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Conserved domains on  [gi|1237938074|ref|NP_001341538|]
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serine/threonine-protein kinase B-raf isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
463-715 0e+00

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: 581.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLH 542
Cdd:cd14062     1 IGSGSFGTVYKGRWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWCEGSSLYKHLH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 543 IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAP 622
Cdd:cd14062    81 VLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQFEQPTGSILWMAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 623 EVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRD 702
Cdd:cd14062   161 EVIRMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRGYLRPDLSKVRSDTPKALRRLMEDCIKFQRD 240
                         250
                  ....*....|...
gi 1237938074 703 ERPLFPQILASIE 715
Cdd:cd14062   241 ERPLFPQILASLE 253
RBD_BRAF cd17134
Ras-binding domain (RBD) found in serine/threonine-protein kinase BRAF; BRAF, also termed ...
154-232 2.64e-50

Ras-binding domain (RBD) found in serine/threonine-protein kinase BRAF; BRAF, also termed proto-oncogene B-Raf, or p94, or v-Raf murine sarcoma viral oncogene homolog B1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. BRAF is the most effective RAF kinase in terms of induction of MEK/ERK activity. It is somatically mutated in a number of human cancers.


:

Pssm-ID: 340654  Cd Length: 79  Bit Score: 170.21  E-value: 2.64e-50
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 154 KPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPL 232
Cdd:cd17134     1 KPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPL 79
C1_B-Raf cd20871
protein kinase C conserved region 1 (C1 domain) found in B-Raf (Rapidly Accelerated ...
230-289 2.38e-38

protein kinase C conserved region 1 (C1 domain) found in B-Raf (Rapidly Accelerated Fibrosarcoma) kinase and similar proteins; Serine/threonine-protein kinase B-Raf, also called proto-oncogene B-Raf, p94, or v-Raf murine sarcoma viral oncogene homolog B1, 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. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410421  Cd Length: 60  Bit Score: 136.31  E-value: 2.38e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 230 VPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLL 289
Cdd:cd20871     1 VPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLL 60
 
Name Accession Description Interval E-value
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
463-715 0e+00

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: 581.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLH 542
Cdd:cd14062     1 IGSGSFGTVYKGRWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWCEGSSLYKHLH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 543 IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAP 622
Cdd:cd14062    81 VLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQFEQPTGSILWMAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 623 EVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRD 702
Cdd:cd14062   161 EVIRMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRGYLRPDLSKVRSDTPKALRRLMEDCIKFQRD 240
                         250
                  ....*....|...
gi 1237938074 703 ERPLFPQILASIE 715
Cdd:cd14062   241 ERPLFPQILASLE 253
Pkinase pfam00069
Protein kinase domain;
458-716 3.36e-85

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 270.25  E-value: 3.36e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCE 533
Cdd:pfam00069   2 EVLEKLGSGSFGTVYKAKhrdTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDaFEDKDNLYLVLEYVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGSHQFEQL 613
Cdd:pfam00069  82 GGSLFDLLSE-KGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLAR---QLNSGSSLTTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 SGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSkvrSNCPKAMKRLM 693
Cdd:pfam00069 158 VGTPWYMAPEVLG---GNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELP---SNLSEEAKDLL 231
                         250       260
                  ....*....|....*....|...
gi 1237938074 694 AECLKKKRDERPLFPQILASIEL 716
Cdd:pfam00069 232 KKLLKKDPSKRLTATEALQHPWF 254
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
457-711 1.34e-69

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 228.95  E-value: 1.34e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  457 ITVGQRIGSGSFGTVYKGKWHG-------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIV 528
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGkggkkkvEVAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEpLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  529 TQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGSH 608
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGL----SRDLYDD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  609 QFEQLSGSIL---WMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYLSPdlskVRSN 684
Cdd:smart00219 156 DYYRKRGGKLpirWMAPESLK---EGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEE-VLEYLKNGYRLP----QPPN 227
                          250       260
                   ....*....|....*....|....*..
gi 1237938074  685 CPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:smart00219 228 CPPELYDLMLQCWAEDPEDRPTFSELV 254
RBD_BRAF cd17134
Ras-binding domain (RBD) found in serine/threonine-protein kinase BRAF; BRAF, also termed ...
154-232 2.64e-50

Ras-binding domain (RBD) found in serine/threonine-protein kinase BRAF; BRAF, also termed proto-oncogene B-Raf, or p94, or v-Raf murine sarcoma viral oncogene homolog B1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. BRAF is the most effective RAF kinase in terms of induction of MEK/ERK activity. It is somatically mutated in a number of human cancers.


Pssm-ID: 340654  Cd Length: 79  Bit Score: 170.21  E-value: 2.64e-50
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 154 KPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPL 232
Cdd:cd17134     1 KPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPL 79
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
458-733 1.46e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 147.58  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGDVAVKMLNV-TAPTPQQLQAFKNEVGVLRKTRHVN--ILLFMGYSTKPQLAIVTQWCEG 534
Cdd:COG0515     3 RILRKLGEGSFGEVYLARDRKLVALKVLAKkLESKSKEVERFLREIQILASLNHPPniVKLYDFFQDEGSLYLVMEYVDG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLH--IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT-VKIGDFGLATV----KSRWSGS 607
Cdd:COG0515    83 GSLEDLLKkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLlpdpGSTSSIP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNR-------DQIIFMVGRGYLSPDLSK 680
Cdd:COG0515   163 ALPSTSVGTPGYMAPEVLLGLSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSsatsqtlKIILELPTPSLASPLSPS 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 681 VRSNCPKAMKRLMAECLKKKRDERPLfpqilaSIELLARSLPKIHRSASEPSL 733
Cdd:COG0515   243 NPELISKAASDLLKKLLAKDPKNRLS------SSSDLSHDLLAHLKLKESDLS 289
C1_B-Raf cd20871
protein kinase C conserved region 1 (C1 domain) found in B-Raf (Rapidly Accelerated ...
230-289 2.38e-38

protein kinase C conserved region 1 (C1 domain) found in B-Raf (Rapidly Accelerated Fibrosarcoma) kinase and similar proteins; Serine/threonine-protein kinase B-Raf, also called proto-oncogene B-Raf, p94, or v-Raf murine sarcoma viral oncogene homolog B1, 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. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410421  Cd Length: 60  Bit Score: 136.31  E-value: 2.38e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 230 VPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLL 289
Cdd:cd20871     1 VPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLL 60
RBD pfam02196
Raf-like Ras-binding domain;
156-225 2.57e-28

Raf-like Ras-binding domain;


Pssm-ID: 426652  Cd Length: 69  Bit Score: 108.00  E-value: 2.57e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 156 IVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQdGEKKPIGWDTDISWLTGEELHVE 225
Cdd:pfam02196   1 LCRVYLPNGQRTVVQVRPGETVRDALSKLCKKRGLNPEACDVYLVG-GQKYPLDWDTDSSTLEGEEIRVE 69
RBD smart00455
Raf-like Ras-binding domain;
157-227 3.53e-27

Raf-like Ras-binding domain;


Pssm-ID: 128731  Cd Length: 70  Bit Score: 104.67  E-value: 3.53e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074  157 VRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIqdGEKKPIGWDTDISWLTGEELHVEVL 227
Cdd:smart00455   2 CKVHLPDNQRTVVKVRPGKTVRDALAKALKKRGLNPECCVVRLR--GEKKPLDLNQPISSLDGQELVVEEL 70
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
459-657 9.30e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 96.79  E-value: 9.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGK---WHGDVAVKMLNvtaptpQQLQA-------FKNE---VGVLRktrH---VNIllfmgYST- 521
Cdd:NF033483   11 IGERIGRGGMAEVYLAKdtrLDRDVAVKVLR------PDLARdpefvarFRREaqsAASLS---HpniVSV-----YDVg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 522 --KPQLAIVTQWCEGSSL------YHHLHIIETkfemiklIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIG 593
Cdd:NF033483   77 edGGIPYIVMEYVDGRTLkdyireHGPLSPEEA-------VEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVT 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 594 DFGLAtvksRWSGSHQFEQlSGSIL----WMAPEVIR--MQDKnpysfQSDVYAFGIVLYELMTGQLPYS 657
Cdd:NF033483  150 DFGIA----RALSSTTMTQ-TNSVLgtvhYLSPEQARggTVDA-----RSDIYSLGIVLYEMLTGRPPFD 209
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
448-712 9.74e-20

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 94.42  E-value: 9.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  448 DDWEIPDGQITVGQRIGSGSFGTVYKGK---------WHgdvAVKMLNVTAPTPQQLQAfknEVGVLRKTRHVNILLFMG 518
Cdd:PTZ00266     6 DDGESRLNEYEVIKKIGNGRFGEVFLVKhkrtqeffcWK---AISYRGLKEREKSQLVI---EVNVMRELKHKNIVRYID 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  519 Y---STKPQLAIVTQWCEGSSLYHHLHIIETKFEMIK---LIDIARQTAQGMDYLH-------AKSIIHRDLKSNNIFLH 585
Cdd:PTZ00266    80 RflnKANQKLYILMEFCDAGDLSRNIQKCYKMFGKIEehaIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  586 EDL-----------------TVKIGDFGLATVKSRWSGSHQfeqLSGSILWMAPEVIRMQDKNpYSFQSDVYAFGIVLYE 648
Cdd:PTZ00266   160 TGIrhigkitaqannlngrpIAKIGDFGLSKNIGIESMAHS---CVGTPYYWSPELLLHETKS-YDDKSDMWALGCIIYE 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074  649 LMTGQLPYSNINNRDQIIFMVGRGylsPDLS-KVRSncpKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:PTZ00266   236 LCSGKTPFHKANNFSQLISELKRG---PDLPiKGKS---KELNILIKNLLNLSAKERPSALQCLG 294
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
235-280 8.44e-17

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 74.79  E-value: 8.44e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 235 HNFVRKTFFTLAFCDFCRKLL----FQGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLwglgKQGLKCSWCKLNVHKRCHEKVPPEC 50
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
235-280 3.17e-14

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 67.49  E-value: 3.17e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1237938074  235 HNFVRKTFFTLAFCDFCRKLLF----QGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWgsfkQGLRCSECKVKCHKKCADKVPKAC 50
 
Name Accession Description Interval E-value
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
463-715 0e+00

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: 581.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLH 542
Cdd:cd14062     1 IGSGSFGTVYKGRWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWCEGSSLYKHLH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 543 IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAP 622
Cdd:cd14062    81 VLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQFEQPTGSILWMAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 623 EVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRD 702
Cdd:cd14062   161 EVIRMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRGYLRPDLSKVRSDTPKALRRLMEDCIKFQRD 240
                         250
                  ....*....|...
gi 1237938074 703 ERPLFPQILASIE 715
Cdd:cd14062   241 ERPLFPQILASLE 253
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
448-721 0e+00

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: 577.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 448 DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAI 527
Cdd:cd14151     1 DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGS 607
Cdd:cd14151    81 VTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPK 687
Cdd:cd14151   161 HQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPK 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1237938074 688 AMKRLMAECLKKKRDERPLFPQILASIELLARSL 721
Cdd:cd14151   241 AMKRLMAECLKKKRDERPLFPQILASIELLARSL 274
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
456-720 0e+00

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: 522.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd14150     1 EVSMLKRIGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAIITQWCEGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSG 615
Cdd:cd14150    81 SLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSQQVEQPSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAE 695
Cdd:cd14150   161 SILWMAPEVIRMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSPDLSKLSSNCPKAMKRLLID 240
                         250       260
                  ....*....|....*....|....*
gi 1237938074 696 CLKKKRDERPLFPQILASIELLARS 720
Cdd:cd14150   241 CLKFKREERPLFPQILVSIELLQRL 265
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
444-726 7.75e-176

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: 505.34  E-value: 7.75e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 444 RDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP 523
Cdd:cd14149     1 RDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR 603
Cdd:cd14149    81 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRS 683
Cdd:cd14149   161 WSGSQQVEQPTGSILWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1237938074 684 NCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHR 726
Cdd:cd14149   241 NCPKAMKRLVADCIKKVKEERPLFPQILSSIELLQHSLPKINR 283
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
463-711 2.09e-101

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: 312.16  E-value: 2.09e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG-DVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGSSLYHH 540
Cdd:cd13999     1 IGSGSFGEVYKGKWRGtDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPpLCIVTEYMPGGSLYDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 541 LHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHqfEQLSGSILWM 620
Cdd:cd13999    81 LHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKM--TGVVGTPRWM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 621 APEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPdlskVRSNCPKAMKRLMAECLKKK 700
Cdd:cd13999   159 APEVLRGE---PYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPP----IPPDCPPELSKLIKRCWNED 231
                         250
                  ....*....|.
gi 1237938074 701 RDERPLFPQIL 711
Cdd:cd13999   232 PEKRPSFSEIV 242
Pkinase pfam00069
Protein kinase domain;
458-716 3.36e-85

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 270.25  E-value: 3.36e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCE 533
Cdd:pfam00069   2 EVLEKLGSGSFGTVYKAKhrdTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDaFEDKDNLYLVLEYVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGSHQFEQL 613
Cdd:pfam00069  82 GGSLFDLLSE-KGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLAR---QLNSGSSLTTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 SGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSkvrSNCPKAMKRLM 693
Cdd:pfam00069 158 VGTPWYMAPEVLG---GNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELP---SNLSEEAKDLL 231
                         250       260
                  ....*....|....*....|...
gi 1237938074 694 AECLKKKRDERPLFPQILASIEL 716
Cdd:pfam00069 232 KKLLKKDPSKRLTATEALQHPWF 254
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
456-719 5.34e-81

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: 259.97  E-value: 5.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY-STKPQLAIVTQWCEG 534
Cdd:cd14063     1 ELEIKEVIGKGRFGRVHRGRWHGDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGAcMDPPHLAIVTSLCKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLhEDLTVKIGDFGLATVKSRWSGSHQFEQL- 613
Cdd:cd14063    81 RTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDFGLFSLSGLLQPGRREDTLv 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 --SGSILWMAPEVIR-------MQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGyLSPDLSKVRSn 684
Cdd:cd14063   160 ipNGWLCYLAPEIIRalspdldFEESLPFTKASDVYAFGTVWYELLAGRWPFKE-QPAESIIWQVGCG-KKQSLSQLDI- 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1237938074 685 cPKAMKRLMAECLKKKRDERPLFPQILASIELLAR 719
Cdd:cd14063   237 -GREVKDILMQCWAYDPEKRPTFSDLLRMLERLPK 270
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
457-714 1.81e-75

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 244.71  E-value: 1.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKGKWHGD-------VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIV 528
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEgentkikVAVKTLKEGA-DEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEpLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSH 608
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGY--LSPDlskvrsNC 685
Cdd:pfam07714 160 KRGGGKLPIKWMAPESLK---DGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEE-VLEYLEDGYrlPQPE------NC 229
                         250       260
                  ....*....|....*....|....*....
gi 1237938074 686 PKAMKRLMAECLKKKRDERPLFPQILASI 714
Cdd:pfam07714 230 PDELYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
457-711 1.34e-69

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 228.95  E-value: 1.34e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  457 ITVGQRIGSGSFGTVYKGKWHG-------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIV 528
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGkggkkkvEVAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEpLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  529 TQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGSH 608
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGL----SRDLYDD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  609 QFEQLSGSIL---WMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYLSPdlskVRSN 684
Cdd:smart00219 156 DYYRKRGGKLpirWMAPESLK---EGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEE-VLEYLKNGYRLP----QPPN 227
                          250       260
                   ....*....|....*....|....*..
gi 1237938074  685 CPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:smart00219 228 CPPELYDLMLQCWAEDPEDRPTFSELV 254
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
457-711 1.24e-68

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: 226.66  E-value: 1.24e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  457 ITVGQRIGSGSFGTVYKGKWHG-------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIV 528
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGkgdgkevEVAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEpLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  529 TQWCEGSSLYHHLHI-IETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGS 607
Cdd:smart00221  80 MEYMPGGDLLDYLRKnRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGL----SRDLYD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  608 HQFEQLSGSIL---WMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYLSPdlskVRS 683
Cdd:smart00221 156 DDYYKVKGGKLpirWMAPESLK---EGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAE-VLEYLKKGYRLP----KPP 227
                          250       260
                   ....*....|....*....|....*...
gi 1237938074  684 NCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:smart00221 228 NCPPELYKLMLQCWAEDPEDRPTFSELV 255
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
463-715 9.58e-66

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: 218.95  E-value: 9.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGS 535
Cdd:cd00192     3 LGEGAFGEVYKGKLKGgdgktvDVAVKTLKEDA-SESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEpLYLVMEYMEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHL--------HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGS 607
Cdd:cd00192    82 DLLDFLrksrpvfpSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGL----SRDIYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQLSGS----ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNrDQIIFMVGRGY--LSPDlsk 680
Cdd:cd00192   158 DDYYRKKTGgklpIRWMAPESLKDGI---FTSKSDVWSFGVLLWEIFTlGATPYPGLSN-EEVLEYLRKGYrlPKPE--- 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1237938074 681 vrsNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd00192   231 ---NCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
458-712 2.32e-62

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 209.69  E-value: 2.32e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  458 TVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTaPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCE 533
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTgklVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDvFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  534 GSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGSHQFEQL 613
Cdd:smart00220  81 GGDLFDLLKK-RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLAR---QLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  614 SGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKvrSNCPKAMKRLM 693
Cdd:smart00220 157 VGTPEYMAPEVLL---GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPE--WDISPEAKDLI 231
                          250
                   ....*....|....*....
gi 1237938074  694 AECLKKKRDERPLFPQILA 712
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQ 250
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
456-719 3.53e-57

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: 196.38  E-value: 3.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEG 534
Cdd:cd14153     1 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSpPHLAIITSLCKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFlHEDLTVKIGDFGLATVKSRWSGSHQFEQL- 613
Cdd:cd14153    81 RTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-YDNGKVVITDFGLFTISGVLQAGRREDKLr 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 --SGSILWMAPEVIRM------QDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGyLSPDLSKVrsNC 685
Cdd:cd14153   160 iqSGWLCHLAPEIIRQlspeteEDKLPFSKHSDVFAFGTIWYELHAREWPFKT-QPAEAIIWQVGSG-MKPNLSQI--GM 235
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1237938074 686 PKAMKRLMAECLKKKRDERPLFPQILASIELLAR 719
Cdd:cd14153   236 GKEISDILLFCWAYEQEERPTFSKLMEMLEKLPK 269
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
448-707 2.84e-54

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: 188.00  E-value: 2.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 448 DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGD--VAVKMLNvtaPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ- 524
Cdd:cd05068     1 DQWEIDRKSLKLLRKLGSGQFGEVWEGLWNNTtpVAVKTLK---PGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEp 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 LAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrW 604
Cdd:cd05068    78 IYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARV---I 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQLSGS---ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPDLsk 680
Cdd:cd05068   155 KVEDEYEAREGAkfpIKWTAPEAANY---NRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNA-EVLQQVERGYRMPCP-- 228
                         250       260
                  ....*....|....*....|....*..
gi 1237938074 681 vrSNCPKAMKRLMAECLKKKRDERPLF 707
Cdd:cd05068   229 --PNCPPQLYDIMLECWKADPMERPTF 253
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
456-731 2.63e-53

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: 185.94  E-value: 2.63e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEG 534
Cdd:cd14152     1 QIELGELIGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHpPHLAIITSFCKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFlHEDLTVKIGDFGL---ATVKSRWSGSHQFE 611
Cdd:cd14152    81 RTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-YDNGKVVITDFGLfgiSGVVQEGRRENELK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 612 QLSGSILWMAPEVIRM------QDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGY-LSPDLSKVrsN 684
Cdd:cd14152   160 LPHDWLCYLAPEIVREmtpgkdEDCLPFSKAADVYAFGTIWYELQARDWPLKN-QPAEALIWQIGSGEgMKQVLTTI--S 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 685 CPKAMKRLMAECLKKKRDERPLFPQILASIEllarSLPKIHRSASEP 731
Cdd:cd14152   237 LGKEVTEILSACWAFDLEERPSFTLLMDMLE----KLPKLNRRLSHP 279
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
456-705 2.24e-52

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: 182.72  E-value: 2.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQW 531
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLALNLDTgelMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGtERTENTLNIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHiietKF-----EMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSG 606
Cdd:cd06606    81 VPGGSLASLLK----KFgklpePVVRKY--TRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIAT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSkvrSNCP 686
Cdd:cd06606   155 GEGTKSLRGTPYWMAPEVIRGEG---YGRAADIWSLGCTVIEMATGKPPWSELGNPVAALFKIGSSGEPPPIP---EHLS 228
                         250
                  ....*....|....*....
gi 1237938074 687 KAMKRLMAECLKKKRDERP 705
Cdd:cd06606   229 EEAKDFLRKCLQRDPKKRP 247
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
458-721 1.49e-51

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: 180.48  E-value: 1.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVT-APTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWC 532
Cdd:cd14014     3 RLVRLLGRGGMGEVYRArdtLLGRPVAIKVLRPElAEDEEFRERFLREARALARLSHPNIVrVYDVGEDDGRPYIVMEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHhlhIIETKFEMI--KLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwSGSHQF 610
Cdd:cd14014    83 EGGSLAD---LLRERGPLPprEALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGD-SGLTQT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 EQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPdlSKVRSNCPKAMK 690
Cdd:cd14014   159 GSVLGTPAYMAPEQAR---GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPP--SPLNPDVPPALD 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 691 RLMAECLKKKRDERPlfpqilASIELLARSL 721
Cdd:cd14014   234 AIILRALAKDPEERP------QSAAELLAAL 258
RBD_BRAF cd17134
Ras-binding domain (RBD) found in serine/threonine-protein kinase BRAF; BRAF, also termed ...
154-232 2.64e-50

Ras-binding domain (RBD) found in serine/threonine-protein kinase BRAF; BRAF, also termed proto-oncogene B-Raf, or p94, or v-Raf murine sarcoma viral oncogene homolog B1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. BRAF is the most effective RAF kinase in terms of induction of MEK/ERK activity. It is somatically mutated in a number of human cancers.


