSKEVNALECEIQLLKNLLHERIVQYYG-CLRDPQErtl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLvsvKDYTSPriVKIGD 2054
Cdd:cd06652    82 SIFMEYMPGGSIKDQLKS------YGALTENVTRKYT-RQILEGVHYLHSNMIVHRDIKGANIL---RDSVGN--VKLGD 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2055 FGLARDIyknDYYRKRGEGLLPVR----WMAPESLMDGIFTTQSDVWSFGILIWEILT 2108
Cdd:cd06652   150 FGASKRL---QTICLSGTGMKSVTgtpyWMSPEVISGEGYGRKADIWSVGCTVVEMLT 204
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
1903-2163 6.10e-10

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 62.02  E-value: 6.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLKKG--STDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd14073     9 LGKGTYGKVKLAIERA-----TGR-EVAIKSIKKDkiEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLArd 2060
Cdd:cd14073    83 ASGGELYDYISERRRLP-------EREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN-----AKIADFGLS-- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 iyknDYYRKR-------GEGLlpvrWMAPEsLMDGI--FTTQSDVWSFGILIWeILTLGHQPYPAHSNLDVLNYVQTGGR 2131
Cdd:cd14073   149 ----NLYSKDkllqtfcGSPL----YASPE-IVNGTpyQGPEVDCWSLGVLLY-TLVYGTMPFDGSDFKRLVKQISSGDY 218
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767943404 2132 LEPPRncPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14073   219 REPTQ--PSDASGLIRWMLTVNPKRRATIEDI 248
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
1929-2147 6.82e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 63.36  E-value: 6.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGSTdqekiefLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGgDLLTYLRKaRMatfyGPLLTLVDL 2008
Cdd:PHA03209   94 VVLKIGQKGTT-------LIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTK-RS----RPLPIDQAL 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2009 vdlCVD--ISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLAR-DIYKNDYYRKRGEgllpVRWMAPESL 2085
Cdd:PHA03209  161 ---IIEkqILEGLRYLHAQRIIHRDVKTENIFINDVDQ-----VCIGDLGAAQfPVVAPAFLGLAGT----VETNAPEVL 228
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2086 MDGIFTTQSDVWSFGILIWEILTlghqpYPAhsnlDVLNYVQTGGRlEPPRNCPDDLWNLMT 2147
Cdd:PHA03209  229 ARDKYNSKADIWSAGIVLFEMLA-----YPS----TIFEDPPSTPE-EYVKSCHSHLLKIIS 280
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
1902-2116 7.51e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 62.68  E-value: 7.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegTAVDILGVGSgeiKVAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd05632     9 VLGKGGFGEV---CACQVRATGK---MYACKRLEKKRIKKRKGEsmALNEKQILEKVNSQFVVNLAYAYETKDALCLVLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLltylrKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkDYTSpriVKIGDFGLAR 2059
Cdd:cd05632    83 IMNGGDL-----KFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLD--DYGH---IRISDLGLAV 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2060 DIYKNDYYRKRgegLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPA 2116
Cdd:cd05632   153 KIPEGESIRGR---VGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPFRG 205
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
1902-2114 7.51e-10

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 62.65  E-value: 7.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVdilgvGSGEIkVAVKTLKKGST---DQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd05620     2 VLGKGSFGKVLLAELK-----GKGEY-FAVKALKKDVVlidDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLR-KARM----ATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIG 2053
Cdd:cd05620    76 EFLNGGDLMFHIQdKGRFdlyrATFYA------------AEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH-----IKIA 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2054 DFGLARDiykNDYYRKRGEGLLPV-RWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPY 2114
Cdd:cd05620   139 DFGMCKE---NVFGDNRASTFCGTpDYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPF 196
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1902-2166 8.68e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 61.67  E-value: 8.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDILGVgsgeikVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd08220     7 VVGRGAYGTVYLCRRKDDNKL------VIIKQIPvEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDytspRIVKIGDFGLARD 2060
Cdd:cd08220    81 APGGTLFEYIQQRK-----GSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKR----TVVKIGDFGISKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 I-YKNDYYRKRGEgllPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTLgHQPYPAhSNLDVLNYVQTGGRLEPPRN-C 2138
Cdd:cd08220   152 LsSKSKAYTVVGT---PC-YISPELCEGKPYNQKSDIWALGCVLYELASL-KRAFEA-ANLPALVLKIMRGTFAPISDrY 225
                         250       260
                  ....*....|....*....|....*...
gi 767943404 2139 PDDLWNLMTQCWAQEPDQRPTFHRIQDQ 2166
Cdd:cd08220   226 SEELRHLILSMLHLDPNKRPTLSEIMAQ 253
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
1896-2168 9.54e-10

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 61.91  E-value: 9.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1896 KLTLRLLLGSGAFGEVYEGTavdilgvGSGEikVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCLlNEPQ 1974
Cdd:cd14152     1 QIELGELIGQGRWGKVHRGR-------WHGE--VAIRLLEIDGNNQDHLKlFKKEVMNYRQTRHENVVLFMGACM-HPPH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 Y-IILELMEGGDLLTYLRKARMAtfygplLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPRIVkIG 2053
Cdd:cd14152    71 LaIITSFCKGRTLYSFVRDPKTS------LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-----YDNGKVV-IT 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGL--ARDIYKNDyyRKRGEGLLP-----------VRWMAPESLMDGI-FTTQSDVWSFGIlIWEILTLGHQPY---PA 2116
Cdd:cd14152   139 DFGLfgISGVVQEG--RRENELKLPhdwlcylapeiVREMTPGKDEDCLpFSKAADVYAFGT-IWYELQARDWPLknqPA 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2117 HSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14152   216 EALIWQIGSGEGMKQVLTTISLGKEVTEILSACWAFDLEERPSFTLLMDMLE 267
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
1903-2114 9.56e-10

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 61.80  E-value: 9.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGvgsgeiKVAVKTLKK--GSTDQEKIEFLKEAHLMSKFNHPNILKQLGVC-LLNEPQYIILE 1979
Cdd:cd14164     8 IGEGSFSKVKLATSQKYCC------KVAIKIVDRrrASPDFVQKFLPRELSILRRVNHPNIVQMFECIeVANGRLYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGgDLLTYLRKARMatfygplltlvdlvdLCVDISK-------GCV-YLERMHFIHRDLAARNCLVSVKDytspRIVK 2051
Cdd:cd14164    82 AAAT-DLLQKIQEVHH---------------IPKDLARdmfaqmvGAVnYLHDMNIVHRDLKCENILLSADD----RKIK 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2052 IGDFGLARDIykNDYYRKRGEGLLPVRWMAPESLMDGIFTTQS-DVWSFGILIWEILTlGHQPY 2114
Cdd:cd14164   142 IADFGFARFV--EDYPELSTTFCGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPF 202
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
1902-2126 9.57e-10

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 62.05  E-value: 9.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQE--KIEFlKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd07846     8 LVGEGSYGMVMKCRHKE-----TGQI-VAIKKFLESEDDKMvkKIAM-REIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGgDLLTYLRKARMATFYgplltlVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLAR 2059
Cdd:cd07846    81 FVDH-TVLDDLEKYPNGLDE------SRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVS-----QSGVVKLCDFGFAR 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2060 ------DIYkNDYyrkrgeglLPVRWM-APESLM-DGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd07846   149 tlaapgEVY-TDY--------VATRWYrAPELLVgDTKYGKAVDVWAVGCLVTEMLT-GEPLFPGDSDIDQLYHI 213
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
1901-2114 9.80e-10

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 62.71  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1901 LLLGSGAFGEVYEGTAVdilgvGSGEIkVAVKTLKKGSTDQEK-IE-FLKEAHLMSKFNHPNILKQLGVCLLN-EPQYII 1977
Cdd:cd05615    16 MVLGKGSFGKVMLAERK-----GSDEL-YAIKILKKDVVIQDDdVEcTMVEKRVLALQDKPPFLTQLHSCFQTvDRLYFV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLR-----KARMATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd05615    90 MEYVNGGDLMYHIQqvgkfKEPQAVFYA------------AEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH-----IKI 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd05615   153 ADFGMCKEHMVEGVTTRTFCG--TPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPF 211
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
206-281 1.48e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.47  E-value: 1.48e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404    206 APLIRNIESSSPDTVEVSWDPPQFPG--GPILGYNLRLISKN---QKLDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGE 280
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82

                    .
gi 767943404    281 G 281
Cdd:smart00060   83 G 83
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1903-2159 1.53e-09

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 61.37  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNI-------LKQLGVCLlnepqY 1975
Cdd:cd14049    14 LGKGGYGKVYK--VRNKL---DGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIvgyhtawMEHVQLML-----Y 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMATFYGplltLVDLVDLCVDIS----------KGCVYLERMHFIHRDLAARNCLVSVKDYT 2045
Cdd:cd14049    84 IQMQLCELSLWDWIVERNKRPCEEE----FKSAPYTPVDVDvttkilqqllEGVTYIHSMGIVHRDLKPRNIFLHGSDIH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2046 spriVKIGDFGLA-RDIYKND-----YYRKRG----EGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILtlghQPYP 2115
Cdd:cd14049   160 ----VRIGDFGLAcPDILQDGndsttMSRLNGlthtSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF----QPFG 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2116 AH-SNLDVLNYVQTGgrlepprNCPDDL---W----NLMTQCWAQEPDQRPT 2159
Cdd:cd14049   232 TEmERAEVLTQLRNG-------QIPKSLckrWpvqaKYIKLLTSTEPSERPS 276
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
1903-2117 1.75e-09

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 60.76  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdILGVGSGEiKVAVKTLKkgstDQEKIEFLKEAHLMSKfNHPNILKQLGV---------CLLnep 1973
Cdd:cd14089     9 LGLGINGKVLE-----CFHKKTGE-KFALKVLR----DNPKARREVELHWRAS-GCPHIVRIIDVyentyqgrkCLL--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 qyIILELMEGGDLLTYLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPR---IV 2050
Cdd:cd14089    75 --VVMECMEGGELFSRIQERADSAF-----TEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLL-----YSSKGpnaIL 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2051 KIGDFGLARDIYKND---------YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQP-YPAH 2117
Cdd:cd14089   143 KLTDFGFAKETTTKKslqtpcytpYY------------VAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPfYSNH 206
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
1903-2108 1.82e-09

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 61.93  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVyeGTAVDilgvGSGEIKVAVKTLkkgSTDQEKIEFLK----EAHLMSKFNHPNIlkqlgVCLLN--EPQ-- 1974
Cdd:cd07851    23 VGSGAYGQV--CSAFD----TKTGRKVAIKKL---SRPFQSAIHAKrtyrELRLLKHMKHENV-----IGLLDvfTPAss 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 -------YIILELMeGGDLLTYLRKARMAT------FYgplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSv 2041
Cdd:cd07851    89 ledfqdvYLVTHLM-GADLNNIVKCQKLSDdhiqflVY--------------QILRGLKYIHSAGIIHRDLKPSNLAVN- 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2042 KDYTspriVKIGDFGLARdiyKNDyyrKRGEGLLPVRW-MAPESLMDGIFTTQS-DVWSFGILIWEILT 2108
Cdd:cd07851   153 EDCE----LKILDFGLAR---HTD---DEMTGYVATRWyRAPEIMLNWMHYNQTvDIWSVGCIMAELLT 211
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1903-2163 1.87e-09

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 61.04  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEG-TAVDilgvgsgEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ------- 1974
Cdd:cd14048    14 LGRGGFGVVFEAkNKVD-------DCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLERPPEgwqekmd 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 ----YIILELMEGGDLLTYLRkarmatfyGPLLTLVDLVDLCVDI----SKGCVYLERMHFIHRDLAARNCLVSVKDyts 2046
Cdd:cd14048    87 evylYIQMQLCRKENLKDWMN--------RRCTMESRELFVCLNIfkqiASAVEYLHSKGLIHRDLKPSNVFFSLDD--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2047 prIVKIGDFGLARDIYKN----------DYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEIL-TLGHQPYP 2115
Cdd:cd14048   156 --VVKVGDFGLVTAMDQGepeqtvltpmPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIySFSTQMER 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2116 AHSNLDVLNyvqtggrLEPP----RNCPDDlWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14048   234 IRTLTDVRK-------LKFPalftNKYPEE-RDMVQQMLSPSPSERPEAHEV 277
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1903-2166 1.92e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 60.52  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGE--VYEGTAVDILGVGSgEIkvavkTLKKGStDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd08221     8 LGRGAFGEavLYRKTEDNSLVVWK-EV-----NLSRLS-EKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARD 2060
Cdd:cd08221    81 CNGGNLHDKIAQQKNQLF-----PEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFL-----TKADLVKLGDFGISKV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IykNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLgHQPYPAHSNLDVLNYVQTGGRLEPPRNCPD 2140
Cdd:cd08221   151 L--DSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTL-KRTFDATNPLRLAVKIVQGEYEDIDEQYSE 227
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2141 DLWNLMTQCWAQEPDQRPTFHRIQDQ 2166
Cdd:cd08221   228 EIIQLVHDCLHQDPEDRPTAEELLER 253
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
1903-2118 1.94e-09

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 60.74  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVY---EGTAVDILgvgsgeikvAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQYII 1977
Cdd:cd14116    13 LGKGKFGNVYlarEKQSKFIL---------ALKVLFKAQLEKAGVEhqLRREVEIQSHLRHPNILRLYGYFHDATRVYLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRK------ARMATFygplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVK 2051
Cdd:cd14116    84 LEYAPLGTVYRELQKlskfdeQRTATY-------------ITELANALSYCHSKRVIHRDIKPENLLLG-----SAGELK 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2052 IGDFGLArdIYKNDYYRKRGEGLLPvrWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAHS 2118
Cdd:cd14116   146 IADFGWS--VHAPSSRRTTLCGTLD--YLPPEMIEGRMHDEKVDLWSLGVLCYEFL-VGKPPFEANT 207
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
1902-2114 2.23e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 60.81  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegTAVDILGVGSgeiKVAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd05630     7 VLGKGGFGEV---CACQVRATGK---MYACKKLEKKRIKKRKGEamALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMATFYGPLLTLVDLVDLCvdiskGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLAR 2059
Cdd:cd05630    81 LMNGGDLKFHIYHMGQAGFPEARAVFYAAEICC-----GLEDLHRERIVYRDLKPENILLDDHGH-----IRISDLGLAV 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2060 DIYKNDYYRKRgegLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd05630   151 HVPEGQTIKGR---VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPF 201
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1926-2139 2.42e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 61.30  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1926 EIKVAVKTlkkgstdqekiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARM--ATFYGPLL 2003
Cdd:cd06615    37 EIKPAIRN-----------QIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRipENILGKIS 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2004 tlvdlvdlcVDISKGCVYLERMH-FIHRDLAARNCLVSvkdytSPRIVKIGDFGLAR---DIYKNDYYRKRGegllpvrW 2079
Cdd:cd06615   106 ---------IAVLRGLTYLREKHkIMHRDVKPSNILVN-----SRGEIKLCDFGVSGqliDSMANSFVGTRS-------Y 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2080 MAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLD---VLNYVQTGGRLEPPRNCP 2139
Cdd:cd06615   165 MSPERLQGTHYTVQSDIWSLGLSLVEMAI-GRYPIPPPDAKEleaMFGRPVSEGEAKESHRPV 226
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
1903-2170 2.55e-09

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 60.57  E-value: 2.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGtavdiLGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd07836     8 LGEGTYATVYKG-----RNRTTGEI-VALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GgDLLTYlrkarMATFYGPLLTLVDLVDLCV-DISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARDI 2061
Cdd:cd07836    82 K-DLKKY-----MDTHGVRGALDPNTVKSFTyQLLKGIAFCHENRVLHRDLKPQNLLINKRGE-----LKLADFGLARAF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 ------YKND----YYRkrgegllpvrwmAPESLMDG-IFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNyvqtgg 2130
Cdd:cd07836   151 gipvntFSNEvvtlWYR------------APDVLLGSrTYSTSIDIWSVGCIMAEMIT-GRPLFPGTNNEDQLL------ 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767943404 2131 RLEPPRNCPDD-LWNLMTQCwaqePDQRPTFHRI--QDQLQLF 2170
Cdd:cd07836   212 KIFRIMGTPTEsTWPGISQL----PEYKPTFPRYppQDLQQLF 250
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
1929-2114 2.64e-09

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 61.16  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGSTDQEKIEFL-KEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGG---DLltylrkarMATFYGPLLT 2004
Cdd:cd08216    28 VAVKKINLESDSKEDLKFLqQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGscrDL--------LKTHFPEGLP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2005 LVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKdytspRIVKIGDFGLARDIYKNDyYRKRGEGLLPVR------ 2078
Cdd:cd08216   100 ELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGD-----GKVVLSGLRYAYSMVKHG-KRQRVVHDFPKSseknlp 173
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767943404 2079 WMAPESLMDGI--FTTQSDVWSFGILIWEiLTLGHQPY 2114
Cdd:cd08216   174 WLSPEVLQQNLlgYNEKSDIYSVGITACE-LANGVVPF 210
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
1899-2107 2.71e-09

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 61.17  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1899 LRLLLGSGAFGEVY---EGTAVDILgvgsgeikvAVKTLKKGST-DQEKIEFLKEAH-LMSKFNHPNILKQLGVCLLNEP 1973
Cdd:cd05601     5 VKNVIGRGHFGEVQvvkEKATGDIY---------AMKVLKKSETlAQEEVSFFEEERdIMAKANSPWITKLQYAFQDSEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRK------ARMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtsp 2047
Cdd:cd05601    76 LYLVMEYHPGGDLLSLLSRyddifeESMARFY------------LAELVLAIHSLHSMGYVHRDIKPENILIDRTGH--- 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2048 riVKIGDFGLARDIYKNDYYRKRgeglLPV---RWMAPESL--MDGIFT----TQSDVWSFGILIWEIL 2107
Cdd:cd05601   141 --IKLADFGSAAKLSSDKTVTSK----MPVgtpDYIAPEVLtsMNGGSKgtygVECDWWSLGIVAYEML 203
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1902-2160 2.92e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 60.85  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEFLKEAHLMSK-FNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd06618    22 EIGSGTCGQVYKMRHKK-----TGHV-MAVKQMRRSGNKEENKRILMDLDVVLKsHDCPYIVKCYGYFITDSDVFICMEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MegGDLLTYLRKaRMatfYGPLLTLVDLVDLcVDISKGCVYLERMH-FIHRDLAARNCLVSvkdytSPRIVKIGDFGLA- 2058
Cdd:cd06618    96 M--STCLDKLLK-RI---QGPIPEDILGKMT-VSIVKALHYLKEKHgVIHRDVKPSNILLD-----ESGNVKLCDFGISg 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2059 RDIykNDYYRKRGEGLLPvrWMAPESL---MDGIFTTQSDVWSFGILIWEILTlGHQPYP-AHSNLDVLNYVQtggRLEP 2134
Cdd:cd06618   164 RLV--DSKAKTRSAGCAA--YMAPERIdppDNPKYDIRADVWSLGISLVELAT-GQFPYRnCKTEFEVLTKIL---NEEP 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2135 PRNCPD-----DLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd06618   236 PSLPPNegfspDFCSFVDLCLTKDHRYRPKY 266
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
1930-2109 2.95e-09

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 60.49  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1930 AVKTLKK------GSTDQEKIEFlkEAHLMSKFNHPNI--------LKQLGVCLLnepqyiilelME-GGDLLTYLRKAR 1994
Cdd:cd14001    32 AVKKINSkcdkgqRSLYQERLKE--EAKILKSLNHPNIvgfraftkSEDGSLCLA----------MEyGGKSLNDLIEER 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1995 MATFYGPLLTLVDLVDLcVDISKGCVYLermHF----IHRDLAARNCLVSvKDYtspRIVKIGDFGLARDIYKNDYYRKR 2070
Cdd:cd14001   100 YEAGLGPFPAATILKVA-LSIARALEYL---HNekkiLHGDIKSGNVLIK-GDF---ESVKLCDFGVSLPLTENLEVDSD 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767943404 2071 GE----GLLPvrWMAPESLM-DGIFTTQSDVWSFGILIWEILTL 2109
Cdd:cd14001   172 PKaqyvGTEP--WKAKEALEeGGVITDKADIFAYGLVLWEMMTL 213
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
1903-2163 3.13e-09

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 60.09  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDilgvGSGEIKVAVKTLKKgstdqEKI------------EFLKEAHLMS---KFNHPNILKQLGV 1967
Cdd:cd14004     8 MGEGAYGQVN--LAIY----KSKGKEVVIKFIFK-----ERIlvdtwvrdrklgTVPLEIHILDtlnKRSHPNIVKLLDF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1968 CLLNEPQYIILELM-EGGDLLTYL-RKARMATFYGPLLTlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYt 2045
Cdd:cd14004    77 FEDDEFYYLVMEKHgSGMDLFDFIeRKPNMDEKEAKYIF--------RQVADAVKHLHDQGIVHRDIKDENVILDGNGT- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2046 spriVKIGDFGLARDIYKNDYYRKRGEgllpVRWMAPESLMDGIFTTQS-DVWSFGILIWEILtLGHQPYpahSNLD-VL 2123
Cdd:cd14004   148 ----IKLIDFGSAAYIKSGPFDTFVGT----IDYAAPEVLRGNPYGGKEqDIWALGVLLYTLV-FKENPF---YNIEeIL 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767943404 2124 NyvqtgGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14004   216 E-----ADLRIPYAVSEDLIDLISRMLNRDVGDRPTIEEL 250
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
1903-2114 3.47e-09

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 60.19  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilgvGSGEIKVAVKTLKKGST-------DQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd14105    13 LGSGQFAVVKKCRE------KSTGLEYAAKFIKKRRSkasrrgvSREDIE--REVSILRQVLHPNIITLHDVFENKTDVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIvKIGDF 2055
Cdd:cd14105    85 LILELVAGGELFDFLAEKESLS-------EEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPRI-KLIDF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDI-YKNDYYRKRGEgllPvRWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPY 2114
Cdd:cd14105   157 GLAHKIeDGNEFKNIFGT---P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPF 211
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
1903-2107 3.59e-09

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 59.97  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvDILGVgsgeiKVAVKTLK----KGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd14079    10 LGVGSFGKVKLAEH-ELTGH-----KVAVKILNrqkiKSLDMEEKIR--REIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYL-RKARMAT-----FYGplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKI 2052
Cdd:cd14079    82 EYVSGGELFDYIvQKGRLSEdearrFFQ-------------QIISGVEYCHRHMVVHRDLKPENLLL-----DSNMNVKI 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2053 GDFGLArDIYKNDYYRKRGEGlLPvRWMAPE----SLMDGiftTQSDVWSFGILIWEIL 2107
Cdd:cd14079   144 ADFGLS-NIMRDGEFLKTSCG-SP-NYAAPEvisgKLYAG---PEVDVWSCGVILYALL 196
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
1902-2108 4.73e-09