Pssm-ID: 340654  Cd Length: 79  Bit Score: 170.21  E-value: 2.64e-50
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 154 KPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPL 232
Cdd:cd17134     1 KPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPL 79
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
463-716 2.87e-50

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: 176.15  E-value: 2.87e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD-VAVKMLNVTAPTpqqlqafknEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEGSSLYHH 540
Cdd:cd14059     1 LGSGAQGAVFLGKFRGEeVAVKKVRDEKET---------DIKHLRKLNHPNIIKFKGVCTQaPCYCILMEYCPYGQLYEV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 541 LHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFeqlSGSILWM 620
Cdd:cd14059    72 LRA-GREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMSF---AGTVAWM 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 621 APEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNINNrDQIIFMVGRGYLS-PdlskVRSNCPKAMKRLMAECLKK 699
Cdd:cd14059   148 APEVIRNE---PCSEKVDIWSFGVVLWELLTGEIPYKDVDS-SAIIWGVGSNSLQlP----VPSTCPDGFKLLMKQCWNS 219
                         250
                  ....*....|....*..
gi 1237938074 700 KRDERPLFPQILASIEL 716
Cdd:cd14059   220 KPRNRPSFRQILMHLDI 236
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
463-722 1.81e-49

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: 174.55  E-value: 1.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG-DVAVKMLNVTaptpQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGSSLYHH 540
Cdd:cd14058     1 VGRGSFGVVCKARWRNqIVAVKIIESE----SEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKpVCLVMEYAEGGSLYNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 541 LHIIETK--FEMIKLIDIARQTAQGMDYLHA---KSIIHRDLKSNNIFLHEDLTV-KIGDFGLATVKSRWSGSHQfeqls 614
Cdd:cd14058    77 LHGKEPKpiYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTACDISTHMTNNK----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINN-RDQIIFMVGRGYlSPDLSKvrsNCPKAMKRLM 693
Cdd:cd14058   152 GSAAWMAPEVF---EGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGpAFRIMWAVHNGE-RPPLIK---NCPKPIESLM 224
                         250       260
                  ....*....|....*....|....*....
gi 1237938074 694 AECLKKKRDERPLFPQILASIELLARSLP 722
Cdd:cd14058   225 TRCWSKDPEKRPSMKEIVKIMSHLMQFFP 253
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
462-707 5.30e-49

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: 172.85  E-value: 5.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKWHG--DVAVKMLNVTAPTPQqlqAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGSSLY 538
Cdd:cd05034     2 KLGAGQFGEVWMGVWNGttKVAVKTLKPGTMSPE---AFLQEAQIMKKLRHDKLVQLYAVCSDEEpIYIVTELMSKGSLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIE-TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRWSGSHQFEQLSGS- 616
Cdd:cd05034    79 DYLRTGEgRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLA----RLIEDDEYTAREGAk 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 617 --ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPDLskvrSNCPKAMKRLM 693
Cdd:cd05034   155 fpIKWTAPEAALY---GRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNR-EVLEQVERGYRMPKP----PGCPDELYDIM 226
                         250
                  ....*....|....
gi 1237938074 694 AECLKKKRDERPLF 707
Cdd:cd05034   227 LQCWKKEPEERPTF 240
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
463-717 2.46e-48

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: 172.07  E-value: 2.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG--DVAVKMLNVTAPtPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQL-AIVTQWCEGSSLYH 539
Cdd:cd14066     1 IGSGGFGTVYKGVLENgtVVAVKRLNEMNC-AASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEkLLVYEYMPNGSLED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 540 HLHIIETKFEM--IKLIDIARQTAQGMDYLH---AKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLS 614
Cdd:cd14066    80 RLHCHKGSPPLpwPQRLKIAKGIARGLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTSAVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI-----IFM-----VGRGYLSPDLSK---V 681
Cdd:cd14066   160 GTIGYLAPEYIRT---GRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRkdlveWVEskgkeELEDILDKRLVDddgV 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1237938074 682 RSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd14066   237 EEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
463-714 4.88e-48

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: 170.72  E-value: 4.88e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLY 538
Cdd:cd08215     8 IGKGSFGSAYLVRRKSDgklYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYEsFEENGKLCIVMEYADGGDLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLH---IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKsrwsgSHQFEQLS- 614
Cdd:cd08215    88 QKIKkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVL-----ESTTDLAKt 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 --GSILWMAPEVIrmQDKnPYSFQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGRGYLSPdLSKVRSncpKAMKRL 692
Cdd:cd08215   163 vvGTPYYLSPELC--ENK-PYNYKSDIWALGCVLYELCTLKHPF-EANNLPALVYKIVKGQYPP-IPSQYS---SELRDL 234
                         250       260
                  ....*....|....*....|..
gi 1237938074 693 MAECLKKKRDERPLFPQILASI 714
Cdd:cd08215   235 VNSMLQKDPEKRPSANEILSSP 256
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
458-711 9.59e-48

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: 169.69  E-value: 9.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTapTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCE 533
Cdd:cd05122     3 EILEKIGKGGFGVVYKARHKKTgqiVAIKKINLE--SKEKKESILNEIAILKKCKHPNIVKYYGsYLKKDELWIVMEFCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHhlhIIETKFEMIKLIDIA---RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQF 610
Cdd:cd05122    81 GGSLKD---LLKNTNKTLTEQQIAyvcKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRNTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 eqlSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNInNRDQIIFMVGRGyLSPDLsKVRSNCPKAMK 690
Cdd:cd05122   158 ---VGTPYWMAPEVIQ---GKPYGFKADIWSLGITAIEMAEGKPPYSEL-PPMKALFLIATN-GPPGL-RNPKKWSKEFK 228
                         250       260
                  ....*....|....*....|.
gi 1237938074 691 RLMAECLKKKRDERPLFPQIL 711
Cdd:cd05122   229 DFLKKCLQKDPEKRPTAEQLL 249
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
463-714 3.85e-47

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: 166.68  E-value: 3.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTpQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLY 538
Cdd:cd00180     1 LGKGSFGKVYKARDKETgkkVAVKVIPKEKLK-KLLEELLREIEILKKLNHPNIVKLYDvFETENFLYLVMEYCEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSIL 618
Cdd:cd00180    80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPPY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 619 WMAPEvirMQDKNPYSFQSDVYAFGIVLYELmtgqlpysninnrdqiifmvgrgylspdlskvrsncpKAMKRLMAECLK 698
Cdd:cd00180   160 YAPPE---LLGGRYYGPKVDIWSLGVILYEL-------------------------------------EELKDLIRRMLQ 199
                         250
                  ....*....|....*.
gi 1237938074 699 KKRDERPLFPQILASI 714
Cdd:cd00180   200 YDPKKRPSAKELLEHL 215
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
463-715 1.76e-46

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: 166.41  E-value: 1.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD-VAVKMLNVTA--PTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEGSSLY 538
Cdd:cd14061     2 IGVGGFGKVYRGIWRGEeVAVKAARQDPdeDISVTLENVRQEARLFWMLRHPNIIALRGVCLQpPNLCLVMEYARGGALN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLhiIETKFEMIKLIDIARQTAQGMDYLHAK---SIIHRDLKSNNIFLHE--------DLTVKIGDFGLAtvkSRWSGS 607
Cdd:cd14061    82 RVL--AGRKIPPHVLVDWAIQIARGMNYLHNEapvPIIHRDLKSSNILILEaienedleNKTLKITDFGLA---REWHKT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQlSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYLS-PdlskVRSNCP 686
Cdd:cd14061   157 TRMSA-AGTYAWMAPEVIKSS---TFSKASDVWSYGVLLWELLTGEVPYKGIDGL-AVAYGVAVNKLTlP----IPSTCP 227
                         250       260
                  ....*....|....*....|....*....
gi 1237938074 687 KAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd14061   228 EPFAQLMKDCWQPDPHDRPSFADILKQLE 256
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
450-707 5.13e-46

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: 164.92  E-value: 5.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIV 528
Cdd:cd05148     1 WERPREEFTLERKLGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLIsLFAVCSVGEPVYII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHIIETK-FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV-KSRWSG 606
Cdd:cd05148    81 TELMEKGSLLAFLRSPEGQvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLiKEDVYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHqfeqlSGSI--LWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPDLSKvrs 683
Cdd:cd05148   161 SS-----DKKIpyKWTAPEAASHGT---FSTKSDVWSFGILLYEMFTyGQVPYPGMNNH-EVYDQITAGYRMPCPAK--- 228
                         250       260
                  ....*....|....*....|....
gi 1237938074 684 nCPKAMKRLMAECLKKKRDERPLF 707
Cdd:cd05148   229 -CPQEIYKIMLECWAAEPEDRPSF 251
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
450-717 1.11e-45

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: 164.06  E-value: 1.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHGD-VAVKML--NVTAptpqqLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-L 525
Cdd:cd05039     1 WAINKKDLKLGELIGKGEFGDVMLGDYRGQkVAVKCLkdDSTA-----AQAFLAEASVMTTLRHPNLVQLLGVVLEGNgL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLYHHL-----HIIETKfemiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATv 600
Cdd:cd05039    76 YIVTEYMAKGSLVDYLrsrgrAVITRK----DQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 601 ksrwsgSHQFEQLSGS--ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYL--S 675
Cdd:cd05039   151 ------EASSNQDGGKlpIKWTAPEALR---EKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKD-VVPHVEKGYRmeA 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 676 PDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05039   221 PE------GCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
450-707 1.54e-45

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: 164.06  E-value: 1.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHGD--VAVKMLNvtaPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LA 526
Cdd:cd05072     2 WEIPRESIKLVKKLGAGQFGEVWMGYYNNStkVAVKTLK---PGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEpIY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLHIIE-TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrws 605
Cdd:cd05072    79 IITEYMAKGSLLDFLKSDEgGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIE--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 gSHQFEQLSGS---ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYLSPDLskv 681
Cdd:cd05072   156 -DNEYTAREGAkfpIKWTAPEAINF---GSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSD-VMSALQRGYRMPRM--- 227
                         250       260
                  ....*....|....*....|....*.
gi 1237938074 682 rSNCPKAMKRLMAECLKKKRDERPLF 707
Cdd:cd05072   228 -ENCPDELYDIMKTCWKEKAEERPTF 252
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
452-712 1.58e-45

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: 163.70  E-value: 1.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 452 IPDGQITVGQRIGSGSFGTVYKGKWHG------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ- 524
Cdd:cd05033     1 IDASYVTIEKVIGGGEFGEVCSGSLKLpgkkeiDVAIKTLKSGY-SDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 LAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRW 604
Cdd:cd05033    80 VMIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGShqFEQLSG--SILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGY-LSPDLsk 680
Cdd:cd05033   160 EAT--YTTKGGkiPIRWTAPEAIAYRK---FTSASDVWSFGIVMWEVMSyGERPYWDMSNQD-VIKAVEDGYrLPPPM-- 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1237938074 681 vrsNCPKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd05033   232 ---DCPSALYQLMLDCWQKDRNERPTFSQIVS 260
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
463-713 5.50e-45

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: 162.24  E-value: 5.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGSSLY 538
Cdd:cd13978     1 LGSGGFGTVSKARhvsWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRsLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIET------KFEMIklidiaRQTAQGMDYLH--AKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrWSGSHQF 610
Cdd:cd13978    81 SLLEREIQdvpwslRFRII------HEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGM-KSISANR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 EQ----LSGSILWMAPEVIRMQDKNPySFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYlSPDLS-----KV 681
Cdd:cd13978   154 RRgtenLGGTPIYMAPEAFDDFNKKP-TSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVSKGD-RPSLDdigrlKQ 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1237938074 682 RSNCPKaMKRLMAECLKKKRDERPLFPQILAS 713
Cdd:cd13978   232 IENVQE-LISLMIRCWDGNPDARPTFLECLDR 262
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
449-707 1.71e-43

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: 158.13  E-value: 1.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 449 DWEIPDGQITVGQRIGSGSFGTVYKGKWHGD--VAVKMLNVTAPTPQqlqAFKNEVGVLRKTRHVNILLFMGYSTKPQLA 526
Cdd:cd05067     1 EWEVPRETLKLVERLGAGQFGEVWMGYYNGHtkVAIKSLKQGSMSPD---AFLAEANLMKQLQHQRLVRLYAVVTQEPIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLHIIE-TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRWS 605
Cdd:cd05067    78 IITEYMENGSLVDFLKTPSgIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLA----RLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 GSHQFEQLSGS---ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNrDQIIFMVGRGYLSPDlskv 681
Cdd:cd05067   154 EDNEYTAREGAkfpIKWTAPEAI---NYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTN-PEVIQNLERGYRMPR---- 225
                         250       260
                  ....*....|....*....|....*.
gi 1237938074 682 RSNCPKAMKRLMAECLKKKRDERPLF 707
Cdd:cd05067   226 PDNCPEELYQLMRLCWKERPEDRPTF 251
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
461-714 4.44e-43

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: 156.45  E-value: 4.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPtPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGSS 536
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDnteVAVKTCRETLP-PDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQpIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGSHQFEQLSG- 615
Cdd:cd05041    80 LLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGM----SREEEDGEYTVSDGl 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 ---SILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYL--SPDLskvrsnCPKAM 689
Cdd:cd05041   156 kqiPIKWTAPEALNY---GRYTSESDVWSFGILLWEIFSlGATPYPGMSNQ-QTREQIESGYRmpAPEL------CPEAV 225
                         250       260
                  ....*....|....*....|....*
gi 1237938074 690 KRLMAECLKKKRDERPLFPQILASI 714
Cdd:cd05041   226 YRLMLQCWAYDPENRPSFSEIYNEL 250
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
458-655 2.04e-42

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: 154.94  E-value: 2.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCE 533
Cdd:cd05117     3 ELGKVLGRGSFGVVRLAVHKKTgeeYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEvFEDDKNLYLVMELCT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHlhIIE-TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL---HEDLTVKIGDFGLATvksRWSGSHQ 609
Cdd:cd05117    83 GGELFDR--IVKkGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAK---IFEEGEK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1237938074 610 FEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLP 655
Cdd:cd05117   158 LKTVCGTPYYVAPEVLK---GKGYGKKCDIWSLGVILYILLCGYPP 200
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
461-705 4.87e-42

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: 154.00  E-value: 4.87e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGK--WHGD-VAVKMLNVTAPtpQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSS 536
Cdd:cd06613     6 QRIGSGTYGDVYKARniATGElAAVKVIKLEPG--DDFEIIQQEISMLKECRHPNIVAYFGsYLRRDKLWIVMEYCGGGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIETKFEmiKLID-IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQfeQLSG 615
Cdd:cd06613    84 LQDIYQVTGPLSE--LQIAyVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRK--SFIG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLsKVRSNCPKAMKRLMAE 695
Cdd:cd06613   160 TPYWMAPEVAAVERKGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNFDPPKL-KDKEKWSPDFHDFIKK 238
                         250
                  ....*....|
gi 1237938074 696 CLKKKRDERP 705
Cdd:cd06613   239 CLTKNPKKRP 248
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
445-715 1.44e-41

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: 153.42  E-value: 1.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 445 DSSDDWEIPDGqitvGQRIGSGSFGTVYKGKWHG-DVAVKMLN--VTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYST 521
Cdd:cd14158     9 NNFDERPISVG----GNKLGEGGFGVVFKGYINDkNVAVKKLAamVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 522 K-PQLAIVTQWCEGSSLYHHLHIIETKFEMI--KLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd14158    85 DgPQLCLVYTYMPNGSLLDRLACLNDTPPLSwhMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 TVKSRWSGSHQFEQLSGSILWMAPEVIRMQdknpYSFQSDVYAFGIVLYELMTGqLPYSNINNRDQIIFMVGR------- 671
Cdd:cd14158   165 RASEKFSQTIMTERIVGTTAYMAPEALRGE----ITPKSDIFSFGVVLLEIITG-LPPVDENRDPQLLLDIKEeiedeek 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 672 ---GYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd14158   240 tieDYVDKKMGDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQ 286
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
461-715 1.88e-41

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: 151.99  E-value: 1.88e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHG--DVAVKMLNVTAPTPQqlqAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLY 538
Cdd:cd14203     1 VKLGQGCFGEVWMGTWNGttKVAIKTLKPGTMSPE---AFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEFMSKGSLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKF-EMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRWSGSHQFEQLSGS- 616
Cdd:cd14203    78 DFLKDGEGKYlKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLA----RLIEDNEYTARQGAk 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 617 --ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPdlskVRSNCPKAMKRLM 693
Cdd:cd14203   154 fpIKWTAPEAALY---GRFTIKSDVWSFGILLTELVTkGRVPYPGMNNR-EVLEQVERGYRMP----CPPGCPESLHELM 225
                         250       260
                  ....*....|....*....|..
gi 1237938074 694 AECLKKKRDERPLFPQILASIE 715
Cdd:cd14203   226 CQCWRKDPEERPTFEYLQSFLE 247
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
450-715 3.49e-41

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: 152.11  E-value: 3.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTPQQLQaFKNEVGVLRKTRHVNILLFMGYST 521
Cdd:cd05032     1 WELPREKITLIRELGQGSFGMVYEGLAKGvvkgepetRVAIKTVNENASMRERIE-FLNEASVMKEFNCHHVVRLLGVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 522 KPQLA-IVTQWCEGSSLYHHLHIIETKFE---------MIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVK 591
Cdd:cd05032    80 TGQPTlVVMELMAKGDLKSYLRSRRPEAEnnpglgpptLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 592 IGDFGLAtvksRWSGSHQFEQLSGS----ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQII 666
Cdd:cd05032   160 IGDFGMT----RDIYETDYYRKGGKgllpVRWMAPESLK---DGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNEEVLK 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 667 FMVGRGYLS-PDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05032   233 FVIDGGHLDlPE------NCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
456-714 3.52e-41

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: 151.45  E-value: 3.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHG--DVAVKMLNVTAPTPQQlqaFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWC 532
Cdd:cd05059     5 ELTFLKELGSGQFGVVHLGKWRGkiDVAIKMIKEGSMSEDD---FIEEAKVMMKLSHPKLVQLYGVCTKQRpIFIVTEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRWSGSHQFEQ 612
Cdd:cd05059    82 ANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLA----RYVLDDEYTS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGS---ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNrDQIIFMVGRGYLspdLSKVRSnCPKA 688
Cdd:cd05059   158 SVGTkfpVKWSPPEVF---MYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSN-SEVVEHISQGYR---LYRPHL-APTE 229
                         250       260
                  ....*....|....*....|....*.
gi 1237938074 689 MKRLMAECLKKKRDERPLFPQILASI 714
Cdd:cd05059   230 VYTIMYSCWHEKPEERPTFKILLSQL 255
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
464-715 3.71e-41

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: 150.88  E-value: 3.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 464 GSGSFGTVYKGKW---HGDVAVKMLNvtaptpqQLQAfknEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEGSSLYH 539
Cdd:cd14060     2 GGGSFGSVYRAIWvsqDKEVAVKKLL-------KIEK---EAEILSVLSHRNIIQFYGAILEaPNYGIVTEYASYGSLFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 540 HLHIIET-KFEMIKLIDIARQTAQGMDYLHAKS---IIHRDLKSNNIFLHEDLTVKIGDFGlatvKSRWSGSHQFEQLSG 615
Cdd:cd14060    72 YLNSNESeEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFG----ASRFHSHTTHMSLVG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYLSPdlsKVRSNCPKAMKRLMAE 695
Cdd:cd14060   148 TFPWMAPEVIQ---SLPVSETCDTYSYGVVLWEMLTREVPFKGLEGL-QVAWLVVEKNERP---TIPSSCPRSFAELMRR 220
                         250       260
                  ....*....|....*....|
gi 1237938074 696 CLKKKRDERPLFPQILASIE 715
Cdd:cd14060   221 CWEADVKERPSFKQIIGILE 240
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
463-717 7.88e-41

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: 150.52  E-value: 7.88e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD-VAVKM--------LNVTAPTPQQlqafknEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWC 532
Cdd:cd14148     2 IGVGGFGKVYKGLWRGEeVAVKAarqdpdedIAVTAENVRQ------EARLFWMLQHPNIIALRGVCLNpPHLCLVMEYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLyhHLHIIETKFEMIKLIDIARQTAQGMDYLHAKS---IIHRDLKSNNIFLHE--------DLTVKIGDFGLAtvk 601
Cdd:cd14148    76 RGGAL--NRALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEpienddlsGKTLKITDFGLA--- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 602 SRWsgsHQFEQLS--GSILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMTGQLPYSNINnrdqiIFMVGRGYLSPDLS 679
Cdd:cd14148   151 REW---HKTTKMSaaGTYAWMAPEVIRL---SLFSKSSDVWSFGVLLWELLTGEVPYREID-----ALAVAYGVAMNKLT 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 680 -KVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd14148   220 lPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
446-715 8.54e-41

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: 150.99  E-value: 8.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 446 SSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHG--DVAVKMLNVTAPTPQqlqAFKNEVGVLRKTRHVNILLFMGYSTKP 523
Cdd:cd05069     3 AKDAWEIPRESLRLDVKLGQGCFGEVWMGTWNGttKVAIKTLKPGTMMPE---AFLQEAQIMKKLRHDKLVPLYAVVSEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEGSSLYHHLHIIETKF-EMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvks 602
Cdd:cd05069    80 PIYIVTEFMGKGSLLDFLKEGDGKYlKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLA---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RWSGSHQFEQLSGS---ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPdl 678
Cdd:cd05069   156 RLIEDNEYTARQGAkfpIKWTAPEAALY---GRFTIKSDVWSFGILLTELVTkGRVPYPGMVNR-EVLEQVERGYRMP-- 229
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1237938074 679 skVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05069   230 --CPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLE 264
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
456-705 8.61e-41

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: 150.07  E-value: 8.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKG--KWHGD-VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS-TKPQLAIVTQW 531
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGlnLNTGEfVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVkTKDSLYIILEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLyhhLHIIEtKFEMIKLIDIARQTAQ---GMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGSH 608
Cdd:cd06627    81 VENGSL---ASIIK-KFGKFPESLVAVYIYQvleGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAT---KLNEVE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQLS-GSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSN---------INNRDQiifmvgrgylsPDL 678
Cdd:cd06627   154 KDENSVvGTPYWMAPEVIEMS---GVTTASDIWSVGCTVIELLTGNPPYYDlqpmaalfrIVQDDH-----------PPL 219
                         250       260
                  ....*....|....*....|....*..
gi 1237938074 679 SKvrsNCPKAMKRLMAECLKKKRDERP 705
Cdd:cd06627   220 PE---NISPELRDFLLQCFQKDPTLRP 243
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
463-715 1.22e-40

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: 149.60  E-value: 1.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD-VAVKMLNVTA-PTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK--PQLAIVTQWCEGSSLY 538
Cdd:cd14064     1 IGSGSFGKVYKGRCRNKiVAIKRYRANTyCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDdpSQFAIVTQYVSGGSLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLH----IIETKFEMIKLIDIARqtaqGMDYLH--AKSIIHRDLKSNNIFLHEDLTVKIGDFGlatvKSRWSGSHQFEQ 612
Cdd:cd14064    81 SLLHeqkrVIDLQSKLIIAVDVAK----GMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFG----ESRFLQSLDEDN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LS---GSILWMAPEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPdlskVRSNCPKAM 689
Cdd:cd14064   153 MTkqpGNLRWMAPEVFTQCTR--YSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYHHIRPP----IGYSIPKPI 226
                         250       260
                  ....*....|....*....|....*.
gi 1237938074 690 KRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd14064   227 SSLLMRGWNAEPESRPSFVEIVALLE 252
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
456-717 3.28e-40

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: 149.02  E-value: 3.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGD-VAVKM--------LNVTAptpqqlQAFKNEVGVLRKTRHVNILLFMGYS-TKPQL 525
Cdd:cd14147     4 ELRLEEVIGIGGFGKVYRGSWRGElVAVKAarqdpdedISVTA------ESVRQEARLFAMLAHPNIIALKAVClEEPNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLYHHL-------HIietkfemikLIDIARQTAQGMDYLHAKSI---IHRDLKSNNIFL--------HED 587
Cdd:cd14147    78 CLVMEYAAGGPLSRALagrrvppHV---------LVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLlqpienddMEH 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 588 LTVKIGDFGLAtvkSRWsgsHQFEQLS--GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNrdqi 665
Cdd:cd14147   149 KTLKITDFGLA---REW---HKTTQMSaaGTYAWMAPEVIK---ASTFSKGSDVWSFGVLLWELLTGEVPYRGIDC---- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 666 iFMVGRGYLSPDLS-KVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd14147   216 -LAVAYGVAVNKLTlPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
448-715 3.43e-40