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 59.32  E-value: 4.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTA-VDilgvgsGEIKVAVKTLKKGSTDQEKIEFLKE--AHLMSKFnHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd13997     7 QIGSGSFSEVFKVRSkVD------GCLYAVKKSKKPFRGPKERARALREveAHAALGQ-HPNIVRYYSSWEEGGHLYIQM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDL---------LTYLRKARMATFYgplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprI 2049
Cdd:cd13997    80 ELCENGSLqdaleelspISKLSEAEVWDLL-------------LQVALGLAFIHSKGIVHLDIKPDNIFISNKG-----T 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKNDYYRKrGEGllpvRWMAPESLMD-GIFTTQSDVWSFGILIWEILT 2108
Cdd:cd13997   142 CKIGDFGLATRLETSGDVEE-GDS----RYLAPELLNEnYTHLPKADIFSLGVTVYEAAT 196
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
1895-2114 4.83e-09

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 60.07  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEgtAVDILGVGSGEIKvaVKTLKKGSTDQEKIEFLKEA----HLMSKFNHPNILKQLGVCLL 1970
Cdd:cd14040     6 ERYLLLHLLGRGGFSEVYK--AFDLYEQRYAAVK--IHQLNKSWRDEKKENYHKHAcreyRIHKELDHPRIVKLYDYFSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQY-IILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMH--FIHRDLAARNCLVSvkDYTSP 2047
Cdd:cd14040    82 DTDTFcTVLEYCEGNDLDFYLKQHKLMS-------EKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLV--DGTAC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2048 RIVKIGDFGLAR----DIYKNDYYRKRGEGLLPVRWMAPESLMDG----IFTTQSDVWSFGILIWEILtLGHQPY 2114
Cdd:cd14040   153 GEIKITDFGLSKimddDSYGVDGMDLTSQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPF 226
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
1902-2156 4.91e-09

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 60.04  E-value: 4.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyEGTavdiLGVGSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14174     9 LLGEGAYAKV-QGC----VSLQNGK-EYAVKIIEKNAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARmatfygpLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPriVKIGDFGLARDI 2061
Cdd:cd14174    83 RGGSILAHIQKRK-------HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSP--VKICDFDLGSGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYR--KRGEGLLP---VRWMAPESLMdgIFTTQS-------DVWSFGILIWeILTLGHQPYPAHSNLDVlnyvqTG 2129
Cdd:cd14174   154 KLNSACTpiTTPELTTPcgsAEYMAPEVVE--VFTDEAtfydkrcDLWSLGVILY-IMLSGYPPFVGHCGTDC-----GW 225
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2130 GRLEPPRNCPDDLWNLMTQCWAQEPDQ 2156
Cdd:cd14174   226 DRGEVCRVCQNKLFESIQEGKYEFPDK 252
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
1886-2159 5.13e-09

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 60.01  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1886 IENLPAfPREKLTLRLLLGSGAFGEVYEgtavdILGVGSGEIkVAVKTLKKGSTDQEKIEflKEAHLMSKF-NHPNILKQ 1964
Cdd:cd06639    14 LESLAD-PSDTWDIIETIGKGTYGKVYK-----VTNKKDGSL-AAVKILDPISDVDEEIE--AEYNILRSLpNHPNVVKF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1965 LGVcLLNEPQYI------ILELMEGGDLlTYLRKARMATfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCL 2038
Cdd:cd06639    85 YGM-FYKADQYVggqlwlVLELCNGGSV-TELVKGLLKC--GQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2039 VsvkdyTSPRIVKIGDFGLARDIYKNDYYRKRGEGlLPVrWMAPESLM-----DGIFTTQSDVWSFGILIWEiLTLGHQP 2113
Cdd:cd06639   161 L-----TTEGGVKLVDFGVSAQLTSARLRRNTSVG-TPF-WMAPEVIAceqqyDYSYDARCDVWSLGITAIE-LADGDPP 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2114 ypahsnLDVLNYVQTGGRLepPRNCPDDLWN----------LMTQCWAQEPDQRPT 2159
Cdd:cd06639   233 ------LFDMHPVKALFKI--PRNPPPTLLNpekwcrgfshFISQCLIKDFEKRPS 280
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
1903-2107 5.96e-09

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 60.07  E-value: 5.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDilgVGSGEiKVAVKTLKKGS-TDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ------Y 1975
Cdd:cd07855    13 IGSGAYGVVCS--AID---TKSGQ-KVAIKKIPNAFdVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYadfkdvY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGgDL--LTY----LRKARMATFYGplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspri 2049
Cdd:cd07855    87 VVLDLMES-DLhhIIHsdqpLTLEHIRYFLY-------------QLLRGLKYIHSANVIHRDLKPSNLLVN-ENCE---- 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2050 VKIGDFGLARDIYKND----YYRKRGEGLLPVRwmAPESL--MDGiFTTQSDVWSFGILIWEIL 2107
Cdd:cd07855   148 LKIGDFGMARGLCTSPeehkYFMTEYVATRWYR--APELMlsLPE-YTQAIDMWSVGCIFAEML 208
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
1903-2129 6.66e-09

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 58.78  E-value: 6.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDIlgvGSGEIKVA--VKTLKKgstdQEKIEFLKEAHLMSKFNHPNILkQL--------GVCLlne 1972
Cdd:cd14103     1 LGRGKFGTVY--RCVEK---ATGKELAAkfIKCRKA----KDREDVRNEIEIMNQLRHPRLL-QLydafetprEMVL--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 pqyiILELMEGGDL----------LT------YLRKarmatfygplltlvdlvdlcvdISKGCVYLERMHFIHRDLAARN 2036
Cdd:cd14103    68 ----VMEYVAGGELfervvdddfeLTerdcilFMRQ----------------------ICEGVQYMHKQGILHLDLKPEN 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2037 CLVSVKdyTSPRIvKIGDFGLARdiykndyyRKRGEGLLPVRW-----MAPESLMDGIFTTQSDVWSFGIlIWEILTLGH 2111
Cdd:cd14103   122 ILCVSR--TGNQI-KIIDFGLAR--------KYDPDKKLKVLFgtpefVAPEVVNYEPISYATDMWSVGV-ICYVLLSGL 189
                         250
                  ....*....|....*...
gi 767943404 2112 QPYPAHSNLDVLNYVQTG 2129
Cdd:cd14103   190 SPFMGDNDAETLANVTRA 207
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
1903-2157 6.74e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 59.46  E-value: 6.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtAVDILGVGSgeiKVAVKTLKKGSTDQEKIE--FLKEAHLMSKFNHPNIlkqlgVCL---LNEPQYI- 1976
Cdd:cd05577     1 LGRGGFGEVC---ACQVKATGK---MYACKKLDKKRIKKKKGEtmALNEKIILEKVSSPFI-----VSLayaFETKDKLc 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 -ILELMEGGDLLTYLRKARMATFYGPLLTLVDLVDLCvdiskGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDF 2055
Cdd:cd05577    70 lVLTLMNGGDLKYHIYNVGTRGFSEARAIFYAAEIIC-----GLEHLHNRFIVYRDLKPENILLDDHGH-----VRISDL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDIYKNDYYRKRGEgllPVRWMAPESLMDGI-FTTQSDVWSFGILIWEILTlGHQPYPAH----SNLDVLNYVQTGG 2130
Cdd:cd05577   140 GLAVEFKGGKKIKGRVG---THGYMAPEVLQKEVaYDFSVDWFALGCMLYEMIA-GRSPFRQRkekvDKEELKRRTLEMA 215
                         250       260
                  ....*....|....*....|....*..
gi 767943404 2131 RLEPPRNCPdDLWNLMTQCWAQEPDQR 2157
Cdd:cd05577   216 VEYPDSFSP-EARSLCEGLLQKDPERR 241
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
1902-2124 8.15e-09

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 58.77  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVdilgvgSGEIKVAVKTLKKGSTdQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14193    11 ILGGGRFGQVHKCEEK------SSGLKLAAKIIKARSQ-KEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLL------TY-LRKARMATFYGplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSpriVKIGD 2054
Cdd:cd14193    84 DGGELFdriideNYnLTELDTILFIK-------------QICEGIQYMHQMYILHLDLKPENILCVSREANQ---VKIID 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDiYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLN 2124
Cdd:cd14193   148 FGLARR-YKPREKLRVNFG--TPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLS-GLSPFLGEDDNETLN 213
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
1905-2165 8.44e-09

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 59.15  E-value: 8.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1905 SGAFGEVY---EGTAVDIlgvgsgeikVAVKTLKKGSTDQE--KIEFLKEAHLMSKFNHPNILKqLGVCLLNE-PQYIIL 1978
Cdd:cd05579     3 RGAYGRVYlakKKSTGDL---------YAIKVIKKRDMIRKnqVDSVLAERNILSQAQNPFVVK-LYYSFQGKkNLYLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRK-----ARMATFYgplltlvdlvdlcvdISKGCVYLERMH---FIHRDLAARNCLVsvkdyTSPRIV 2050
Cdd:cd05579    73 EYLPGGDLYSLLENvgaldEDVARIY---------------IAEIVLALEYLHshgIIHRDLKPDNILI-----DANGHL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2051 KIGDFGLARDIYKNDYYRKRGEGLLPVR-------------WMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAH 2117
Cdd:cd05579   133 KLTDFGLSKVGLVRRQIKLSIQKKSNGApekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLV-GIPPFHAE 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767943404 2118 SNLDVLNYVQTgGRLEPPR--NCPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd05579   212 TPEEIFQNILN-GKIEWPEdpEVSDEAKDLISKLLTPDPEKRLGAKGIEE 260
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
1903-2128 8.93e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 60.03  E-value: 8.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGVgsgeikVAVKTL-KKGSTDQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd05626     9 LGIGAFGEVCLACKVDTHAL------YAMKTLrKKDVLNRNQVAHVKaERDILAEADNEWVVKLYYSFQDKDNLYFVMDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRK-----ARMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDF 2055
Cdd:cd05626    83 IPGGDMMSLLIRmevfpEVLARFY------------IAELTLAIESVHKMGFIHRDIKPDNILIDLDGH-----IKLTDF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLA---RDIYKNDYYRK----RGEGLLPV--------------------------------------RWMAPESLMDGIF 2090
Cdd:cd05626   146 GLCtgfRWTHNSKYYQKgshiRQDSMEPSdlwddvsncrcgdrlktleqratkqhqrclahslvgtpNYIAPEVLLRKGY 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2091 TTQSDVWSFGILIWEILtLGHQPY----PAHSNLDVLNYVQT 2128
Cdd:cd05626   226 TQLCDWWSVGVILFEML-VGQPPFlaptPTETQLKVINWENT 266
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
1903-2108 9.32e-09

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 59.79  E-value: 9.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDilgvGSGEIKVAVKtlKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCL-----LNEPQ-- 1974
Cdd:cd07854    13 LGCGSNGLVF--SAVD----SDCDKRVAVK--KIVLTDPQSVKhALREIKIIRRLDHDNIVKVYEVLGpsgsdLTEDVgs 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 -------YIILELMEGgDLLTYLRKARMATFYgplltlvdLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtsp 2047
Cdd:cd07854    85 ltelnsvYIVQEYMET-DLANVLEQGPLSEEH--------ARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDL--- 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2048 rIVKIGDFGLARdIYKNDYYRK--RGEGLLPVRWMAPESLMDGIFTTQS-DVWSFGILIWEILT 2108
Cdd:cd07854   153 -VLKIGDFGLAR-IVDPHYSHKgyLSEGLVTKWYRSPRLLLSPNNYTKAiDMWAAGCIFAEMLT 214
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
1897-2119 9.53e-09

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 58.96  E-value: 9.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTAVDILgvgsgeIKVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGV--CLLNEP 1973
Cdd:cd14031    12 LKFDIELGRGAFKTVYKGLDTETW------VEVAWCELQdRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSweSVLKGK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIIL--ELMEGGDLLTYLRKARMatfygplLTLVDLVDLCVDISKGCVYLERMH--FIHRDLAARNCLVsvkdyTSPR- 2048
Cdd:cd14031    86 KCIVLvtELMTSGTLKTYLKRFKV-------MKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI-----TGPTg 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2049 IVKIGDFGLArDIYKNDYYRKRgegLLPVRWMAPEsLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSN 2119
Cdd:cd14031   154 SVKIGDLGLA-TLMRTSFAKSV---IGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMAT-SEYPYSECQN 218
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
1898-2117 1.11e-08

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 58.91  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1898 TLRL--LLGSGAFGEVYegtAVDILGVGSgeiKVAVKTLKKGSTDQEKIEF--LKEAHLMSKFNHPNILK-------QLG 1966
Cdd:cd05605     1 TFRQyrVLGKGGFGEVC---ACQVRATGK---MYACKKLEKKRIKKRKGEAmaLNEKQILEKVNSRFVVSlayayetKDA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1967 VCLlnepqyiILELMEGGDLltylrKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkDYTS 2046
Cdd:cd05605    75 LCL-------VLTIMNGGDL-----KFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLD--DHGH 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2047 priVKIGDFGLARDIYKNDYYRKRgegLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAH 2117
Cdd:cd05605   141 ---VRISDLGLAVEIPEGETIRGR---VGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIE-GQAPFRAR 204
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
2017-2170 1.20e-08

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 59.05  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2017 KGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIVkIGDFG--LARDI------YKNDYYRKRGEGLLpvrwMAPE--SLM 2086
Cdd:cd14018   149 EGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLV-IADFGccLADDSiglqlpFSSWYVDRGGNACL----MAPEvsTAV 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2087 DGIFT----TQSDVWSFGILIWEILTLGHqPYPAHSNLDVLNYVQTGGRLEP-PRNCPDDLWNLMTQCWAQEPDQRPTFH 2161
Cdd:cd14018   224 PGPGVvinySKADAWAVGAIAYEIFGLSN-PFYGLGDTMLESRSYQESQLPAlPSAVPPDVRQVVKDLLQRDPNKRVSAR 302

                  ....*....
gi 767943404 2162 RIQDQLQLF 2170
Cdd:cd14018   303 VAANVLHLS 311
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
1900-2168 1.27e-08

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 58.50  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1900 RLLLGSGAFGEVYEGTAvdilgVGSGeIKVAVKTLKKGSTDQEKiEFLKEAHLMSKF-NHPNIlkqlgVCLL------NE 1972
Cdd:cd13985     5 TKQLGEGGFSYVYLAHD-----VNTG-RRYALKRMYFNDEEQLR-VAIKEIEIMKRLcGHPNI-----VQYYdsailsSE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELME--GGDLLTYLRKarmaTFYGPLLTLVDLVDLCvDISKGcvyLERMH-----FIHRDLAARNCLvsvkdYT 2045
Cdd:cd13985    73 GRKEVLLLMEycPGSLVDILEK----SPPSPLSEEEVLRIFY-QICQA---VGHLHsqsppIIHRDIKIENIL-----FS 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2046 SPRIVKIGDFGLARDIYKnDYYRKRGEGLLPVRW--------MAPESL---MDGIFTTQSDVWSFGILIWEILTLGHqPY 2114
Cdd:cd13985   140 NTGRFKLCDFGSATTEHY-PLERAEEVNIIEEEIqknttpmyRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKL-PF 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2115 PAHSNLDVL--NYvqtggRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd13985   218 DESSKLAIVagKY-----SIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIIT 268
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
1903-2163 1.42e-08

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 58.08  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilgvGSGEIKVAVKTLKKGSTDQEKIE-FL-KEAHLMSKFNHPNILKQLGVCLLNEPQ-YIILE 1979
Cdd:cd14163     8 IGEGTYSKVKEAFS------KKHQRKVAIKIIDKSGGPEEFIQrFLpRELQIVERLDHKNIIHVYEMLESADGKiYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTY------LRKARMATFYgplltlvDLVDLCVDISKGCvylermHFIHRDLAARNCLVSVKDytspriVKIG 2053
Cdd:cd14163    82 LAEDGDVFDCvlhggpLPEHRAKALF-------RQLVEAIRYCHGC------GVAHRDLKCENALLQGFT------LKLT 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNdyYRKRGEGLL-PVRWMAPEsLMDGI--FTTQSDVWSFGILIWeILTLGHQPYPAHSNLDVLNYVQTG- 2129
Cdd:cd14163   143 DFGFAKQLPKG--GRELSQTFCgSTAYAAPE-VLQGVphDSRKGDIWSMGVVLY-VMLCAQLPFDDTDIPKMLCQQQKGv 218
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2130 ---GRLEPPRNCPDDLWNLMtqcwaqEPDQ--RPTFHRI 2163
Cdd:cd14163   219 slpGHLGVSRTCQDLLKRLL------EPDMvlRPSIEEV 251
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
1903-2108 1.44e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 58.66  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEIkVAvktLKKGSTDQEK----IEFLKEAHLMSKFNHPNIL--------KQLGVCLL 1970
Cdd:cd07864    15 IGEGTYGQVYK--AKDKD---TGEL-VA---LKKVRLDNEKegfpITAIREIKILRQLNHRSVVnlkeivtdKQDALDFK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQ--YIILELMEGgDLLTYLrKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspr 2048
Cdd:cd07864    86 KDKGafYLVFEYMDH-DLMGLL-ESGLVHF-----SEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQ---- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2049 iVKIGDFGLARdIYKNDYYRKRGEGLLPVRWMAPESLM-DGIFTTQSDVWSFGILIWEILT 2108
Cdd:cd07864   155 -IKLADFGLAR-LYNSEESRPYTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFT 213
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
1903-2078 1.56e-08

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 58.04  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDilgVGSGEiKVAVKTLKKGSTDQekieFLK-EAHlmskfnhpnILKQL----GVCLL----NEP 1973
Cdd:cd14017     8 IGGGGFGEIYK--VRD---VVDGE-EVAMKVESKSQPKQ----VLKmEVA---------VLKKLqgkpHFCRLigcgRTE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QY--IILELMeGGDLLTYLRKARMATFygplltlvdlvdlcvdiSKGCVY---------LERMH---FIHRDLAARNCLV 2039
Cdd:cd14017    69 RYnyIVMTLL-GPNLAELRRSQPRGKF-----------------SVSTTLrlgiqilkaIEDIHevgFLHRDVKPSNFAI 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767943404 2040 SVKDYTSpRIVKIGDFGLARdiyknDYYRKRGEGLLPVR 2078
Cdd:cd14017   131 GRGPSDE-RTVYILDFGLAR-----QYTNKDGEVERPPR 163
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
1903-2165 1.58e-08

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 59.28  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQ--EKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd05600    19 VGQGGYGSVFLARKKD-----TGEI-CALKIMKKKVLFKlnEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLR-----KARMATFYgplltlvdLVDLCVDISKgcvyLERMHFIHRDLAARNCLVSVKDYtspriVKIGDF 2055
Cdd:cd05600    93 VPGGDFRTLLNnsgilSEEHARFY--------IAEMFAAISS----LHQLGYIHRDLKPENFLIDSSGH-----IKLTDF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLA--------------------------------RDIYKNdyYRKRGEGLL-----PVRWMAPESLMDGIFTTQSDVWS 2098
Cdd:cd05600   156 GLAsgtlspkkiesmkirleevkntafleltakerRNIYRA--MRKEDQNYAnsvvgSPDYMAPEVLRGEGYDLTVDYWS 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2099 FGILIWEILTlGHQPYPAHSNLDVLNY-----------VQTGGRLEPprNCPDDLWNLMTQCWAQEPDQrptFHRIQD 2165
Cdd:cd05600   234 LGCILFECLV-GFPPFSGSTPNETWANlyhwkktlqrpVYTDPDLEF--NLSDEAWDLITKLITDPQDR---LQSPEQ 305
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
1903-2125 1.64e-08

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 58.09  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYE----GTAVDilgVGSGEIKVAVKTLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd14195    13 LGSGQFAIVRKcrekGTGKE---YAAKFIKKRRLSSSRRGVSREEIE--REVNILREIQHPNIITLHDIFENKTDVVLIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIvKIGDFGLA 2058
Cdd:cd14195    88 ELVSGGELFDFLAEKESLT-------EEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRI-KLIDFGIA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2059 RDIYKNDYYRKRgegLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILT-----LGHQPYPAHSNLDVLNY 2125
Cdd:cd14195   160 HKIEAGNEFKNI---FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSgaspfLGETKQETLTNISAVNY 228
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
1904-2114 1.66e-08

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 58.78  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1904 GSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGST-DQEKIEFLK-EAHLMSKFNHPNILK-----QLGVCLlnepqYI 1976
Cdd:cd05599    10 GRGAFGEVRLVRKKD-----TGHV-YAMKKLRKSEMlEKEQVAHVRaERDILAEADNPWVVKlyysfQDEENL-----YL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRK-----ARMATFYgplltlvdlvdlcvdISKGCVYLERMH---FIHRDLAARNCLVSVKDYtspr 2048
Cdd:cd05599    79 IMEFLPGGDMMTLLMKkdtltEEETRFY---------------IAETVLAIESIHklgYIHRDIKPDNLLLDARGH---- 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2049 iVKIGDFGLARDIYKN----------DYyrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPY 2114
Cdd:cd05599   140 -IKLSDFGLCTGLKKShlaystvgtpDY-------------IAPEVFLQKGYGKECDWWSLGVIMYEML-IGYPPF 200
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
1904-2109 1.88e-08

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 58.45  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1904 GSGAFGEVYEgtAVDILGVGSGEIkvAVKTLKKGSTDQEKIEF--LKEAHLMSKFNHPNILKQLGVCL--LNEPQYIILE 1979
Cdd:cd07842     9 GRGTYGRVYK--AKRKNGKDGKEY--AIKKFKGDKEQYTGISQsaCREIALLRELKHENVVSLVEVFLehADKSVYLLFD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGgDLL---TYLRKARMATFYGPLLTLVDLvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRiVKIGDFG 2056
Cdd:cd07842    85 YAEH-DLWqiiKFHRQAKRVSIPPSMVKSLLW-----QILNGIHYLHSNWVLHRDLKPANILVMGEGPERGV-VKIGDLG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2057 LARDIYKNDYYRKRGEGLLPVRWM-APESLMdGI--FTTQSDVWSFGILIWEILTL 2109
Cdd:cd07842   158 LARLFNAPLKPLADLDPVVVTIWYrAPELLL-GArhYTKAIDIWAIGCIFAELLTL 212
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
1902-2159 1.91e-08

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 57.66  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdiLGVGSGEIkVAVKTLK--KGSTDQEKIEfLKEAHLMSKF---NHPNILKQLGVCLLNEPQYI 1976
Cdd:cd14133     6 VLGKGTFGQVVKC-----YDLLTGEE-VALKIIKnnKDYLDQSLDE-IRLLELLNKKdkaDKYHIVRLKDVFYFKNHLCI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMeGGDLLTYLRKARMATFYGPLLTLVDLvdlcvDISKGCVYLERMHFIHRDLAARNCLVsvKDYTSPRIvKIGDFG 2056
Cdd:cd14133    79 VFELL-SQNLYEFLKQNKFQYLSLPRIRKIAQ-----QILEALVFLHSLGLIHCDLKPENILL--ASYSRCQI-KIIDFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 ----LARDIY---KNDYYRkrgegllpvrwmAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNY-VQT 2128
Cdd:cd14133   150 sscfLTQRLYsyiQSRYYR------------APEVILGLPYDEKIDMWSLGCILAELYT-GEPLFPGASEVDQLARiIGT 216
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767943404 2129 GGRLePPR-----NCPD-DLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14133   217 IGIP-PAHmldqgKADDeLFVDFLKKLLEIDPKERPT 252
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
1949-2159 2.14e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 59.26  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1949 EAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLrKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMhfI 2028
Cdd:PTZ00267  115 ELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQI-KQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKM--M 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2029 HRDLAARNCLVsvkdyTSPRIVKIGDFGLARDiYKNDYYRKRGEGLLPV-RWMAPESLMDGIFTTQSDVWSFGILIWEIL 2107
Cdd:PTZ00267  192 HRDLKSANIFL-----MPTGIIKLGDFGFSKQ-YSDSVSLDVASSFCGTpYYLAPELWERKRYSKKADMWSLGVILYELL 265
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2108 TLgHQPYPAHSNLDVLNYVQTGGRlePPRNCP--DDLWNLMTQCWAQEPDQRPT 2159
Cdd:PTZ00267  266 TL-HRPFKGPSQREIMQQVLYGKY--DPFPCPvsSGMKALLDPLLSKNPALRPT 316
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
1903-2115 2.48e-08