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: 149.02  E-value: 3.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 448 DDWEIPDGQITVGQRIGSGSFGTVYKGKW--HGDVAVKMLNvtaPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQL 525
Cdd:cd05073     4 DAWEIPRESLKLEKKLGAGQFGEVWMATYnkHTKVAVKTMK---PGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLYHHLHIIE-TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRW 604
Cdd:cd05073    81 YIITEFMAKGSLLDFLKSDEgSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLA----RV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQLSGS---ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNrDQIIFMVGRGYLSPDlsk 680
Cdd:cd05073   157 IEDNEYTAREGAkfpIKWTAPEAI---NFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSN-PEVIRALERGYRMPR--- 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1237938074 681 vRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05073   230 -PENCPEELYNIMMRCWKNRPEERPTFEYIQSVLD 263
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
448-715 5.29e-40

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: 148.68  E-value: 5.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 448 DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGD--VAVKMLNVTAPTPQqlqAFKNEVGVLRKTRHVNILLFMGYSTKPQL 525
Cdd:cd05070     2 DVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNtkVAIKTLKPGTMSPE---SFLEEAQIMKKLKHDKLVQLYAVVSEEPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLYHHLHIIETK-FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRW 604
Cdd:cd05070    79 YIVTEYMSKGSLLDFLKDGEGRaLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLA----RL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQLSGS---ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPdlsk 680
Cdd:cd05070   155 IEDNEYTARQGAkfpIKWTAPEAALY---GRFTIKSDVWSFGILLTELVTkGRVPYPGMNNR-EVLEQVERGYRMP---- 226
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1237938074 681 VRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05070   227 CPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLE 261
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
451-719 5.89e-40

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: 148.72  E-value: 5.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKGKWHGD-------VAVKMLNVTAPtPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP 523
Cdd:cd05057     3 IVKETELEKGKVLGSGAFGTVYKGVWIPEgekvkipVAIKVLREETG-PKANEEILDEAYVMASVDHPHLVRLLGICLSS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR 603
Cdd:cd05057    82 QVQLITQLMPLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRG--YLSPDLsk 680
Cdd:cd05057   162 DEKEYHAEGGKVPIKWMALESIQYRI---YTHKSDVWSYGVTVWELMTfGAKPYEGIPAVE-IPDLLEKGerLPQPPI-- 235
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 681 vrsnCPKAMKRLMAECLKKKRDERPLFPQILASIELLAR 719
Cdd:cd05057   236 ----CTIDVYMVLVKCWMIDAESRPTFKELANEFSKMAR 270
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
453-718 7.64e-40

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: 148.30  E-value: 7.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKGKW--HGD-----VAVKMLNVTAPtPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ- 524
Cdd:cd05038     2 EERHLKFIKQLGEGHFGSVELCRYdpLGDntgeqVAVKSLQPSGE-EQHMSDFKREIEILRTLDHEYIVKYKGVCESPGr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 --LAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKS 602
Cdd:cd05038    81 rsLRLIMEYLPSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RWSGSHQFEQLSGS-ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGYLSPDL-- 678
Cdd:cd05038   161 EDKEYYYVKEPGESpIFWYAPECLR---ESRFSSASDVWSFGVTLYELFTyGDPSQSPPALFLRMIGIAQGQMIVTRLle 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 679 ---SKVR----SNCPKAMKRLMAECLKKKRDERPLFPQILASIELLA 718
Cdd:cd05038   238 llkSGERlprpPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
448-715 3.43e-39

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: 146.37  E-value: 3.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 448 DDWEIPDGQITVGQRIGSGSFGTVYKGKWHG--DVAVKMLNVTAPTPQqlqAFKNEVGVLRKTRHVNILLFMGYSTKPQL 525
Cdd:cd05071     2 DAWEIPRESLRLEVKLGQGCFGEVWMGTWNGttRVAIKTLKPGTMSPE---AFLQEAQVMKKLRHEKLVQLYAVVSEEPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLYHHLHIIETKF-EMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRW 604
Cdd:cd05071    79 YIVTEYMSKGSLLDFLKGEMGKYlRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLA----RL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQLSGS---ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPdlsk 680
Cdd:cd05071   155 IEDNEYTARQGAkfpIKWTAPEAALY---GRFTIKSDVWSFGILLTELTTkGRVPYPGMVNR-EVLDQVERGYRMP---- 226
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1237938074 681 VRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05071   227 CPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLE 261
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
458-712 6.29e-39

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: 144.58  E-value: 6.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCE 533
Cdd:cd14003     3 ELGKTLGEGSFGKVKLArhkLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIkLYEVIETENKIYLVMEYAS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHH------LHIIETKFEMIKLIDiarqtaqGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGS 607
Cdd:cd14003    83 GGELFDYivnngrLSEDEARRFFQQLIS-------AVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSN---EFRGG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQLSGSILWMAPEVIrmQDKNPYSFQSDVYAFGIVLYELMTGQLPY--SNINNRDQIIfMVGRGYLSPDLSKvrsNC 685
Cdd:cd14003   153 SLLKTFCGTPAYAAPEVL--LGRKYDGPKADVWSLGVILYAMLTGYLPFddDNDSKLFRKI-LKGKYPIPSHLSP---DA 226
                         250       260
                  ....*....|....*....|....*..
gi 1237938074 686 pkamKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd14003   227 ----RDLIRRMLVVDPSKRITIEEILN 249
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
451-710 8.86e-39

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: 145.21  E-value: 8.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK 522
Cdd:cd05048     1 EIPLSAVRFLEELGEGAFGKVYKGELLGpsseesaiSVAIKTLKENA-SPKTQQDFRREAELMSDLQHPNIVCLLGVCTK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 523 PQ-LAIVTQWCEGSSLYHHL---------------HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE 586
Cdd:cd05048    80 EQpQCMLFEYMAHGDLHEFLvrhsphsdvgvssddDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 587 DLTVKIGDFGLatvkSRWSGSHQ-FEQLSGSIL---WMAPEVIrMQDKnpYSFQSDVYAFGIVLYELMT-GQLPYSNINN 661
Cdd:cd05048   160 GLTVKISDFGL----SRDIYSSDyYRVQSKSLLpvrWMPPEAI-LYGK--FTTESDVWSFGVVLWEIFSyGLQPYYGYSN 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 662 RDqIIFMV-GRGYLS-PDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05048   233 QE-VIEMIrSRQLLPcPE------DCPARVYSLMVECWHEIPSRRPRFKEI 276
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
458-733 1.46e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 147.58  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGDVAVKMLNV-TAPTPQQLQAFKNEVGVLRKTRHVN--ILLFMGYSTKPQLAIVTQWCEG 534
Cdd:COG0515     3 RILRKLGEGSFGEVYLARDRKLVALKVLAKkLESKSKEVERFLREIQILASLNHPPniVKLYDFFQDEGSLYLVMEYVDG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLH--IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT-VKIGDFGLATV----KSRWSGS 607
Cdd:COG0515    83 GSLEDLLKkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLlpdpGSTSSIP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNR-------DQIIFMVGRGYLSPDLSK 680
Cdd:COG0515   163 ALPSTSVGTPGYMAPEVLLGLSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSsatsqtlKIILELPTPSLASPLSPS 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 681 VRSNCPKAMKRLMAECLKKKRDERPLfpqilaSIELLARSLPKIHRSASEPSL 733
Cdd:COG0515   243 NPELISKAASDLLKKLLAKDPKNRLS------SSSDLSHDLLAHLKLKESDLS 289
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
463-717 1.98e-38

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: 143.56  E-value: 1.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAptpqQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLY 538
Cdd:cd06612    11 LGEGSYGSVYKAIHKETgqvVAIKVVPVEE----DLQEIIKEISILKQCDSPYIVKYYGsYFKNTDLWIVMEYCGAGSVS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKF--EMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQLSGS 616
Cdd:cd06612    87 DIMKITNKTLteEEIAAI--LYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLT--DTMAKRNTVIGT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 617 ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQiIFMVGRgYLSPDLSKvRSNCPKAMKRLMAEC 696
Cdd:cd06612   163 PFWMAPEVIQ---EIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRA-IFMIPN-KPPPTLSD-PEKWSPEFNDFVKKC 236
                         250       260
                  ....*....|....*....|.
gi 1237938074 697 LKKKRDERPlfpqilASIELL 717
Cdd:cd06612   237 LVKDPEERP------SAIQLL 251
C1_B-Raf cd20871
protein kinase C conserved region 1 (C1 domain) found in B-Raf (Rapidly Accelerated ...
230-289 2.38e-38

protein kinase C conserved region 1 (C1 domain) found in B-Raf (Rapidly Accelerated Fibrosarcoma) kinase and similar proteins; Serine/threonine-protein kinase B-Raf, also called proto-oncogene B-Raf, p94, or v-Raf murine sarcoma viral oncogene homolog B1, 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. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410421  Cd Length: 60  Bit Score: 136.31  E-value: 2.38e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 230 VPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLL 289
Cdd:cd20871     1 VPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLL 60
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
451-717 3.58e-38

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: 143.19  E-value: 3.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKG------KWHGDVAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-P 523
Cdd:cd05063     1 EIHPSHITKQKVIGAGEFGEVFRGilkmpgRKEVAVAIKTLK-PGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKfK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV-KS 602
Cdd:cd05063    80 PAMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVlED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RWSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPdlskV 681
Cdd:cd05063   160 DPEGTYTTSGGKIPIRWTAPEAIAYRK---FTSASDVWSFGIVMWEVMSfGERPYWDMSNH-EVMKAINDGFRLP----A 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1237938074 682 RSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05063   232 PMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKL 267
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
461-710 6.55e-38

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: 142.10  E-value: 6.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWH---GD---VAVKMLNVTAPT-PQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCE 533
Cdd:cd05040     1 EKLGDGSFGVVRRGEWTtpsGKviqVAVKCLKSDVLSqPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLMMVTELAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGSHQ---- 609
Cdd:cd05040    81 LGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGL----MRALPQNEdhyv 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 610 -FEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGY--LS-PDlskvrsN 684
Cdd:cd05040   157 mQEHRKVPFAWCAPESLKTRK---FSHASDVWMFGVTLWEMFTyGEEPWLGLNGS-QILEKIDKEGerLErPD------D 226
                         250       260
                  ....*....|....*....|....*.
gi 1237938074 685 CPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05040   227 CPQDIYNVMLQCWAHKPADRPTFVAL 252
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
451-711 7.30e-38

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: 142.49  E-value: 7.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKGKWHGD-VAVKML--NVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-PQLA 526
Cdd:cd14145     2 EIDFSELVLEEIIGIGGFGKVYRAIWIGDeVAVKAArhDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKePNLC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLHiiETKFEMIKLIDIARQTAQGMDYLHAKSI---IHRDLKSNNIFLHE-----DL---TVKIGDF 595
Cdd:cd14145    82 LVMEFARGGPLNRVLS--GKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEkvengDLsnkILKITDF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 596 GLAtvkSRWsgsHQFEQLS--GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNrdqiiFMVGRGY 673
Cdd:cd14145   160 GLA---REW---HRTTKMSaaGTYAWMAPEVIR---SSMFSKGSDVWSYGVLLWELLTGEVPFRGIDG-----LAVAYGV 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 674 LSPDLS-KVRSNCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd14145   226 AMNKLSlPIPSTCPEPFARLMEDCWNPDPHSRPPFTNIL 264
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
463-714 9.97e-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: 142.10  E-value: 9.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG-DVAVKmlnVTAPTPQQ-----LQAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEGS 535
Cdd:cd14146     2 IGVGGFGKVYRATWKGqEVAVK---AARQDPDEdikatAESVRQEAKLFSMLRHPNIIKLEGVCLEePNLCLVMEFARGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIK--------LIDIARQTAQGMDYLHAKS---IIHRDLKSNNIFL-----HEDL---TVKIGDFG 596
Cdd:cd14146    79 TLNRALAAANAAPGPRRarripphiLVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLlekieHDDIcnkTLKITDFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 597 LAtvkSRWsgsHQFEQLS--GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNrdqiiFMVGRGYL 674
Cdd:cd14146   159 LA---REW---HRTTKMSaaGTYAWMAPEVIK---SSLFSKGSDIWSYGVLLWELLTGEVPYRGIDG-----LAVAYGVA 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1237938074 675 SPDLS-KVRSNCPKAMKRLMAECLKKKRDERPLFPQILASI 714
Cdd:cd14146   225 VNKLTlPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
459-711 1.08e-37

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: 141.39  E-value: 1.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQWCEG 534
Cdd:cd08529     4 ILNKLGKGSFGVVYKVVRKVDgrvYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYdSFVDKGKLNIVMEYAEN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIIETKFEMIKLI-DIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSHQFEQ- 612
Cdd:cd08529    84 GDLHSLIKSQRGRPLPEDQIwKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKI---LSDTTNFAQt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGSILWMAPEVIrmQDKnPYSFQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGRGYLSPdlskVRSNCPKAMKRL 692
Cdd:cd08529   161 IVGTPYYLSPELC--EDK-PYNEKSDVWALGCVLYELCTGKHPF-EAQNQGALILKIVRGKYPP----ISASYSQDLSQL 232
                         250
                  ....*....|....*....
gi 1237938074 693 MAECLKKKRDERPLFPQIL 711
Cdd:cd08529   233 IDSCLTKDYRQRPDTTELL 251
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
450-721 1.53e-37

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: 142.17  E-value: 1.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG---------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMGY 519
Cdd:cd05053     7 WELPRDRLTLGKPLGEGAFGQVVKAEAVGldnkpnevvTVAVKMLKDDA-TEKDLSDLVSEMEMMKMIgKHKNIINLLGA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 520 ST-KPQLAIVTQWCEGSSLYHHL---------------HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIF 583
Cdd:cd05053    86 CTqDGPLYVVVEYASKGNLREFLrarrppgeeaspddpRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 584 LHEDLTVKIGDFGLAtvksRWSGSHQFEQLSGS----ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSN 658
Cdd:cd05053   166 VTEDNVMKIADFGLA----RDIHHIDYYRKTTNgrlpVKWMAPEAL---FDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 659 InNRDQIIFMVGRGYlspDLSKvRSNCPKAMKRLMAECLKKKRDERPLFPQIlasIELLARSL 721
Cdd:cd05053   239 I-PVEELFKLLKEGH---RMEK-PQNCTQELYMLMRDCWHEVPSQRPTFKQL---VEDLDRIL 293
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
457-717 1.85e-37

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: 141.16  E-value: 1.85e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTV------YKGKWHGDVAVKMLNVtAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLA-IVT 529
Cdd:cd05066     6 IKIEKVIGAGEFGEVcsgrlkLPGKREIPVAIKTLKA-GYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVmIVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwSGSHQ 609
Cdd:cd05066    85 EYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLED-DPEAA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 610 FEQLSGSI--LWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYLSPdlskVRSNCP 686
Cdd:cd05066   164 YTTRGGKIpiRWTAPEAIAYRK---FTSASDVWSYGIVMWEVMSyGERPYWEMSNQD-VIKAIEEGYRLP----APMDCP 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 687 KAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05066   236 AALHQLMLDCWQKDRNERPKFEQIVSILDKL 266
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
463-714 1.94e-37

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: 141.28  E-value: 1.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFkNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLY 538
Cdd:cd13996    14 LGSGGFGSVYKVRNKVDgvtYAIKKIRLTEKSSASEKVL-REVKALAKLNHPNIVRYYTaWVEEPPLYIQMELCEGGTLR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLH-IIETKFEMIKLI-DIARQTAQGMDYLHAKSIIHRDLKSNNIFLH-EDLTVKIGDFGLATV-----KSRWSGSHQF 610
Cdd:cd13996    93 DWIDrRNSSSKNDRKLAlELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATSignqkRELNNLNNNN 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 EQLS-------GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMtgqLPYSNINNRDQIIFMVGRGYLSPDLskvRS 683
Cdd:cd13996   173 NGNTsnnsvgiGTPLYASPEQL---DGENYNEKADIYSLGIILFEML---HPFKTAMERSTILTDLRNGILPESF---KA 243
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 684 NCPKaMKRLMAECLKKKRDERPLFPQILASI 714
Cdd:cd13996   244 KHPK-EADLIQSLLSKNPEERPSAEQLLRSL 273
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
461-656 4.58e-37

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: 139.65  E-value: 4.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAptpQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSS 536
Cdd:cd06614     6 EKIGEGASGEVYKATDRATgkeVAIKKMRLRK---QNKELIINEILIMKECKHPNIVDYYDsYLVGDELWVVMEYMDGGS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHhlhIIETKFemIKLID-----IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksrwsgshqfe 611
Cdd:cd06614    83 LTD---IITQNP--VRMNEsqiayVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAA------------ 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 612 QLS----------GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd06614   146 QLTkekskrnsvvGTPYWMAPEVIK---RKDYGPKVDIWSLGIMCIEMAEGEPPY 197
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
457-717 4.65e-37

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: 140.00  E-value: 4.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKG------KWHGDVAVKMLNVtAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVT 529
Cdd:cd05065     6 VKIEEVIGAGEFGEVCRGrlklpgKREIFVAIKTLKS-GYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRpVMIIT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKSRWSGSH 608
Cdd:cd05065    85 EFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfLEDDTSDPT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQLSGSI--LWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGY-LSPDLskvrsN 684
Cdd:cd05065   165 YTSSLGGKIpiRWTAPEAIAYRK---FTSASDVWSYGIVMWEVMSyGERPYWDMSNQD-VINAIEQDYrLPPPM-----D 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1237938074 685 CPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05065   236 CPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKM 268
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
463-711 5.10e-37

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: 139.67  E-value: 5.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG--KWHG-DVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY---STKPQLAIVTQWCEGSS 536
Cdd:cd13983     9 LGRGSFKTVYRAfdTEEGiEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSwesKSKKEVIFITELMTSGT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLhiieTKFEMIKLIDI---ARQTAQGMDYLHAK--SIIHRDLKSNNIFLHEDL-TVKIGDFGLATVKSrwsgsHQF 610
Cdd:cd13983    89 LKQYL----KRFKRLKLKVIkswCRQILEGLNYLHTRdpPIIHRDLKCDNIFINGNTgEVKIGDLGLATLLR-----QSF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 EQlsgSIL----WMAPEvirMQDKNpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCp 686
Cdd:cd13983   160 AK---SVIgtpeFMAPE---MYEEH-YDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPESLSKVKDPE- 231
                         250       260
                  ....*....|....*....|....*
gi 1237938074 687 kaMKRLMAECLKKKrDERPLFPQIL 711
Cdd:cd13983   232 --LKDFIEKCLKPP-DERPSARELL 253
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
456-715 2.16e-36

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: 137.70  E-value: 2.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHG--DVAVKMLNVTAPTPQQlqaFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWC 532
Cdd:cd05113     5 DLTFLKELGTGQFGVVKYGKWRGqyDVAIKMIKEGSMSEDE---FIEEAKVMMNLSHEKLVQLYGVCTKQRpIFIITEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGSHQFEQ 612
Cdd:cd05113    82 ANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGL----SRYVLDDEYTS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGS---ILWMAPEVIrMQDKnpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMV-GRGYLSPDLSKVRsncpk 687
Cdd:cd05113   158 SVGSkfpVRWSPPEVL-MYSK--FSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSqGLRLYRPHLASEK----- 229
                         250       260
                  ....*....|....*....|....*...
gi 1237938074 688 aMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05113   230 -VYTIMYSCWHEKADERPTFKILLSNIL 256
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
460-712 4.27e-36

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: 136.76  E-value: 4.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYKGkWHGD----VAVKMLNVTAPTPQQLQAFKN---EVGVLRKTRHVNILLFMGYST-KPQLAIVTQW 531
Cdd:cd06632     5 GQLLGSGSFGSVYEG-FNGDtgdfFAVKEVSLVDDDKKSRESVKQleqEIALLSKLRHPNIVQYYGTEReEDNLYIFLEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHIIETKFE-MIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQF 610
Cdd:cd06632    84 VPGGSIHKLLQRYGAFEEpVIRLY--TRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 EqlsGSILWMAPEVIRMQDkNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRgylSPDLSKVRSNCPKAMK 690
Cdd:cd06632   162 K---GSPYWMAPEVIMQKN-SGYGLAVDIWSLGCTVLEMATGKPPWSQYEGV-AAIFKIGN---SGELPPIPDHLSPDAK 233
                         250       260
                  ....*....|....*....|..
gi 1237938074 691 RLMAECLKKKRDERPLFPQILA 712
Cdd:cd06632   234 DFIRLCLQRDPEDRPTASQLLE 255
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
450-733 1.63e-35

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: 136.25  E-value: 1.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVY--------KGKWHGDVAVKMLNVTAPTPQQLQaFKNEVGVLR--KTRHVNILLFMGY 519
Cdd:cd05061     1 WEVSREKITLLRELGQGSFGMVYegnardiiKGEAETRVAVKTVNESASLRERIE-FLNEASVMKgfTCHHVVRLLGVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 520 STKPQLAIVTQWCEGSsLYHHLHIIETKFE---------MIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTV 590
Cdd:cd05061    80 KGQPTLVVMELMAHGD-LKSYLRSLRPEAEnnpgrppptLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 591 KIGDFGLatvkSRWSGSHQFEQLSGSIL----WMAPEVIRMQDKNPYsfqSDVYAFGIVLYELMT-GQLPYSNINNRDQI 665
Cdd:cd05061   159 KIGDFGM----TRDIYETDYYRKGGKGLlpvrWMAPESLKDGVFTTS---SDMWSFGVVLWEITSlAEQPYQGLSNEQVL 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 666 IFMVGRGYLS-PDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQIlasIELLARSLpkiHRSASEPSL 733
Cdd:cd05061   232 KFVMDGGYLDqPD------NCPERVTDLMRMCWQFNPKMRPTFLEI---VNLLKDDL---HPSFPEVSF 288
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
450-715 1.95e-35

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: 135.00  E-value: 1.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHGD-VAVKML--NVTAptpqqlQAFKNEVGVLRKTRHVNILLFMGYSTKPQLA 526
Cdd:cd05083     1 WLLNLQKLTLGEIIGEGEFGAVLQGEYMGQkVAVKNIkcDVTA------QAFLEETAVMTKLQHKNLVRLLGVILHNGLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLHII-ETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWS 605
Cdd:cd05083    75 IVMELMSKGNLVNFLRSRgRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMGV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 GSHQFeqlsgSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYL--SPDlskvr 682
Cdd:cd05083   155 DNSRL-----PVKWTAPEALK---NKKFSSKSDVWSYGVLLWEVFSyGRAPYPKMSVK-EVKEAVEKGYRmePPE----- 220
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1237938074 683 sNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05083   221 -GCPPDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
460-710 2.29e-35

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: 134.67  E-value: 2.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPtPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGS 535
Cdd:cd05084     1 GERIGRGNFGEVFSGRLRADntpVAVKSCRETLP-PDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQpIYIVMELVQGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR--WSGSHQFEQL 613
Cdd:cd05084    80 DFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDgvYAATGGMKQI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 sgSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPdlskVRSNCPKAMKRL 692
Cdd:cd05084   160 --PVKWTAPEAL---NYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQ-QTREAVEQGVRLP----CPENCPDEVYRL 229
                         250
                  ....*....|....*...
gi 1237938074 693 MAECLKKKRDERPLFPQI 710
Cdd:cd05084   230 MEQCWEYDPRKRPSFSTV 247
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
459-669 8.22e-35

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: 133.15  E-value: 8.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEG 534
Cdd:cd14002     5 VLELIGEGSFGKVYKGRRKYTgqvVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDsFETKKEFVVVTEYAQG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SsLYHhlhIIE--TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQ 612
Cdd:cd14002    85 E-LFQ---ILEddGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMS--CNTLVLTS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 613 LSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMV 669
Cdd:cd14002   159 IKGTPLYMAPELVQEQ---PYDHTADLWSLGCILYELFVGQPPFYT-NSIYQLVQMI 211
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
463-715 1.35e-34

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: 132.93  E-value: 1.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG---------KWHGDVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMG--YSTKPQLaIVTQW 531
Cdd:cd05044     3 LGSGAFGEVFEGtakdilgdgSGETKVAVKTLRKGA-TDQEKAEFLKEAHLMSNFKHPNILKLLGvcLDNDPQY-IILEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLH------IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE----DLTVKIGDFGLAtvk 601
Cdd:cd05044    81 MEGGDLLSYLRaarptaFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSkdyrERVVKIGDFGLA--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 602 sRWSGSHQFEQLSGSIL----WMAPEVIrMQDKnpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGYLS- 675
Cdd:cd05044   158 -RDIYKNDYYRKEGEGLlpvrWMAPESL-VDGV--FTTQSDVWAFGVLMWEILTlGQQPYPARNNLEVLHFVRAGGRLDq 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1237938074 676 PDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05044   234 PD------NCPDDLYELMLRCWSTDPEERPSFARILEQLQ 267
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
450-715 1.95e-34

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: 133.38  E-value: 1.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTPQQlQAFKNEVGVLRKT-RHVNILLFMGYS 520
Cdd:cd05055    30 WEFPRNNLSFGKTLGAGAFGKVVEATAYGlsksdavmKVAVKMLKPTAHSSER-EALMSELKIMSHLgNHENIVNLLGAC 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 521 TK--PQLaIVTQWCEGSSLYHHLHIIETKF-EMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL 597
Cdd:cd05055   109 TIggPIL-VITEYCCYGDLLNFLRRKRESFlTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 AtvKSRWSGSHQFEQLSG--SILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGY- 673
Cdd:cd05055   188 A--RDIMNDSNYVVKGNArlPVKWMAPESIF---NCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGYr 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1237938074 674 -LSPDLSkvrsncPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05055   263 mAQPEHA------PAEIYDIMKTCWDADPLKRPTFKQIVQLIG 299
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
453-711 2.33e-34

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: 132.00  E-value: 2.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDgQITVGQRIGSGSFGTVYKGKWHGD--VAVKMLNVTAPTPQQlqaFKNEVGVLRKTRHVNILLFMGYST-KPQLAIVT 529
Cdd:cd05112     3 PS-ELTFVQEIGSGQFGLVHLGYWLNKdkVAIKTIREGAMSEED---FIEEAEVMMKLSHPKLVQLYGVCLeQAPICLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGSHQ 609
Cdd:cd05112    79 EFMEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGM----TRFVLDDQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 610 FEQLSGS---ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNrDQIIFMVGRGY--LSPDLskvrs 683
Cdd:cd05112   155 YTSSTGTkfpVKWSSPEVFSFSR---YSSKSDVWSFGVLMWEVFSeGKIPYENRSN-SEVVEDINAGFrlYKPRL----- 225
                         250       260
                  ....*....|....*....|....*...
gi 1237938074 684 nCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd05112   226 -ASTHVYEIMNHCWKERPEDRPSFSLLL 252
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
449-705 2.57e-34

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: 132.12  E-value: 2.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 449 DWEipdgQITVGQRIGSGSFGTVYKGKWHGD-VAVKMLNVTAPTPQQLQAFKNEVGVLRkTRHVNILLFMGYSTKPQLA- 526
Cdd:cd13979     1 DWE----PLRLQEPLGSGGFGSVYKATYKGEtVAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVRVLAAETGTDFAs 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 ---IVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR 603
Cdd:cd13979    76 lglIIMEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSG-SHQFEQLSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYSNInnRDQIIFMVGRGYLSPDLSKVR 682
Cdd:cd13979   156 GNEvGTPRSHIGGTYTYRAPELLKGERVTP---KADIYSFGITLWQMLTRELPYAGL--RQHVLYAVVAKDLRPDLSGLE 230
                         250       260
                  ....*....|....*....|....
gi 1237938074 683 SNCPK-AMKRLMAECLKKKRDERP 705
Cdd:cd13979   231 DSEFGqRLRSLISRCWSAQPAERP 254
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
445-711 4.56e-34

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: 131.79  E-value: 4.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 445 DSSDDWEIpdgqitVGQrIGSGSFGTVYKGKwHGD----VAVKMLNVTAPtpQQLQAFKNEVGVLRKTRHVNIL-LFMGY 519
Cdd:cd06611     2 NPNDIWEI------IGE-LGDGAFGKVYKAQ-HKEtglfAAAKIIQIESE--EELEDFMVEIDILSECKHPNIVgLYEAY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 520 STKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL-A 598
Cdd:cd06611    72 FYENKLWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVsA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 TVKSRWSGSHQFeqlSGSILWMAPEVI---RMQDkNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYlS 675
Cdd:cd06611   152 KNKSTLQKRDTF---IGTPYWMAPEVVaceTFKD-NPYDYKADIWSLGITLIELAQMEPPHHELNPM-RVLLKILKSE-P 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1237938074 676 PDLSKvRSNCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd06611   226 PTLDQ-PSKWSSSFNDFLKSCLVKDPDDRPTAAELL 260
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
461-715 1.11e-33

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: 130.91  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWH------GDV-AVKMLNVTapTPQQLQAFKNEVGVLRKTRHVNILLFMG--YST-KPQLAIVTQ 530
Cdd:cd14205    10 QQLGKGNFGSVEMCRYDplqdntGEVvAVKKLQHS--TEEHLRDFEREIEILKSLQHDNIVKYKGvcYSAgRRNLRLIME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQF 610
Cdd:cd14205    88 YLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 EQLSGS-ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTgqlpYSNINNRDQIIFMVGRG---------YLSPDLSK 680
Cdd:cd14205   168 KEPGESpIFWYAPESL---TESKFSVASDVWSFGVVLYELFT----YIEKSKSPPAEFMRMIGndkqgqmivFHLIELLK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1237938074 681 VR------SNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd14205   241 NNgrlprpDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVD 281
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
463-715 2.07e-33

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: 129.89  E-value: 2.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD--------VAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY--STKPQLaIVTQWC 532
Cdd:cd05046    13 LGRGEFGEVFLAKAKGIeeeggetlVLVKALQ-KTKDENLQSEFRRELDMFRKLSHKNVVRLLGLcrEAEPHY-MILEYT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLHIIETKFEMIK--------LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRw 604
Cdd:cd05046    91 DLGDLKQFLRATKSKDEKLKppplstkqKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDVYN- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNrDQIIFMVGRGYLSpdlSKVRS 683
Cdd:cd05046   170 SEYYKLRNALIPLRWLAPEAVQEDD---FSTKSDVWSFGVLMWEVFTqGELPFYGLSD-EEVLNRLQAGKLE---LPVPE 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1237938074 684 NCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05046   243 GCPSRLYKLMTRCWAVNPKDRPSFSELVSALG 274
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
463-717 2.56e-33

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: 129.13  E-value: 2.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD------VAVKMLNVTAPTpQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ---LAIVTQWCE 533
Cdd:cd05058     3 IGKGHFGCVYHGTLIDSdgqkihCAVKSLNRITDI-EEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEgspLVVLPYMKH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLyhhlHII--ETKFEMIK-LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA--TVKSRWSGSH 608
Cdd:cd05058    82 GDLR----NFIrsETHNPTVKdLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLArdIYDKEYYSVH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMV-GRGYLSPDLskvrsnCP 686
Cdd:cd05058   158 NHTGAKLPVKWMALESLQTQK---FTTKSDVWSFGVLLWELMTrGAPPYPDVDSFDITVYLLqGRRLLQPEY------CP 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 687 KAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05058   229 DPLYEVMLSCWHPKPEMRPTFSELVSRISQI 259
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
462-696 2.60e-33

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: 129.70  E-value: 2.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKWHGD-VAVKMLNVTaptpqQLQAFKNEVGV--LRKTRHVNILLF-------MGYSTkpQLAIVTQW 531
Cdd:cd14056     2 TIGKGRYGEVWLGKYRGEkVAVKIFSSR-----DEDSWFRETEIyqTVMLRHENILGFiaadiksTGSWT--QLWLITEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHL--HIIETKfEMIKLidiARQTAQGMDYLHAK--------SIIHRDLKSNNIFLHEDLTVKIGDFGLATVK 601
Cdd:cd14056    75 HEHGSLYDYLqrNTLDTE-EALRL---AYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCIADLGLAVRY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 602 SRWSGS--HQFEQLSGSILWMAPEVIRmQDKNPYSFQS----DVYAFGIVLYELM-----TG-----QLPYSNINNRD-- 663
Cdd:cd14056   151 DSDTNTidIPPNPRVGTKRYMAPEVLD-DSINPKSFESfkmaDIYSFGLVLWEIArrceiGGiaeeyQLPYFGMVPSDps 229
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 664 ----QIIFMVGRgyLSPDLSKVRSNCP--KAMKRLMAEC 696
Cdd:cd14056   230 feemRKVVCVEK--LRPPIPNRWKSDPvlRSMVKLMQEC 266
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
450-715 2.92e-33

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: 129.08  E-value: 2.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKW---HGDVAVKMLNVTAptpQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-PQL 525
Cdd:cd05052     1 WEIERTDITMKHKLGGGQYGEVYEGVWkkyNLTVAVKTLKEDT---MEVEEFLKEAAVMKEIKHPNLVQLLGVCTRePPF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQW-CEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRW 604
Cdd:cd05052    78 YIITEFmPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLS----RL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQLSGS---ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNInNRDQIIFMVGRGYL--SPdl 678
Cdd:cd05052   154 MTGDTYTAHAGAkfpIKWTAPESLAY---NKFSIKSDVWAFGVLLWEIATyGMSPYPGI-DLSQVYELLEKGYRmeRP-- 227
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1237938074 679 skvrSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05052   228 ----EGCPPKVYELMRACWQWNPSDRPSFAEIHQALE 260
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
463-663 3.54e-33

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: 128.11  E-value: 3.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKwH----GDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS-TKPQLAIVTQWCEGSSL 537
Cdd:cd14009     1 IGRGSFATVWKGR-HkqtgEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQkTEDFIYLVLEYCAGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIIETKFEmikliDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFL---HEDLTVKIGDFGLATVKSRWSGShqf 610
Cdd:cd14009    80 SQYIRKRGRLPE-----AVARhfmqQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARSLQPASMA--- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 611 EQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNINNRD 663
Cdd:cd14009   152 ETLCGSPLYMAPEILQFQ---KYDAKADLWSVGAILFEMLVGKPPFRGSNHVQ 201
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
460-713 5.67e-33

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: 128.42  E-value: 5.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYKG--KWHGDV-AVKMLNVTAPTPQQ-------LQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIV 528
Cdd:cd06628     5 GALIGSGSFGSVYLGmnASSGELmAVKQVELPSVSAENkdrkksmLDALQREIALLRELQHENIVQYLGSSSDANhLNIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHIIeTKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL-----ATVKSR 603
Cdd:cd06628    85 LEYVPGGSVATLLNNY-GAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGIskkleANSLST 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQfEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGrGYLSPDLSkvrS 683
Cdd:cd06628   164 KNNGAR-PSLQGSVFWMAPEVVK---QTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQM-QAIFKIG-ENASPTIP---S 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 1237938074 684 NCPKAMKRLMAECLKKKRDERPLFPQILAS 713
Cdd:cd06628   235 NISSEARDFLEKTFEIDHNKRPTADELLKH 264
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
458-713 5.81e-33

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: 128.07  E-value: 5.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKW-----HGDVAVKMLNVTAPTPQQLQAF-KNEVGVLRKTRHVNILLFmgYS---TKPQLAIV 528
Cdd:cd14080     3 RLGKTIGEGSYSKVKLAEYtksglKEKVACKIIDKKKAPKDFLEKFlPRELEILRKLRHPNIIQV--YSifeRGSKVFIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHH------LHIIETKFEMiklidiaRQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvks 602
Cdd:cd14080    81 MEYAEHGDLLEYiqkrgaLSESQARIWF-------RQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFA---- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RWSGSHQFEQLS----GSILWMAPEVIRmqdKNPYS-FQSDVYAFGIVLYELMTGQLPY--SNINN--RDQIifmvGRG- 672
Cdd:cd14080   150 RLCPDDDGDVLSktfcGSAAYAAPEILQ---GIPYDpKKYDIWSLGVILYIMLCGSMPFddSNIKKmlKDQQ----NRKv 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1237938074 673 YLSPDLSKVRSNCpkamKRLMAECLKKKRDERPLFPQILAS 713
Cdd:cd14080   223 RFPSSVKKLSPEC----KDLIDQLLEPDPTKRATIEEILNH 259
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
465-710 1.67e-32

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: 126.85  E-value: 1.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 465 SGSFGTVYKG--KWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP-QLAIVTQWCEGSSLYHHL 541
Cdd:cd14027     3 SGGFGKVSLCfhRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEgKYSLVMEYMEKGNLMHVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 542 HIIETKFEMIKLIDIarQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKsRWSGSHQFE---------- 611
Cdd:cd14027    83 KKVSVPLSVKGRIIL--EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFK-MWSKLTKEEhneqrevdgt 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 612 --QLSGSILWMAPEVIRMQDKNPySFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYlSPDLSKVRSNCPKAM 689
Cdd:cd14027   160 akKNAGTLYYMAPEHLNDVNAKP-TEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGN-RPDVDDITEYCPREI 237
                         250       260
                  ....*....|....*....|.
gi 1237938074 690 KRLMAECLKKKRDERPLFPQI 710
Cdd:cd14027   238 IDLMKLCWEANPEARPTFPGI 258
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
450-715 3.93e-32

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: 126.00  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP 523
Cdd:cd05056     1 YEIQREDITLGRCIGEGQFGDVYQGVYMSpenekiAVAVKTCKNCT-SPSVREKFLQEAYIMRQFDHPHIVKLIGVITEN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSR 603
Cdd:cd05056    80 PVWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGL----SR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQFEQLSGS---ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYE-LMTGQLPYSNINNRDqIIFMVGRGYLSPdls 679
Cdd:cd05056   156 YMEDESYYKASKGklpIKWMAPESINFRR---FTSASDVWMFGVCMWEiLMLGVKPFQGVKNND-VIGRIENGERLP--- 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1237938074 680 kVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05056   229 -MPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLS 263
RBD_RAF cd01816
Ras-binding domain (RBD) found in RAF family serine/threonine kinases; The RAF family includes ...
155-227 4.65e-32

Ras-binding domain (RBD) found in RAF family serine/threonine kinases; The RAF family includes three RAF serine/threonine kinases ARAF, BRAF, and RAF1/CRAF. These are encoded by proto-oncogenes, and activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340514  Cd Length: 71  Bit Score: 118.83  E-value: 4.65e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 155 PIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEkkPIGWDTDISWLTGEELHVEVL 227
Cdd:cd01816     1 SVIRAHLPNQQRTTVEVKPGQTLREALEKAMKRRGLTPEMCVVYRKGTRE--PVSWDTDISTLEGEEISVEIL 71
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
233-281 4.91e-32

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They 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 (C1), 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. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410361  Cd Length: 49  Bit Score: 117.78  E-value: 4.91e-32
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1237938074 233 TTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCV 281
Cdd:cd20811     1 ISHNFVRKTFFTLAFCDVCRKLLFQGFRCQTCGFKFHQRCSDQVPALCE 49
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
461-711 5.38e-32

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: 125.35  E-value: 5.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILlfmGY------STKPQLAIVTQW 531
Cdd:cd08217     6 ETIGKGSFGTVRKVRRKSDgkiLVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIV---RYydrivdRANTTLYIVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEG---SSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKS-----IIHRDLKSNNIFLHEDLTVKIGDFGLAtvksR 603
Cdd:cd08217    83 CEGgdlAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFGLA----R 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQFEQLS--GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGRGYLSPdLSKV 681
Cdd:cd08217   159 VLSHDSSFAKTyvGTPYYMSPELLN---EQSYDEKSDIWSLGCLIYELCALHPPF-QAANQLELAKKIKEGKFPR-IPSR 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 1237938074 682 RSncpKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd08217   234 YS---SELNEVIKSMLNVDPDKRPSVEELL 260
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
450-715 6.63e-32

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: 125.53  E-value: 6.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTPQQLQaFKNEVGVLRK--TRHVNILLFMGY 519
Cdd:cd05062     1 WEVAREKITMSRELGQGSFGMVYEGIAKGvvkdepetRVAIKTVNEAASMRERIE-FLNEASVMKEfnCHHVVRLLGVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 520 STKPQLAIVTQWCEGSsLYHHLHIIETKFE---------MIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTV 590
Cdd:cd05062    80 QGQPTLVIMELMTRGD-LKSYLRSLRPEMEnnpvqappsLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 591 KIGDFGLatvkSRWSGSHQFEQLSGS----ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQI 665
Cdd:cd05062   159 KIGDFGM----TRDIYETDYYRKGGKgllpVRWMSPESLK---DGVFTTYSDVWSFGVVLWEIATlAEQPYQGMSNEQVL 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 666 IFMVGRGYL-SPDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05062   232 RFVMEGGLLdKPD------NCPDMLFELMRMCWQYNPKMRPSFLEIISSIK 276
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
461-722 7.58e-32

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: 124.91  E-value: 7.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQlAIVTQWCEGSSL 537
Cdd:cd14025     2 EKVGSGGFGQVYKVRhkhWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEPV-GLVMEYMETGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHL--HII--ETKFEMIklidiaRQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRWSG---SH 608
Cdd:cd14025    81 EKLLasEPLpwELRFRII------HETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLA----KWNGlshSH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQ--LSGSILWMAPEVIrMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGyLSPDLSKVRSNCP 686
Cdd:cd14025   151 DLSRdgLRGTIAYLPPERF-KEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKG-HRPSLSPIPRQRP 228
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 687 KA---MKRLMAECLKKKRDERPLFPQILASIELLaRSLP 722
Cdd:cd14025   229 SEcqqMICLMKRCWDQDPRKRPTFQDITSETENL-LSLL 266
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
463-704 7.62e-32

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: 124.55  E-value: 7.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK------GKWHgdvAVKMLN-VTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 534
Cdd:cd05123     1 LGKGSFGKVLLvrkkdtGKLY---AMKVLRkKEIIKRKEVEHTLNERNILERVNHPFIVkLHYAFQTEEKLYLVLDYVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIiETKF--EMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQ 612
Cdd:cd05123    78 GELFSHLSK-EGRFpeERARFY--AAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELS--SDGDRTYT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVgrgyLSPDLsKVRSNCPKAMKRL 692
Cdd:cd05123   153 FCGTPEYLAPEVLL---GKGYGKAVDWWSLGVLLYEMLTGKPPFYA-ENRKEIYEKI----LKSPL-KFPEYVSPEAKSL 223
                         250
                  ....*....|..
gi 1237938074 693 MAECLKKKRDER 704
Cdd:cd05123   224 ISGLLQKDPTKR 235
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
451-715 9.58e-32

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: 124.81  E-value: 9.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS-- 520
Cdd:cd05036     2 EVPRKNLTLIRALGQGAFGEVYEGTVSGmpgdpsplQVAVKTLP-ELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCfq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 521 TKPQLaIVTQWCEGSSLYHHLHIIETKFE------MIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL---HEDLTVK 591
Cdd:cd05036    81 RLPRF-ILLELMAGGDLKSFLRENRPRPEqpssltMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLtckGPGRVAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 592 IGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVirMQDkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVG 670
Cdd:cd05036   160 IGDFGMARDIYRADYYRKGGKAMLPVKWMPPEA--FLD-GIFTSKTDVWSFGVLLWEIFSlGYMPYPGKSNQEVMEFVTS 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1237938074 671 RGYLSPDlskvrSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05036   237 GGRMDPP-----KNCPGPVYRIMTQCWQHIPEDRPNFSTILERLN 276
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
460-672 1.44e-31

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: 123.95  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYKG--KWHGDV-AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYST-KPQLAIVTQWCEGS 535
Cdd:cd06626     5 GNKIGEGTFGKVYTAvnLDTGELmAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVhREEVYIFMEYCQEG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIklidIARQTAQ---GMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQ 612
Cdd:cd06626    85 TLEELLRHGRILDEAV----IRVYTLQlleGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTTMAPGE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 613 LS---GSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRG 672
Cdd:cd06626   161 VNslvGTPAYMAPEVITGNKGEGHGRAADIWSLGCVVLEMATGKRPWSELDNEWAIMYHVGMG 223
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
463-705 1.56e-31

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: 123.86  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG--KWHGD-VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLy 538
Cdd:cd06623     9 LGQGSSGVVYKVrhKPTGKiYALKKIHVDG-DEEFRKQLLRELKTLRSCESPYVVKCYGaFYKEGEISIVLEYMDGGSL- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 hhlHIIETKFEMIK---LIDIARQTAQGMDYLHAKS-IIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwsGSHQFEQLS 614
Cdd:cd06623    87 ---ADLLKKVGKIPepvLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKVLEN--TLDQCNTFV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSILWMAPEviRMQDKnPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI----IFMVGRGYLSPDlskvrSNCPKAMK 690
Cdd:cd06623   162 GTVTYMSPE--RIQGE-SYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFelmqAICDGPPPSLPA-----EEFSPEFR 233
                         250
                  ....*....|....*
gi 1237938074 691 RLMAECLKKKRDERP 705
Cdd:cd06623   234 DFISACLQKDPKKRP 248
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
461-711 1.82e-31

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: 123.53  E-value: 1.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSS 536
Cdd:cd08225     6 KKIGEGSFGKIYLAKAKSDsehCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFAsFQENGRLFIVMEYCDGGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIE-TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED-LTVKIGDFGLATVksrWSGSHQFEQL- 613
Cdd:cd08225    86 LMKRINRQRgVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNgMVAKLGDFGIARQ---LNDSMELAYTc 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 SGSILWMAPEVIrmQDKnPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYLSPdlskVRSNCPKAMKRLM 693
Cdd:cd08225   163 VGTPYYLSPEIC--QNR-PYNNKTDIWSLGCVLYELCTLKHPFEG-NNLHQLVLKICQGYFAP----ISPNFSRDLRSLI 234
                         250
                  ....*....|....*...
gi 1237938074 694 AECLKKKRDERPLFPQIL 711
Cdd:cd08225   235 SQLFKVSPRDRPSITSIL 252
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
456-670 1.97e-31