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 58.08  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEV----YEGTavdilgvgsGEIkVAVKTLKKG---STDQ------EKIEFlkeaHLMSKFNHPNILKQLGVCL 1969
Cdd:cd05589     7 LGRGHFGKVllaeYKPT---------GEL-FAIKALKKGdiiARDEveslmcEKRIF----ETVNSARHPFLVNLFACFQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 LNEPQYIILELMEGGDLLTYLR----KARMATFYGplltlvdlvdLCVDIskGCVYLERMHFIHRDLAARNCLVSVKDYt 2045
Cdd:cd05589    73 TPEHVCFVMEYAAGGDLMMHIHedvfSEPRAVFYA----------ACVVL--GLQFLHEHKIVYRDLKLDNLLLDTEGY- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2046 spriVKIGDFGLARdiykndyyrkrgEGLLP----------VRWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYP 2115
Cdd:cd05589   140 ----VKIADFGLCK------------EGMGFgdrtstfcgtPEFLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFP 202
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
1949-2114 2.60e-08

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 57.83  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1949 EAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKAR-----MATFYGplltlvdlvdlcVDISKGCVYLE 2023
Cdd:cd05612    51 EKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGGELFSYLRNSGrfsnsTGLFYA------------SEIVCALEYLH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2024 RMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARDIykndyyRKRGEGLLPV-RWMAPESLMDGIFTTQSDVWSFGIL 2102
Cdd:cd05612   119 SKEIVYRDLKPENILLDKEGH-----IKLTDFGFAKKL------RDRTWTLCGTpEYLAPEVIQSKGHNKAVDWWALGIL 187
                         170
                  ....*....|..
gi 767943404 2103 IWEILTlGHQPY 2114
Cdd:cd05612   188 IYEMLV-GYPPF 198
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
1944-2165 2.71e-08

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 57.37  E-value: 2.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1944 IEFLKEAHLmsKFNHPNILKQLGVCLLNEPQ------YIILELMEGGDLLTYLR--------KARMATfygplltlvdlv 2009
Cdd:cd14012    45 LEKELESLK--KLRHPNLVSYLAFSIERRGRsdgwkvYLLTEYAPGGSLSELLDsvgsvpldTARRWT------------ 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2010 dlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSprIVKIGDFGLARDIYKNDYYRKRGEgLLPVRWMAPE-SLMDG 2088
Cdd:cd14012   111 ---LQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTG--IVKLTDYSLGKTLLDMCSRGSLDE-FKQTYWLPPElAQGSK 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2089 IFTTQSDVWSFGILIWEILTlghqpypahsNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd14012   185 SPTRKTDVWDLGLLFLQMLF----------GLDVLEKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELLP 251
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
1898-2108 2.75e-08

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 58.08  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1898 TLRLLLGSGAFGEVYegTAVDILgvgSGeIKVAVKtlkkgstdqeKIE-F---------LKEAHLMSKFNHPNILKQLGV 1967
Cdd:cd07849     8 QNLSYIGEGAYGMVC--SAVHKP---TG-QKVAIK----------KISpFehqtyclrtLREIKILLRFKHENIIGILDI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1968 ------CLLNEpQYIILELMEGgDLLTYLRKARMAT------FYgplltlvdlvdlcvDISKGCVYLERMHFIHRDLAAR 2035
Cdd:cd07849    72 qrpptfESFKD-VYIVQELMET-DLYKLIKTQHLSNdhiqyfLY--------------QILRGLKYIHSANVLHRDLKPS 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2036 NCLVSVK-DytspriVKIGDFGLARDIYKN-DYYRKRGEgLLPVRWM-APE-SLMDGIFTTQSDVWSFGILIWEILT 2108
Cdd:cd07849   136 NLLLNTNcD------LKICDFGLARIADPEhDHTGFLTE-YVATRWYrAPEiMLNSKGYTKAIDIWSVGCILAEMLS 205
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1926-2115 3.45e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 57.76  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1926 EIKVAVKTlkkgstdqekiEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKArmatfygPLLTL 2005
Cdd:cd06650    41 EIKPAIRN-----------QIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKA-------GRIPE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2006 VDLVDLCVDISKGCVYLERMHFI-HRDLAARNCLVSVKDYtspriVKIGDFGLAR---DIYKNDYYRKRGegllpvrWMA 2081
Cdd:cd06650   103 QILGKVSIAVIKGLTYLREKHKImHRDVKPSNILVNSRGE-----IKLCDFGVSGqliDSMANSFVGTRS-------YMS 170
                         170       180       190
                  ....*....|....*....|....*....|....
gi 767943404 2082 PESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYP 2115
Cdd:cd06650   171 PERLQGTHYSVQSDIWSMGLSLVE-MAVGRYPIP 203
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
1902-2159 4.33e-08

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 56.84  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegtavdiLGVGSGEIKVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNH-PNILKQLGVCLLNEPQYIILe 1979
Cdd:cd14131     8 QLGKGGSSKVY-------KVLNPKKKIYALKRVDlEGADEQTLQSYKNEIELLKKLKGsDRIIQLYDYEVTDEDDYLYM- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGG--DLLTYLRKARMATFygplltlvdlvdlcvDISKGCVYLERM----HFIHR------DLAARNCLVsVKDytsp 2047
Cdd:cd14131    80 VMECGeiDLATILKKKRPKPI---------------DPNFIRYYWKQMleavHTIHEegivhsDLKPANFLL-VKG---- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 rIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQ----------SDVWSFGILIWEiLTLGHQPYPah 2117
Cdd:cd14131   140 -RLKLIDFGIAKAIQNDTTSIVRDSQVGTLNYMSPEAIKDTSASGEgkpkskigrpSDVWSLGCILYQ-MVYGKTPFQ-- 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767943404 2118 snlDVLNYVQTGGRL-------EPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14131   216 ---HITNPIAKLQAIidpnheiEFPDIPNPDLIDVMKRCLQRDPKKRPS 261
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
1897-2119 4.50e-08

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 56.62  E-value: 4.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTAVDILgvgsgeIKVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGV-------- 1967
Cdd:cd14032     3 LKFDIELGRGSFKTVYKGLDTETW------VEVAWCELQdRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFwescakgk 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1968 -CLLnepqyIILELMEGGDLLTYLRKARMatfygplLTLVDLVDLCVDISKGCVYLERMH--FIHRDLAARNCLVsvkdy 2044
Cdd:cd14032    77 rCIV-----LVTELMTSGTLKTYLKRFKV-------MKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFI----- 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2045 TSPR-IVKIGDFGLArdIYKNDYYRKRGEGllPVRWMAPEsLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSN 2119
Cdd:cd14032   140 TGPTgSVKIGDLGLA--TLKRASFAKSVIG--TPEFMAPE-MYEEHYDESVDVYAFGMCMLEMAT-SEYPYSECQN 209
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
1902-2114 4.51e-08

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 56.94  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVDILgvgsgEIK-VAVKT--LKKGSTDQEKIEFLK----EAHLMSKFNHPNILKQLGVCLLNEPQ 1974
Cdd:cd13990     7 LLGKGGFSEVYK--AFDLV-----EQRyVACKIhqLNKDWSEEKKQNYIKhalrEYEIHKSLDHPRIVKLYDVFEIDTDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YI-ILELMEGGDLLTYL--------RKARmatfygplltlvdlvDLCVDISKGCVYLE--RMHFIHRDLAARNCLVSvkD 2043
Cdd:cd13990    80 FCtVLEYCDGNDLDFYLkqhksipeREAR---------------SIIMQVVSALKYLNeiKPPIIHYDLKPGNILLH--S 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2044 YTSPRIVKIGDFGLARdIYKNDYYRKRG-----EGLLPVRWMAPESLMDG----IFTTQSDVWSFGILIWEILtLGHQPY 2114
Cdd:cd13990   143 GNVSGEIKITDFGLSK-IMDDESYNSDGmeltsQGAGTYWYLPPECFVVGktppKISSKVDVWSVGVIFYQML-YGRKPF 220
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1945-2115 4.80e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 57.37  E-value: 4.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1945 EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLER 2024
Cdd:cd06649    49 QIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIP-------EEILGKVSIAVLRGLAYLRE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2025 MHFI-HRDLAARNCLVSVKDYtspriVKIGDFGLAR---DIYKNDYYRKRGegllpvrWMAPESLMDGIFTTQSDVWSFG 2100
Cdd:cd06649   122 KHQImHRDVKPSNILVNSRGE-----IKLCDFGVSGqliDSMANSFVGTRS-------YMSPERLQGTHYSVQSDIWSMG 189
                         170
                  ....*....|....*
gi 767943404 2101 ILIWEiLTLGHQPYP 2115
Cdd:cd06649   190 LSLVE-LAIGRYPIP 203
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
1893-2165 4.99e-08

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 57.74  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLKKGSTDQEKieflkEAHLMSKFNHPNI--LKQL--GVC 1968
Cdd:PTZ00036   64 PNKSYKLGNIIGNGSFGVVYEAICID-----TSE-KVAIKKVLQDPQYKNR-----ELLIMKNLNHINIifLKDYyyTEC 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1969 LLNEPQYIILELmeggdLLTYLRKA--RMATFYGPLLTLVDLVDLCVDISKGCVYLERMH--FI-HRDLAARNCLVSVKD 2043
Cdd:PTZ00036  133 FKKNEKNIFLNV-----VMEFIPQTvhKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHskFIcHRDLKPQNLLIDPNT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2044 YTspriVKIGDFGLARDIYKNdyyrKRGEGLLPVR-WMAPEsLMDGI--FTTQSDVWSFGILIWEILtLGHQPYPAHSNL 2120
Cdd:PTZ00036  208 HT----LKLCDFGSAKNLLAG----QRSVSYICSRfYRAPE-LMLGAtnYTTHIDLWSLGCIIAEMI-LGYPIFSGQSSV 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2121 DVL-NYVQTGGR--------LEP-------------------PRNCPDDLWNLMTQCWAQEPDQR---------PTFHRI 2163
Cdd:PTZ00036  278 DQLvRIIQVLGTptedqlkeMNPnyadikfpdvkpkdlkkvfPKGTPDDAINFISQFLKYEPLKRlnpiealadPFFDDL 357

                  ..
gi 767943404 2164 QD 2165
Cdd:PTZ00036  358 RD 359
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
1906-2159 5.23e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 56.56  E-value: 5.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1906 GAFGEVYegTAVDIlgvgsgeikvavKTLKKGSTDQEKIEFLKEA--HLMSKFNHPNILKQLGVCLLNEPQYIILELMEG 1983
Cdd:cd13995    15 GAFGKVY--LAQDT------------KTKKRMACKLIPVEQFKPSdvEIQACFRHENIAELYGALLWEETVHLFMEAGEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1984 GDLLTYLRKArmatfyGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPRIVKIgDFGLARDIYK 2063
Cdd:cd13995    81 GSVLEKLESC------GPMREFEIIWVT-KHVLKGLDFLHSKNIIHHDIKPSNIV-----FMSTKAVLV-DFGLSVQMTE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2064 NDYYRK--RGEGLlpvrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQP----YP--AHSNLDVLNYVQTGGRLEPP 2135
Cdd:cd13995   148 DVYVPKdlRGTEI----YMSPEVILCRGHNTKADIYSLGATIIHMQT-GSPPwvrrYPrsAYPSYLYIIHKQAPPLEDIA 222
                         250       260
                  ....*....|....*....|....
gi 767943404 2136 RNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd13995   223 QDCSPAMRELLEAALERNPNHRSS 246
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
1903-2126 5.33e-08

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 57.36  E-value: 5.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDilgvGSGEIKVAVKTLKK--GSTDQEKIEFlKEAHLMSKFNHPNILKQLGVCL----LNEPQ-- 1974
Cdd:cd07877    25 VGSGAYGSVC--AAFD----TKTGLRVAVKKLSRpfQSIIHAKRTY-RELRLLKHMKHENVIGLLDVFTparsLEEFNdv 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMeGGDLLTYLRKARMATFYgplltlvdLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGD 2054
Cdd:cd07877    98 YLVTHLM-GADLNNIVKCQKLTDDH--------VQFLIYQILRGLKYIHSADIIHRDLKPSNLAVN-EDCE----LKILD 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2055 FGLARdiykndYYRKRGEGLLPVRWM-APESLMDGIFTTQS-DVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd07877   164 FGLAR------HTDDEMTGYVATRWYrAPEIMLNWMHYNQTvDIWSVGCIMAELLT-GRTLFPGTDHIDQLKLI 230
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
1902-2128 5.74e-08

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 57.38  E-value: 5.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGST-DQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd05627     9 VIGRGAFGEVRLVQKKD-----TGHI-YAMKILRKADMlEKEQVAHIRaERDILVEADGAWVVKMFYSFQDKRNLYLIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMAT-----FYgplltlvdlvdlcvdISKGCVYLERMH---FIHRDLAARNCLVSVKDYtspriVK 2051
Cdd:cd05627    83 FLPGGDMMTLLMKKDTLSeeatqFY---------------IAETVLAIDAIHqlgFIHRDIKPDNLLLDAKGH-----VK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLA---RDIYKNDYYR------------------KRGEGLLPVR------------WMAPESLMDGIFTTQSDVWS 2098
Cdd:cd05627   143 LSDFGLCtglKKAHRTEFYRnlthnppsdfsfqnmnskRKAETWKKNRrqlaystvgtpdYIAPEVFMQTGYNKLCDWWS 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767943404 2099 FGILIWEILtLGHQPY----PAHSNLDVLNYVQT 2128
Cdd:cd05627   223 LGVIMYEML-IGYPPFcsetPQETYRKVMNWKET 255
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
1903-2162 6.31e-08

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 56.36  E-value: 6.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEIkVAVKTLKKgSTDQEKI--EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd07860     8 IGEGTYGVVYK--ARNKL---TGEV-VALKKIRL-DTETEGVpsTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEgGDLLTYLRKARMATFYGPLLTLVDLvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARD 2060
Cdd:cd07860    81 LH-QDLKKFMDASALTGIPLPLIKSYLF-----QLLQGLAFCHSHRVLHRDLKPQNLLINTEGA-----IKLADFGLARA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYkndyyrkrgeglLPVR----------WMAPESLMDG-IFTTQSDVWSFGILIWEILTLgHQPYPAHSNLDVLNYV-QT 2128
Cdd:cd07860   150 FG------------VPVRtythevvtlwYRAPEILLGCkYYSTAVDIWSLGCIFAEMVTR-RALFPGDSEIDQLFRIfRT 216
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2129 GGrlepprnCPDD-LWNLMTQCwaqePDQRPTFHR 2162
Cdd:cd07860   217 LG-------TPDEvVWPGVTSM----PDYKPSFPK 240
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1894-2114 6.31e-08

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 56.23  E-value: 6.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYegTAVDilgVGSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVclLNEP 1973
Cdd:cd14083     2 RDKYEFKEVLGTGAFSEVV--LAED---KATGK-LVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDI--YESK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 Q--YIILELMEGGDLLTYLrkarmatfygplltlvdlvdlcvdISKGCvYLER---------------MH---FIHRDLA 2033
Cdd:cd14083    74 ShlYLVMELVTGGELFDRI------------------------VEKGS-YTEKdashlirqvleavdyLHslgIVHRDLK 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2034 ARNCLVSVKDYTSPriVKIGDFGLArdiykndyyRKRGEGLLPVR-----WMAPESLMDGIFTTQSDVWSFGIlIWEILT 2108
Cdd:cd14083   129 PENLLYYSPDEDSK--IMISDFGLS---------KMEDSGVMSTAcgtpgYVAPEVLAQKPYGKAVDCWSIGV-ISYILL 196

                  ....*.
gi 767943404 2109 LGHQPY 2114
Cdd:cd14083   197 CGYPPF 202
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
993-1099 6.35e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.11  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  993 PSAPENPRIfilpsgKCCNKNEVVVefRWNKPKHENGVLTKFEIFYNISNQsitnktcEDWIAVNVTP-SVMSFQLEGMS 1071
Cdd:cd00063     1 PSPPTNLRV------TDVTSTSVTL--SWTPPEDDGGPITGYVVEYREKGS-------GDWKEVEVTPgSETSYTLTGLK 65
                          90       100
                  ....*....|....*....|....*...
gi 767943404 1072 PRCFIAFQVRAFTSKGPGPYADVVKSTT 1099
Cdd:cd00063    66 PGTEYEFRVRAVNGGGESPPSESVTVTT 93
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1958-2114 6.95e-08

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 56.80  E-value: 6.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1958 HPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNC 2037
Cdd:cd14180    60 HPNIVALHEVLHDQYHTYLVMELLRGGELLDRIKKKARFS-------ESEASQLMRSLVSAVSFMHEAGVVHRDLKPENI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2038 LVSvkDYTSPRIVKIGDFGLARdiykndyyrKRGEGLLP-------VRWMAPESLMDGIFTTQSDVWSFGILIWEILTlG 2110
Cdd:cd14180   133 LYA--DESDGAVLKVIDFGFAR---------LRPQGSRPlqtpcftLQYAAPELFSNQGYDESCDLWSLGVILYTMLS-G 200

                  ....
gi 767943404 2111 HQPY 2114
Cdd:cd14180   201 QVPF 204
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
1902-2157 6.96e-08

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 56.94  E-value: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtaVDILGVGSGeIKVAVKTLKKGS--TDQEKIEFLKEAHLMSKFNHPnILKQLGVCLLNEPQY-IIL 1978
Cdd:cd05595     2 LLGKGTFGKV-----ILVREKATG-RYYAMKILRKEViiAKDEVAHTVTESRVLQNTRHP-FLTALKYAFQTHDRLcFVM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIG 2053
Cdd:cd05595    75 EYANGGELFFHLSRERVftedrARFYG------------AEIVSALEYLHSRDVVYRDIKLENLMLDKDGH-----IKIT 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDYYRKRGEGLlPvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY--PAHSNLDVLNYVQtggR 2131
Cdd:cd05595   138 DFGLCKEGITDGATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFynQDHERLFELILME---E 211
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2132 LEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05595   212 IRFPRTLSPEAKSLLAGLLKKDPKQR 237
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1930-2114 7.06e-08

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 56.37  E-value: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1930 AVKTLKKgsTDQEKIeFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKArmaTFYGPLLTLVDLV 2009
Cdd:cd14085    32 AVKKLKK--TVDKKI-VRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEK---GYYSERDAADAVK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2010 DLCVDISkgcvYLERMHFIHRDLAARNCLVSVKDYTSPriVKIGDFGLARdIYKNDYYRKRGEGLlPvRWMAPESLMDGI 2089
Cdd:cd14085   106 QILEAVA----YLHENGIVHRDLKPENLLYATPAPDAP--LKIADFGLSK-IVDQQVTMKTVCGT-P-GYCAPEILRGCA 176
                         170       180
                  ....*....|....*....|....*
gi 767943404 2090 FTTQSDVWSFGILIWeILTLGHQPY 2114
Cdd:cd14085   177 YGPEVDMWSVGVITY-ILLCGFEPF 200
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1928-2157 7.06e-08

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 56.59  E-value: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1928 KVAVKTLKK--GSTDQEKIEFLKEAHlmskfNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATfygplltl 2005
Cdd:cd14179    34 EYAVKIVSKrmEANTQREIAALKLCE-----GHPNIVKLHEVYHDQLHTFLVMELLKGGELLERIKKKQHFS-------- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2006 vdlVDLCVDISKGCVY-LERMH---FIHRDLAARNCLVSvkDYTSPRIVKIGDFGLARDIYKNDYYRKrgEGLLPVRWMA 2081
Cdd:cd14179   101 ---ETEASHIMRKLVSaVSHMHdvgVVHRDLKPENLLFT--DESDNSEIKIIDFGFARLKPPDNQPLK--TPCFTLHYAA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2082 PESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAH-------SNLDVLNYVQTGG---RLEPPRNCPDDLWNLMTQCWA 2151
Cdd:cd14179   174 PELLNYNGYDESCDLWSLGVILYTMLS-GQVPFQCHdksltctSAEEIMKKIKQGDfsfEGEAWKNVSQEAKDLIQGLLT 252

                  ....*.
gi 767943404 2152 QEPDQR 2157
Cdd:cd14179   253 VDPNKR 258
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
1903-2108 7.13e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 56.27  E-value: 7.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTavdilGVGSGEIkVAVKTLKKGSTDqEKI--EFLKEAHLMSKFNHPNILKQLGVcLLNEPQ-YIILE 1979
Cdd:cd07861     8 IGEGTYGVVYKGR-----NKKTGQI-VAMKKIRLESEE-EGVpsTAIREISLLKELQHPNIVCLEDV-LMQENRlYLVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGgDLLTYLRKARMATFYGPLLTLVDLVdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLAR 2059
Cdd:cd07861    80 FLSM-DLKKYLDSLPKGKYMDAELVKSYLY----QILQGILFCHSRRVLHRDLKPQNLLIDNKG-----VIKLADFGLAR 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2060 DIYkndyyrkrgeglLPVR----------WMAPESLMDGI-FTTQSDVWSFGILIWEILT 2108
Cdd:cd07861   150 AFG------------IPVRvythevvtlwYRAPEVLLGSPrYSTPVDIWSIGTIFAEMAT 197
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1968-2134 7.48e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 56.15  E-value: 7.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1968 CLLnepqyIILELMEGGDLLTYLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSp 2047
Cdd:cd14172    75 CLL-----IIMECMEGGELFSRIQERGDQAF-----TEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDA- 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 rIVKIGDFGLARDIYKND---------YYrkrgegllpvrwMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPYpahs 2118
Cdd:cd14172   144 -VLKLTDFGFAKETTVQNalqtpcytpYY------------VAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGFPPF---- 205
                         170
                  ....*....|....*.
gi 767943404 2119 nldvlnYVQTGGRLEP 2134
Cdd:cd14172   206 ------YSNTGQAISP 215
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1611-1700 7.57e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.11  E-value: 7.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1611 PEKPYSLVPEN---TSLQFNWKAPL--NVNLIRFWVELQKWKYNEFYHVKTSCSQGPAYVcnITNLQPYTSYNVRVVVVY 1685
Cdd:cd00063     1 PSPPTNLRVTDvtsTSVTLSWTPPEddGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT--LTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....*
gi 767943404 1686 KTGENSTSLPESFKT 1700
Cdd:cd00063    79 GGGESPPSESVTVTT 93
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
1903-2165 8.07e-08