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: 124.03  E-value: 1.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKG--KWHGDV-AVKMLNVTAPTPQQ--------LQAFKNEVGVLRKTRHVNILLFMGYSTKPQ 524
Cdd:cd06629     2 KWVKGELIGKGTYGRVYLAmnATTGEMlAVKQVELPKTSSDRadsrqktvVDALKSEIDTLKDLDHPNIVQYLGFEETED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 -LAIVTQWCEGSSLYHHLHIIeTKFE--MIKliDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVK 601
Cdd:cd06629    82 yFSIFLEYVPGGSIGSCLRKY-GKFEedLVR--FFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 602 SRWSGSHQFEQLSGSILWMAPEVIrMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVG 670
Cdd:cd06629   159 DDIYGNNGATSMQGSVFWMAPEVI-HSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSD-DEAIAAMFKLG 225
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
449-722 2.19e-31

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: 125.08  E-value: 2.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 449 DWEIPDGQITVGQRIGSGSFGTVYKGKWHG----------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFM 517
Cdd:cd05099     6 KWEFPRDRLVLGKPLGEGCFGQVVRAEAYGidksrpdqtvTVAVKMLKDNA-TDKDLADLISEMELMKLIgKHKNIINLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 518 GYSTKP-QLAIVTQWCEGSSLYHHLH---------------IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNN 581
Cdd:cd05099    85 GVCTQEgPLYVIVEYAAKGNLREFLRarrppgpdytfditkVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 582 IFLHEDLTVKIGDFGLAtvksrwSGSHQFEQLSGS------ILWMAPEVI--RMqdknpYSFQSDVYAFGIVLYELMT-G 652
Cdd:cd05099   165 VLVTEDNVMKIADFGLA------RGVHDIDYYKKTsngrlpVKWMAPEALfdRV-----YTHQSDVWSFGILMWEIFTlG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 653 QLPYSNInNRDQIIFMVGRGYL--SPdlskvrSNCPKAMKRLMAECLKKKRDERPLFPQ-------ILASI--ELLARSL 721
Cdd:cd05099   234 GSPYPGI-PVEELFKLLREGHRmdKP------SNCTHELYMLMRECWHAVPTQRPTFKQlvealdkVLAAVseEYLDLSM 306

                  .
gi 1237938074 722 P 722
Cdd:cd05099   307 P 307
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
462-710 2.59e-31

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: 123.23  E-value: 2.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKWHG------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd05060     2 ELGHGNFGSVRKGVYLMksgkevEVAVKTLKQEH-EKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEPLMLVMELAPLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSG 615
Cdd:cd05060    81 PLLKYL-KKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMS--RALGAGSDYYRATTA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 S---ILWMAPEVIrmqdkNPYSF--QSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYL--SPDlskvrsNCPK 687
Cdd:cd05060   158 GrwpLKWYAPECI-----NYGKFssKSDVWSYGVTLWEAFSyGAKPYGEMKGPE-VIAMLESGERlpRPE------ECPQ 225
                         250       260
                  ....*....|....*....|...
gi 1237938074 688 AMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05060   226 EIYSIMLSCWKYRPEDRPTFSEL 248
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
452-717 2.59e-31

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: 123.87  E-value: 2.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 452 IPDGQITVGQRIGSGSFGTVYKGKWHGD------VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS----T 521
Cdd:cd05074     6 IQEQQFTLGRMLGKGEFGSVREAQLKSEdgsfqkVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSlrsrA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 522 KPQLAI---VTQWCEGSSLYHHL---HIIETKFE-----MIK-LIDIARqtaqGMDYLHAKSIIHRDLKSNNIFLHEDLT 589
Cdd:cd05074    86 KGRLPIpmvILPFMKHGDLHTFLlmsRIGEEPFTlplqtLVRfMIDIAS----GMEYLSSKNFIHRDLAARNCMLNENMT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 590 VKIGDFGLAtvKSRWSGSHqFEQLSGSIL---WMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQI 665
Cdd:cd05074   162 VCVADFGLS--KKIYSGDY-YRQGCASKLpvkWLALESLA---DNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIY 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 666 IFMVGRGYLspdlsKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05074   236 NYLIKGNRL-----KQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
463-721 4.40e-31

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: 123.00  E-value: 4.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK--GKWHGDVAVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNILLFMG--YSTKpQLAIVTQWCEGSSLY 538
Cdd:cd14154     1 LGKGFFGQAIKvtHRETGEVMVMKELIRFDEEAQ-RNFLKEVKVMRSLDHPNVLKFIGvlYKDK-KLNLITEYIPGGTLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA---------------TVKSR 603
Cdd:cd14154    79 DVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerlpsgnmspSETLR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQFEQ---LSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELmtgqlpysninnrdqiifmVGRGYLSPD--- 677
Cdd:cd14154   159 HLKSPDRKKrytVVGNPYWMAPEMLNGRS---YDEKVDIFSFGIVLCEI-------------------IGRVEADPDylp 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 678 ------------LSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSL 721
Cdd:cd14154   217 rtkdfglnvdsfREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEALYLHL 272
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
457-711 5.91e-31

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: 122.02  E-value: 5.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKGKW--HG-DVAVKMLNVTAPTPQQLQAF-KNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQW 531
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYStkHKcKVAIKIVSKKKAPEDYLQKFlPREIEVIKGLKHPNLICFYeAIETTSRVYIIMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLyhhLHIIETKfemiKLID------IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA-----TV 600
Cdd:cd14162    82 AENGDL---LDYIRKN----GALPepqarrWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFArgvmkTK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 601 KSRWSGSHQFeqlSGSILWMAPEVIRMQDKNPysFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYLSPDLSK 680
Cdd:cd14162   155 DGKPKLSETY---CGSYAYASPEILRGIPYDP--FLSDIWSMGVVLYTMVYGRLPFDDSNLK-VLLKQVQRRVVFPKNPT 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 681 VRSNCPKAMKRLMAeclkkKRDERPLFPQIL 711
Cdd:cd14162   229 VSEECKDLILRMLS-----PVKKRITIEEIK 254
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
456-713 5.94e-31

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: 122.11  E-value: 5.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQW 531
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSDnqvYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKeAFLDGNRLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHIIETKFEMIKLIDIAR---QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSH 608
Cdd:cd08530    81 APFGDLSKLISKRKKKRRLFPEDDIWRifiQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLAKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFeqlsGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY-----SNINNRdqiifmVGRGYLSPdlskVRS 683
Cdd:cd08530   161 QI----GTPLYAAPEVWKGR---PYDYKSDIWSLGCLLYEMATFRPPFeartmQELRYK------VCRGKFPP----IPP 223
                         250       260       270
                  ....*....|....*....|....*....|
gi 1237938074 684 NCPKAMKRLMAECLKKKRDERPLFPQILAS 713
Cdd:cd08530   224 VYSQDLQQIIRSLLQVNPKKRPSCDKLLQS 253
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
459-712 6.30e-31

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: 121.81  E-value: 6.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKwHGD----VAVKMLNVtaptpQQLQA------FKNEVGVLRKTRHVNILLFMGY-STKPQLAI 527
Cdd:cd14007     4 IGKPLGKGKFGNVYLAR-EKKsgfiVALKVISK-----SQLQKsglehqLRREIEIQSHLRHPNILRLYGYfEDKKRIYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrwSGS 607
Cdd:cd14007    78 ILEYAPNGELYKELKK-QKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVH----APS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLP---------YSNINNRDqiIFMVgrGYLSPDL 678
Cdd:cd14007   153 NRRKTFCGTLDYLPPEMVEGK---EYDYKVDIWSLGVLCYELLVGKPPfeskshqetYKRIQNVD--IKFP--SSVSPEA 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1237938074 679 skvrsncpkamKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd14007   226 -----------KDLISKLLQKDPSKRLSLEQVLN 248
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
458-712 6.68e-31

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: 121.89  E-value: 6.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAPT-PQQLQAFKNEVGVLRKTRHVNILLFMGYST-KPQLAIVTQWC 532
Cdd:cd14099     4 RRGKFLGKGGFAKCYEVTDMStgkVYAGKVVPKSSLTkPKQREKLKSEIKIHRSLKHPNIVKFHDCFEdEENVYILLELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYH------HLHIIETKFEMiklidiaRQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKsrwsg 606
Cdd:cd14099    84 SNGSLMEllkrrkALTEPEVRYFM-------RQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARL----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQ---LSGSILWMAPEVIRmqDKNPYSFQSDVYAFGIVLYELMTGQLP---------YSNINNRDqiifmvgrgYL 674
Cdd:cd14099   152 EYDGERkktLCGTPNYIAPEVLE--KKKGHSFEVDIWSLGVILYTLLVGKPPfetsdvketYKRIKKNE---------YS 220
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1237938074 675 SPDLSKVRSNCpkamKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd14099   221 FPSHLSISDEA----KDLIRSMLQPDPTKRPSLDEILS 254
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
450-715 1.96e-30

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: 120.47  E-value: 1.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHGD-VAVKMLNVTAPTpqqlQAFKNEVGVLRKTRHVNILLFMGY--STKPQLA 526
Cdd:cd05082     1 WALNMKELKLLQTIGKGEFGDVMLGDYRGNkVAVKCIKNDATA----QAFLAEASVMTQLRHSNLVQLLGVivEEKGGLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLHII-ETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWS 605
Cdd:cd05082    77 IVTEYMAKGSLVDYLRSRgRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 GSHQFeqlsgSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYL--SPDlskvr 682
Cdd:cd05082   157 DTGKL-----PVKWTAPEALR---EKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKD-VVPRVEKGYKmdAPD----- 222
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1237938074 683 sNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05082   223 -GCPPAVYDVMKNCWHLDAAMRPSFLQLREQLE 254
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
461-712 3.26e-30

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: 119.80  E-value: 3.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKT-RHVNIL-LFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd13997     6 EQIGSGSFSEVFKVRSKVDgclYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVrYYSSWEEGGHLYIQMELCENG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHII--ETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGSHQFEQl 613
Cdd:cd13997    86 SLQDALEELspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLAT---RLETSGDVEE- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 sGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTG-QLPysniNNRDQIIfMVGRGYLSPDLSKVRSncpKAMKRL 692
Cdd:cd13997   162 -GDSRYLAPEL--LNENYTHLPKADIFSLGVTVYEAATGePLP----RNGQQWQ-QLRQGKLPLPPGLVLS---QELTRL 230
                         250       260
                  ....*....|....*....|
gi 1237938074 693 MAECLKKKRDERPLFPQILA 712
Cdd:cd13997   231 LKVMLDPDPTRRPTADQLLA 250
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
460-710 3.41e-30

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: 119.73  E-value: 3.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQ-AFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGSSL 537
Cdd:cd05085     1 GELLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKiKFLSEARILKQYDHPNIVKLIGVCTQRQpIYIVMELVPGGDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKS----RWSGSHQFeql 613
Cdd:cd05085    81 LSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDdgvySSSGLKQI--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 sgSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYlspdLSKVRSNCPKAMKRL 692
Cdd:cd05085   158 --PIKWTAPEAL---NYGRYSSESDVWSFGILLWETFSlGVCPYPGMTNQ-QAREQVEKGY----RMSAPQRCPEDIYKI 227
                         250
                  ....*....|....*...
gi 1237938074 693 MAECLKKKRDERPLFPQI 710
Cdd:cd05085   228 MQRCWDYNPENRPKFSEL 245
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
461-710 3.65e-30

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: 120.51  E-value: 3.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD--------VAVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQW 531
Cdd:cd05091    12 EELGEDRFGKVYKGHLFGTapgeqtqaVAIKTLKDKAEGPLR-EEFRHEAMLRSRLQHPNIVCLLGVVTKEQpMSMIFSY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHL---------------HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG 596
Cdd:cd05091    91 CSHGDLHEFLvmrsphsdvgstdddKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 597 LAtvksRWSGSHQFEQLSGS----ILWMAPEVIrMQDKnpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGR 671
Cdd:cd05091   171 LF----REVYAADYYKLMGNsllpIRWMSPEAI-MYGK--FSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMIRNR 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1237938074 672 GYLS-PDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05091   244 QVLPcPD------DCPAWVYTLMLECWNEFPSRRPRFKDI 277
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
463-705 4.27e-30

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: 120.62  E-value: 4.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD-VAVKMLNVtaptpQQLQAFKNEVGVLRKT--RHVNILLFM-----GYSTKPQLAIVTQWCEG 534
Cdd:cd13998     3 IGKGRFGEVWKASLKNEpVAVKIFSS-----RDKQSWFREKEIYRTPmlKHENILQFIaaderDTALRTELWLVTAFHPN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSL--YHHLHIIETkfemIKLIDIARQTAQGMDYLHAK---------SIIHRDLKSNNIFLHEDLTVKIGDFGLATvksR 603
Cdd:cd13998    78 GSL*dYLSLHTIDW----VSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGLAV---R 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQFEQLS-----GSILWMAPEVI--RMQDKNPYSF-QSDVYAFGIVLYELMTgqlpysninnRDQIIFMVGRGYLS 675
Cdd:cd13998   151 LSPSTGEEDNAnngqvGTKRYMAPEVLegAINLRDFESFkRVDIYAMGLVLWEMAS----------RCTDLFGIVEEYKP 220
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 676 PDLSKVRSN-CPKAMKRLMaeCLKKKRDERP 705
Cdd:cd13998   221 PFYSEVPNHpSFEDMQEVV--VRDKQRPNIP 249
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
463-655 4.68e-30

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: 119.91  E-value: 4.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKW--HGDVAVKMLNVTAPTPQQLQaFKNEVGVLRKTRHVNILLFMGY-STKPQLAIVTQWCEGSSLYH 539
Cdd:cd14664     1 IGRGGAGTVYKGVMpnGTLVAVKRLKGEGTQGGDHG-FQAEIQTLGMIRHRNIVRLRGYcSNPTTNLLVYEYMPNGSLGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 540 HLHIIETKFEMI---KLIDIARQTAQGMDYLH---AKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrWSGSHQFEQL 613
Cdd:cd14664    80 LLHSRPESQPPLdweTRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMD-DKDSHVMSSV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 614 SGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLP 655
Cdd:cd14664   159 AGSYGYIAPEYAYTGKVSE---KSDVYSYGVVLLELITGKRP 197
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
451-710 5.48e-30

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: 119.64  E-value: 5.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKG------KWHGDVAVKMLNVTAPTPQQLqAFKNEVGVLRKTRHVNILLFMGYSTKPQ 524
Cdd:cd05064     1 ELDNKSIKIERILGTGRFGELCRGclklpsKRELPVAIHTLRAGCSDKQRR-GFLAEALTLGQFDHSNIVRLEGVITRGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 -LAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG------L 597
Cdd:cd05064    80 tMMIVTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRrlqedkS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 ATVKSRWSGShqfeqlsGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYLSP 676
Cdd:cd05064   160 EAIYTTMSGK-------SPVLWAAPEAIQYHH---FSSASDVWSFGIVMWEVMSyGERPYWDMSGQD-VIKAVEDGFRLP 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1237938074 677 dlskVRSNCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05064   229 ----APRNCPNLLHQLMLDCWQKERGERPRFSQI 258
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
456-705 5.99e-30

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: 119.66  E-value: 5.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKG--KWHGD-VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQW 531
Cdd:cd06609     2 LFTLLERIGKGSFGEVYKGidKRTNQvVAIKVIDLEE-AEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKgSKLWIIMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHIIetKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKSRWSGSHQF 610
Cdd:cd06609    81 CGGGSVLDLLKPG--PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGqLTSTMSKRNTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 eqlSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRgyLSPDlSKVRSNCPKAMK 690
Cdd:cd06609   159 ---VGTPFWMAPEVIK---QSGYDEKADIWSLGITAIELAKGEPPLSDLHPM-RVLFLIPK--NNPP-SLEGNKFSKPFK 228
                         250
                  ....*....|....*
gi 1237938074 691 RLMAECLKKKRDERP 705
Cdd:cd06609   229 DFVELCLNKDPKERP 243
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
456-712 1.44e-29

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: 118.31  E-value: 1.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKG--KWHGDVAVKMLNVTAPTP----QQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIV 528
Cdd:cd06631     2 QWKKGNVLGKGAYGTVYCGltSTGQLIAVKQVELDTSDKekaeKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNvVSIF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHIIETKFEMIkLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG----LATVKSRW 604
Cdd:cd06631    82 MEFVPGGSIASILARFGALEEPV-FCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrLCINLSSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNInNRDQIIFMVGRGY-LSPDLSKVRS 683
Cdd:cd06631   161 SQSQLLKSMRGTPYWMAPEVIN---ETGHGRKSDIWSIGCTVFEMATGKPPWADM-NPMAAIFAIGSGRkPVPRLPDKFS 236
                         250       260
                  ....*....|....*....|....*....
gi 1237938074 684 ncpKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd06631   237 ---PEARDFVHACLTRDQDERPSAEQLLK 262
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
444-712 2.52e-29

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: 117.79  E-value: 2.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 444 RDSSDDWEIpdgqitvGQRIGSGSFGTVYKGKwHGD----VAVKMLNvtaPTPQQLQAFKNEVGVLRK-TRHVNILLFMG 518
Cdd:cd06608     2 PDPAGIFEL-------VEVIGEGTYGKVYKAR-HKKtgqlAAIKIMD---IIEDEEEEIKLEINILRKfSNHPNIATFYG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKP-------QLAIVTQWCEGSS---LYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL 588
Cdd:cd06608    71 AFIKKdppggddQLWLVMEYCGGGSvtdLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 589 TVKIGDFGL-ATVKSRWSGSHQFeqlSGSILWMAPEVIrMQDKNP---YSFQSDVYAFGIVLYELMTGQLPYSNinnrdq 664
Cdd:cd06608   151 EVKLVDFGVsAQLDSTLGRRNTF---IGTPYWMAPEVI-ACDQQPdasYDARCDVWSLGITAIELADGKPPLCD------ 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 665 iifmvgrgyLSPD--LSKVRSNCPKAMKR----------LMAECLKKKRDERPLFPQILA 712
Cdd:cd06608   221 ---------MHPMraLFKIPRNPPPTLKSpekwskefndFISECLIKNYEQRPFTEELLE 271
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
463-705 2.63e-29

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: 117.46  E-value: 2.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKW---HGDVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLY 538
Cdd:cd06610     9 IGSGATAVVYAAYClpkKEKVAIKRIDLEK-CQTSMDELRKEIQAMSQCNHPNVVSYYTsFVVGDELWLVMPLLSGGSLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HhlhIIETKFEMiKLID------IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG----LATVKSRWSGSH 608
Cdd:cd06610    88 D---IMKSSYPR-GGLDeaiiatVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGvsasLATGGDRTRKVR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QfeQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDqiIFMVGRGYLSPDLSKVRSN--CP 686
Cdd:cd06610   164 K--TFVGTPCWMAPEV--MEQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMK--VLMLTLQNDPPSLETGADYkkYS 237
                         250
                  ....*....|....*....
gi 1237938074 687 KAMKRLMAECLKKKRDERP 705
Cdd:cd06610   238 KSFRKMISLCLQKDPSKRP 256
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
451-710 3.12e-29

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: 118.21  E-value: 3.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTV---------------YKGKWHGD----VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHV 511
Cdd:cd05051     1 EFPREKLEFVEKLGEGQFGEVhlceanglsdltsddFIGNDNKDepvlVAVKMLRPDA-SKNAREDFLKEVKIMSQLKDP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 512 NILLFMGYSTK-PQLAIVTQWCEGSSLYHHL--HIIETKFEMIK---------LIDIARQTAQGMDYLHAKSIIHRDLKS 579
Cdd:cd05051    80 NIVRLLGVCTRdEPLCMIVEYMENGDLNQFLqkHEAETQGASATnsktlsygtLLYMATQIASGMKYLESLNFVHRDLAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 580 NNIFLHEDLTVKIGDFGLatvkSRWSGSHQFEQLSGS----ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT--GQ 653
Cdd:cd05051   160 RNCLVGPNYTIKIADFGM----SRNLYSGDYYRIEGRavlpIRWMAWESILL---GKFTTKSDVWAFGVTLWEILTlcKE 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 654 LPYSNINNrDQIIFMVGRGYLSPD----LSKVRsNCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05051   233 QPYEHLTD-EQVIENAGEFFRDDGmevyLSRPP-NCPKEIYELMLECWRRDEEDRPTFREI 291
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
463-705 4.18e-29

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: 116.78  E-value: 4.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAP-TPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLA-IVTQWCEGSSL 537
Cdd:cd06607     9 IGHGSFGAVYYARNKRTsevVAIKKMSYSGKqSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAwLVMEYCLGSAS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 yhhlHIIETKFEMIKLIDIA---RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwsgSHQFeqlS 614
Cdd:cd06607    89 ----DIVEVHKKPLQEVEIAaicHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCP---ANSF---V 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDLSKvrSNCPKAMKRLMA 694
Cdd:cd06607   159 GTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQND--SPTLSS--GEWSDDFRNFVD 234
                         250
                  ....*....|.
gi 1237938074 695 ECLKKKRDERP 705
Cdd:cd06607   235 SCLQKIPQDRP 245
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
453-704 4.87e-29

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: 116.57  E-value: 4.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLqaFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIV 528
Cdd:cd06647     5 PKKKYTRFEKIGQGASGTVYTAidvATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL-ATVKSRWSgs 607
Cdd:cd06647    83 MEYLAGGSLTDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQS-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 hQFEQLSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDLSKVRSNCPk 687
Cdd:cd06647   159 -KRSTMVGTPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQNPEKLSA- 231
                         250
                  ....*....|....*..
gi 1237938074 688 AMKRLMAECLKKKRDER 704
Cdd:cd06647   232 IFRDFLNRCLEMDVEKR 248
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
450-710 5.27e-29

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: 117.59  E-value: 5.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMGYS 520
Cdd:cd05054     2 WEFPRDRLKLGKPLGRGAFGKVIQASAFGidksatcrTVAVKMLKEGA-TASEHKALMTELKILIHIgHHLNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 521 TKPQ--LAIVTQWCEGSSLYHHL------------------HIIETKFEMIK-------LIDIARQTAQGMDYLHAKSII 573
Cdd:cd05054    81 TKPGgpLMVIVEFCKFGNLSNYLrskreefvpyrdkgardvEEEEDDDELYKepltledLICYSFQVARGMEFLASRKCI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 574 HRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGS--ILWMAPEVIRmqDKnPYSFQSDVYAFGIVLYELMT 651
Cdd:cd05054   161 HRDLAARNILLSENNVVKICDFGLA--RDIYKDPDYVRKGDARlpLKWMAPESIF--DK-VYTTQSDVWSFGVLLWEIFS 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 652 -GQLPYSNINNRDQIIFMVGRGY--LSPDLSkvrsncPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05054   236 lGASPYPGVQMDEEFCRRLKEGTrmRAPEYT------TPEIYQIMLDCWHGEPKERPTFSEL 291
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
460-705 6.54e-29