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 56.28  E-value: 8.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdILGVGSGEIkVAVKTLKKGSTDQEKIEFLKEAHL-MSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd06617     9 LGRGAYGVVDK-----MRHVPTGTI-MAVKRIRATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICMEVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EggdllTYLRKarmatFY------GPLLTLVDLVDLCVDISKGCVYL-ERMHFIHRDLAARNCLVSVKDYtspriVKIGD 2054
Cdd:cd06617    83 D-----TSLDK-----FYkkvydkGLTIPEDILGKIAVSIVKALEYLhSKLSVIHRDVKPSNVLINRNGQ-----VKLCD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2055 FGLARDIYkNDYYRKRGEGLLPvrWMAPESL-----MDGiFTTQSDVWSFGILIWEILTLGHqPYPA-HSNLDVLNYVQT 2128
Cdd:cd06617   148 FGISGYLV-DSVAKTIDAGCKP--YMAPERInpelnQKG-YDVKSDVWSLGITMIELATGRF-PYDSwKTPFQQLKQVVE 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2129 ggrlEPPRNCPD-----DLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:cd06617   223 ----EPSPQLPAekfspEFQDFVNKCLKKNYKERPNYPELLQ 260
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
1895-2168 8.41e-08

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 56.29  E-value: 8.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEGTAvdilgvgSGEiKVAVKTLKkgSTDQEkiEFLKEAHLMSK--FNHPNILKQLG------ 1966
Cdd:cd14142     5 RQITLVECIGKGRYGEVWRGQW-------QGE-SVAVKIFS--SRDEK--SWFRETEIYNTvlLRHENILGFIAsdmtsr 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1967 ---VCLlnepqYIILELMEGGDLLTYLRKARMATfygplltlVDLVDLCVDISKGCVYLERMHF--------IHRDLAAR 2035
Cdd:cd14142    73 nscTQL-----WLITHYHENGSLYDYLQRTTLDH--------QEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSK 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2036 NCLVsvkdyTSPRIVKIGDFGLArdiykndYYRKRGEGLLPV---------RWMAPESLMDGIFTT------QSDVWSFG 2100
Cdd:cd14142   140 NILV-----KSNGQCCIADLGLA-------VTHSQETNQLDVgnnprvgtkRYMAPEVLDETINTDcfesykRVDIYAFG 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2101 ILIWEI--------LTLGHQP-----YPAHSNLDVLNYVQTGGRLEP--PRNCPDD-----LWNLMTQCWAQEPDQRPTF 2160
Cdd:cd14142   208 LVLWEVarrcvsggIVEEYKPpfydvVPSDPSFEDMRKVVCVDQQRPniPNRWSSDptltaMAKLMKECWYQNPSARLTA 287

                  ....*...
gi 767943404 2161 HRIQDQLQ 2168
Cdd:cd14142   288 LRIKKTLL 295
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1903-2166 9.57e-08

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 55.76  E-value: 9.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGevyegTAVDILGVGSGEIkVAVKTLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14665     8 IGSGNFG-----VARLMRDKQTKEL-VAVKYIERGEKIDENVQ--REIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLltYLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkDYTSPRIvKIGDFGLARdiy 2062
Cdd:cd14665    80 GGEL--FERICNAGRF-----SEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLD--GSPAPRL-KICDFGYSK--- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 KNDYYRKRGEGLLPVRWMAPESLMDGIFTTQ-SDVWSFGILIWEILTlghQPYPAHSNLDVLNYVQTGGR-LEPPRNCPD 2140
Cdd:cd14665   147 SSVLHSQPKSTVGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLV---GAYPFEDPEEPRNFRKTIQRiLSVQYSIPD 223
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767943404 2141 DLW------NLMTQCWAQEPDQRPTFHRIQDQ 2166
Cdd:cd14665   224 YVHispecrHLISRIFVADPATRITIPEIRNH 255
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
1902-2168 1.01e-07

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 55.91  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGtavdilgVGSGEiKVAVKTLkkgSTDQEKIEFlKEAHLMSK--FNHPNIL-------------KQLg 1966
Cdd:cd14143     2 SIGKGRFGEVWRG-------RWRGE-DVAVKIF---SSREERSWF-REAEIYQTvmLRHENILgfiaadnkdngtwTQL- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1967 vcllnepqYIILELMEGGDLLTYLRKARMATFygplltlvDLVDLCVDISKGCVYLErMHFI---------HRDLAARNC 2037
Cdd:cd14143    69 --------WLVSDYHEHGSLFDYLNRYTVTVE--------GMIKLALSIASGLAHLH-MEIVgtqgkpaiaHRDLKSKNI 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2038 LVSvKDYTSPrivkIGDFGLAR---------DIYKNDYYRKRgegllpvRWMAPESLMDGIFTT------QSDVWSFGIL 2102
Cdd:cd14143   132 LVK-KNGTCC----IADLGLAVrhdsatdtiDIAPNHRVGTK-------RYMAPEVLDDTINMKhfesfkRADIYALGLV 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2103 IWEI--------LTLGHQ-PY----PAHSNLDVLNYVQTGGRLEPprNCPD---------DLWNLMTQCWAQEPDQRPTF 2160
Cdd:cd14143   200 FWEIarrcsiggIHEDYQlPYydlvPSDPSIEEMRKVVCEQKLRP--NIPNrwqscealrVMAKIMRECWYANGAARLTA 277

                  ....*...
gi 767943404 2161 HRIQDQLQ 2168
Cdd:cd14143   278 LRIKKTLS 285
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
111-194 1.03e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.73  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  111 PTAPFASSIGSHNMTLRWKSANFSG---VKYIIQWKYAQLLGSWTYTKT-VSRPSYVVKPLHPFTEYIFRVVWIFTAQlq 186
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGgpiTGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNGGG-- 81

                  ....*...
gi 767943404  187 lYSPPSPS 194
Cdd:cd00063    82 -ESPPSES 88
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1902-2157 1.25e-07

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 56.24  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtaVDILGVGSGEIkVAVKTLKKGS--TDQEKIEFLKEAHLMSKFNHPnILKQLGVCLLNEPQY-IIL 1978
Cdd:cd05593    22 LLGKGTFGKV-----ILVREKASGKY-YAMKILKKEViiAKDEVAHTLTESRVLKNTRHP-FLTSLKYSFQTKDRLcFVM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRKARMAT-----FYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIG 2053
Cdd:cd05593    95 EYVNGGELFFHLSRERVFSedrtrFYG------------AEIVSALDYLHSGKIVYRDLKLENLMLDKDGH-----IKIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2054 DFGLARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY--PAHSNLDVLNYVQTggr 2131
Cdd:cd05593   158 DFGLCKEGITDAATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFynQDHEKLFELILMED--- 231
                         250       260
                  ....*....|....*....|....*.
gi 767943404 2132 LEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05593   232 IKFPRTLSADAKSLLSGLLIKDPNKR 257
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
111-178 1.26e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 1.26e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404    111 PTAPFASSIGSHNMTLRWKSANFSG-VKYIIQWK--YAQLLGSW-TYTKTVSRPSYVVKPLHPFTEYIFRVV 178
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGiTGYIVGYRveYREEGSEWkEVNVTPSSTSYTLTGLKPGTEYEFRVR 75
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
2014-2176 1.32e-07

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 55.41  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2014 DISKGCVYL-ERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDI----YKNDYYRKRGEGLLPV-----RWMAPE 2083
Cdd:cd14011   122 QISEALSFLhNDVKLVHGNICPESVVIN-----SNGEWKLAGFDFCISSeqatDQFPYFREYDPNLPPLaqpnlNYLAPE 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2084 SLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVL--NYVQTGGRLEPPRNC-PDDLWNLMTQCWAQEPDQRPtf 2160
Cdd:cd14011   197 YILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYkkNSNQLRQLSLSLLEKvPEELRDHVKTLLNVTPEVRP-- 274
                         170
                  ....*....|....*..
gi 767943404 2161 hriqDQLQLFR-NFFLN 2176
Cdd:cd14011   275 ----DAEQLSKiPFFDD 287
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
1903-2159 1.32e-07

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 56.03  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDIlgvGSGEIkVAvktLKK------GSTDQEK----IEFLKEAHlmskfNHPNILKQLGVcLLNE 1972
Cdd:cd07852    15 LGKGAYGIVWK--AIDK---KTGEV-VA---LKKifdafrNATDAQRtfreIMFLQELN-----DHPNIIKLLNV-IRAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQ---YIILELMEGgDLLTYLRKarmatfygplltlvdlvDLCVDISKGCV---------YLERMHFIHRDLAARNCLVS 2040
Cdd:cd07852    80 NDkdiYLVFEYMET-DLHAVIRA-----------------NILEDIHKQYImyqllkalkYLHSGGVIHRDLKPSNILLN 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2041 vkdytSPRIVKIGDFGLARDIYKNDYYRKRgegllPV-------RWM-APESLMDGI-FTTQSDVWSFGILIWEILT--- 2108
Cdd:cd07852   142 -----SDCRVKLADFGLARSLSQLEEDDEN-----PVltdyvatRWYrAPEILLGSTrYTKGVDMWSVGCILGEMLLgkp 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2109 -----------------LG----------HQPYpAHSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd07852   212 lfpgtstlnqlekiievIGrpsaediesiQSPF-AATMLESLPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLT 288
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
1903-2126 1.33e-07

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 55.25  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVdilgvgSGEIKVAVKTLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14104     8 LGRGQFGIVHRCVET------SSKKTYMAKFVKVKGADQVLVK--KEISILNIARHRNILRLHESFESHEELVMIFEFIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMatfygplltlVDLVDLCVD-ISKGCVYLERMH---FIHRDLAARNCLvsvkdYTSPR--IVKIGDFG 2056
Cdd:cd14104    80 GVDIFERITTARF----------ELNEREIVSyVRQVCEALEFLHsknIGHFDIRPENII-----YCTRRgsYIKIIEFG 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARDIYKNDYYRKRgegLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd14104   145 QSRQLKPGDKFRLQ---YTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLS-GINPFEAETNQQTIENI 210
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1902-2163 1.36e-07

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 54.94  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVdilgvgSGEIKVAVKTLKKGSTDQEK-----------IEFLKEAhlmSKFNHPNILKQLGVCLL 1970
Cdd:cd14005     7 LLGKGGFGTVYSGVRI------RDGLPVAVKFVPKSRVTEWAmingpvpvpleIALLLKA---SKPGVPGVIRLLDWYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQYIILELMEGG-DLLTYLRKarmatfYGPLLTLVDLV------DLCVDISKGCVylermhfIHRDLAARNCLVSVKD 2043
Cdd:cd14005    78 PDGFLLIMERPEPCqDLFDFITE------RGALSENLARIifrqvvEAVRHCHQRGV-------LHRDIKDENLLINLRT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2044 YTspriVKIGDFG---LARDIYKNDYyrkRGEGLlpvrWMAPESLMDGIF-TTQSDVWSFGILIWEILTlGHQPYpaHSN 2119
Cdd:cd14005   145 GE----VKLIDFGcgaLLKDSVYTDF---DGTRV----YSPPEWIRHGRYhGRPATVWSLGILLYDMLC-GDIPF--END 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767943404 2120 LDVL-NYVQTGGRLEPprNCPDdlwnLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14005   211 EQILrGNVLFRPRLSK--ECCD----LISRCLQFDPSKRPSLEQI 249
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
1895-2114 1.39e-07

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 55.84  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1895 EKLTLRLLLGSGAFGEVYEgtAVDIlgVGSGEIKVAVKTLKKGSTDQEKIEFLKEA----HLMSKFNHPNILKQLGVCLL 1970
Cdd:cd14041     6 DRYLLLHLLGRGGFSEVYK--AFDL--TEQRYVAVKIHQLNKNWRDEKKENYHKHAcreyRIHKELDHPRIVKLYDYFSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1971 NEPQY-IILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMH--FIHRDLAARNCLVSvkDYTSP 2047
Cdd:cd14041    82 DTDSFcTVLEYCEGNDLDFYLKQHKLMS-------EKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLV--NGTAC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2048 RIVKIGDFGLARDIYKNDYYRKRG-----EGLLPVRWMAPESLMDG----IFTTQSDVWSFGILIWEILtLGHQPY 2114
Cdd:cd14041   153 GEIKITDFGLSKIMDDDSYNSVDGmeltsQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFYQCL-YGRKPF 227
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1894-2114 1.46e-07

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 55.38  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYEgtavdILGVGSGEIkVAVKTLKKGSTDQEKiEFLKEAHLMSKFNHPNILKQLGVCLLNEP 1973
Cdd:cd14166     2 RETFIFMEVLGSGAFSEVYL-----VKQRSTGKL-YALKCIKKSPLSRDS-SLENEIAVLKRIKHENIVTLEDIYESTTH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPriVKIG 2053
Cdd:cd14166    75 YYLVMQLVSGGELFDRILERGVYT-------EKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSK--IMIT 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2054 DFGLArdiykndyyRKRGEGLLPVR-----WMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPY 2114
Cdd:cd14166   146 DFGLS---------KMEQNGIMSTAcgtpgYVAPEVLAQKPYSKAVDCWSIGVITY-ILLCGYPPF 201
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
1893-2108 1.54e-07

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 55.09  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRL--LLGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLK----KGSTDQEKIEFLKEAHLMSKFNHPNILKQLG 1966
Cdd:cd06651     3 PSAPINWRRgkLLGQGAFGRVYLCYDVD-----TGR-ELAAKQVQfdpeSPETSKEVSALECEIQLLKNLQHERIVQYYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1967 vCLLNEPQ---YIILELMEGGDLLTYLRKarmatfYGPLLTLVDLVDLcVDISKGCVYLERMHFIHRDLAARNCLvsvKD 2043
Cdd:cd06651    77 -CLRDRAEktlTIFMEYMPGGSVKDQLKA------YGALTESVTRKYT-RQILEGMSYLHSNMIVHRDIKGANIL---RD 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2044 ytSPRIVKIGDFGLARDIyknDYYRKRGEGLLPVR----WMAPESLMDGIFTTQSDVWSFGILIWEILT 2108
Cdd:cd06651   146 --SAGNVKLGDFGASKRL---QTICMSGTGIRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 209
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
1902-2170 1.55e-07

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 55.52  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAvdilgvgSGEIkVAVKTLkkgsTDQEKIEFLKEAHLMSKFN--HPNILKQLG----VCLLNEPQY 1975
Cdd:cd13998     2 VIGKGRFGEVWKASL-------KNEP-VAVKIF----SSRDKQSWFREKEIYRTPMlkHENILQFIAaderDTALRTELW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMATfygplltlvdlvDLCVDI----SKGCVYLERMHFI---------HRDLAARNCLVSvK 2042
Cdd:cd13998    70 LVTAFHPNGSL*DYLSLHTIDW------------VSLCRLalsvARGLAHLHSEIPGctqgkpaiaHRDLKSKNILVK-N 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2043 DYTSPrivkIGDFGLA------RDIYKNDYYRKRGEgllpVRWMAPESLMDGIFTT------QSDVWSFGILIWEIL--- 2107
Cdd:cd13998   137 DGTCC----IADFGLAvrlspsTGEEDNANNGQVGT----KRYMAPEVLEGAINLRdfesfkRVDIYAMGLVLWEMAsrc 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2108 --TLG-HQPY--------PAHSNLDVLNYVQTGGRLEPprNCPD---------DLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd13998   209 tdLFGiVEEYkppfysevPNHPSFEDMQEVVVRDKQRP--NIPNrwlshpglqSLAETIEECWDHDAEARLTAQCIEERL 286

                  ...
gi 767943404 2168 QLF 2170
Cdd:cd13998   287 SEF 289
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
1897-2119 1.56e-07

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 55.01  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTAVDIlgvgsgEIKVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILK---------QLG 1966
Cdd:cd14033     3 LKFNIEIGRGSFKTVYRGLDTET------TVEVAWCELQtRKLSKGERQRFSEEVEMLKGLQHPNIVRfydswkstvRGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1967 VCLLnepqyIILELMEGGDLLTYLRKARmatfygpLLTLVDLVDLCVDISKGCVYLERMH--FIHRDLAARNCLVsvkdy 2044
Cdd:cd14033    77 KCII-----LVTELMTSGTLKTYLKRFR-------EMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFI----- 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2045 TSPR-IVKIGDFGLArdIYKNDYYRKRGEGlLPvRWMAPEsLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSN 2119
Cdd:cd14033   140 TGPTgSVKIGDLGLA--TLKRASFAKSVIG-TP-EFMAPE-MYEEKYDEAVDVYAFGMCILEMAT-SEYPYSECQN 209
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
1902-2163 1.84e-07

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 54.63  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKkgSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14188     8 VLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSK--PHQREKID--KEIELHRILHHKHVVQFYHYFEDKENIYILLEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDI 2061
Cdd:cd14188    84 SRRSMAHILKARKVLT-------EPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN-----ENMELKVGDFGLAARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2062 YKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAhSNLDVLNYVQTGGRLEPPRNCPDD 2141
Cdd:cd14188   152 EPLEHRRRTICG--TPNYLSPEVLNKQGHGCESDIWALGCVMYTML-LGRPPFET-TNLKETYRCIREARYSLPSSLLAP 227
                         250       260
                  ....*....|....*....|..
gi 767943404 2142 LWNLMTQCWAQEPDQRPTFHRI 2163
Cdd:cd14188   228 AKHLIASMLSKNPEDRPSLDEI 249
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
1903-2129 2.29e-07

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 55.37  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVyegtavdILGVGSGE--IKVAVKTLKKGSTDQEKI--EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:PTZ00426   38 LGTGSFGRV-------ILATYKNEdfPPVAIKRFEKSKIIKQKQvdHVFSERKILNYINHPFCVNLYGSFKDESYLYLVL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRKAR-----MATFYGPLLTLVDLvdlcvdiskgcvYLERMHFIHRDLAARNCLVSVKDYtspriVKIG 2053
Cdd:PTZ00426  111 EFVIGGEFFTFLRRNKrfpndVGCFYAAQIVLIFE------------YLQSLNIVYRDLKPENLLLDKDGF-----IKMT 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2054 DFGLARdIYKNDYYRKRGEGllpvRWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAHSNLDVLNYVQTG 2129
Cdd:PTZ00426  174 DFGFAK-VVDTRTYTLCGTP----EYIAPEILLNVGHGKAADWWTLGIFIYEIL-VGCPPFYANEPLLIYQKILEG 243
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
1929-2121 2.42e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 55.39  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGSTdqekiefLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGgDLLTYLRKARMATFYGPLLTLVdl 2008
Cdd:PHA03212  120 VVIKAGQRGGT-------ATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIER-- 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2009 vdlcvDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLA---RDIYKNDYYRKRGEgllpVRWMAPESL 2085
Cdd:PHA03212  190 -----SVLRAIQYLHENRIIHRDIKAENIFIN-----HPGDVCLGDFGAAcfpVDINANKYYGWAGT----IATNAPELL 255
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767943404 2086 MDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLD 2121
Cdd:PHA03212  256 ARDPYGPAVDIWSAGIVLFEMAT-CHDSLFEKDGLD 290
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
1903-2123 2.67e-07

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 56.28  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCL--LNEPQYIILEL 1980
Cdd:PTZ00266   21 IGNGRFGEVFL-----VKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLnkANQKLYILMEF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGGDLLTYLRKARmaTFYGplltlVDLVDLCVDISKGCVY-LERMH----------FIHRDLAARNCLVSV-------- 2041
Cdd:PTZ00266   96 CDAGDLSRNIQKCY--KMFG-----KIEEHAIVDITRQLLHaLAYCHnlkdgpngerVLHRDLKPQNIFLSTgirhigki 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2042 ----KDYTSPRIVKIGDFGLARDI-YKNDYYRKRGEgllPVRWmAPESLMDGI--FTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:PTZ00266  169 taqaNNLNGRPIAKIGDFGLSKNIgIESMAHSCVGT---PYYW-SPELLLHETksYDDKSDMWALGCIIYELCS-GKTPF 243

                  ....*....
gi 767943404 2115 PAHSNLDVL 2123
Cdd:PTZ00266  244 HKANNFSQL 252
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
1903-2123 2.69e-07

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 54.60  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEIkVAvktLKKGSTDQEK----------IEFLKEahlmskFNHPNILKQLGVCLLNE 1972
Cdd:cd07835     7 IGEGTYGVVYK--ARDKL---TGEI-VA---LKKIRLETEDegvpstaireISLLKE------LNHPNIVRLLDVVHSEN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGgDLLTYLRKARMATFyGPLLTLVDLVDLCvdisKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKI 2052
Cdd:cd07835    72 KLYLVFEFLDL-DLKKYMDSSPLTGL-DPPLIKSYLYQLL----QGIAFCHSHRVLHRDLKPQNLLIDTEG-----ALKL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYkndyyrkrgeglLPVR---------WM-APESLMDG-IFTTQSDVWSFGILIWEILTlgHQP-YPAHSNL 2120
Cdd:cd07835   141 ADFGLARAFG------------VPVRtythevvtlWYrAPEILLGSkHYSTPVDIWSVGCIFAEMVT--RRPlFPGDSEI 206

                  ...
gi 767943404 2121 DVL 2123
Cdd:cd07835   207 DQL 209
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
2026-2165 2.82e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 55.65  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2026 HFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARdIYKNDYYRKRGEGLLPV-RWMAPESLMDGIFTTQSDVWSFGILIW 2104
Cdd:PTZ00283  163 HMIHRDIKSANILL-----CSNGLVKLGDFGFSK-MYAATVSDDVGRTFCGTpYYVAPEIWRRKPYSKKADMFSLGVLLY 236
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2105 EILTLgHQPYPAHSNLDVLNYVqTGGRLEP-PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQD 2165
Cdd:PTZ00283  237 ELLTL-KRPFDGENMEEVMHKT-LAGRYDPlPPSISPEMQEIVTALLSSDPKRRPSSSKLLN 296
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
1903-2114 3.24e-07

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 54.71  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVyegtavdILG--VGSGEIkVAVKTLKKGSTDQ-EKIE-FLKEAHLMSKFNHPNILKQLGVCLLNEPQ-YII 1977
Cdd:cd05587     4 LGKGSFGKV-------MLAerKGTDEL-YAIKILKKDVIIQdDDVEcTMVEKRVLALSGKPPFLTQLHSCFQTMDRlYFV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLR-----KARMATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd05587    76 MEYVNGGDLMYHIQqvgkfKEPVAVFYA------------AEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGH-----IKI 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2053 GDFGLARDIYKNDYYRKRGEGlLPvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd05587   139 ADFGMCKEGIFGGKTTRTFCG-TP-DYIAPEIIAYQPYGKSVDWWAYGVLLYEMLA-GQPPF 197
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
1930-2114 3.51e-07

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 54.08  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1930 AVKTLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLltYLRKARMATFYGPLLTLVDLV 2009
Cdd:cd14087    30 AIKMIETKCRGREVCE--SELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGEL--FDRIIAKGSFTERDATRVLQM 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2010 dlcvdISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPRI---VKIGDFGLArdiykndYYRKRGEGLL-------PvRW 2079
Cdd:cd14087   106 -----VLDGVKYLHGLGITHRDLKPENLL-----YYHPGPdskIMITDFGLA-------STRKKGPNCLmkttcgtP-EY 167
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767943404 2080 MAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPY 2114
Cdd:cd14087   168 IAPEILLRKPYTQSVDMWAVGVIAY-ILLSGTMPF 201
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
1902-2114 3.71e-07