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: 116.37  E-value: 6.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYKGKwhgDV------AVKML----NVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYST-KPQLAIV 528
Cdd:cd06630     5 GPLLGTGAFSSCYQAR---DVktgtlmAVKQVsfcrNSSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQhKSHFNIF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHIIeTKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLheDLT---VKIGDFGLAT-VKSRW 604
Cdd:cd06630    82 VEWMAGGSVASLLSKY-GAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLV--DSTgqrLRIADFGAAArLASKG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFE-QLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY--SNINNRDQIIFMVGRGYLSPDLSKV 681
Cdd:cd06630   159 TGAGEFQgQLLGTIAFMAPEVLRGE---QYGRSCDVWSVGCVIIEMATAKPPWnaEKISNHLALIFKIASATTPPPIPEH 235
                         250       260
                  ....*....|....*....|....
gi 1237938074 682 RSncpKAMKRLMAECLKKKRDERP 705
Cdd:cd06630   236 LS---PGLRDVTLRCLELQPEDRP 256
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
456-718 7.37e-29

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: 116.11  E-value: 7.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKW--HGDVAVKMLNVTAPTPQQlqaFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWC 532
Cdd:cd05114     5 ELTFMKELGSGLFGVVRLGKWraQYKVAIKAIREGAMSEED---FIEEAKVMMKLTHPKLVQLYGVCTQQKpIYIVTEFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRWSGSHQFEQ 612
Cdd:cd05114    82 ENGCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMT----RYVLDDQYTS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGS---ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGY--LSPDLSkvrsncP 686
Cdd:cd05114   158 SSGAkfpVKWSPPEVFNY---SKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNY-EVVEMVSRGHrlYRPKLA------S 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1237938074 687 KAMKRLMAECLKKKRDERPLFPQILASIELLA 718
Cdd:cd05114   228 KSVYEVMYSCWHEKPEGRPTFADLLRTITEIA 259
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
463-710 7.72e-29

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: 116.56  E-value: 7.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG-DVAVKMLNVTAP-------------------TPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK 522
Cdd:cd14000     2 LGDGGFGSVYRASYKGePVAVKIFNKHTSsnfanvpadtmlrhlratdAMKNFRLLRQELTVLSHLHHPSIVYLLGIGIH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 523 PqLAIVTQWCEGSSLYHHL--------HIIETKFEMIKLidiarQTAQGMDYLHAKSIIHRDLKSNNIFL-----HEDLT 589
Cdd:cd14000    82 P-LMLVLELAPLGSLDHLLqqdsrsfaSLGRTLQQRIAL-----QVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAII 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 590 VKIGDFGLATVKSRwSGSHQFEQLSGsilWMAPEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMV 669
Cdd:cd14000   156 IKIADYGISRQCCR-MGAKGSEGTPG---FRAPEIARGNVI--YNEKVDVFSFGMLLYEILSGGAPMVG-HLKFPNEFDI 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1237938074 670 GRGyLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd14000   229 HGG-LRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTV 268
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
463-711 7.81e-29

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: 116.11  E-value: 7.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLN------------VTAPTPQQLQAFKNEVGVLRKTRHVNIL-LF--MGYSTKPQ 524
Cdd:cd14008     1 LGRGSFGKVKLALDTETgqlYAIKIFNksrlrkrregknDRGKIKNALDDVRREIAIMKKLDHPNIVrLYevIDDPESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 LAIVTQWCEGSSLYHhlhiIETKFEMIKLID-----IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLat 599
Cdd:cd14008    81 LYLVLEYCEGGPVME----LDSGDRVPPLPEetarkYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGV-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 600 vksrwsgSHQFEQ-------LSGSILWMAPEVIRMQDKnPYS-FQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGR 671
Cdd:cd14008   155 -------SEMFEDgndtlqkTAGTPAFLAPELCDGDSK-TYSgKAADIWALGVTLYCLVFGRLPF-NGDNILELYEAIQN 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1237938074 672 GYLSPDLSKvrsNCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd14008   226 QNDEFPIPP---ELSPELKDLLRRMLEKDPEKRITLKEIK 262
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
463-724 8.76e-29

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: 116.56  E-value: 8.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQ-QLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGSSL 537
Cdd:cd14026     5 LSRGAFGTVSRARhadWRVTVAIKCLKLDSPVGDsERNCLLKEAEILHKARFSYILPILGICNEPEfLGIVTEYMTNGSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIiETKFEMIKL---IDIARQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRW-------S 605
Cdd:cd14026    85 NELLHE-KDIYPDVAWplrLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGL----SKWrqlsisqS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 GSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYlSPDLSK--VRS 683
Cdd:cd14026   160 RSSKSAPEGGTIIYMPPEEYEPSQKRRASVKHDIYSYAIIMWEVLSRKIPFEEVTNPLQIMYSVSQGH-RPDTGEdsLPV 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1237938074 684 NCP--KAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKI 724
Cdd:cd14026   239 DIPhrATLINLIESGWAQNPDERPSFLKCLIELEPVLRTFDEI 281
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
461-659 1.01e-28

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: 116.66  E-value: 1.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHG-DVAVKMLNvtaptPQQLQAFKNEVGV--LRKTRHVNILLFMG-----YSTKPQLAIVTQWC 532
Cdd:cd14053     1 EIKARGRFGAVWKAQYLNrLVAVKIFP-----LQEKQSWLTEREIysLPGMKHENILQFIGaekhgESLEAEYWLITEFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHL--HIIETKfEMIKlidIARQTAQGMDYLHA----------KSIIHRDLKSNNIFLHEDLTVKIGDFGLATv 600
Cdd:cd14053    76 ERGSLCDYLkgNVISWN-ELCK---IAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLLKSDLTACIADFGLAL- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 601 ksRWSGSHQFEQLSGSI---LWMAPEVIrmqdKNPYSFQS------DVYAFGIVLYELMTG-----------QLPYSNI 659
Cdd:cd14053   151 --KFEPGKSCGDTHGQVgtrRYMAPEVL----EGAINFTRdaflriDMYAMGLVLWELLSRcsvhdgpvdeyQLPFEEE 223
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
463-734 1.41e-28

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: 115.65  E-value: 1.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKwHGD----VAVKMLNVTAPTpQQLQAFKNEVGVLRKTRHV---NILLFMG-YSTKPQLAIVTQWCEG 534
Cdd:cd06917     9 VGRGSYGAVYRGY-HVKtgrvVALKVLNLDTDD-DDVSDIQKEVALLSQLKLGqpkNIIKYYGsYLKGPSLWIIMDYCEG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIIETKFEMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvkSRWSGSHQFEQLS 614
Cdd:cd06917    87 GSIRTLMRAGPIAERYIAVI--MREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAA--SLNQNSSKRSTFV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSILWMAPEVIRmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIifmvgrgYLSPDLSKVRSN---CPKAMKR 691
Cdd:cd06917   163 GTPYWMAPEVIT--EGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAV-------MLIPKSKPPRLEgngYSPLLKE 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1237938074 692 LMAECLKKKRDERplfpqiLASIELLARSLPKIHRSASEPSLN 734
Cdd:cd06917   234 FVAACLDEEPKDR------LSADELLKSKWIKQHSKTPTSVLK 270
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
461-711 1.81e-28

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: 114.91  E-value: 1.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGT--VYKGKWHGD-VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQWCEGSS 536
Cdd:cd08218     6 KKIGEGSFGKalLVKSKEDGKqYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQeSFEENGNLYIVMDYCDGGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIE-TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQLSG 615
Cdd:cd08218    86 LYKRINAQRgVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLN--STVELARTCIG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVgRGYLSPdlskVRSNCPKAMKRLMAE 695
Cdd:cd08218   164 TPYYLSPEIC---ENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKII-RGSYPP----VPSRYSYDLRSLVSQ 235
                         250
                  ....*....|....*.
gi 1237938074 696 CLKKKRDERPLFPQIL 711
Cdd:cd08218   236 LFKRNPRDRPSINSIL 251
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
458-710 1.85e-28

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: 115.18  E-value: 1.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFG---TVYKGKWHGD--VAVKMLN-VTAPTPQQLQAFKNevgvLRKTRHVNILLFMGYST-KPQLAIVTQ 530
Cdd:cd13992     1 ASCGSGASSHTGepkYVKKVGVYGGrtVAIKHITfSRTEKRTILQELNQ----LKELVHDNLNKFIGICInPPNIAVVTE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSII-HRDLKSNNIFLHEDLTVKIGDFGLATVKSRWsGSHQ 609
Cdd:cd13992    77 YCTRGSLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQ-TNHQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 610 FE--QLSGSILWMAPEVIRMQDKNPY-SFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRG---YLSPDLSKVRS 683
Cdd:cd13992   156 LDedAQHKKLLWTAPELLRGSLLEVRgTQKGDVYSFAIILYEILFRSDPFALEREV-AIVEKVISGgnkPFRPELAVLLD 234
                         250       260
                  ....*....|....*....|....*..
gi 1237938074 684 NCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd13992   235 EFPPRLVLLVKQCWAENPEKRPSFKQI 261
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
463-721 2.50e-28

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: 114.49  E-value: 2.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK--GKWHGDV-AVKMLNVTAPTPQQLQafknEVGVLRKTRHVNILLFMGYST-KPQLAIVTQWCEGSSLY 538
Cdd:cd14155     1 IGSGFFSEVYKvrHRTSGQVmALKMNTLSSNRANMLR----EVQLMNRLSHPNILRFMGVCVhQGQLHALTEYINGGNLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKFEMIKL---IDIARqtaqGMDYLHAKSIIHRDLKSNNIFLHED---LTVKIGDFGLAT-VKSRWSGSHQFE 611
Cdd:cd14155    77 QLLDSNEPLSWTVRVklaLDIAR----GLSYLHSKGIFHRDLTSKNCLIKRDengYTAVVGDFGLAEkIPDYSDGKEKLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 612 QLsGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMT------GQLPYSNINNRDQIIF--MVGrgylspdlskvrs 683
Cdd:cd14155   153 VV-GSPYWMAPEVLRGE---PYNEKADVFSYGIILCEIIAriqadpDYLPRTEDFGLDYDAFqhMVG------------- 215
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1237938074 684 NCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSL 721
Cdd:cd14155   216 DCPPDFLQLAFNCCNMDPKSRPSFHDIVKTLEEILEKL 253
RBD pfam02196
Raf-like Ras-binding domain;
156-225 2.57e-28

Raf-like Ras-binding domain;


Pssm-ID: 426652  Cd Length: 69  Bit Score: 108.00  E-value: 2.57e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 156 IVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQdGEKKPIGWDTDISWLTGEELHVE 225
Cdd:pfam02196   1 LCRVYLPNGQRTVVQVRPGETVRDALSKLCKKRGLNPEACDVYLVG-GQKYPLDWDTDSSTLEGEEIRVE 69
C1_A_C-Raf cd20870
protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated ...
232-283 4.20e-28

protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma) kinases, and similar proteins; This group includes A-Raf and C-Raf, both of which are serine/threonine-protein kinases. A-Raf, also called proto-oncogene A-Raf or proto-oncogene A-Raf-1, 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. C-Raf, also known as proto-oncogene 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 mid-gestation 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. Both A- and C-Raf are mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), 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. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410420  Cd Length: 52  Bit Score: 106.96  E-value: 4.20e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 232 LTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNY 283
Cdd:cd20870     1 LTTHNFVRKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDW 52
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
463-707 4.54e-28

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: 113.95  E-value: 4.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG----KWHGDVAVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNILLFMGYST-KPQLAIVTQWCEGSSL 537
Cdd:cd14202    10 IGHGAFAVVFKGrhkeKHDLEVAVKCINKKNLAKSQ-TLLGKEIKILKELKHENIVALYDFQEiANSVYLVMEYCNGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIIETKFE-MIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLH---------EDLTVKIGDFGLAtvksRW-SG 606
Cdd:cd14202    89 ADYLHTMRTLSEdTIRLF--LQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFA----RYlQN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKvRSNCP 686
Cdd:cd14202   163 NMMAATLCGSPMYMAPEVIMSQH---YDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPR-ETSSH 238
                         250       260
                  ....*....|....*....|.
gi 1237938074 687 kaMKRLMAECLKKKRDERPLF 707
Cdd:cd14202   239 --LRQLLLGLLQRNQKDRMDF 257
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
456-664 5.52e-28

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: 113.58  E-value: 5.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTV---YKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQW 531
Cdd:cd14069     2 DWDLVQTLGEGAFGEVflaVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEfQYLFLEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHlhiIETKFEMIKliDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGS 607
Cdd:cd14069    82 ASGGELFDK---IEPDVGMPE--DVAQfyfqQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 608 HQFEQLSGSILWMAPEVIRmqdKNPYSFQ-SDVYAFGIVLYELMTGQLPYSNINNRDQ 664
Cdd:cd14069   157 RLLNKMCGTLPYVAPELLA---KKKYRAEpVDVWSCGIVLFAMLAGELPWDQPSDSCQ 211
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
451-715 9.32e-28

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: 113.77  E-value: 9.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTpqQLQA-FKNEVGVLRKTRHVNI-------- 513
Cdd:cd05050     1 EYPRNNIEYVRDIGQGAFGRVFQARAPGllpyepftMVAVKMLKEEASA--DMQAdFQREAALMAEFDHPNIvkllgvca 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 514 ------LLF--MGYS------------TKPQLAIVTQWCEGSSLyHHLHIIETKfemikLIDIARQTAQGMDYLHAKSII 573
Cdd:cd05050    79 vgkpmcLLFeyMAYGdlneflrhrsprAQCSLSHSTSSARKCGL-NPLPLSCTE-----QLCIAKQVAAGMAYLSERKFV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 574 HRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGSHQFEQLSGS----ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYEL 649
Cdd:cd05050   153 HRDLATRNCLVGENMVVKIADFGL----SRNIYSADYYKASENdaipIRWMPPESIFY---NRYTTESDVWAYGVVLWEI 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 650 MT-GQLPYSNINNrDQIIFMVGRGYL--SPDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05050   226 FSyGMQPYYGMAH-EEVIYYVRDGNVlsCPD------NCPLELYNLMRLCWSKLPSDRPSFASINRILQ 287
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
443-712 9.46e-28

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: 113.20  E-value: 9.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 443 RRDSSDDWEIPdgqitvgQRIGSGSFGTVYKGK--WHGDVA-VKMLNVTAPtpQQLQAFKNEVGVLRKTRHVNILLFMG- 518
Cdd:cd06646     4 RRNPQHDYELI-------QRVGSGTYGDVYKARnlHTGELAaVKIIKLEPG--DDFSLIQQEIFMVKECKHCNIVAYFGs 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL- 597
Cdd:cd06646    75 YLSREKLWICMEYCGGGSLQDIYHVTGPLSEL-QIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVa 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 ----ATVKSRWSgshqfeqLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGY 673
Cdd:cd06646   154 akitATIAKRKS-------FIGTPYWMAPEVAAVEKNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNF 226
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 674 LSPDLsKVRSNCPKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd06646   227 QPPKL-KDKTKWSSTFHNFVKISLTKNPKKRPTAERLLT 264
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
461-717 1.18e-27

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: 113.98  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVY---KGKWHGDVAVKMLNVTAP-TPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLA-IVTQWCEGS 535
Cdd:cd06633    27 HEIGHGSFGAVYfatNSHTNEVVAIKKMSYSGKqTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAwLVMEYCLGS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SlYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwsgshQFEQLSG 615
Cdd:cd06633   107 A-SDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIAS------PANSFVG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDLskvRSN-CPKAMKRLMA 694
Cdd:cd06633   180 TPYWMAPEVILAMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQND--SPTL---QSNeWTDSFRGFVD 254
                         250       260
                  ....*....|....*....|...
gi 1237938074 695 ECLKKKRDERPlfpqilASIELL 717
Cdd:cd06633   255 YCLQKIPQERP------SSAELL 271
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
463-719 1.21e-27

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: 114.01  E-value: 1.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKW--HGD-----VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd05110    15 LGSGAFGTVYKGIWvpEGEtvkipVAIKILNETT-GPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPHG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSG 615
Cdd:cd05110    94 CLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKM 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYLSPDlskvRSNCPKAMKRLMA 694
Cdd:cd05110   174 PIKWMALECIHYRK---FTHQSDVWSYGVTIWELMTfGGKPYDGIPTR-EIPDLLEKGERLPQ----PPICTIDVYMVMV 245
                         250       260
                  ....*....|....*....|....*
gi 1237938074 695 ECLKKKRDERPLFPQILASIELLAR 719
Cdd:cd05110   246 KCWMIDADSRPKFKELAAEFSRMAR 270
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
455-677 1.91e-27

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: 111.96  E-value: 1.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 455 GQITVGQRIGSGSFGTVYKGKwHGD----VAVKMLNVT-APTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIV 528
Cdd:cd14081     1 GPYRLGKTLGKGQTGLVKLAK-HCVtgqkVAIKIVNKEkLSKESVLMKVEREIAIMKLIEHPNVLkLYDVYENKKYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKsrwSGSH 608
Cdd:cd14081    80 LEYVSGGELFDYL-VKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQ---PEGS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 609 QFEQLSGSILWMAPEVIRmqdKNPYSFQ-SDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRG------YLSPD 677
Cdd:cd14081   156 LLETSCGSPHYACPEVIK---GEKYDGRkADIWSCGVILYALLVGALPFDDDNLR-QLLEKVKRGvfhiphFISPD 227
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
460-723 2.10e-27

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: 112.36  E-value: 2.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYKGKW--HGD-----VAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWC 532
Cdd:cd05111    12 LKVLGSGVFGTVHKGIWipEGDsikipVAIKVIQ-DRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGASLQLVTQLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQ 612
Cdd:cd05111    91 PLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYPDDKKYFYSE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGSILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRD-QIIFMVGRGYLSPDLskvrsnCPKAMK 690
Cdd:cd05111   171 AKTPIKWMALESIHF---GKYTHQSDVWSYGVTVWEMMTfGAEPYAGMRLAEvPDLLEKGERLAQPQI------CTIDVY 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1237938074 691 RLMAECLKKKRDERPLFPQILASIELLARSLPK 723
Cdd:cd05111   242 MVMVKCWMIDENIRPTFKELANEFTRMARDPPR 274
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
451-710 2.28e-27

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: 112.56  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKGKWH-----GD---VAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK 522
Cdd:cd05049     1 HIKRDTIVLKRELGEGAFGKVFLGECYnlepeQDkmlVAVKTLK-DASSPDARKDFEREAELLTNLQHENIVKFYGVCTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 523 -PQLAIVTQWCEGSSLYHHLH-------------IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL 588
Cdd:cd05049    80 gDPLLMVFEYMEHGDLNKFLRshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 589 TVKIGDFGLatvkSRWSGSHQFEQLSGS----ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRD 663
Cdd:cd05049   160 VVKIGDFGM----SRDIYSTDYYRVGGHtmlpIRWMPPESILYRK---FTTESDVWSFGVVLWEIFTyGKQPWFQLSNTE 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 664 QIIFMVGRGYLSPDlskvrSNCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05049   233 VIECITQGRLLQRP-----RTCPSEVYAVMLGCWKREPQQRLNIKDI 274
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
472-719 2.38e-27

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: 112.30  E-value: 2.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 472 YKGKWhgdVAVKMLNVTaPTPQQLQAFKnEVGVLRKTRHVNILLFMGYST-KPQLAIVTQWCEGSSLYHhlhIIETkfEM 550
Cdd:cd14042    28 YKGNL---VAIKKVNKK-RIDLTREVLK-ELKHMRDLQHDNLTRFIGACVdPPNICILTEYCPKGSLQD---ILEN--ED 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 551 IKL---------IDIARqtaqGMDYLHAKSII-HRDLKSNNIFLHEDLTVKIGDFGLATVKS---RWSGSHQFEQlsgSI 617
Cdd:cd14042    98 IKLdwmfrysliHDIVK----GMHYLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGLHSFRSgqePPDDSHAYYA---KL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 618 LWMAPEVIRMQDKNPYSFQ-SDVYAFGIVLYELMTGQLPYSNINNR---DQIIF----MVGRGYLSPDLSkvRSNCPKAM 689
Cdd:cd14042   171 LWTAPELLRDPNPPPPGTQkGDVYSFGIILQEIATRQGPFYEEGPDlspKEIIKkkvrNGEKPPFRPSLD--ELECPDEV 248
                         250       260       270
                  ....*....|....*....|....*....|
gi 1237938074 690 KRLMAECLKKKRDERPLFPQILASIELLAR 719
Cdd:cd14042   249 LSLMQRCWAEDPEERPDFSTLRNKLKKLNK 278
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
463-650 2.71e-27

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: 111.43  E-value: 2.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKwHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP-QLAIVTQWCEGSSLYHHL 541
Cdd:cd14065     1 LGKGFFGEVYKVT-HRETGKVMVMKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDnKLNFITEYVNGGTLEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 542 HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE---DLTVKIGDFGLAT--VKSRWSGSHQFEQLS-- 614
Cdd:cd14065    80 KSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREanrGRNAVVADFGLARemPDEKTKKPDRKKRLTvv 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1237938074 615 GSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELM 650
Cdd:cd14065   160 GSPYWMAPEMLRGE---SYDEKVDVFSFGIVLCEII 192
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
463-704 2.92e-27

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: 111.63  E-value: 2.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY---STKPQLAI--VTQWCEG 534
Cdd:cd14033     9 IGRGSFKTVYRGldtETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSwksTVRGHKCIilVTELMTS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLhiieTKFEMIKLIDI---ARQTAQGMDYLHAKS--IIHRDLKSNNIFLH-EDLTVKIGDFGLATVKSrwsgSH 608
Cdd:cd14033    89 GTLKTYL----KRFREMKLKLLqrwSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATLKR----AS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQLSGSILWMAPEVIrmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGyLSPDlSKVRSNCPKa 688
Cdd:cd14033   161 FAKSVIGTPEFMAPEMY----EEKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSG-IKPD-SFYKVKVPE- 233
                         250
                  ....*....|....*.
gi 1237938074 689 MKRLMAECLKKKRDER 704
Cdd:cd14033   234 LKEIIEGCIRTDKDER 249
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
463-705 3.13e-27

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: 111.83  E-value: 3.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD----VAVKMLNVTAPT--------PQQLQAFKNEVGVLRKT-RHVNILLFmgYST---KPQLA 526
Cdd:cd08528     8 LGSGAFGCVYKVRKKSNgqtlLALKEINMTNPAfgrteqerDKSVGDIISEVNIIKEQlRHPNIVRY--YKTfleNDRLY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLHIIETK---FEMIKLIDIARQTAQGMDYLH-AKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKS 602
Cdd:cd08528    86 IVMELIEGAPLGEHFSSLKEKnehFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQKG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RwsGSHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYlSPDLSKVR 682
Cdd:cd08528   166 P--ESSKMTSVVGTILYSCPEIVQNE---PYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEY-EPLPEGMY 239
                         250       260
                  ....*....|....*....|...
gi 1237938074 683 SNcpkAMKRLMAECLKKKRDERP 705
Cdd:cd08528   240 SD---DITFVIRSCLTPDPEARP 259
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
463-704 3.22e-27