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 53.78  E-value: 3.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTavDILGVGSGEIKVAVKTLKKGSTDQEKIefLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd14189     8 LLGKGGFARCYEMT--DLATNKTYAVKVIPHSRVAKPHQREKI--VNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLlTYLRKARMaTFYGPLLTLVDLvdlcvDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARDI 2061
Cdd:cd14189    84 SRKSL-AHIWKARH-TLLEPEVRYYLK-----QIISGLKYLHLKGILHRDLKLGNFFI-----NENMELKVGDFGLAARL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2062 YKNDYYRKRGEGLlPvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd14189   152 EPPEQRKKTICGT-P-NYLAPEVLLRQGHGPESDVWSLGCVMYTLLC-GNPPF 201
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
1903-2107 3.81e-07

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 54.75  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVclLNEPQ------- 1974
Cdd:cd07853     8 IGYGAFGVVWSVTDPR-----DGK-RVALKKMPNVFQNLVSCKrVFRELKMLCFFKHDNVLSALDI--LQPPHidpfeei 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGgDLLTYL-RKARMATFYgplltlvdLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIG 2053
Cdd:cd07853    80 YVVTELMQS-DLHKIIvSPQPLSSDH--------VKVFLYQILRGLKYLHSAGILHRDIKPGNLLVN-----SNCVLKIC 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2054 DFGLAR----DIYKN-------DYYRkrgegllpvrwmAPESLMDGI-FTTQSDVWSFGILIWEIL 2107
Cdd:cd07853   146 DFGLARveepDESKHmtqevvtQYYR------------APEILMGSRhYTSAVDIWSVGCIFAELL 199
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
1902-2128 3.82e-07

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 54.66  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGST-DQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd05628     8 VIGRGAFGEVRLVQKKD-----TGHV-YAMKILRKADMlEKEQVGHIRaERDILVEADSLWVVKMFYSFQDKLNLYLIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMAT-----FYgplltlvdlvdlcvdISKGCVYLERMH---FIHRDLAARNCLVSVKDYtspriVK 2051
Cdd:cd05628    82 FLPGGDMMTLLMKKDTLTeeetqFY---------------IAETVLAIDSIHqlgFIHRDIKPDNLLLDSKGH-----VK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLA---RDIYKNDYYR------------------------KRGEGLLPVR------WMAPESLMDGIFTTQSDVWS 2098
Cdd:cd05628   142 LSDFGLCtglKKAHRTEFYRnlnhslpsdftfqnmnskrkaetwKRNRRQLAFStvgtpdYIAPEVFMQTGYNKLCDWWS 221
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767943404 2099 FGILIWEILtLGHQPY----PAHSNLDVLNYVQT 2128
Cdd:cd05628   222 LGVIMYEML-IGYPPFcsetPQETYKKVMNWKET 254
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
1903-2125 3.90e-07

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 53.81  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilgvGSGEIKVAVKTLKKGSTD-------QEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd14196    13 LGSGQFAIVKKCRE------KSTGLEYAAKFIKKRQSRasrrgvsREEIE--REVSILRQVLHPNIITLHDVYENRTDVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIvKIGDF 2055
Cdd:cd14196    85 LILELVSGGELFDFLAQKESLS-------EEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHI-KLIDF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDI-----YKNDYYRKrgegllpvRWMAPESLMDGIFTTQSDVWSFGILIWEILT-----LGHQPYPAHSNLDVLNY 2125
Cdd:cd14196   157 GLAHEIedgveFKNIFGTP--------EFVAPEIVNYEPLGLEADMWSIGVITYILLSgaspfLGDTKQETLANITAVSY 228
pknD PRK13184
serine/threonine-protein kinase PknD;
1902-2114 4.13e-07

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 55.55  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVdilgVGSGeiKVAVKTLKKGSTDQE--KIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:PRK13184    9 LIGKGGMGEVYLAYDP----VCSR--RVALKKIREDLSENPllKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDI-SKGCVYLERMH---FIHRDLAARNCLVSVkdYTSpriVKIGDF 2055
Cdd:PRK13184   83 YIEGYTLKSLLKSVWQKESLSKELAEKTSVGAFLSIfHKICATIEYVHskgVLHRDLKPDNILLGL--FGE---VVILDW 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2056 GLA------RDIYKNDYYRKRG----EGLLPVR------WMAPESLMDGIFTTQSDVWSFGILIWEILTLGHqPY 2114
Cdd:PRK13184  158 GAAifkkleEEDLLDIDVDERNicysSMTIPGKivgtpdYMAPERLLGVPASESTDIYALGVILYQMLTLSF-PY 231
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1883-2114 4.17e-07

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 54.28  E-value: 4.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1883 QEEIENLpafpREKLTLRLLLGSGAFGEVyegtavdILGVGSGEIKV-AVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNI 1961
Cdd:cd14168     2 KKQVEDI----KKIFEFKEVLGTGAFSEV-------VLAEERATGKLfAVKCIPKKALKGKESSIENEIAVLRKIKHENI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1962 LKQLGVCLLNEPQYIILELMEGGDLLTYLRKArmaTFYGPLLTLVDLVdlcvDISKGCVYLERMHFIHRDLAARNCLVSV 2041
Cdd:cd14168    71 VALEDIYESPNHLYLVMQLVSGGELFDRIVEK---GFYTEKDASTLIR----QVLDAVYYLHRMGIVHRDLKPENLLYFS 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2042 KDYTSPriVKIGDFGLARDIYKNDYYrkrGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPY 2114
Cdd:cd14168   144 QDEESK--IMISDFGLSKMEGKGDVM---STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 210
fn3 pfam00041
Fibronectin type III domain;
994-1091 4.27e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 49.72  E-value: 4.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404   994 SAPENPRIfilpsgkcCNKNEVVVEFRWNKPKHENGVLTKFEIFYNISNQSitnktcEDWIAVNVTPSVMSFQLEGMSPR 1073
Cdd:pfam00041    1 SAPSNLTV--------TDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSG------EPWNEITVPGTTTSVTLTGLKPG 66
                           90
                   ....*....|....*...
gi 767943404  1074 CFIAFQVRAFTSKGPGPY 1091
Cdd:pfam00041   67 TEYEVRVQAVNGGGEGPP 84
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
1902-2157 4.64e-07

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 54.11  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDILGVgsgeikVAVKTLKKGS--TDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRI------YALKTIRKAHivSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKarmatfygplltlvdlvDLCVDISKGCVY-------LERMH---FIHRDLAARNCLVsvkDYTSPri 2049
Cdd:cd05585    75 FINGGELFHHLQR-----------------EGRFDLSRARFYtaellcaLECLHkfnVIYRDLKPENILL---DYTGH-- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTg 2129
Cdd:cd05585   133 IALCDFGLCKLNMKDDDKTNTFCG--TPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLT-GLPPFYDENTNEMYRKILQ- 208
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2130 grlEP---PRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05585   209 ---EPlrfPDGFDRDAKDLLIGLLNRDPTKR 236
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
1903-2167 4.65e-07

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 53.89  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdiLGVGSGEiKVAVKTLkkgsTDQEKIEFLKEAHLMSK--FNHPNILKQLGVCLLNEPQ----YI 1976
Cdd:cd14220     3 IGKGRYGEVW-------MGKWRGE-KVAVKVF----FTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTGSwtqlYL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKARMATfygplltlVDLVDLCVDISKGCVYLE--------RMHFIHRDLAARNCLVSvKDYTSPr 2048
Cdd:cd14220    71 ITDYHENGSLYDFLKCTTLDT--------RALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIK-KNGTCC- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 ivkIGDFGLARDiYKNDYYrkrgEGLLPV-------RWMAPESLMDGIFTTQ------SDVWSFGILIWEI----LTLG- 2110
Cdd:cd14220   141 ---IADLGLAVK-FNSDTN----EVDVPLntrvgtkRYMAPEVLDESLNKNHfqayimADIYSFGLIIWEMarrcVTGGi 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2111 ----HQPY----PAHSNLDVLNYVQTGGRLEP-------PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14220   213 veeyQLPYydmvPSDPSYEDMREVVCVKRLRPtvsnrwnSDECLRAVLKLMSECWAHNPASRLTALRIKKTL 284
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
1903-2120 5.78e-07

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 53.43  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGtavdiLGVGSGEIkVAVKTLKKGStdQEKIEF--LKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd07870     8 LGEGSYATVYKG-----ISRINGQL-VALKVISMKT--EEGVPFtaIREASLLKGLKHANIVLLHDIIHTKETLTFVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGgDLLTYLRK---------ARMATFygplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVK 2051
Cdd:cd07870    80 MHT-DLAQYMIQhpgglhpynVRLFMF---------------QLLRGLAYIHGQHILHRDLKPQNLLISYLGE-----LK 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2052 IGDFGLARDiyKNDYYRKRGEGLLPVRWMAPESLMDGI-FTTQSDVWSFGILIWEILTlGHQPYPAHSNL 2120
Cdd:cd07870   139 LADFGLARA--KSIPSQTYSSEVVTLWYRPPDVLLGATdYSSALDIWGAGCIFIEMLQ-GQPAFPGVSDV 205
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
1941-2120 5.80e-07

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 53.38  E-value: 5.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1941 QEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLrkARMATFygpllTLVDLVDLCVDISKGCV 2020
Cdd:cd14110    41 EDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNL--AERNSY-----SEAEVTDYLWQILSAVD 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2021 YLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARDIYKNDYY--RKRGEGLLPvrwMAPESLMDGIFTTQSDVWS 2098
Cdd:cd14110   114 YLHSRRILHLDLRSENMII-----TEKNLLKIVDLGNAQPFNQGKVLmtDKKGDYVET---MAPELLEGQGAGPQTDIWA 185
                         170       180
                  ....*....|....*....|..
gi 767943404 2099 FGILIWEILTlghQPYPAHSNL 2120
Cdd:cd14110   186 IGVTAFIMLS---ADYPVSSDL 204
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1902-2122 6.10e-07

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 53.50  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtavdILGVGSGEiKVAVKTLKKGSTDQEKIEFLKEA----HLMSKFNHPNILKQLGVCLLnepqyII 1977
Cdd:cd14170     9 VLGLGINGKVLQ-----IFNKRTQE-KFALKMLQDCPKARREVELHWRAsqcpHIVRIVDVYENLYAGRKCLL-----IV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPR---IVKIGD 2054
Cdd:cd14170    78 MECLDGGELFSRIQDRGDQAF-----TEREASEIMKSIGEAIQYLHSINIAHRDVKPENLL-----YTSKRpnaILKLTD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2055 FGLARDIYKNDyyrKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPYPAHSNLDV 2122
Cdd:cd14170   148 FGFAKETTSHN---SLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPFYSNHGLAI 211
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
1883-2108 6.91e-07

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 53.75  E-value: 6.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1883 QEEIEN-LPAFPREKLTLRLLlGSGAFGEVYegTAVDIlgvGSGEiKVAVKTLKKGStdQEKIeFLKEAH----LMSKFN 1957
Cdd:cd07879     3 REEVNKtVWELPERYTSLKQV-GSGAYGSVC--SAIDK---RTGE-KVAIKKLSRPF--QSEI-FAKRAYreltLLKHMQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1958 HPNILKQLGV----CLLNEPQ--YIILELMEggdllTYLRKARmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRD 2031
Cdd:cd07879    73 HENVIGLLDVftsaVSGDEFQdfYLVMPYMQ-----TDLQKIM-----GHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRD 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2032 LAARNCLVSvKDYTspriVKIGDFGLARdiykndYYRKRGEGLLPVRWM-APESLMDGIFTTQS-DVWSFGILIWEILT 2108
Cdd:cd07879   143 LKPGNLAVN-EDCE----LKILDFGLAR------HADAEMTGYVVTRWYrAPEVILNWMHYNQTvDIWSVGCIMAEMLT 210
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
1903-2129 6.99e-07

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 53.08  E-value: 6.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtavdILGVGSGeiKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14191    10 LGSGKFGQVFR-----LVEKKTK--KVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLRKARMAtfygplLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSpriVKIGDFGLARdiy 2062
Cdd:cd14191    83 GGELFERIIDEDFE------LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTK---IKLIDFGLAR--- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2063 kndyyRKRGEGLLPV-----RWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPYPAHSNLDVLNYVQTG 2129
Cdd:cd14191   151 -----RLENAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANVTSA 216
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
1903-2123 7.52e-07

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 53.80  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDilgvGSGEIKVAVKTLKKG-STDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQ------Y 1975
Cdd:cd07880    23 VGSGAYGTVC--SALD----RRTGAKVAIKKLYRPfQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfhdfY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMeGGDLLTYLRKARMATfygplltlVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGDF 2055
Cdd:cd07880    97 LVMPFM-GTDLGKLMKHEKLSE--------DRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVN-EDCE----LKILDF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2056 GLARDIykndyyRKRGEGLLPVRWM-APESLMDGIFTTQS-DVWSFGILIWEILTlGHQPYPAHSNLDVL 2123
Cdd:cd07880   163 GLARQT------DSEMTGYVVTRWYrAPEVILNWMHYTQTvDIWSVGCIMAEMLT-GKPLFKGHDHLDQL 225
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
1897-2121 7.84e-07

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 53.51  E-value: 7.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEFLK-----EAHLMSKFNHPNIlkqlgVCL-- 1969
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKAD-----TGKM-YAMKCLDKKRIKMKQGETLAlneriMLSLVSTGDCPFI-----VCMsy 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 -LNEPQYI--ILELMEGGDLLTYLRKARMAT-----FYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSV 2041
Cdd:cd14223    71 aFHTPDKLsfILDLMNGGDLHYHLSQHGVFSeaemrFYA------------AEIILGLEHMHSRFVVYRDLKPANILLDE 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2042 KDYtspriVKIGDFGLARDIYKNDYYRKRGEGllpvRWMAPESLMDGI-FTTQSDVWSFGILIWEILTlGHQPYPAHSNL 2120
Cdd:cd14223   139 FGH-----VRISDLGLACDFSKKKPHASVGTH----GYMAPEVLQKGVaYDSSADWFSLGCMLFKLLR-GHSPFRQHKTK 208

                  .
gi 767943404 2121 D 2121
Cdd:cd14223   209 D 209
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1903-2126 8.04e-07

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 53.08  E-value: 8.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTA--VDILgvgsgeikVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd07873    10 LGEGTYATVYKGRSklTDNL--------VALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGgDLLTYLRKArmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLAR- 2059
Cdd:cd07873    82 LDK-DLKQYLDDC------GNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGE-----LKLADFGLARa 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2060 -----DIYKNDyyrkrgeglLPVRWMAPESLMDGI--FTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd07873   150 ksiptKTYSNE---------VVTLWYRPPDILLGStdYSTQIDMWGVGCIFYEMST-GRPLFPGSTVEEQLHFI 213
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
1902-2116 8.30e-07

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 53.26  E-value: 8.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtavdILGVGSGEIKV-AVKTLKKGSTDQ-EKIE-FLKEAHLMS-KFNHPnILKQLGVCLLNEPQ-YI 1976
Cdd:cd05591     2 VLGKGSFGKV-------MLAERKGTDEVyAIKVLKKDVILQdDDVDcTMTEKRILAlAAKHP-FLTALHSCFQTKDRlFF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVK 2051
Cdd:cd05591    74 VMEYVNGGDLMFQIQRARKfdeprARFYA------------AEVTLALMFLHRHGVIYRDLKLDNILLDAEGH-----CK 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2052 IGDFGLARdiykndyyrkrgEGLLPVR----------WMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPA 2116
Cdd:cd05591   137 LADFGMCK------------EGILNGKttttfcgtpdYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEA 198
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
1903-2056 9.20e-07

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 50.13  E-value: 9.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDILGVgsgeIKVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd13968     1 MGEGASAKVF--WAEGECTT----IGVAVKIGDdVNNEEGEDLESEMDILRRLKGLELNIPKVLVTEDVDGPNILLMELV 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 1982 EGGDLLTYLRKARMatfygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSPRIVKIGDFG 2056
Cdd:cd13968    75 KGGTLIAYTQEEEL--------DEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNIL-----LSEDGNVKLIDFG 136
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
1902-2167 9.35e-07

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 52.86  E-value: 9.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegtavdiLGVGSGEiKVAVKTLkkgSTDQEKIEF----LKEAHLMskfNHPNILKQLGVCLLNEPQ--- 1974
Cdd:cd14144     2 SVGKGRYGEVW-------KGKWRGE-KVAVKIF---FTTEEASWFreteIYQTVLM---RHENILGFIAADIKGTGSwtq 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 -YIILELMEGGDLLTYLRKARMATfygplltlVDLVDLCVDISKGCVYLERMHF--------IHRDLAARNCLVSvKDYT 2045
Cdd:cd14144    68 lYLITDYHENGSLYDFLRGNTLDT--------QSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVK-KNGT 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2046 spriVKIGDFGLAR---------DIYKNDYYRKRgegllpvRWMAPE----SLMDGIFTT--QSDVWSFGILIWEI---- 2106
Cdd:cd14144   139 ----CCIADLGLAVkfisetnevDLPPNTRVGTK-------RYMAPEvldeSLNRNHFDAykMADMYSFGLVLWEIarrc 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2107 LTLG-----HQPY----PAHSNLDVLNYVQTGGRLEPP---RNCPDD----LWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14144   208 ISGGiveeyQLPYydavPSDPSYEDMRRVVCVERRRPSipnRWSSDEvlrtMSKLMSECWAHNPAARLTALRVKKTL 284
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
1903-2114 1.26e-06

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 52.77  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtAVDILGVGsgeIKVAVKTLKK------GSTDQEKIE-----------FLkeAHLMSKFNHPNILkql 1965
Cdd:cd05592     3 LGKGSFGKVM---LAELKGTN---QYFAIKALKKdvvledDDVECTMIErrvlalasqhpFL--THLFCTFQTESHL--- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1966 gvcllnepqYIILELMEGGDLLTYLRKA-----RMATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVS 2040
Cdd:cd05592    72 ---------FFVMEYLNGGDLMFHIQQSgrfdeDRARFYG------------AEIICGLQFLHSRGIIYRDLKLDNVLLD 130
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2041 VKDYtspriVKIGDFGLArdiyKNDYYRKRGEGLL---PvRWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPY 2114
Cdd:cd05592   131 REGH-----IKIADFGMC----KENIYGENKASTFcgtP-DYIAPEILKGQKYNQSVDWWSFGVLLYEML-IGQSPF 196
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
1902-2157 1.39e-06

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 52.44  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEFL--KEAHLMSKFNH----PNIlkqlgVCL---LNE 1972
Cdd:cd05606     1 IIGRGGFGEVYGCRKAD-----TGKM-YAMKCLDKKRIKMKQGETLalNERIMLSLVSTggdcPFI-----VCMtyaFQT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYI--ILELMEGGDLLTYLRKARMAT-----FYGplltlvdlvdlcVDISKGcvyLERMH---FIHRDLAARNCLVSVK 2042
Cdd:cd05606    70 PDKLcfILDLMNGGDLHYHLSQHGVFSeaemrFYA------------AEVILG---LEHMHnrfIVYRDLKPANILLDEH 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2043 DYtspriVKIGDFGLARDIYKNDYYRKRG-EGllpvrWMAPESLMDGI-FTTQSDVWSFGILIWEILTlGHQPYPAHSNL 2120
Cdd:cd05606   135 GH-----VRISDLGLACDFSKKKPHASVGtHG-----YMAPEVLQKGVaYDSSADWFSLGCMLYKLLK-GHSPFRQHKTK 203
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767943404 2121 D--VLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05606   204 DkhEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDVSKR 242
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
993-1089 1.41e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.99  E-value: 1.41e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404    993 PSAPENPRIfilpsgKCCNKNEVVVefRWNKPKHENGvlTKFEIFYNISNQSitnkTCEDWIAVNVTPSVMSFQLEGMSP 1072
Cdd:smart00060    1 PSPPSNLRV------TDVTSTSVTL--SWEPPPDDGI--TGYIVGYRVEYRE----EGSEWKEVNVTPSSTSYTLTGLKP 66
                            90
                    ....*....|....*..
gi 767943404   1073 RCFIAFQVRAFTSKGPG 1089
Cdd:smart00060   67 GTEYEFRVRAVNGAGEG 83
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
1903-2107 1.56e-06

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 52.79  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDIlgvgSGEIKVAVKtlKKGSTDQEKI---EFLKEAHLMSKF-NHPNIlkqlgVCL--------- 1969
Cdd:cd07857     8 LGQGAYGIVCSARNAET----SEEETVAIK--KITNVFSKKIlakRALRELKLLRHFrGHKNI-----TCLydmdivfpg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 -LNEpQYIILELMEGgDLLTYLRK------ARMATF-YgplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVsv 2041
Cdd:cd07857    77 nFNE-LYLYEELMEA-DLHQIIRSgqpltdAHFQSFiY--------------QILCGLKYIHSANVLHRDLKPGNLLV-- 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2042 kdyTSPRIVKIGDFGLARDIYKNdyyRKRGEGLL----PVRWM-APESLMD-GIFTTQSDVWSFGILIWEIL 2107
Cdd:cd07857   139 ---NADCELKICDFGLARGFSEN---PGENAGFMteyvATRWYrAPEIMLSfQSYTKAIDVWSVGCILAELL 204
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
1903-2128 1.61e-06

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 52.70  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDILGVgsgeikVAVKTLKKGSTDQ-EKIEFLK-EAHLMSKFNHPNILK-----QLGVCLlnepqY 1975
Cdd:cd05598     9 IGVGAFGEVSLVRKKDTNAL------YAMKTLRKKDVLKrNQVAHVKaERDILAEADNEWVVKlyysfQDKENL-----Y 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKA-----RMATFYgplltlvdlvdlcvdISKGCVYLERMH---FIHRDLAARNCLVSVKDYtsp 2047
Cdd:cd05598    78 FVMDYIPGGDLMSLLIKKgifeeDLARFY---------------IAELVCAIESVHkmgFIHRDIKPDNILIDRDGH--- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 riVKIGDFGLA---RDIYKNDYYRKRGEGLLPvRWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPY----PAHSNL 2120
Cdd:cd05598   140 --IKLTDFGLCtgfRWTHDSKYYLAHSLVGTP-NYIAPEVLLRTGYTQLCDWWSVGVILYEML-VGQPPFlaqtPAETQL 215

                  ....*...
gi 767943404 2121 DVLNYVQT 2128
Cdd:cd05598   216 KVINWRTT 223
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
1893-2114 1.63e-06

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 52.16  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1893 PREKLTLRLLLGSGAFGEVYEgtavdILGVGSGEiKVAVKTLK----KGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVC 1968
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRR-----CIHRETGQ-QFAVKIVDvakfTSSPGLSTEDLKREASICHMLKHPHIVELLETY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1969 LLNEPQYIILELMEGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDISKGCvylERMHFIHRDLAARNCLVSVKDYTSPr 2048
Cdd:cd14094    75 SSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYC---HDNNIIHRDVKPHCVLLASKENSAP- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2049 iVKIGDFGLARDIykndyyrkrGEGLLPV-------RWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPY 2114
Cdd:cd14094   151 -VKLGGFGVAIQL---------GESGLVAggrvgtpHFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPF 212
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1705-1794 1.64e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.26  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1705 PNKPGIPKLLEGSKNSI--QWEKAEDNGCRITYYILEIRKSTSNnlqnqnlRWKmTFNGSCSSVCTWKSKNLK--GIFQF 1780
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVtlSWTPPEDDGGPITGYVVEYREKGSG-------DWK-EVEVTPGSETSYTLTGLKpgTEYEF 72
                          90
                  ....*....|....
gi 767943404 1781 RVVAANNLGFGEYS 1794
Cdd:cd00063    73 RVRAVNGGGESPPS 86
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1898-2126 1.75e-06

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 52.20  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1898 TLRLLLGSGAFGEVyegtavdILGVGSGEIK-VAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYI 1976
Cdd:cd14169     6 ELKEKLGEGAFSEV-------VLAQERGSQRlVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLL-------TYLRKARMATFYgplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLvsvkdYTSP-- 2047
Cdd:cd14169    79 AMELVTGGELFdriiergSYTEKDASQLIG--------------QVLQAVKYLHQLGIVHRDLKPENLL-----YATPfe 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2048 --RIVkIGDFGLARdiykndyyrKRGEGLLPVR-----WMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPYPAHSNL 2120
Cdd:cd14169   140 dsKIM-ISDFGLSK---------IEAQGMLSTAcgtpgYVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPFYDENDS 208

                  ....*.
gi 767943404 2121 DVLNYV 2126
Cdd:cd14169   209 ELFNQI 214
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
1902-2107 1.86e-06

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 52.33  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegtavdILGVGSGEIKVAVKTLKKGSTDQEKieflKEAHLMSKFN-------HPNILKQLGVCLLNEPQ 1974
Cdd:cd05602    14 VIGKGSFGKVL------LARHKSDEKFYAVKVLQKKAILKKK----EEKHIMSERNvllknvkHPFLVGLHFSFQTTDKL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGGDLLTYLRKAR-----MATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspri 2049
Cdd:cd05602    84 YFVLDYINGGELFYHLQRERcflepRARFYA------------AEIASALGYLHSLNIVYRDLKPENILLDSQGH----- 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2050 VKIGDFGLARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEIL 2107
Cdd:cd05602   147 IVLTDFGLCKENIEPNGTTSTFCG--TPEYLAPEVLHKQPYDRTVDWWCLGAVLYEML 202
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
1903-2108 1.90e-06

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 52.37  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEiKVAVKtlKKGSTDQEKIE---FLKEAHLMSKFNHPNILKQLGVCLLNEPQ----- 1974
Cdd:cd07858    13 IGRGAYGIVCSAKNSE-----TNE-KVAIK--KIANAFDNRIDakrTLREIKLLRHLDHENVIAIKDIMPPPHREafndv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGgDLLTYLRKARMATfygplltlvdlVDLC----VDISKGCVYLERMHFIHRDLAARNCLVSVK-Dytspri 2049
Cdd:cd07858    85 YIVYELMDT-DLHQIIRSSQTLS-----------DDHCqyflYQLLRGLKYIHSANVLHRDLKPSNLLLNANcD------ 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2050 VKIGDFGLAR-----DIYKNDYYRKRgegllpvRWMAPESLMD-GIFTTQSDVWSFGILIWEILT 2108
Cdd:cd07858   147 LKICDFGLARttsekGDFMTEYVVTR-------WYRAPELLLNcSEYTTAIDVWSVGCIFAELLG 204
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
1894-2132 2.44e-06

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 52.32  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVYegtavdILGVGSGEIKVAVKTLKKGstdqekiEFLKEAHLMSKFNHPNIL--------KQL 1965
Cdd:cd05624    71 RDDFEIIKVIGRGAFGEVA------VVKMKNTERIYAMKILNKW-------EMLKRAETACFREERNVLvngdcqwiTTL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1966 GVCLLNEPQ-YIILELMEGGDLLTYLRKAR------MATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCL 2038
Cdd:cd05624   138 HYAFQDENYlYLVMDYYVGGDLLTLLSKFEdklpedMARFY------------IGEMVLAIHSIHQLHYVHRDIKPDNVL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2039 VSVKDYtspriVKIGDFGLARDIYKNDYYRKRGEGLLPvRWMAPESLM---DGI--FTTQSDVWSFGILIWEILtLGHQP 2113
Cdd:cd05624   206 LDMNGH-----IRLADFGSCLKMNDDGTVQSSVAVGTP-DYISPEILQameDGMgkYGPECDWWSLGVCMYEML-YGETP 278
                         250
                  ....*....|....*....
gi 767943404 2114 YPAHSnldvlnYVQTGGRL 2132
Cdd:cd05624   279 FYAES------LVETYGKI 291
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1621-1689 2.51e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 2.51e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404   1621 NTSLQFNWKAPLNVNLIRFWVELQKWKYNEFYHVKTSCSQGPAYVCNITNLQPYTSYNVRVVVVYKTGE 1689
Cdd:smart00060   14 STSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
1902-2108 2.72e-06

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 52.09  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyeGTAVDILgvgSGEiKVAVKTLK---KGSTDQEKIefLKEAHLMSKFNHPNILKQLGVCLLNEPQ---- 1974
Cdd:cd07859     7 VIGKGSYGVV--CSAIDTH---TGE-KVAIKKINdvfEHVSDATRI--LREIKLLRLLRHPDIVEIKHIMLPPSRRefkd 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 -YIILELMEGgDLLTYLRKARMAT-----FYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPR 2048
Cdd:cd07859    79 iYVVFELMES-DLHQVIKANDDLTpehhqFF------------LYQLLRALKYIHTANVFHRDLKPKNILAN-----ADC 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2049 IVKIGDFGLAR--------DIYKNDYyrkrgeglLPVRWM-APEsLMDGIFTTQS---DVWSFGILIWEILT 2108
Cdd:cd07859   141 KLKICDFGLARvafndtptAIFWTDY--------VATRWYrAPE-LCGSFFSKYTpaiDIWSIGCIFAEVLT 203
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
1884-2157 3.32e-06

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 51.57  E-value: 3.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1884 EEIENLPAFPREKLTLR-----LLLGSGAFGEVyegtaVDILGVGSGEIkVAVKTLKKGS--TDQEKIEFLKEAHLMSKF 1956
Cdd:cd05594     9 EEMEVSLTKPKHKVTMNdfeylKLLGKGTFGKV-----ILVKEKATGRY-YAMKILKKEVivAKDEVAHTLTENRVLQNS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1957 NHPnILKQLGVCLLNEPQY-IILELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcVDISKGCVYLE-RMHFIH 2029
Cdd:cd05594    83 RHP-FLTALKYSFQTHDRLcFVMEYANGGELFFHLSRERVfsedrARFYG------------AEIVSALDYLHsEKNVVY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2030 RDLAARNCLVSVKDYtspriVKIGDFGLARDIYKNDYYRKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTl 2109
Cdd:cd05594   150 RDLKLENLMLDKDGH-----IKITDFGLCKEGIKDGATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC- 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767943404 2110 GHQPY--PAHSNLDVLNYVQtggRLEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05594   222 GRLPFynQDHEKLFELILME---EIRFPRTLSPEAKSLLSGLLKKDPKQR 268
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
1902-2157 3.72e-06

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 51.20  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtavdILG--VGSGEIkVAVKTLKKgSTDQEKIEF---LKEAHLMSKFNHPnILKQLGVCLlNEPQYI 1976
Cdd:cd05571     2 VLGKGTFGKV-------ILCreKATGEL-YAIKILKK-EVIIAKDEVahtLTENRVLQNTRHP-FLTSLKYSF-QTNDRL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 --ILELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspri 2049
Cdd:cd05571    71 cfVMEYVNGGELFFHLSRERVfsedrTRFYG------------AEIVLALGYLHSQGIVYRDLKLENLLLDKDGH----- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2050 VKIGDFGLAR-DIyknDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHsNLDVLNYVQT 2128
Cdd:cd05571   134 IKITDFGLCKeEI---SYGATTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNR-DHEVLFELIL 208
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2129 GGRLEPPRNCPDDLWNLMTQCWAQEPDQR 2157
Cdd:cd05571   209 MEEVRFPSTLSPEAKSLLAGLLKKDPKKR 237
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
1896-2121 3.96e-06

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 51.60  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1896 KLTLRLLLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEFLK-----EAHLMSKFNHPNIlkqlgVCL- 1969
Cdd:cd05633     6 DFSVHRIIGRGGFGEVYGCRKAD-----TGKM-YAMKCLDKKRIKMKQGETLAlneriMLSLVSTGDCPFI-----VCMt 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1970 --LNEPQYI--ILELMEGGDLLTYLRK-----ARMATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVS 2040
Cdd:cd05633    75 yaFHTPDKLcfILDLMNGGDLHYHLSQhgvfsEKEMRFYA------------TEIILGLEHMHNRFVVYRDLKPANILLD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2041 VKDYTsprivKIGDFGLARDIYKNDYYRKRGEGllpvRWMAPESLMDGI-FTTQSDVWSFGILIWEILTlGHQPYPAHSN 2119
Cdd:cd05633   143 EHGHV-----RISDLGLACDFSKKKPHASVGTH----GYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPFRQHKT 212

                  ..
gi 767943404 2120 LD 2121
Cdd:cd05633   213 KD 214
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
1902-2127 3.99e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 51.15  E-value: 3.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQE-KIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILEL 1980
Cdd:cd07848     8 VVGEGAYGVVLKCRHKE-----TKEI-VAIKKFKDSEENEEvKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1981 MEGgDLLTYLRKarMATFYGPLLTLVDLvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDytsprIVKIGDFGLARD 2060
Cdd:cd07848    82 VEK-NMLELLEE--MPNGVPPEKVRSYI----YQLIKAIHWCHKNDIVHRDIKPENLLISHND-----VLKLCDFGFARN 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2061 IYK--NDYYRKrgegLLPVRWM-APESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYPAHSNLDVLNYVQ 2127
Cdd:cd07848   150 LSEgsNANYTE----YVATRWYrSPELLLGAPYGKAVDMWSVGCILGE-LSDGQPLFPGESEIDQLFTIQ 214
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1902-2118 4.00e-06

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 51.54  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtavDILGVGSGEIKVAVKTLKKGST--DQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd05621    59 VIGRGAFGEV------QLVRHKASQKVYAMKLLSKFEMikRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVME 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLL----TYLRKARMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDF 2055
Cdd:cd05621   133 YMPGGDLVnlmsNYDVPEKWAKFY------------TAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGH-----LKLADF 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2056 GLARDIYKNDYYRKRGEGLLPvRWMAPESLM----DGIFTTQSDVWSFGILIWEILtLGHQPYPAHS 2118
Cdd:cd05621   196 GTCMKMDETGMVHCDTAVGTP-DYISPEVLKsqggDGYYGRECDWWSVGVFLFEML-VGDTPFYADS 260
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
1897-2119 4.04e-06

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 51.20  E-value: 4.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1897 LTLRLLLGSGAFGEVYEGTAVDIlgvgsgEIKVAVKTLK-KGSTDQEKIEFLKEAHLMSKFNHPNILK---------QLG 1966
Cdd:cd14030    27 LKFDIEIGRGSFKTVYKGLDTET------TVEVAWCELQdRKLSKSERQRFKEEAGMLKGLQHPNIVRfydswestvKGK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1967 VCLLnepqyIILELMEGGDLLTYLRKARMATFygplltlVDLVDLCVDISKGCVYLERMH--FIHRDLAARNCLVsvkdy 2044
Cdd:cd14030   101 KCIV-----LVTELMTSGTLKTYLKRFKVMKI-------KVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI----- 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2045 TSPR-IVKIGDFGLArdIYKNDYYRKRGEGllPVRWMAPEsLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSN 2119
Cdd:cd14030   164 TGPTgSVKIGDLGLA--TLKRASFAKSVIG--TPEFMAPE-MYEEKYDESVDVYAFGMCMLEMAT-SEYPYSECQN 233
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
1903-2168 4.40e-06

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 50.65  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtAVDIlgvgsGEIKVAVKTLKKGSTDQEKI---EFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd14160     1 IGEGEIFEVY---RVRI-----GNRSYAVKLFKQEKKMQWKKhwkRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMATfygPLLTLVDlvdlcVDISKGCVylERMHFIHRdlaARNCLVSVKDYTSPRIV-------KI 2052
Cdd:cd14160    73 YMQNGTLFDRLQCHGVTK---PLSWHER-----INILIGIA--KAIHYLHN---SQPCTVICGNISSANILlddqmqpKL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLAR----DIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGH--QPYPAHSNL-DVL-N 2124
Cdd:cd14160   140 TDFALAHfrphLEDQSCTINMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCKvvLDDPKHLQLrDLLhE 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2125 YVQTGG----------RLEP-PRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQ 2168
Cdd:cd14160   220 LMEKRGldsclsfldlKFPPcPRNFSAKLFRLAGRCTATKAKLRPDMDEVLQRLE 274
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
1902-2117 4.41e-06

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 50.67  E-value: 4.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYeGTAVDILGVGSGEIKVAVKTLKKGSTdqEKIEFLkEAHLMSKFNHPNILK-------QLGVCLlnepq 1974
Cdd:cd05607     9 VLGKGGFGEVC-AVQVKNTGQMYACKKLDKKRLKKKSG--EKMALL-EKEILEKVNSPFIVSlayafetKTHLCL----- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 yiILELMEGGDLLTYL-----RKARMA--TFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSvkDYTSP 2047
Cdd:cd05607    80 --VMSLMNGGDLKYHIynvgeRGIEMErvIFYS------------AQITCGILHLHSLKIVYRDMKPENVLLD--DNGNC 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2048 RivkIGDFGLARDIYKNDYYRKRG--EGllpvrWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAH 2117
Cdd:cd05607   144 R---LSDLGLAVEVKEGKPITQRAgtNG-----YMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPFRDH 206
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1927-2161 4.50e-06

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 50.81  E-value: 4.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1927 IKVAVKTLKKGSTDQE-KIEFLKE-AHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATfygpllt 2004
Cdd:cd14106    34 KEYAAKFLRKRRRGQDcRNEILHEiAVLELCKDCPRVVNLHEVYETRSELILILELAAGGELQTLLDEEECLT------- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2005 LVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRI---VKIGDFGLARDIYKNDYYRkrgEGLLPVRWMA 2081
Cdd:cd14106   107 EADVRRLMRQILEGVQYLHERNIVHLDLKPQNILL-----TSEFPlgdIKLCDFGISRVIGEGEEIR---EILGTPDYVA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2082 PESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDV-LNYVQtgGRLEPPRNCPDDLWNL----MTQCWAQEPDQ 2156
Cdd:cd14106   179 PEILSYEPISLATDMWSIGVLTYVLLT-GHSPFGGDDKQETfLNISQ--CNLDFPEELFKDVSPLaidfIKRLLVKDPEK 255

                  ....*
gi 767943404 2157 RPTFH 2161
Cdd:cd14106   256 RLTAK 260
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
1902-2135 4.57e-06

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 50.49  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEiKVAVKTLKKG--STDQEkiEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd14082    10 VLGSGQFGIVYGGKHRK-----TGR-DVAIKVIDKLrfPTKQE--SQLRnEVAILQQLSHPGVVNLECMFETPERVFVVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRKA------RMATFygplltlvdlvdLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTSPRiVKI 2052
Cdd:cd14082    82 EKLHGDMLEMILSSEkgrlpeRITKF------------LVTQILVALRYLHSKNIVHCDLKPENVLLA-SAEPFPQ-VKL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARdIYKNDYYRKRGEGLlPVrWMAPESLMDGIFTTQSDVWSFGILIWEILTlghQPYPAHSNLDVLNYVQTGGRL 2132
Cdd:cd14082   148 CDFGFAR-IIGEKSFRRSVVGT-PA-YLAPEVLRNKGYNRSLDMWSVGVIIYVSLS---GTFPFNEDEDINDQIQNAAFM 221

                  ...
gi 767943404 2133 EPP 2135
Cdd:cd14082   222 YPP 224
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
1902-2073 6.47e-06

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 51.00  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGST-DQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIILE 1979
Cdd:cd05629     8 VIGKGAFGEVRLVQKKD-----TGKI-YAMKTLLKSEMfKKDQLAHVKaERDVLAESDSPWVVSLYYSFQDAQYLYLIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1980 LMEGGDLLTYLRKARMAT-----FYgplltlvdlVDLCVDISKGcvyLERMHFIHRDLAARNCLVSVKDYtspriVKIGD 2054
Cdd:cd05629    82 FLPGGDLMTMLIKYDTFSedvtrFY---------MAECVLAIEA---VHKLGFIHRDIKPDNILIDRGGH-----IKLSD 144
                         170       180
                  ....*....|....*....|..
gi 767943404 2055 FGLARDIYK---NDYYRKRGEG 2073
Cdd:cd05629   145 FGLSTGFHKqhdSAYYQKLLQG 166
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
1902-2141 6.58e-06

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 50.81  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtAVDILgVGSGEIkVAVKTLKKGSTDQ--EKIEFLKEAHLMSKFNHPNILKqLGVCLLNEPQ-YIIL 1978
Cdd:cd05597     8 VIGRGAFGEV----AVVKL-KSTEKV-YAMKILNKWEMLKraETACFREERDVLVNGDRRWITK-LHYAFQDENYlYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRK------ARMATFYgplltlVDLVDLCVDiskgcvYLERMHFIHRDLAARNCLVsvkDYTSPriVKI 2052
Cdd:cd05597    81 DYYCGGDLLTLLSKfedrlpEEMARFY------LAEMVLAID------SIHQLGYVHRDIKPDNVLL---DRNGH--IRL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFG----LARD--IYKN------DYyrkrgegllpvrwMAPESL--MD---GIFTTQSDVWSFGILIWEILtLGHQPYP 2115
Cdd:cd05597   144 ADFGsclkLREDgtVQSSvavgtpDY-------------ISPEILqaMEdgkGRYGPECDWWSLGVCMYEML-YGETPFY 209
                         250       260
                  ....*....|....*....|....*....
gi 767943404 2116 AHSnldvlnYVQTGGRLEPPRNC---PDD 2141
Cdd:cd05597   210 AES------LVETYGKIMNHKEHfsfPDD 232
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
1930-2172 1.07e-05

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 50.03  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1930 AVKTLKKG-STDQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQ-YIILELMEGGDLLTYLRKARM-----ATFYgp 2001
Cdd:cd05618    49 AMKVVKKElVNDDEDIDWVQtEKHVFEQASNHPFLVGLHSCFQTESRlFFVIEYVNGGDLMFHMQRQRKlpeehARFY-- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2002 lltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARdiykndyyrkrgEGLLP----- 2076
Cdd:cd05618   127 ----------SAEISLALNYLHERGIIYRDLKLDNVLLDSEGH-----IKLTDYGMCK------------EGLRPgdtts 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2077 -----VRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY--------PAHSNLDVLNYVQTGGRLEPPRNCPDDLW 2143
Cdd:cd05618   180 tfcgtPNYIAPEILRGEDYGFSVDWWALGVLMFEMMA-GRSPFdivgssdnPDQNTEDYLFQVILEKQIRIPRSLSVKAA 258
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767943404 2144 NLMTQCWAQEPDQR------PTFHRIQDQlQLFRN 2172
Cdd:cd05618   259 SVLKSFLNKDPKERlgchpqTGFADIQGH-PFFRN 292
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
1935-2104 1.15e-05

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 49.56  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1935 KKGSTDQEKI-----EFLKEAHLMSKFNHPNILKQLGVclLNEPQ----YIILELMEGGDLLT--------------YLR 1991
Cdd:cd14200    54 KAAQGEQAKPlapleRVYQEIAILKKLDHVNIVKLIEV--LDDPAednlYMVFDLLRKGPVMEvpsdkpfsedqarlYFR 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1992 karmatfygplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARDIYKNDYYRKRG 2071
Cdd:cd14200   132 ----------------------DIVLGIEYLHYQKIVHRDIKPSNLLLGDDGH-----VKIADFGVSNQFEGNDALLSST 184
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767943404 2072 EGlLPVrWMAPESLMDgifTTQS------DVWSFGILIW 2104
Cdd:cd14200   185 AG-TPA-FMAPETLSD---SGQSfsgkalDVWAMGVTLY 218
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1903-2126 1.15e-05

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 49.61  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilgvGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd07872    14 LGEGTYATVFKGRS------KLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GgDLLTYLRKArmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLAR--- 2059
Cdd:cd07872    88 K-DLKQYMDDC------GNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGE-----LKLADFGLARaks 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2060 ---DIYKNDyyrkrgeglLPVRWMAPESLMDGI--FTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd07872   156 vptKTYSNE---------VVTLWYRPPDVLLGSseYSTQIDMWGVGCIFFEMAS-GRPLFPGSTVEDELHLI 217
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
1902-2105 1.16e-05

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 49.29  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtavdilgvgsgeIKV---------AVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNE 1972
Cdd:cd14046    13 VLGKGAFGQV---------------VKVrnkldgryyAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGGDLltylrkaRMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd14046    78 NLYIQMEYCEKSTL-------RDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN-----VKI 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2053 GDFGLAR-----------DIYKNDYYRKRGEGLLPVR-----WMAPESL--MDGIFTTQSDVWSFGILIWE 2105
Cdd:cd14046   146 GDFGLATsnklnvelatqDINKSTSAALGSSGDLTGNvgtalYVAPEVQsgTKSTYNEKVDMYSLGIIFFE 216
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
1896-2168 1.23e-05

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 49.43  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1896 KLTLRLLLGSGAFGEVYEgtAVDilgVGSGEiKVAVKTLKkGSTDQEKIEFLKEAHLMSKFN-HPNILKQLGVCLLNEP- 1973
Cdd:cd14036     1 KLRIKRVIAEGGFAFVYE--AQD---VGTGK-EYALKRLL-SNEEEKNKAIIQEINFMKKLSgHPNIVQFCSAASIGKEe 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 ------QYIIL-ELMEGGdLLTYLRKARMATFYGPLLTLVDLVDLCVDISkgcvyleRMH-----FIHRDLAARNCLVSv 2041
Cdd:cd14036    74 sdqgqaEYLLLtELCKGQ-LVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQ-------HMHkqsppIIHRDLKIENLLIG- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2042 kdytSPRIVKIGDFGLARDI--YKNDYYRKRGEGLL---------PVrWMAPESL---MDGIFTTQSDVWSFGILIWeIL 2107
Cdd:cd14036   145 ----NQGQIKLCDFGSATTEahYPDYSWSAQKRSLVedeitrnttPM-YRTPEMIdlySNYPIGEKQDIWALGCILY-LL 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2108 TLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCwaqEPDQRPTFHRIQDQLQ 2168
Cdd:cd14036   219 CFRKHPFEDGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKV---NPEERLSITEIVEQLQ 276
fn3 pfam00041
Fibronectin type III domain;
111-178 1.28e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 1.28e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404   111 PTAPFASSIGSHNMTLRWKSANFSG---VKYIIQWKYAQLLGSWTyTKTVSRP--SYVVKPLHPFTEYIFRVV 178
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNSGEPWN-EITVPGTttSVTLTGLKPGTEYEVRVQ 74
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
1929-2114 1.32e-05