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: 111.62  E-value: 3.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTaptpqQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLy 538
Cdd:cd14010     8 IGRGKHSVVYKGRRKGTiefVAIKCVDKS-----KRPEVLNEVRLTHELKHPNVLKFYEwYETSNHLWLVVEYCTGGDL- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 hhLHIIE--TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA-------------TVKSR 603
Cdd:cd14010    82 --ETLLRqdGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeilkelfgqFSDEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQFEQ-LSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYLSPDLSKVR 682
Cdd:cd14010   160 NVNKVSKKQaKRGTPYYMAPELFQGG---VHSFASDLWALGCVLYEMFTGKPPFVA-ESFTELVEKILNEDPPPPPPKVS 235
                         250       260
                  ....*....|....*....|..
gi 1237938074 683 SNCPKAMKRLMAECLKKKRDER 704
Cdd:cd14010   236 SKPSPDFKSLLKGLLEKDPAKR 257
RBD smart00455
Raf-like Ras-binding domain;
157-227 3.53e-27

Raf-like Ras-binding domain;


Pssm-ID: 128731  Cd Length: 70  Bit Score: 104.67  E-value: 3.53e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074  157 VRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIqdGEKKPIGWDTDISWLTGEELHVEVL 227
Cdd:smart00455   2 CKVHLPDNQRTVVKVRPGKTVRDALAKALKKRGLNPECCVVRLR--GEKKPLDLNQPISSLDGQELVVEEL 70
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
458-711 3.76e-27

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: 110.99  E-value: 3.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILlfmGYSTKPQ-----LAIVT 529
Cdd:cd08223     3 QFLRVIGKGSYGEVWLVRHKRDrkqYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIV---SYKESFEgedgfLYIVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHiiETKFEMI---KLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSG 606
Cdd:cd08223    80 GFCEGGDLYTRLK--EQKGVLLeerQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLE--SS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGRGYLsPDLSKVRSncp 686
Cdd:cd08223   156 SDMATTLIGTPYYMSPELFSNK---PYNHKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYKILEGKL-PPMPKQYS--- 227
                         250       260
                  ....*....|....*....|....*
gi 1237938074 687 KAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd08223   228 PELGELIKAMLHQDPEKRPSVKRIL 252
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
463-717 4.89e-27

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: 111.52  E-value: 4.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWH--GD-----VAVKMLNvtAPTPQQLQAFKNEVGVLRKTRHVNILLFMG--YST-KPQLAIVTQWC 532
Cdd:cd05081    12 LGKGNFGSVELCRYDplGDntgalVAVKQLQ--HSGPDQQRDFQREIQILKALHSDFIVKYRGvsYGPgRRSLRLVMEYL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQ 612
Cdd:cd05081    90 PSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDYYVVRE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGS-ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTgqlpYSN--INNRDQIIFMVGRGYLSPDLSK--------- 680
Cdd:cd05081   170 PGQSpIFWYAPESL---SDNIFSRQSDVWSFGVVLYELFT----YCDksCSPSAEFLRMMGCERDVPALCRllelleegq 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1237938074 681 ---VRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05081   243 rlpAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
450-715 5.02e-27

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: 112.03  E-value: 5.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG----------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMG 518
Cdd:cd05098     8 WELPRDRLVLGKPLGEGCFGQVVLAEAIGldkdkpnrvtKVAVKMLKSDA-TEKDLSDLISEMEMMKMIgKHKNIINLLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKP-QLAIVTQWCEGSSLYHHL---------------HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNI 582
Cdd:cd05098    87 ACTQDgPLYVIVEYASKGNLREYLqarrppgmeycynpsHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 583 FLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVI--RMqdknpYSFQSDVYAFGIVLYELMT-GQLPYSNI 659
Cdd:cd05098   167 LVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALfdRI-----YTHQSDVWSFGVLLWEIFTlGGSPYPGV 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 660 nNRDQIIFMVGRGYlspDLSKvRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05098   242 -PVEELFKLLKEGH---RMDK-PSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD 292
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
441-711 5.58e-27

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: 110.91  E-value: 5.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 441 LGRRDSSDDWEIPdgqitvgQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTP-QQLQAFKNEVGVLRKTRHVNILLFMG- 518
Cdd:cd06645     4 LSRRNPQEDFELI-------QRIGSGTYGDVYKARNVNTGELAAIKVIKLEPgEDFAVVQQEIIMMKDCKHSNIVAYFGs 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL- 597
Cdd:cd06645    77 YLRRDKLWICMEFCGGGSLQDIYHVTGPLSES-QIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVs 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 ----ATVKSRWSgshqfeqLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGY 673
Cdd:cd06645   156 aqitATIAKRKS-------FIGTPYWMAPEVAAVERKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNF 228
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1237938074 674 LSPDLsKVRSNCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd06645   229 QPPKL-KDKMKWSNSFHHFVKMALTKNPKKRPTAEKLL 265
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
451-714 5.99e-27

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: 111.26  E-value: 5.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKGKWHGD-------VAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP 523
Cdd:cd05090     1 ELPLSAVRFMEELGECAFGKIYKGHLYLPgmdhaqlVAIKTLK-DYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 Q-LAIVTQWCEGSSLYHHLHI----------------IETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE 586
Cdd:cd05090    80 QpVCMLFEFMNQGDLHEFLIMrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 587 DLTVKIGDFGLatvkSRWSGSHQFEQLSGSIL----WMAPEVIrMQDKnpYSFQSDVYAFGIVLYELMT-GQLPYSNINN 661
Cdd:cd05090   160 QLHVKISDLGL----SREIYSSDYYRVQNKSLlpirWMPPEAI-MYGK--FSSDSDIWSFGVVLWEIFSfGLQPYYGFSN 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 662 RdQIIFMVGRGYLSPdlskVRSNCPKAMKRLMAECLKKKRDERPLFPQILASI 714
Cdd:cd05090   233 Q-EVIEMVRKRQLLP----CSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARL 280
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
457-715 9.25e-27

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: 110.32  E-value: 9.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKGKWHGD------VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-------P 523
Cdd:cd05035     1 LKLGKILGEGEFGSVMEAQLKQDdgsqlkVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTasdlnkpP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEGSSLYHHLHIIET-----KFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd05035    81 SPMVILPFMKHGDLHSYLLYSRLgglpeKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 tvKSRWSGSHqFEQLSGSIL---WMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGYL 674
Cdd:cd05035   161 --RKIYSGDY-YRQGRISKMpvkWIALESLA---DNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNGNRL 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1237938074 675 spdlsKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05035   235 -----KQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLE 270
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
462-672 9.32e-27

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: 110.26  E-value: 9.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYK------GKWHgdvAVKMLNVT--APTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWC 532
Cdd:cd14098     7 RLGSGTFAEVKKavevetGKMR---AIKQIVKRkvAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQhIYLVMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLhiieTKFEMIKLID---IARQTAQGMDYLHAKSIIHRDLKSNNIFLHED--LTVKIGDFGLATVKsrwSGS 607
Cdd:cd14098    84 EGGDLMDFI----MAWGAIPEQHareLTKQILEAMAYTHSMGITHRDLKPENILITQDdpVIVKISDFGLAKVI---HTG 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 608 HQFEQLSGSILWMAPEVIRMQDKNP---YSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRG 672
Cdd:cd14098   157 TFLVTFCGTMAYLAPEILMSKEQNLqggYSNLVDMWSVGCLVYVMLTGALPFDG-SSQLPVEKRIRKG 223
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
461-715 1.05e-26

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: 109.50  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHG-DVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLY 538
Cdd:cd14057     1 TKINETHSGELWKGRWQGnDIVAKILKVRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGaCNSPPNLVVISQYMPYGSLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLH----IIETKFEMIKL-IDIARqtaqGMDYLHA-KSIIHR-DLKSNNIFLHEDLTVKIGdfgLATVKSRWSGSHQFE 611
Cdd:cd14057    81 NVLHegtgVVVDQSQAVKFaLDIAR----GMAFLHTlEPLIPRhHLNSKHVMIDEDMTARIN---MADVKFSFQEPGKMY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 612 QLSgsilWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGyLSPDLSKVRSncpKAMKR 691
Cdd:cd14057   154 NPA----WMAPEALQKKPEDINRRSADMWSFAILLWELVTREVPFADLSNMEIGMKIALEG-LRVTIPPGIS---PHMCK 225
                         250       260
                  ....*....|....*....|....
gi 1237938074 692 LMAECLKKKRDERPLFPQILASIE 715
Cdd:cd14057   226 LMKICMNEDPGKRPKFDMIVPILE 249
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
448-711 1.21e-26

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: 110.50  E-value: 1.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 448 DDWEIpdgqitVGQrIGSGSFGTVYKG--KWHGDVAVKMLnVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQ 524
Cdd:cd06643     5 DFWEI------VGE-LGDGAFGKVYKAqnKETGILAAAKV-IDTKSEEELEDYMVEIDILASCDHPNIVkLLDAFYYENN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 LAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRw 604
Cdd:cd06643    77 LWILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTR- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 sGSHQFEQLSGSILWMAPEVIRMQDKN--PYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYlSPDLSKVR 682
Cdd:cd06643   156 -TLQRRDSFIGTPYWMAPEVVMCETSKdrPYDYKADVWSLGVTLIEMAQIEPPHHELNPM-RVLLKIAKSE-PPTLAQPS 232
                         250       260
                  ....*....|....*....|....*....
gi 1237938074 683 SNCPKaMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd06643   233 RWSPE-FKDFLRKCLEKNVDARWTTSQLL 260
RBD_ARAF cd17133
Ras-binding domain (RBD) found in serine/threonine-protein kinase ARAF; ARAF, also termed ...
157-227 1.88e-26

Ras-binding domain (RBD) found in serine/threonine-protein kinase ARAF; ARAF, also termed proto-oncogene ARAF, or proto-oncogene ARAF1, or proto-oncogene PKS2, belongs to the RAF protein family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. ARAF is predominantly found in urogenital tissue with a low basal kinase activity. It directly cross-talks with NODAL/SMAD2 signaling in a MAPK-independent manner. It also promotes MAPK pathway activation and cell migration in a cell type-dependent manner. Moreover, ARAF acts as a scaffold to stabilize BRAF-CRAF heterodimers. Mice deleted for ARAF are viable but die perinatally.


Pssm-ID: 340653  Cd Length: 73  Bit Score: 102.68  E-value: 1.88e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 157 VRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVL 227
Cdd:cd17133     3 IKVYLPNKQRTVVNVRPGMTVYDSLDKALKVRGLNQDCCAVYRLIKGRKTLTDWETDITPLVGEELLVEVL 73
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
447-719 1.95e-26

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: 111.86  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 447 SDDWEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTPQQlQAFKNEVGVLRKT-RHVNILLFM 517
Cdd:cd05106    30 NEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGlgkednvlRVAVKMLKASAHTDER-EALMSELKILSHLgQHKNIVNLL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 518 GYSTK--PQLAIvTQWC---------------------------EGSSLYHHLHI---------------IETKFEM--- 550
Cdd:cd05106   109 GACTHggPVLVI-TEYCcygdllnflrkkaetflnfvmalpeisETSSDYKNITLekkyirsdsgfssqgSDTYVEMrpv 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 551 ---------------------IKLIDIAR---QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA-------- 598
Cdd:cd05106   188 sssssqssdskdeedtedswpLDLDDLLRfssQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLArdimndsn 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 -TVKsrwsGSHQFeqlsgSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGYL-- 674
Cdd:cd05106   268 yVVK----GNARL-----PVKWMAPESIF---DCVYTVQSDVWSYGILLWEIFSlGKSPYPGILVNSKFYKMVKRGYQms 335
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1237938074 675 SPDLSkvrsncPKAMKRLMAECLKKKRDERPLFPQILASIELLAR 719
Cdd:cd05106   336 RPDFA------PPEIYSIMKMCWNLEPTERPTFSQISQLIQRQLG 374
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
459-711 2.02e-26

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: 109.05  E-value: 2.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVY-----KGKWHGDVAV-KMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQW 531
Cdd:cd08222     4 VVRKLGSGNFGTVYlvsdlKATADEELKVlKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHdSFVEKESFCIVTEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHII---ETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLtVKIGDFGLATVksrWSGSH 608
Cdd:cd08222    84 CEGGDLDDKISEYkksGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRI---LMGTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QF-EQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINnrdqiiFM-VGRGYLSPDLSKVRSNCP 686
Cdd:cd08222   160 DLaTTFTGTPYYMSPEVLKHEG---YNSKSDIWSLGCILYEMCCLKHAFDGQN------LLsVMYKIVEGETPSLPDKYS 230
                         250       260
                  ....*....|....*....|....*
gi 1237938074 687 KAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd08222   231 KELNAIYSRMLNKDPALRPSAAEIL 255
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
463-719 2.06e-26

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: 110.50  E-value: 2.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD-------VAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd05108    15 LGSGAFGTVYKGLWIPEgekvkipVAIKELR-EATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSG 615
Cdd:cd05108    94 CLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRD-QIIFMVGRGYLSPDLskvrsnCPKAMKRLM 693
Cdd:cd05108   174 PIKWMALESILHR---IYTHQSDVWSYGVTVWELMTfGSKPYDGIPASEiSSILEKGERLPQPPI------CTIDVYMIM 244
                         250       260
                  ....*....|....*....|....*.
gi 1237938074 694 AECLKKKRDERPLFPQILASIELLAR 719
Cdd:cd05108   245 VKCWMIDADSRPKFRELIIEFSKMAR 270
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
461-711 2.38e-26

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: 109.60  E-value: 2.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTV--YKGKWHGD-----VAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK---PQLAIVTQ 530
Cdd:cd05080    10 RDLGEGHFGKVslYCYDPTNDgtgemVAVKALK-ADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqggKSLQLIME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHiiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGsHQF 610
Cdd:cd05080    89 YVPLGSLRDYLP--KHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLA--KAVPEG-HEY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 EQLS----GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYsnINNRDQIIFMVGRGylSPDLSKVR---- 682
Cdd:cd05080   164 YRVRedgdSPVFWYAPECLK---EYKFYYASDVWSFGVTLYELLTHCDSS--QSPPTKFLEMIGIA--QGQMTVVRliel 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 683 ----------SNCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd05080   237 lergerlpcpDKCPQEVYHLMKNCWETEASFRPTFENLI 275
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
458-656 2.44e-26

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: 109.18  E-value: 2.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKG-------KWhgdvAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVT 529
Cdd:cd14097     4 TFGRKLGQGSFGVVIEAthketqtKW----AIKKINREKAGSSAVKLLEREVDILKHVNHAHIIhLEEVFETPKRMYLVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLyHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL-------HEDLTVKIGDFGLATVKS 602
Cdd:cd14097    80 ELCEDGEL-KELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnNDKLNIKVTDFGLSVQKY 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 603 RWSGSHqFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14097   159 GLGEDM-LQETCGTPIYMAPEVISAHG---YSQQCDIWSIGVIMYMLLCGEPPF 208
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
453-711 3.08e-26

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: 109.42  E-value: 3.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLqafKNEVGVLRK-TRHVNILLFMGYSTKP----- 523
Cdd:cd06637     4 PAGIFELVELVGNGTYGQVYKGrhvKTGQLAAIKVMDVTGDEEEEI---KQEINMLKKySHHRNIATYYGAFIKKnppgm 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 --QLAIVTQWCEGSSLYHHlhIIETKFEMIK---LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd06637    81 ddQLWLVMEFCGAGSVTDL--IKNTKGNTLKeewIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 TVKSRWSGSHQfeQLSGSILWMAPEVIRMqDKNP---YSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGyLS 675
Cdd:cd06637   159 AQLDRTVGRRN--TFIGTPYWMAPEVIAC-DENPdatYDFKSDLWSLGITAIEMAEGAPPLCDMHPM-RALFLIPRN-PA 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1237938074 676 PDLSKVRSNcpKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd06637   234 PRLKSKKWS--KKFQSFIESCLVKNHSQRPSTEQLM 267
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
461-696 3.28e-26

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: 109.07  E-value: 3.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHG-DVAVKMLNVtaptpqqlqafKNEVGVLRKT--------RHVNILLFMGYSTK-----PQLA 526
Cdd:cd14143     1 ESIGKGRFGEVWRGRWRGeDVAVKIFSS-----------REERSWFREAeiyqtvmlRHENILGFIAADNKdngtwTQLW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHL-HIIETKFEMIKLidiARQTAQGMDYLHAK--------SIIHRDLKSNNIFLHEDLTVKIGDFGL 597
Cdd:cd14143    70 LVSDYHEHGSLFDYLnRYTVTVEGMIKL---ALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTCCIADLGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 AtVKSRwSGSHQFE----QLSGSILWMAPEVI--RMQDKNPYSF-QSDVYAFGIVLYEL-----MTG-----QLPYSNIN 660
Cdd:cd14143   147 A-VRHD-SATDTIDiapnHRVGTKRYMAPEVLddTINMKHFESFkRADIYALGLVFWEIarrcsIGGihedyQLPYYDLV 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 661 NRDQII----FMVGRGYLSPDLSKVRSNCP--KAMKRLMAEC 696
Cdd:cd14143   225 PSDPSIeemrKVVCEQKLRPNIPNRWQSCEalRVMAKIMREC 266
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
456-717 3.81e-26

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: 109.28  E-value: 3.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKG--------KWHGDVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK--PQL 525
Cdd:cd05045     1 NLVLGKTLGEGEFGKVVKAtafrlkgrAGYTTVAVKMLKENA-SSSELRDLLSEFNLLKQVNHPHVIKLYGACSQdgPLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVtQWCEGSSLYHHL-----------------------HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNI 582
Cdd:cd05045    80 LIV-EYAKYGSLRSFLresrkvgpsylgsdgnrnssyldNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 583 FLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGSI--LWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNI 659
Cdd:cd05045   159 LVAEGRKMKISDFGLS--RDVYEEDSYVKRSKGRIpvKWMAIESLF---DHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 660 NNrDQIIFMVGRGYL--SPDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05045   234 AP-ERLFNLLKTGYRmeRPE------NCSEEMYNLMLTCWKQEPDKRPTFADISKELEKM 286
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
462-658 3.90e-26

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: 108.30  E-value: 3.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTV---YKGKWHGDVAVKMLNVTapTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd06648    14 KIGEGSTGIVciaTDKSTGRQVAVKKMDLR--KQQRRELLFNEVVIMRDYQHPNIVeMYSSYLVGDELWVVMEFLEGGAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQLSGSI 617
Cdd:cd06648    92 TDI--VTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVS--KEVPRRKSLVGTP 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1237938074 618 LWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSN 658
Cdd:cd06648   168 YWMAPEVI---SRLPYGTEVDIWSLGIMVIEMVDGEPPYFN 205
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
456-711 5.06e-26

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: 107.96  E-value: 5.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYK------GKWHGDVAVKMLNVTAptpqqlqafKNEVGVLRKTRHVNILLFMG----------- 518
Cdd:cd14047     7 DFKEIELIGSGGFGQVFKakhridGKTYAIKRVKLNNEKA---------EREVKALAKLDHPNIVRYNGcwdgfdydpet 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 -YSTKPQLA-----IVTQWCEGSSLYHHlhiIE----TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL 588
Cdd:cd14047    78 sSSNSSRSKtkclfIQMEFCEKGTLESW---IEkrngEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 589 TVKIGDFGLATVKsrwSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTgqlPYSNINNRDQIIFM 668
Cdd:cd14047   155 KVKIGDFGLVTSL---KNDGKRTKSKGTLSYMSPEQISSQD---YGKEVDIYALGLILFELLH---VCDSAFEKSKFWTD 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1237938074 669 VGRGYLSPDLSKVRsncpKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd14047   226 LRNGILPDIFDKRY----KIEKTIIKKMLSKKPEDRPNASEIL 264
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
453-711 7.31e-26

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: 107.84  E-value: 7.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIV 528
Cdd:cd06642     2 PEELFTKLERIGKGSFGEVYKGidnRTKEVVAIKIIDLEE-AEDEIEDIQQEITVLSQCDSPYITRYYGsYLKGTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHiiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSH 608
Cdd:cd06642    81 MEYLGGGSALDLLK--PGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLT--DTQI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGylSPdlSKVRSNCPKA 688
Cdd:cd06642   157 KRNTFVGTPFWMAPEVIK---QSAYDFKADIWSLGITAIELAKGEPPNSDLHPM-RVLFLIPKN--SP--PTLEGQHSKP 228
                         250       260
                  ....*....|....*....|...
gi 1237938074 689 MKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd06642   229 FKEFVEACLNKDPRFRPTAKELL 251
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
453-711 7.65e-26

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: 108.17  E-value: 7.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLqafKNEVGVLRK-TRHVNILLFMGYSTKP----- 523
Cdd:cd06636    14 PAGIFELVEVVGNGTYGQVYKGrhvKTGQLAAIKVMDVTEDEEEEI---KLEINMLKKySHHRNIATYYGAFIKKsppgh 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 --QLAIVTQWCEGSSLYHHLHiiETKFEMIK---LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd06636    91 ddQLWLVMEFCGAGSVTDLVK--NTKGNALKedwIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 TVKSRWSGSHQfeQLSGSILWMAPEVIRMqDKNP---YSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRgylS 675
Cdd:cd06636   169 AQLDRTVGRRN--TFIGTPYWMAPEVIAC-DENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPM-RALFLIPR---N 241
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1237938074 676 PDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd06636   242 PPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLL 277
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
443-660 1.47e-25

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: 107.42  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 443 RRD--SSDDWEIpdgqitVGQrIGSGSFGTVYKGKWHGDVAVKMLNVT-APTPQQLQAFKNEVGVLRKTRHVNILLFMG- 518
Cdd:cd06644     5 RRDldPNEVWEI------IGE-LGDGAFGKVYKAKNKETGALAAAKVIeTKSEEELEDYMVEIEILATCNHPYIVKLLGa 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd06644    78 FYWDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVS 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 -----TVKSRwsgshqfEQLSGSILWMAPEVI---RMQDkNPYSFQSDVYAFGIVLYELMTGQLPYSNIN 660
Cdd:cd06644   158 aknvkTLQRR-------DSFIGTPYWMAPEVVmceTMKD-TPYDYKADIWSLGITLIEMAQIEPPHHELN 219
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
461-705 1.58e-25

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: 107.46  E-value: 1.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD-------VAVKMLnvtapTPQQLQAFKNEVGVLR--KTRHVNILLFM-----GYSTKPQLA 526
Cdd:cd14055     1 KLVGKGRFAEVWKAKLKQNasgqyetVAVKIF-----PYEEYASWKNEKDIFTdaSLKHENILQFLtaeerGVGLDRQYW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHL--HIIEtkfeMIKLIDIARQTAQGMDYLHAKS---------IIHRDLKSNNIFLHEDLTVKIGDF 595
Cdd:cd14055    76 LITAYHENGSLQDYLtrHILS----WEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCVLADF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 596 GLATvksRWSGSHQFEQLS-----GSILWMAPEVI--RMQDKNPYSF-QSDVYAFGIVLYELMtgqlpysninNRDQIIF 667
Cdd:cd14055   152 GLAL---RLDPSLSVDELAnsgqvGTARYMAPEALesRVNLEDLESFkQIDVYSMALVLWEMA----------SRCEASG 218
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 668 MVGRgYLSPDLSKVRSN-CPKAMKRLMaeCLKKKRDERP 705
Cdd:cd14055   219 EVKP-YELPFGSKVRERpCVESMKDLV--LRDRGRPEIP 254
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
461-696 1.65e-25