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 49.20  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTY------LRKARMATFYGpl 2002
Cdd:cd14113    35 VATKFVNKKLMKRDQVT--HELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRLLDYvvrwgnLTEEKIRFYLR-- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2003 ltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSvKDYTSPrIVKIGDFGLARDIYKNDYYRKRgegLLPVRWMAP 2082
Cdd:cd14113   111 -----------EILEALQYLHNCRIAHLDLKPENILVD-QSLSKP-TIKLADFGDAVQLNTTYYIHQL---LGSPEFAAP 174
                         170       180       190
                  ....*....|....*....|....*....|..
gi 767943404 2083 ESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd14113   175 EIILGNPVSLTSDLWSIGVLTYVLLS-GVSPF 205
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
1929-2114 1.43e-05

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 48.80  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRK-----ARMATFYgpll 2003
Cdd:cd14115    21 VAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYLMNhdelmEEKVAFY---- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2004 tlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTsPRiVKIGDFGLARDIyknDYYRKRGEGLLPVRWMAPE 2083
Cdd:cd14115    95 --------IRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPV-PR-VKLIDLEDAVQI---SGHRHVHHLLGNPEFAAPE 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 767943404 2084 SLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd14115   162 VIQGTPVSLATDIWSIGVLTYVMLS-GVSPF 191
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
1903-2108 1.45e-05

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 49.29  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDILgvgSGEIkVAvktLKKGSTDQEK----IEFLKEAHLMSKFNHPNILKQLGVCLlNEPQ---- 1974
Cdd:cd07865    20 IGQGTFGEVFK--ARHRK---TGQI-VA---LKKVLMENEKegfpITALREIKILQLLKHENVVNLIEICR-TKATpynr 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 -----YIILELMEGgDLLTYLRKARMaTFygplltlvdlvdLCVDISK-------GCVYLERMHFIHRDLAARNCLVsvk 2042
Cdd:cd07865    90 ykgsiYLVFEFCEH-DLAGLLSNKNV-KF------------TLSEIKKvmkmllnGLYYIHRNKILHRDMKAANILI--- 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2043 dyTSPRIVKIGDFGLAR--DIYKNDYYRKRGEGLLPVRWMAPESLM-DGIFTTQSDVWSFGILIWEILT 2108
Cdd:cd07865   153 --TKDGVLKLADFGLARafSLAKNSQPNRYTNRVVTLWYRPPELLLgERDYGPPIDMWGAGCIMAEMWT 219
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
1949-2105 1.54e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 49.89  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1949 EAHLMSKFNHPNILKQL------GVCLLNEPQYiilelmeGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDiskgcvYL 2022
Cdd:PHA03211  210 EARLLRRLSHPAVLALLdvrvvgGLTCLVLPKY-------RSDLYTYLGARLRPLGLAQVTAVARQLLSAID------YI 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2023 ERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDIykndyyrkRGEGLLPVRW--------MAPESLMDGIFTTQS 2094
Cdd:PHA03211  277 HGEGIIHRDIKTENVLVN-----GPEDICLGDFGAACFA--------RGSWSTPFHYgiagtvdtNAPEVLAGDPYTPSV 343
                         170
                  ....*....|.
gi 767943404 2095 DVWSFGILIWE 2105
Cdd:PHA03211  344 DIWSAGLVIFE 354
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1902-2114 1.69e-05

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 49.23  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegTAVDILGVGSGEIkVAVKTLKKGSTDQE--KIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQ-YII 1977
Cdd:cd05613     7 VLGTGAYGKVF--LVRKVSGHDAGKL-YAMKVLKKATIVQKakTAEHTRtERQVLEHIRQSPFLVTLHYAFQTDTKlHLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLRKARMATfygplltlvdLVDLCVDISKGCVYLERMH---FIHRDLAARNCLVSVKDYtspriVKIGD 2054
Cdd:cd05613    84 LDYINGGELFTHLSQRERFT----------ENEVQIYIGEIVLALEHLHklgIIYRDIKLENILLDSSGH-----VVLTD 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2055 FGLARDIYKNDYYRKRgEGLLPVRWMAPESLMDGI--FTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd05613   149 FGLSKEFLLDENERAY-SFCGTIEYMAPEIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPF 208
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
2015-2159 1.80e-05

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 48.78  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2015 ISKGCVYLERMHFIHRDLAARNCLVSVKdytSPR-IVKIGDFGLARDIYKNDYYRkrgEGLLPVRWMAPESLMDGIFTTQ 2093
Cdd:cd14197   120 ILEGVSFLHNNNVVHLDLKPQNILLTSE---SPLgDIKIVDFGLSRILKNSEELR---EIMGTPEYVAPEILSYEPISTA 193
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767943404 2094 SDVWSFGILIWEILT-----LGHQPYPAHSNLDVLNYVQTGGRLEpprNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14197   194 TDMWSIGVLAYVMLTgispfLGDDKQETFLNISQMNVSYSEEEFE---HLSESAIDFIKTLLIKKPENRAT 261
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
1902-2171 2.94e-05

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 48.53  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEGTavdiLGVGSGEIK--VAVKTL---KKGSTDQEKiEFLKEAHLmskfNHPNILKQL-----GVCLln 1971
Cdd:cd14055     2 LVGKGRFAEVWKAK----LKQNASGQYetVAVKIFpyeEYASWKNEK-DIFTDASL----KHENILQFLtaeerGVGL-- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1972 EPQY-IILELMEGGDLLTYLRK--------ARMATfygplltlvdlvdlcvDISKGCVYLE---------RMHFIHRDLA 2033
Cdd:cd14055    71 DRQYwLITAYHENGSLQDYLTRhilswedlCKMAG----------------SLARGLAHLHsdrtpcgrpKIPIAHRDLK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2034 ARNCLVSvkdytSPRIVKIGDFGLA--------RDIYKNDyyrkrGEGLLPvRWMAPESLMDGIFTT------QSDVWSF 2099
Cdd:cd14055   135 SSNILVK-----NDGTCVLADFGLAlrldpslsVDELANS-----GQVGTA-RYMAPEALESRVNLEdlesfkQIDVYSM 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2100 GILIWEIL----TLGH-QPY--------PAHSNLDVLNYVQTGGRLEPPrnCPDD---------LWNLMTQCWAQEPDQR 2157
Cdd:cd14055   204 ALVLWEMAsrceASGEvKPYelpfgskvRERPCVESMKDLVLRDRGRPE--IPDSwlthqgmcvLCDTITECWDHDPEAR 281
                         330
                  ....*....|....
gi 767943404 2158 PTFHRIQDQLQLFR 2171
Cdd:cd14055   282 LTASCVAERFNELK 295
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
1902-2130 3.20e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 48.49  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtaVDILGVGSGEIkVAVKTLKKGST--DQEKIEFLKEAHLMSK-FNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd14229     7 FLGRGTFGQV-----VKCWKRGTNEI-VAVKILKNHPSyaRQGQIEVGILARLSNEnADEFNFVRAYECFQHRNHTCLVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGgDLLTYLRKARMATFygpllTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVsVKDYTSPRIVKIGDFGLA 2058
Cdd:cd14229    81 EMLEQ-NLYDFLKQNKFSPL-----PLKVIRPILQQVATALKKLKSLGLIHADLKPENIML-VDPVRQPYRVKVIDFGSA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2059 RDIYK---NDYYRKRgegllpvRWMAPESLMDGIFTTQSDVWSFGILIWEiLTLGHQPYPAHSNLDVLNYV-QTGG 2130
Cdd:cd14229   154 SHVSKtvcSTYLQSR-------YYRAPEIILGLPFCEAIDMWSLGCVIAE-LFLGWPLYPGALEYDQIRYIsQTQG 221
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1903-2164 3.27e-05

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 47.84  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGevyegTAVDILGVGSGEIkVAVKTLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14662     8 IGSGNFG-----VARLMRNKETKEL-VAVKYIERGLKIDENVQ--REIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLltYLRKARMATFYGPLLTLVDLVDLCvdiskGCVYLERMHFIHRDLAARNCLVSvkDYTSPRiVKIGDFGlardiy 2062
Cdd:cd14662    80 GGEL--FERICNAGRFSEDEARYFFQQLIS-----GVSYCHSMQICHRDLKLENTLLD--GSPAPR-LKICDFG------ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2063 kndyYRKrgEGLLPVR---------WMAPESL----MDGiftTQSDVWSFGILIWEILTlghQPYPAHSNLDVLNYVQTG 2129
Cdd:cd14662   144 ----YSK--SSVLHSQpkstvgtpaYIAPEVLsrkeYDG---KVADVWSCGVTLYVMLV---GAYPFEDPDDPKNFRKTI 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767943404 2130 GR-LEPPRNCPD------DLWNLMTQCWAQEPDQRPTFHRIQ 2164
Cdd:cd14662   212 QRiMSVQYKIPDyvrvsqDCRHLLSRIFVANPAKRITIPEIK 253
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
1902-2120 3.91e-05

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 48.33  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYEgtAVDIlgvGSGEiKVAVKTLKKGS--TDQEKIE-----FLKEA---------HLMSKFNHPNilkql 1965
Cdd:cd14134    19 LLGEGTFGKVLE--CWDR---KRKR-YVAVKIIRNVEkyREAAKIEidvleTLAEKdpngkshcvQLRDWFDYRG----- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1966 GVCllnepqyIILELMeGGDLLTYLRKARMATFYGPLltlvdlvdlCVDISKGCV----YLERMHFIHRDLAARNCL--- 2038
Cdd:cd14134    88 HMC-------IVFELL-GPSLYDFLKKNNYGPFPLEH---------VQHIAKQLLeavaFLHDLKLTHTDLKPENILlvd 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2039 ---------VSVKDYTSPR--IVKIGDFGLArdIYKNDY---------YRkrgegllpvrwmAPESLMDGIFTTQSDVWS 2098
Cdd:cd14134   151 sdyvkvynpKKKRQIRVPKstDIKLIDFGSA--TFDDEYhssivstrhYR------------APEVILGLGWSYPCDVWS 216
                         250       260
                  ....*....|....*....|..
gi 767943404 2099 FGILIWEILTlGHQPYPAHSNL 2120
Cdd:cd14134   217 IGCILVELYT-GELLFQTHDNL 237
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
1929-2114 4.11e-05

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 48.02  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGSTDQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDlltylRKARMATFYGPLLTLVD 2007
Cdd:cd08227    28 VTVRRINLEACTNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS-----AKDLICTHFMDGMSELA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2008 LVDLCVDISKGCVYLERMHFIHRDLAARNCLVSV--KDYTS--PRIVKIGDFGLARDIYKNdyYRKRGEGLLPvrWMAPE 2083
Cdd:cd08227   103 IAYILQGVLKALDYIHHMGYVHRSVKASHILISVdgKVYLSglRSNLSMINHGQRLRVVHD--FPKYSVKVLP--WLSPE 178
                         170       180       190
                  ....*....|....*....|....*....|...
gi 767943404 2084 SLMDGI--FTTQSDVWSFGILIWEiLTLGHQPY 2114
Cdd:cd08227   179 VLQQNLqgYDAKSDIYSVGITACE-LANGHVPF 210
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
1902-2107 4.15e-05

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 48.04  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtavdILGVGSGEIKV-AVKTLKKGSTDQEKieflKEAHLMSKFN-------HPNILKQLGVCLLNEP 1973
Cdd:cd05603     2 VIGKGSFGKV-------LLAKRKCDGKFyAVKVLQKKTILKKK----EQNHIMAERNvllknlkHPFLVGLHYSFQTSEK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKAR-----MATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspr 2048
Cdd:cd05603    71 LYFVLDYVNGGELFFHLQRERcflepRARFYA------------AEVASAIGYLHSLNIIYRDLKPENILLDCQGH---- 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2049 iVKIGDFGLARdiykndyyrkrgEGLLP----------VRWMAPESLMDGIFTTQSDVWSFGILIWEIL 2107
Cdd:cd05603   135 -VVLTDFGLCK------------EGMEPeettstfcgtPEYLAPEVLRKEPYDRTVDWWCLGAVLYEML 190
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
1899-2107 4.25e-05

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 47.38  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1899 LRLLLGSGAFGEVyeGTAVDILgvgSGEiKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd14078     7 LHETIGSGGFAKV--KLATHIL---TGE-KVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYL-RKARMA-----TFYGplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSvkDYTSpriVKI 2052
Cdd:cd14078    81 EYCPGGELFDYIvAKDRLSedearVFFR-------------QIVSAVAYVHSQGYAHRDLKPENLLLD--EDQN---LKL 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLA---RDIYKNDYYRKRGEgllPVrWMAPEsLMDG--IFTTQSDVWSFGILIWEIL 2107
Cdd:cd14078   143 IDFGLCakpKGGMDHHLETCCGS---PA-YAAPE-LIQGkpYIGSEADVWSMGVLLYALL 197
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
2015-2127 4.28e-05

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 47.61  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2015 ISKGCVYLERMHFIHRDLAARNCLVSVkdyTSPR-IVKIGDFGLARDIYKNDYYRkrgEGLLPVRWMAPESLMDGIFTTQ 2093
Cdd:cd14198   119 ILEGVYYLHQNNIVHLDLKPQNILLSS---IYPLgDIKIVDFGMSRKIGHACELR---EIMGTPEYLAPEILNYDPITTA 192
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767943404 2094 SDVWSFGILIWEILTlGHQPYPAHSNLDV-LNYVQ 2127
Cdd:cd14198   193 TDMWNIGVIAYMLLT-HESPFVGEDNQETfLNISQ 226
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
1903-2127 4.30e-05

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 47.58  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilgVGSGEIKVAVKTLKKGSTDQEKIEflKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd14114    10 LGTGAFGVVHRCTE-----RATGNNFAAKFIMTPHESDKETVR--KEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GGDLLTYLrkarmaTFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSpriVKIGDFGLARDIY 2062
Cdd:cd14114    83 GGELFERI------AAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNE---VKLIDFGLATHLD 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2063 KNDYYrKRGEGllPVRWMAPESLMDGIFTTQSDVWSFGILIWeILTLGHQPYPAHSNLDVLNYVQ 2127
Cdd:cd14114   154 PKESV-KVTTG--TAEFAAPEIVEREPVGFYTDMWAVGVLSY-VLLSGLSPFAGENDDETLRNVK 214
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1383-1711 4.50e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 48.85  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1383 AYSSVMQPFPDKAFLSLASDTVEPTILNATNTSLTIRLPLAKTNLTWYGITSPTPTYLVYYAEVNDRKNSSDLKYRILEF 1462
Cdd:COG3401   110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1463 QDSIALIEDLQPFSTYMIQIAVKNYYSDPlehlPPGKEIWGKTKNGVPEAVQLINTTVRSDTSLIISWReshkPNGPKES 1542
Cdd:COG3401   190 TTLVDGGGDIEPGTTYYYRVAATDTGGES----APSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWD----PVTESDA 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1543 VRYQLaishlalipetplRQSEFPNGRLTLL---------VTRLSGGNIYVLKVLACHSEEMWCTESHPVTVEMFNT-PE 1612
Cdd:COG3401   262 TGYRV-------------YRSNSGDGPFTKVatvtttsytDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTpPA 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1613 KPYSL---VPENTSLQFNWKAPLNVNLIRFWVELQKWKYNEFYHVKTSCSqGPAYVcnITNLQPYTSYNVRVVVVYKTGE 1689
Cdd:COG3401   329 APSGLtatAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAETVT-TTSYT--DTGLTPGTTYYYKVTAVDAAGN 405
                         330       340
                  ....*....|....*....|..
gi 767943404 1690 NSTSLPESFKTKAGVPNKPGIP 1711
Cdd:COG3401   406 ESAPSEEVSATTASAASGESLT 427
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1902-2118 4.60e-05

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 48.14  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegtavdiLGVGSGEIKV-AVKTLKKgstdQEKIE------FLKEAHLMSKFNHPNILkQLGVCLLNEPQ 1974
Cdd:cd05596    33 VIGRGAFGEVQ-------LVRHKSTKKVyAMKLLSK----FEMIKrsdsafFWEERDIMAHANSEWIV-QLHYAFQDDKY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 -YIILELMEGGDLLTYLRK----ARMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspri 2049
Cdd:cd05596   101 lYMVMDYMPGGDLVNLMSNydvpEKWARFY------------TAEVVLALDAIHSMGFVHRDVKPDNMLLDASGH----- 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2050 VKIGDFGLARDIYKNDYYRKRGEGLLPvRWMAPESLM----DGIFTTQSDVWSFGILIWEILtLGHQPYPAHS 2118
Cdd:cd05596   164 LKLADFGTCMKMDKDGLVRSDTAVGTP-DYISPEVLKsqggDGVYGRECDWWSVGVFLYEML-VGDTPFYADS 234
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
2024-2159 6.06e-05

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 47.28  E-value: 6.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2024 RMHF-----IHRDLAARNCLVSvkdytSPRIVKIGDFG-----------------LARDIYKNDY--YRkrgegllpvrw 2079
Cdd:cd14037   123 AMHYlkpplIHRDLKVENVLIS-----DSGNYKLCDFGsattkilppqtkqgvtyVEEDIKKYTTlqYR----------- 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2080 mAPE--SLMDG-IFTTQSDVWSFGILIWEIL--TLghqPYPAHSNLDVLNyvqtgGRLEPPRNCP--DDLWNLMTQCWAQ 2152
Cdd:cd14037   187 -APEmiDLYRGkPITEKSDIWALGCLLYKLCfyTT---PFEESGQLAILN-----GNFTFPDNSRysKRLHKLIRYMLEE 257

                  ....*..
gi 767943404 2153 EPDQRPT 2159
Cdd:cd14037   258 DPEKRPN 264
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1903-2118 6.27e-05

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 47.31  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAvdilgvGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELME 1982
Cdd:cd07871    13 LGEGTYATVFKGRS------KLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1983 GgDLLTYLRKArmatfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLAR--- 2059
Cdd:cd07871    87 S-DLKQYLDNC------GNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGE-----LKLADFGLARaks 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2060 ---DIYKNDyyrkrgeglLPVRWMAPESLMDGI--FTTQSDVWSFGILIWEILTlGHQPYPAHS 2118
Cdd:cd07871   155 vptKTYSNE---------VVTLWYRPPDVLLGSteYSTPIDMWGVGCILYEMAT-GRPMFPGST 208
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
1902-2130 6.63e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 47.78  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtaVDILGVGSGEIkVAVKTLKKGST--DQEKIEFLKEAHLMSK-FNHPNILKQLGVCLLNEPQYIIL 1978
Cdd:cd14227    22 FLGRGTFGQV-----VKCWKRGTNEI-VAIKILKNHPSyaRQGQIEVSILARLSTEsADDYNFVRAYECFQHKNHTCLVF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGgDLLTYLRKARMATFygPLLTLVDLVDlcvDISKGCVYLERMHFIHRDLAARNCLVsVKDYTSPRIVKIGDFGLA 2058
Cdd:cd14227    96 EMLEQ-NLYDFLKQNKFSPL--PLKYIRPILQ---QVATALMKLKSLGLIHADLKPENIML-VDPSRQPYRVKVIDFGSA 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2059 RDIYK---NDYYRKRgegllpvRWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAHSNLDVLNYV-QTGG 2130
Cdd:cd14227   169 SHVSKavcSTYLQSR-------YYRAPEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPGASEYDQIRYIsQTQG 236
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
1902-2107 9.39e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 46.88  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVyegtavdILGVGSGEIKV-AVKTLKKGSTDQEKieflKEAHLMSKFN-------HPNILKQLGVCLLNEP 1973
Cdd:cd05604     3 VIGKGSFGKV-------LLAKRKRDGKYyAVKVLQKKVILNRK----EQKHIMAERNvllknvkHPFLVGLHYSFQTTDK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1974 QYIILELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspr 2048
Cdd:cd05604    72 LYFVLDFVNGGELFFHLQRERSfpeprARFYA------------AEIASALGYLHSINIVYRDLKPENILLDSQGH---- 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2049 iVKIGDFGLARDIYKNDYYRKRGEGLlPvRWMAPESLMDGIFTTQSDVWSFGILIWEIL 2107
Cdd:cd05604   136 -IVLTDFGLCKEGISNSDTTTTFCGT-P-EYLAPEVIRKQPYDNTVDWWCLGSVLYEML 191
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
1902-2130 9.99e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 47.01  E-value: 9.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVY--------EGTAVDILG-----VGSGEIKVAVKTlKKGSTDQEKIEFLKEAHLMSKFNHpnilkqlgVC 1968
Cdd:cd14228    22 FLGRGTFGQVAkcwkrstkEIVAIKILKnhpsyARQGQIEVSILS-RLSSENADEYNFVRSYECFQHKNH--------TC 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1969 LlnepqyiILELMEGgDLLTYLRKARMATFygPLLTLVDLVDlcvDISKGCVYLERMHFIHRDLAARNCLVsVKDYTSPR 2048
Cdd:cd14228    93 L-------VFEMLEQ-NLYDFLKQNKFSPL--PLKYIRPILQ---QVATALMKLKSLGLIHADLKPENIML-VDPVRQPY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 IVKIGDFGLARDIYK---NDYYRKRgegllpvRWMAPESLMDGIFTTQSDVWSFGILIWEILtLGHQPYPAHSNLDVLNY 2125
Cdd:cd14228   159 RVKVIDFGSASHVSKavcSTYLQSR-------YYRAPEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPGASEYDQIRY 230

                  ....*.
gi 767943404 2126 V-QTGG 2130
Cdd:cd14228   231 IsQTQG 236
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
1894-2118 1.00e-04

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 47.32  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1894 REKLTLRLLLGSGAFGEVyegtavDILGVGSGEIKVAVKTLKKGstdqekiEFLKEAHLMSKFNHPNIL--------KQL 1965
Cdd:cd05623    71 KEDFEILKVIGRGAFGEV------AVVKLKNADKVFAMKILNKW-------EMLKRAETACFREERDVLvngdsqwiTTL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1966 GVCLLNEPQ-YIILELMEGGDLLTYLRK------ARMATFYgplltlVDLVDLCVDiskgcvYLERMHFIHRDLAARNCL 2038
Cdd:cd05623   138 HYAFQDDNNlYLVMDYYVGGDLLTLLSKfedrlpEDMARFY------LAEMVLAID------SVHQLHYVHRDIKPDNIL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2039 VSVKDYtspriVKIGDFGLARDIYKNDYYRKRGEGLLPvRWMAPESLM-----DGIFTTQSDVWSFGILIWEILtLGHQP 2113
Cdd:cd05623   206 MDMNGH-----IRLADFGSCLKLMEDGTVQSSVAVGTP-DYISPEILQamedgKGKYGPECDWWSLGVCMYEML-YGETP 278

                  ....*
gi 767943404 2114 YPAHS 2118
Cdd:cd05623   279 FYAES 283
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1902-2114 1.02e-04

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 46.84  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegTAVDILGVGSGEIkVAVKTLKKGSTDQEK--IEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQ-YII 1977
Cdd:cd05614     7 VLGTGAYGKVF--LVRKVSGHDANKL-YAMKVLRKAALVQKAktVEHTRtERNVLEHVRQSPFLVTLHYAFQTDAKlHLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1978 LELMEGGDLLTYLR-----KARMATFYGPlltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKI 2052
Cdd:cd05614    84 LDYVSGGELFTHLYqrdhfSEDEVRFYSG------------EIILALEHLHKLGIVYRDIKLENILLDSEGH-----VVL 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767943404 2053 GDFGLARDIYKNDyyRKRGEGLL-PVRWMAPEslmdgIFTTQS------DVWSFGILIWEILTlGHQPY 2114
Cdd:cd05614   147 TDFGLSKEFLTEE--KERTYSFCgTIEYMAPE-----IIRGKSghgkavDWWSLGILMFELLT-GASPF 207
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
1902-2114 1.22e-04

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 46.94  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1902 LLGSGAFGEVYegtavdILGVGSGEIKVAVKTLKKGST-DQEKIEFLK-EAHLMSKFNHPNILKQLGVCLLNEPQ-YIIL 1978
Cdd:cd05617    22 VIGRGSYAKVL------LVRLKKNDQIYAMKVVKKELVhDDEDIDWVQtEKHVFEQASSNPFLVGLHSCFQTTSRlFLVI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1979 ELMEGGDLLTYLRKARM-----ATFYGplltlvdlvdlcvdiSKGCVYLERMH---FIHRDLAARNCLVSVKDYtspriV 2050
Cdd:cd05617    96 EYVNGGDLMFHMQRQRKlpeehARFYA---------------AEICIALNFLHergIIYRDLKLDNVLLDADGH-----I 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2051 KIGDFGLARdiykndyyrkrgEGLLP----------VRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd05617   156 KLTDYGMCK------------EGLGPgdttstfcgtPNYIAPEILRGEEYGFSVDWWALGVLMFEMMA-GRSPF 216
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
1903-2167 1.26e-04

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 46.58  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegtavdiLGVGSGEiKVAVKTLkkgsTDQEKIEFLKEAHLMSK--FNHPNILKQLGVCLLNEPQ----YI 1976
Cdd:cd14219    13 IGKGRYGEVW-------MGKWRGE-KVAVKVF----FTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTGSwtqlYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1977 ILELMEGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSprivkIGDFG 2056
Cdd:cd14219    81 ITDYHENGSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCC-----IADLG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2057 LARDiykndYYRKRGEGLLPV-------RWMAPESLMDGIFTTQ------SDVWSFGILIWEI----LTLG--------- 2110
Cdd:cd14219   156 LAVK-----FISDTNEVDIPPntrvgtkRYMPPEVLDESLNRNHfqsyimADMYSFGLILWEVarrcVSGGiveeyqlpy 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767943404 2111 HQPYPAHSNLDVLNYVQTGGRLEPP-------RNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQL 2167
Cdd:cd14219   231 HDLVPSDPSYEDMREIVCIKRLRPSfpnrwssDECLRQMGKLMTECWAHNPASRLTALRVKKTL 294
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
1903-2123 1.27e-04

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 46.27  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvgSGEIkVAVKTLKKGSTDQEKIEF-LKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELM 1981
Cdd:cd07839     8 IGEGTYGTVFKAKNRE-----THEI-VALKRVRLDDDDEGVPSSaLREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGgDLLTYLRKARmatfygPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvKDYTspriVKIGDFGLARDI 2061
Cdd:cd07839    82 DQ-DLKKYFDSCN------GDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLIN-KNGE----LKLADFGLARAF 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404 2062 YkndyyrkrgeglLPVR---------WMAPESLMDG--IFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVL 2123
Cdd:cd07839   150 G------------IPVRcysaevvtlWYRPPDVLFGakLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQL 210
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
2022-2130 1.32e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 46.67  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2022 LERMHFIHRDLAARNCLVsVKDYTSPRIVKIGDFGLARDIYK--------NDYYRkrgegllpvrwmAPESLMDGIFTTQ 2093
Cdd:cd14211   117 LKSLGLIHADLKPENIML-VDPVRQPYRVKVIDFGSASHVSKavcstylqSRYYR------------APEIILGLPFCEA 183
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767943404 2094 SDVWSFGILIWEiLTLGHQPYPAHSNLDVLNYV-QTGG 2130
Cdd:cd14211   184 IDMWSLGCVIAE-LFLGWPLYPGSSEYDQIRYIsQTQG 220
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
1903-2107 1.72e-04

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 46.17  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVD-ILGvgsgeIKVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCL----LNEPQ-- 1974
Cdd:cd07876    29 IGSGAQGIVC--AAFDtVLG-----INVAVKKLSRPFQNQTHAKrAYRELVLLKCVNHKNIISLLNVFTpqksLEEFQdv 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 YIILELMEGG---DLLTYLRKARMATFYgplltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVK 2051
Cdd:cd07876   102 YLVMELMDANlcqVIHMELDHERMSYLL-------------YQMLCGIKHLHSAGIIHRDLKPSNIVVK-----SDCTLK 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2052 IGDFGLARDIYKN---------DYYRkrgegllpvrwmAPESLMDGIFTTQSDVWSFGILIWEIL 2107
Cdd:cd07876   164 ILDFGLARTACTNfmmtpyvvtRYYR------------APEVILGMGYKENVDIWSVGCIMGELV 216
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2013-2114 1.89e-04

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 45.58  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2013 VDISKGCVYLERMHFIHRDLAARNCLVsvkdyTSPRIVKIGDFGLARDiYKNDYYRKRGEGLLPVRWMAPESLMDGIFTT 2092
Cdd:cd14111   106 VQILQGLEYLHGRRVLHLDIKPDNIMV-----TNLNAIKIVDFGSAQS-FNPLSLRQLGRRTGTLEYMAPEMVKGEPVGP 179
                          90       100
                  ....*....|....*....|..
gi 767943404 2093 QSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd14111   180 PADIWSIGVLTYIMLS-GRSPF 200
fn3 pfam00041
Fibronectin type III domain;
1621-1693 2.04e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.02  E-value: 2.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767943404  1621 NTSLQFNWKAPLNVNLIRFWVELQKWKYNEFYHVKTSCSQGPAYVCNITNLQPYTSYNVRVVVVYKTGENSTS 1693
Cdd:pfam00041   13 STSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
2021-2108 2.55e-04

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 45.65  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2021 YL-ERMHFIHRDLAARNCLVSVKDYtsprIVKIGDFGLARDIYK---NDY----YRkrgegllpvrwmAPESLMDGIFTT 2092
Cdd:cd14136   134 YLhTKCGIIHTDIKPENVLLCISKI----EVKIADLGNACWTDKhftEDIqtrqYR------------SPEVILGAGYGT 197
                          90
                  ....*....|....*.
gi 767943404 2093 QSDVWSFGILIWEILT 2108
Cdd:cd14136   198 PADIWSTACMAFELAT 213
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1920-2117 3.34e-04

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 45.14  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1920 LGVG-SGEIKVAVK--TLKKGS----TDQEKIEFLKEAHLMSKfNHPNILKQLGVcLLNEPQY-----------IILELM 1981
Cdd:cd14171    14 LGTGiSGPVRVCVKksTGERFAlkilLDRPKARTEVRLHMMCS-GHPNIVQIYDV-YANSVQFpgessprarllIVMELM 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 EGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLvsVKDYTSPRIVKIGDFGLArdi 2061
Cdd:cd14171    92 EGGELFDRISQHRHFT-------EKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLL--LKDNSEDAPIKLCDFGFA--- 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767943404 2062 yKNDyyrkRGEGLLP---VRWMAPESL---------MDGIFTTQS--------DVWSFGILIWeILTLGHQP-YPAH 2117
Cdd:cd14171   160 -KVD----QGDLMTPqftPYYVAPQVLeaqrrhrkeRSGIPTSPTpytydkscDMWSLGVIIY-IMLCGYPPfYSEH 230
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
1906-2108 4.74e-04

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 44.87  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1906 GAFGEVYegtavdiLGVGSGEIKV-AVKTLKKGS------TDQEKIEflKEAHLMSKfnhpnilKQLGVCLLNEPQ---- 1974
Cdd:cd05610    15 GAFGKVY-------LGRKKNNSKLyAVKVVKKADminknmVHQVQAE--RDALALSK-------SPFIVHLYYSLQsann 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1975 -YIILELMEGGDLLTYLR-----KARMATFYgplltlvdlvdlCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspr 2048
Cdd:cd05610    79 vYLVMEYLIGGDVKSLLHiygyfDEEMAVKY------------ISEVALALDYLHRHGIIHRDLKPDNMLISNEGH---- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2049 iVKIGDFGLAR----------DIY--------KNDYYRKRGE------------------------GLLPVR-------- 2078
Cdd:cd05610   143 -IKLTDFGLSKvtlnrelnmmDILttpsmakpKNDYSRTPGQvlslisslgfntptpyrtpksvrrGAARVEgerilgtp 221
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767943404 2079 -WMAPESLMDGIFTTQSDVWSFGILIWEILT 2108
Cdd:cd05610   222 dYLAPELLLGKPHGPAVDWWALGVCLFEFLT 252
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
1907-2129 5.46e-04

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 44.11  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1907 AFGEVYEGtavdilgVGSGEIKVAVKTLKKGSTDQEKIEFL-----------KEAHLMSKFNHPNILKQLGVCLLNEPQY 1975
Cdd:cd14107     2 SVYEVKEE-------IGRGTFGFVKRVTHKGNGECCAAKFIplrsstrarafQERDILARLSHRRLTCLLDQFETRKTLI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGGDLLTYLRKARMATfygplltLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdYTSPRIVKIGDF 2055
Cdd:cd14107    75 LILELCSSEELLDRLFLKGVVT-------EAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMV---SPTREDIKICDF 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767943404 2056 GLARDIYKNDY-YRKRGEgllPvRWMAPESLMDGIFTTQSDVWSFGILIWEILTLgHQPYPAHSNLDVLNYVQTG 2129
Cdd:cd14107   145 GFAQEITPSEHqFSKYGS---P-EFVAPEIVHQEPVSAATDIWALGVIAYLSLTC-HSPFAGENDRATLLNVAEG 214
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1903-2123 5.72e-04

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 44.42  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGtavdilgvgSGEIKVAVKTLKKGSTDQE----------KIEFLKEAHlmskfnHPNILKQLGVCLLNE 1972
Cdd:PLN00009   10 IGEGTYGVVYKA---------RDRVTNETIALKKIRLEQEdegvpstairEISLLKEMQ------HGNIVRLQDVVHSEK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1973 PQYIILELMEGgDLltylrKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdyTSPRIVKI 2052
Cdd:PLN00009   75 RLYLVFEYLDL-DL-----KKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLID----RRTNALKL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2053 GDFGLARDIYkndyyrkrgeglLPVR----------WMAPESLMDG-IFTTQSDVWSFGILIWEILTlgHQP-YPAHSNL 2120
Cdd:PLN00009  145 ADFGLARAFG------------IPVRtfthevvtlwYRAPEILLGSrHYSTPVDIWSVGCIFAEMVN--QKPlFPGDSEI 210

                  ...
gi 767943404 2121 DVL 2123
Cdd:PLN00009  211 DEL 213
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
561-619 6.24e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.94  E-value: 6.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404  561 YEVKVSTQDPPEVTHI-FLNISGTMLNVPELQSAMKYKVSVRASSPKRPGPWSEPSVGTT 619
Cdd:cd00063    34 YVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
1903-2115 6.70e-04

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 44.49  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYegTAVDILGVGSGEIKvavKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLL-NEPQYIILELM 1981
Cdd:cd07856    18 VGMGAFGLVC--SARDQLTGQNVAVK---KIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISpLEDIYFVTELL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1982 eGGDLLTYLRKARMATFYgplltlvdLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVK-DytspriVKIGDFGLAR- 2059
Cdd:cd07856    93 -GTDLHRLLTSRPLEKQF--------IQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENcD------LKICDFGLARi 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2060 -DIYKNDYYRKRgegllpvRWMAPESLMD-GIFTTQSDVWSFGILIWEILtLGHQPYP 2115
Cdd:cd07856   158 qDPQMTGYVSTR-------YYRAPEIMLTwQKYDVEVDIWSAGCIFAEML-EGKPLFP 207
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
1930-2107 7.58e-04

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 43.88  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1930 AVKTLKKGSTDQEKIE-------FLKEAHLMSKFN-HPNILKQLGVclLNEPQYIIL--ELMEGGDLLTYL--------R 1991
Cdd:cd14093    32 AVKIIDITGEKSSENEaeelreaTRREIEILRQVSgHPNIIELHDV--FESPTFIFLvfELCRKGELFDYLtevvtlseK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1992 KAR--MAtfygplltlvdlvdlcvDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARDIYKNDYYRk 2069
Cdd:cd14093   110 KTRriMR-----------------QLFEAVEFLHSLNIVHRDLKPENILLDDNLN-----VKISDFGFATRLDEGEKLR- 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767943404 2070 rgEGLLPVRWMAPE----SLMDGI--FTTQSDVWSFGILIWEIL 2107
Cdd:cd14093   167 --ELCGTPGYLAPEvlkcSMYDNApgYGKEVDMWACGVIMYTLL 208
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
1947-2159 9.77e-04

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 43.27  E-value: 9.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1947 LKEAHLMSKFNHPNILKQLGVCLLNEPQY-IILELMEGGDLLT--------YLRKARMATFygplltlvdlvdlcvdISK 2017
Cdd:cd14109    44 MREVDIHNSLDHPNIVQMHDAYDDEKLAVtVIDNLASTIELVRdnllpgkdYYTERQVAVF----------------VRQ 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2018 GCVYLERMH---FIHRDLAARNCLVSVKdytsprIVKIGDFGLARDIYKNDYYrkrGEGLLPVRWMAPESLMDGIFTTQS 2094
Cdd:cd14109   108 LLLALKHMHdlgIAHLDLRPEDILLQDD------KLKLADFGQSRRLLRGKLT---TLIYGSPEFVSPEIVNSYPVTLAT 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767943404 2095 DVWSFGILIWEILTlGHQPYPAHSNLDVLNYVQTGG---RLEPPRNCPDDLWNLMTQCWAQEPDQRPT 2159
Cdd:cd14109   179 DMWSVGVLTYVLLG-GISPFLGDNDRETLTNVRSGKwsfDSSPLGNISDDARDFIKKLLVYIPESRLT 245
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
1930-2114 1.20e-03

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 43.56  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1930 AVKTLKKG-STDQEKIEFLK-EAHLM-SKFNHPnILKQLGVCLLNEPQ-YIILELMEGGDLLTYLRKARM-----ATFYG 2000
Cdd:cd05588    24 AMKVIKKElVNDDEDIDWVQtEKHVFeTASNHP-FLVGLHSCFQTESRlFFVIEFVNGGDLMFHMQRQRRlpeehARFYS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2001 plltlvdlvdlcVDISKGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLARdiykndyyrkrgEGLLP---- 2076
Cdd:cd05588   103 ------------AEISLALNFLHEKGIIYRDLKLDNVLLDSEGH-----IKLTDYGMCK------------EGLRPgdtt 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767943404 2077 ------VRWMAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPY 2114
Cdd:cd05588   154 stfcgtPNYIAPEILRGEDYGFSVDWWALGVLMFEMLA-GRSPF 196
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
1924-2114 2.04e-03

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 42.32  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1924 SGEIKVAVKTLKKGSTDQEKIEfLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKarmATFYGPLL 2003
Cdd:cd14088    25 TGKLYTCKKFLKRDGRKVRKAA-KNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILD---QGYYSERD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2004 TLVDLVdlcvDISKGCVYLERMHFIHRDLAARNcLVSVKDYTSPRIVkIGDFGLARdiYKNDYYRkrgEGLLPVRWMAPE 2083
Cdd:cd14088   101 TSNVIR----QVLEAVAYLHSLKIVHRNLKLEN-LVYYNRLKNSKIV-ISDFHLAK--LENGLIK---EPCGTPEYLAPE 169
                         170       180       190
                  ....*....|....*....|....*....|.
gi 767943404 2084 SLMDGIFTTQSDVWSFGILIWeILTLGHQPY 2114
Cdd:cd14088   170 VVGRQRYGRPVDCWAIGVIMY-ILLSGNPPF 199
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2017-2119 2.23e-03

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 42.37  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2017 KGCVYLERMHFIHRDLAARNCLVSVKDYtspriVKIGDFGLAR------DIYKND----YYRkrgegllpvrwmAPESLM 2086
Cdd:cd07844   109 RGLAYCHQRRVLHRDLKPQNLLISERGE-----LKLADFGLARaksvpsKTYSNEvvtlWYR------------PPDVLL 171
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767943404 2087 DGI-FTTQSDVWSFGILIWEILTlGHQPYPAHSN 2119
Cdd:cd07844   172 GSTeYSTSLDMWGVGCIFYEMAT-GRPLFPGSTD 204
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
1899-2069 2.74e-03

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 42.06  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1899 LRLLLGSGAFGEVYEGtaVDILgvgSGEIkVAVKtLKKGSTDQEKIEFlkEAHLMSKFN-HPNI--LKQLGVCllNEPQY 1975
Cdd:cd14016     4 LVKKIGSGSFGEVYLG--IDLK---TGEE-VAIK-IEKKDSKHPQLEY--EAKVYKLLQgGPGIprLYWFGQE--GDYNV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMegGDLLTYLRKARMATFygplltlvdlvdlcvdiSKGCV------------YLERMHFIHRDLAARNCLVSVKD 2043
Cdd:cd14016    73 MVMDLL--GPSLEDLFNKCGRKF-----------------SLKTVlmladqmisrleYLHSKGYIHRDIKPENFLMGLGK 133
                         170       180
                  ....*....|....*....|....*.
gi 767943404 2044 ytSPRIVKIGDFGLARdiykndYYRK 2069
Cdd:cd14016   134 --NSNKVYLIDFGLAK------KYRD 151
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
1926-2126 3.31e-03

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 42.34  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1926 EIKVAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCL----LNEPQ--YIILELMEGG---DLLTYLRKARM 1995
Cdd:cd07875    49 ERNVAIKKLSRPFQNQTHAKrAYRELVLMKCVNHKNIIGLLNVFTpqksLEEFQdvYIVMELMDANlcqVIQMELDHERM 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1996 ATFYgplltlvdLVDLCvdiskGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLARDIYKN---------DY 2066
Cdd:cd07875   129 SYLL--------YQMLC-----GIKHLHSAGIIHRDLKPSNIVVK-----SDCTLKILDFGLARTAGTSfmmtpyvvtRY 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2067 YRkrgegllpvrwmAPESLMDGIFTTQSDVWSFGILIWEILTlGHQPYPAHSNLDVLNYV 2126
Cdd:cd07875   191 YR------------APEVILGMGYKENVDIWSVGCIMGEMIK-GGVLFPGTDHIDQWNKV 237
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
1947-2123 4.74e-03

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 41.04  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1947 LKEAHLMSKFNHPNIL-------KQLGVCllnepqyIILELMEGGDLLTYLRKarmatfygPLLTLVDLVDLCVDISKGC 2019
Cdd:cd14108    46 RRELALLAELDHKSIVrfhdafeKRRVVI-------IVTELCHEELLERITKR--------PTVCESEVRSYMRQLLEGI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2020 VYLERMHFIHRDLAARNCLVSvkDYTSPRiVKIGDFGLARDIYKND-YYRKRGeglLPvRWMAPESLMDGIFTTQSDVWS 2098
Cdd:cd14108   111 EYLHQNDVLHLDLKPENLLMA--DQKTDQ-VRICDFGNAQELTPNEpQYCKYG---TP-EFVAPEIVNQSPVSKVTDIWP 183
                         170       180
                  ....*....|....*....|....*
gi 767943404 2099 FGILIWEILTlGHQPYPAHSNLDVL 2123
Cdd:cd14108   184 VGVIAYLCLT-GISPFVGENDRTTL 207
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
1903-2107 7.41e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 40.98  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEGTAVDilgvGSGEIKVAVKTLKKGSTDQEKIEFLKeahlmsKFNHPNILKQLG-------VCLLnEPQY 1975
Cdd:PHA03207  100 LTPGSEGEVFVCTKHG----DEQRKKVIVKAVTGGKTPGREIDILK------TISHRAIINLIHayrwkstVCMV-MPKY 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IIlelmeggDLLTYLRKArmatfyGPLLTLVDlvdlcVDISKGC----VYLERMHFIHRDLAARNCLVsvkDYtsPRIVK 2051
Cdd:PHA03207  169 KC-------DLFTYVDRS------GPLPLEQA-----ITIQRRLlealAYLHGRGIIHRDVKTENIFL---DE--PENAV 225
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767943404 2052 IGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEIL 2107
Cdd:PHA03207  226 LGDFGAACKLDAHPDTPQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMS 281
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
1903-2123 8.15e-03

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 40.59  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1903 LGSGAFGEVYEgtAVDIlgvGSGEIkVAVKTLKKgSTDQEKI--EFLKEAHLMSKFNH-PNILKQLGVCLLNE---PQ-Y 1975
Cdd:cd07837     9 IGEGTYGKVYK--ARDK---NTGKL-VALKKTRL-EMEEEGVpsTALREVSLLQMLSQsIYIVRLLDVEHVEEngkPLlY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1976 IILELMEGgDLLTYLRKARMATfyGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSvkdyTSPRIVKIGDF 2055
Cdd:cd07837    82 LVFEYLDT-DLKKFIDSYGRGP--HNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVD----KQKGLLKIADL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767943404 2056 GLAR--DIYKNDYYRKrgegLLPVRWMAPESLMDGI-FTTQSDVWSFGILIWEILTlgHQP-YPAHSNLDVL 2123
Cdd:cd07837   155 GLGRafTIPIKSYTHE----IVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSR--KQPlFPGDSELQQL 220
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
1929-2186 9.72e-03

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 40.84  E-value: 9.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1929 VAVKTLKKGSTDQEKIE-FLKEAHLMSKFNHPNILKQLGVCL----LNEPQ--YIILELMEGG---DLLTYLRKARMATF 1998
Cdd:cd07874    45 VAIKKLSRPFQNQTHAKrAYRELVLMKCVNHKNIISLLNVFTpqksLEEFQdvYLVMELMDANlcqVIQMELDHERMSYL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 1999 YgplltlvdLVDLCvdiskGCVYLERMHFIHRDLAARNCLVSvkdytSPRIVKIGDFGLAR----DIYKNDYYRKRgegl 2074
Cdd:cd07874   125 L--------YQMLC-----GIKHLHSAGIIHRDLKPSNIVVK-----SDCTLKILDFGLARtagtSFMMTPYVVTR---- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767943404 2075 lpvRWMAPESLMDGIFTTQSDVWSFGILIWEILTlgHQP-YPAHSNLDVLNYVQTggRLEPPrnCPDDLWNLMTQCwAQE 2153
Cdd:cd07874   183 ---YYRAPEVILGMGYKENVDIWSVGCIMGEMVR--HKIlFPGRDYIDQWNKVIE--QLGTP--CPEFMKKLQPTV-RNY 252
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767943404 2154 PDQRPTFHRIQdqlqlFRNFFLNSIYKSRDEAN 2186
Cdd:cd07874   253 VENRPKYAGLT-----FPKLFPDSLFPADSEHN 280
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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