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: 107.18  E-value: 1.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHG-DVAVKMLNVTaptpqqlqafkNEVGVLRKT--------RHVNILLFM-----GYSTKPQLA 526
Cdd:cd14144     1 RSVGKGRYGEVWKGKWRGeKVAVKIFFTT-----------EEASWFRETeiyqtvlmRHENILGFIaadikGTGSWTQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHL--HIIETKfEMIKLidiARQTAQGMDYLHAK--------SIIHRDLKSNNIFLHEDLTVKIGDFG 596
Cdd:cd14144    70 LITDYHENGSLYDFLrgNTLDTQ-SMLKL---AYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 597 LATVKSRWSGSHQFEQLS--GSILWMAPEVIRmQDKNPYSFQS----DVYAFGIVLYEL----MTG------QLPYSNIN 660
Cdd:cd14144   146 LAVKFISETNEVDLPPNTrvGTKRYMAPEVLD-ESLNRNHFDAykmaDMYSFGLVLWEIarrcISGgiveeyQLPYYDAV 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 661 NRD------QIIFMVGRgyLSPDLSK--VRSNCPKAMKRLMAEC 696
Cdd:cd14144   225 PSDpsyedmRRVVCVER--RRPSIPNrwSSDEVLRTMSKLMSEC 266
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
461-732 1.70e-25

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: 106.70  E-value: 1.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKG---KWHGDVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSS 536
Cdd:cd06641    10 EKIGKGSFGEVFKGidnRTQKVVAIKIIDLEE-AEDEIEDIQQEITVLSQCDSPYVTKYYGsYLKDTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LyhhLHIIET-KFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQLSG 615
Cdd:cd06641    89 A---LDLLEPgPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLT--DTQIKRN*FVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGylSPDLskVRSNCPKAMKRLMAE 695
Cdd:cd06641   164 TPFWMAPEVIK---QSAYDSKADIWSLGITAIELARGEPPHSELHPM-KVLFLIPKN--NPPT--LEGNYSKPLKEFVEA 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1237938074 696 CLKKKRDERPlfpqilASIELLARSLpkIHRSASEPS 732
Cdd:cd06641   236 CLNKEPSFRP------TAKELLKHKF--ILRNAKKTS 264
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
456-722 1.75e-25

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: 107.02  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGD-----VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-------P 523
Cdd:cd05075     1 KLALGKTLGEGEFGSVMEGQLNQDdsvlkVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQntesegyP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEGSSL-----YHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd05075    81 SPVVILPFMKHGDLhsfllYSRLGDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 tvKSRWSGSH--QFEQLSGSILWMAPEviRMQDKnPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGYLs 675
Cdd:cd05075   161 --KKIYNGDYyrQGRISKMPVKWIAIE--SLADR-VYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYDYLRQGNRL- 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 676 pdlsKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLP 722
Cdd:cd05075   235 ----KQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKDLP 277
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
453-704 1.88e-25

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: 107.11  E-value: 1.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLqaFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIV 528
Cdd:cd06656    17 PKKKYTRFEKIGQGASGTVYTAidiATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL-ATVKSRWSgs 607
Cdd:cd06656    95 MEYLAGGSLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQS-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 hQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDLSKvRSNCPK 687
Cdd:cd06656   171 -KRSTMVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQN-PERLSA 243
                         250
                  ....*....|....*..
gi 1237938074 688 AMKRLMAECLKKKRDER 704
Cdd:cd06656   244 VFRDFLNRCLEMDVDRR 260
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
463-717 1.94e-25

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: 106.94  E-value: 1.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKW--HGDVAVKMLNVTAPTPQ----QLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ---LAIVTQWCE 533
Cdd:cd05079    12 LGEGHFGKVELCRYdpEGDNTGEQVAVKSLKPEsggnHIADLKKEIEILRNLYHENIVKYKGICTEDGgngIKLIMEFLP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA-TVKSRWSGSHQFEQ 612
Cdd:cd05079    92 SGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkAIETDKEYYTVKDD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGSILWMAPEVIrMQDKnpYSFQSDVYAFGIVLYELMTgqlpYSNINNRDQIIFMVGRGYLSPDLSKVR---------- 682
Cdd:cd05079   172 LDSPVFWYAPECL-IQSK--FYIASDVWSFGVTLYELLT----YCDSESSPMTLFLKMIGPTHGQMTVTRlvrvleegkr 244
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 683 ----SNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05079   245 lprpPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAI 283
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
463-655 2.18e-25

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: 106.83  E-value: 2.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGDV-AVKMLNVTAPTPQQL--QAFKNEVGVLRKTRHVNILLFMGYSTKPQL-AIVTQWCEGSSLY 538
Cdd:cd14159     1 IGEGGFGCVYQAVMRNTEyAVKRLKEDSELDWSVvkNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNyCLIYVYLPNGSLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLH--IIETKFEMIKLIDIARQTAQGMDYLH--AKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLS 614
Cdd:cd14159    81 DRLHcqVSCPCLSWSQRLHVLLGTARAIQYLHsdSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPKQPGMSSTLA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 615 ------GSILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMTGQLP 655
Cdd:cd14159   161 rtqtvrGTLAYLPEEYVKT---GTLSVEIDVYSFGVVLLELLTGRRA 204
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
463-712 2.40e-25

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: 105.97  E-value: 2.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQWCEGSSLY 538
Cdd:cd08220     8 VGRGAYGTVYLCRRKDDnklVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYeSFLEDKALMIVMEYAPGGTLF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKF-EMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT-VKIGDFGLATVKSRWSGSHqfeQLSGS 616
Cdd:cd08220    88 EYIQQRKGSLlSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKILSSKSKAY---TVVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 617 ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYLSPdLSKVRSncpKAMKRLMAEC 696
Cdd:cd08220   165 PCYISPELC---EGKPYNQKSDIWALGCVLYELASLKRAFEA-ANLPALVLKIMRGTFAP-ISDRYS---EELRHLILSM 236
                         250
                  ....*....|....*.
gi 1237938074 697 LKKKRDERPLFPQILA 712
Cdd:cd08220   237 LHLDPNKRPTLSEIMA 252
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
459-661 2.82e-25

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: 106.15  E-value: 2.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHGD---VAVKMLNvtaptPQQL------QAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIV 528
Cdd:cd05581     5 FGKPLGEGSYSTVVLAKEKETgkeYAIKVLD-----KRHIikekkvKYVTIEKEVLSRLAHPGIVkLYYTFQDESKLYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHIIET-KFEMIKLIdiarqTAQ---GMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRW 604
Cdd:cd05581    80 LEYAPNGDLLEYIRKYGSlDEKCTRFY-----TAEivlALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPD 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 605 SGSHQFEQLS---------------GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINN 661
Cdd:cd05581   155 SSPESTKGDAdsqiaynqaraasfvGTAEYVSPELL---NEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNE 223
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
463-719 3.46e-25

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: 105.88  E-value: 3.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD-------VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd05109    15 LGSGAFGTVYKGIWIPDgenvkipVAIKVLRENT-SPKANKEILDEAYVMAGVGSPYVCRLLGICLTSTVQLVTQLMPYG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSG 615
Cdd:cd05109    94 CLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYLSPDlskvRSNCPKAMKRLMA 694
Cdd:cd05109   174 PIKWMALESIL---HRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPARE-IPDLLEKGERLPQ----PPICTIDVYMIMV 245
                         250       260
                  ....*....|....*....|....*
gi 1237938074 695 ECLKKKRDERPLFPQILASIELLAR 719
Cdd:cd05109   246 KCWMIDSECRPRFRELVDEFSRMAR 270
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
458-701 3.61e-25

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: 105.49  E-value: 3.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYK------GKWHgdvAVKMLNVTaptpqQLQA----FKNEVGVLRKTRHVNI-LLFMGYSTKPQLA 526
Cdd:cd14095     3 DIGRVIGDGNFAVVKEcrdkatDKEY---ALKIIDKA-----KCKGkehmIENEVAILRRVKHPNIvQLIEEYDTDTELY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED----LTVKIGDFGLATVKS 602
Cdd:cd14095    75 LVMELVKGGDLFDAI-TSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHedgsKSLKLADFGLATEVK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 rwsgshqfEQLS---GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIF---MVGR-GYLS 675
Cdd:cd14095   154 --------EPLFtvcGTPTYVAPEIL---AETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQEELFdliLAGEfEFLS 222
                         250       260
                  ....*....|....*....|....*.
gi 1237938074 676 PDLSKVrSNCPKAMKRLMAECLKKKR 701
Cdd:cd14095   223 PYWDNI-SDSAKDLISRMLVVDPEKR 247
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
466-712 3.72e-25

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: 106.00  E-value: 3.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 466 GSFGTVYKGKWHG------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNIL--------------LFMGYSTKPQL 525
Cdd:cd05043    17 GTFGRIFHGILRDekgkeeEVLVKTVKDHA-SEIQVTMLLQESSLLYGLSHQNLLpilhvciedgekpmVLYPYMNWGNL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLyHHLHIIETkfemIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWS 605
Cdd:cd05043    96 KLFLQQCRLSEA-NNPQALST----QQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNAL----SRDL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 GSHQFEQLSGS----ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNrDQIIFMVGRGY--LSPdl 678
Cdd:cd05043   167 FPMDYHCLGDNenrpIKWMSLESLV---NKEYSSASDVWSFGVLLWELMTlGQTPYVEIDP-FEMAAYLKDGYrlAQP-- 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1237938074 679 skvrSNCPKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd05043   241 ----INCPDELFAVMACCWALDPEERPSFQQLVQ 270
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
463-718 4.17e-25

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: 105.41  E-value: 4.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK--GKWHGDVAVkMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEGSSLYH 539
Cdd:cd14222     1 LGKGFFGQAIKvtHKATGKVMV-MKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKdKRLNLLTEFIEGGTLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 540 HLHIIETkFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL---------------ATVKSRW 604
Cdd:cd14222    80 FLRADDP-FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLsrliveekkkpppdkPTTKKRT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQ---LSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELmtgqlpysninnrdqiifmVGRGYLSPD-LSK 680
Cdd:cd14222   159 LRKNDRKKrytVVGNPYWMAPEMLNGKS---YDEKVDIFSFGIVLCEI-------------------IGQVYADPDcLPR 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 681 ---------------VRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLA 718
Cdd:cd14222   217 tldfglnvrlfwekfVPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEALS 269
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
460-705 4.78e-25

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: 105.13  E-value: 4.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVY------KGKwhgDVAVKMLNV---TAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVT 529
Cdd:cd06625     5 GKLLGQGAFGQVYlcydadTGR---ELAVKQVEIdpiNTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKsLSIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIIETKFEMIKLiDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG----LATVKSrws 605
Cdd:cd06625    82 EYMPGGSVKDEIKAYGALTENVTR-KYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGaskrLQTICS--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 gSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYLSPDLSkvrSNC 685
Cdd:cd06625   158 -STGMKSVTGTPYWMSPEVINGEG---YGRKADIWSVGCTVVEMLTTKPPWAEFEPM-AAIFKIATQPTNPQLP---PHV 229
                         250       260
                  ....*....|....*....|
gi 1237938074 686 PKAMKRLMAECLKKKRDERP 705
Cdd:cd06625   230 SEDARDFLSLIFVRNKKQRP 249
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
456-649 4.85e-25

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: 105.99  E-value: 4.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGD-VAVKMLNVtaptpqqlqafKNEVGVLRKT--------RHVNILLFMG-----YST 521
Cdd:cd14142     6 QITLVECIGKGRYGEVWRGQWQGEsVAVKIFSS-----------RDEKSWFRETeiyntvllRHENILGFIAsdmtsRNS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 522 KPQLAIVTQWCEGSSLYHHLHiiETKFEMIKLIDIARQTAQGMDYLHAK--------SIIHRDLKSNNIFLHEDLTVKIG 593
Cdd:cd14142    75 CTQLWLITHYHENGSLYDYLQ--RTTLDHQEMLRLALSAASGLVHLHTEifgtqgkpAIAHRDLKSKNILVKSNGQCCIA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 594 DFGLATVKSRWSGshqfeQLS-------GSILWMAPEVIRmQDKNPYSFQS----DVYAFGIVLYEL 649
Cdd:cd14142   153 DLGLAVTHSQETN-----QLDvgnnprvGTKRYMAPEVLD-ETINTDCFESykrvDIYAFGLVLWEV 213
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
458-660 5.00e-25

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: 105.05  E-value: 5.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPT-PQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWC 532
Cdd:cd08224     3 EIEKKIGKGQFSVVYRARCLLDgrlVALKKVQIFEMMdAKARQDCLKEIDLLQQLNHPNIIkYLASFIENNELNIVLELA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHhlhIIETKFEMIKLID------IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSG 606
Cdd:cd08224    83 DAGDLSR---LIKHFKKQKRLIPertiwkYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL----GRFFS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 607 SHQFEQLS--GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY--SNIN 660
Cdd:cd08224   156 SKTTAAHSlvGTPYYMSPERIR---EQGYDFKSDIWSLGCLLYEMAALQSPFygEKMN 210
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
463-712 5.16e-25

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: 105.12  E-value: 5.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK--GKWHGDV-AVKMLNVTaPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLY 538
Cdd:cd06605     9 LGEGNGGVVSKvrHRPSGQImAVKVIRLE-IDEALQKQILRELDVLHKCNSPYIVGFYGaFYSEGDISICMEYMDGGSLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKFEMIkLIDIARQTAQGMDYLHAK-SIIHRDLKSNNIFLHEDLTVKIGDFGLATvksrwsgshqfeQLSGSI 617
Cdd:cd06605    88 KILKEVGRIPERI-LGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSG------------QLVDSL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 618 L--------WMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI-IFMVGRGYL---SPDLSKvrSNC 685
Cdd:cd06605   155 AktfvgtrsYMAPERI---SGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMmIFELLSYIVdepPPLLPS--GKF 229
                         250       260
                  ....*....|....*....|....*..
gi 1237938074 686 PKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd06605   230 SPDFQDFVSQCLQKDPTERPSYKELME 256
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
450-715 5.21e-25

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: 106.25  E-value: 5.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG----------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMG 518
Cdd:cd05101    19 WEFPRDKLTLGKPLGEGCFGQVVMAEAVGidkdkpkeavTVAVKMLKDDA-TEKDLSDLVSEMEMMKMIgKHKNIINLLG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKP-QLAIVTQWCEGSSLYHHLHI-----IETKFEMIK----------LIDIARQTAQGMDYLHAKSIIHRDLKSNNI 582
Cdd:cd05101    98 ACTQDgPLYVIVEYASKGNLREYLRArrppgMEYSYDINRvpeeqmtfkdLVSCTYQLARGMEYLASQKCIHRDLAARNV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 583 FLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNInN 661
Cdd:cd05101   178 LVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALF---DRVYTHQSDVWSFGVLMWEIFTlGGSPYPGI-P 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 662 RDQIIFMVGRGYlspDLSKvRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05101   254 VEELFKLLKEGH---RMDK-PANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD 303
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
461-696 6.56e-25

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: 105.52  E-value: 6.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD-VAVKMLnvtapTPQQLQAFKNEVGV--LRKTRHVNILLFMGYSTKP------QLAIVTQW 531
Cdd:cd14054     1 QLIGQGRYGTVWKGSLDERpVAVKVF-----PARHRQNFQNEKDIyeLPLMEHSNILRFIGADERPtadgrmEYLLVLEY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHiiETKFEMIKLIDIARQTAQGMDYLHAK---------SIIHRDLKSNNIFLHEDLTVKIGDFGLATVKS 602
Cdd:cd14054    76 APKGSLCSYLR--ENTLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLAMVLR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RWSGSHQFEQLS--------GSILWMAPEV----IRMQDKNPYSFQSDVYAFGIVLYELMTG-------------QLPY- 656
Cdd:cd14054   154 GSSLVRGRPGAAenasisevGTLRYMAPEVlegaVNLRDCESALKQVDVYALGLVLWEIAMRcsdlypgesvppyQMPYe 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1237938074 657 ---SNINNRDQIIFMVGRGYLS---PDLSKVRSNCPKAMKRLMAEC 696
Cdd:cd14054   234 aelGNHPTFEDMQLLVSREKARpkfPDAWKENSLAVRSLKETIEDC 279
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
462-713 7.99e-25

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: 104.90  E-value: 7.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYK--GKWHGDV-AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILlfmGYST------KPQLAIVTQWC 532
Cdd:cd14049    13 RLGKGGYGKVYKvrNKLDGQYyAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIV---GYHTawmehvQLMLYIQMQLC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 E-------------------GSSLYHHLHIIETkfemiklIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH-EDLTVKI 592
Cdd:cd14049    90 ElslwdwivernkrpceeefKSAPYTPVDVDVT-------TKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 593 GDFGLA-----------TVKSRWSGSHQFEQLsGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMtgqLPYSNINN 661
Cdd:cd14049   163 GDFGLAcpdilqdgndsTTMSRLNGLTHTSGV-GTCLYAAPEQLEGSH---YDFKSDMYSIGVILLELF---QPFGTEME 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 662 RDQIIFMVGRGYLSPDLSKvrsNCPKAMKRLMAeCLKKKRDERPLFPQILAS 713
Cdd:cd14049   236 RAEVLTQLRNGQIPKSLCK---RWPVQAKYIKL-LTSTEPSERPSASQLLES 283
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
461-667 9.19e-25

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: 104.87  E-value: 9.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKwhgD------VAVKMLnvtaptpqQLQAFKN--------EVGVLRKTRHVNILLFMG-YSTKPQL 525
Cdd:cd07829     5 EKLGEGTYGVVYKAK---DkktgeiVALKKI--------RLDNEEEgipstalrEISLLKELKHPNIVKLLDvIHTENKL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEgSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA---TVKS 602
Cdd:cd07829    74 YLVFEYCD-QDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLArafGIPL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RwsgshqfeQLSGSI--LWM-APEVIrMQDKNpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI--IF 667
Cdd:cd07829   153 R--------TYTHEVvtLWYrAPEIL-LGSKH-YSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLfkIF 212
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
438-711 1.16e-24

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: 104.69  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 438 MKTLGrrDSSDDWEIPDgqitvgqRIGSGSFGTVYK--GKWHGDVA-VKMLNVTAPTPQQLQAfknEVGVLRK-TRHVNI 513
Cdd:cd06639    14 LESLA--DPSDTWDIIE-------TIGKGTYGKVYKvtNKKDGSLAaVKILDPISDVDEEIEA---EYNILRSlPNHPNV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 514 LLFMGYSTKP------QLAIVTQWCEGSS---LYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL 584
Cdd:cd06639    82 VKFYGMFYKAdqyvggQLWLVLELCNGGSvteLVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 585 HEDLTVKIGDFG----LATVKSRWSGShqfeqlSGSILWMAPEVIRMQDKNPYSFQS--DVYAFGIVLYELMTGQLPYSN 658
Cdd:cd06639   162 TTEGGVKLVDFGvsaqLTSARLRRNTS------VGTPFWMAPEVIACEQQYDYSYDArcDVWSLGITAIELADGDPPLFD 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 659 INNRdQIIFMVGRGyLSPDLSKVRSNCpKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd06639   236 MHPV-KALFKIPRN-PPPTLLNPEKWC-RGFSHFISQCLIKDFEKRPSVTHLL 285
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
461-722 1.28e-24

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: 105.10  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGK---WHGDVAVKMLNVTAP-TPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLA-IVTQWCEGS 535
Cdd:cd06634    21 REIGHGSFGAVYFARdvrNNEVVAIKKMSYSGKqSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAwLVMEYCLGS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SlYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwsgshQFEQLSG 615
Cdd:cd06634   101 A-SDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMA------PANSFVG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDLSKvrSNCPKAMKRLMAE 695
Cdd:cd06634   174 TPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNE--SPALQS--GHWSEYFRNFVDS 249
                         250       260
                  ....*....|....*....|....*..
gi 1237938074 696 CLKKKRDERPLfPQILASIELLARSLP 722
Cdd:cd06634   250 CLQKIPQDRPT-SDVLLKHRFLLRERP 275
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
463-704 1.34e-24

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: 104.00  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG----KWHgDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY-----STKPQLAIVTQWCE 533
Cdd:cd14032     9 LGRGSFKTVYKGldteTWV-EVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFwescaKGKRCIVLVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLhiieTKFEMIK---LIDIARQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDL-TVKIGDFGLATVKsRWSGS 607
Cdd:cd14032    88 SGTLKTYL----KRFKVMKpkvLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLK-RASFA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 hqfEQLSGSILWMAPEVIrmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSncpK 687
Cdd:cd14032   163 ---KSVIGTPEFMAPEMY----EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKPASFEKVTD---P 232
                         250
                  ....*....|....*..
gi 1237938074 688 AMKRLMAECLKKKRDER 704
Cdd:cd14032   233 EIKEIIGECICKNKEER 249
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
463-665 1.87e-24

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: 103.58  E-value: 1.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKwhgD------VAVKMLNVTAPTPQQLQAFK-----NEVGVLRK-TRHVNILLFMG-YSTKPQLAIVT 529
Cdd:cd13993     8 IGEGAYGVVYLAV---DlrtgrkYAIKCLYKSGPNSKDGNDFQklpqlREIDLHRRvSRHPNIITLHDvFETEVAIYIVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLH---IIETKFEMIKliDIARQTAQGMDYLHAKSIIHRDLKSNNIFL-HEDLTVKIGDFGLATvKSRWS 605
Cdd:cd13993    85 EYCPNGDLFEAITenrIYVGKTELIK--NVFLQLIDAVKHCHSLGIYHRDIKPENILLsQDEGTVKLCDFGLAT-TEKIS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 606 gshqFEQLSGSILWMAPEVIRMQDKNPYSFQS---DVYAFGIVLYELMTGQLPYSNINNRDQI 665
Cdd:cd13993   162 ----MDFGVGSEFYMAPECFDEVGRSLKGYPCaagDIWSLGIILLNLTFGRNPWKIASESDPI 220
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
453-704 2.34e-24

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: 104.04  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQQLqaFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIV 528
Cdd:cd06655    17 PKKKYTRYEKIGQGASGTVFTAIdvaTGQEVAIKQINLQKQPKKEL--IINEILVMKELKNPNIVNFLdSFLVGDELFVV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL-ATVKSRWSgs 607
Cdd:cd06655    95 MEYLAGGSLTDV--VTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFcAQITPEQS-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 hQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDLSKVRSNCPk 687
Cdd:cd06655   171 -KRSTMVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQNPEKLSP- 243
                         250
                  ....*....|....*..
gi 1237938074 688 AMKRLMAECLKKKRDER 704
Cdd:cd06655   244 IFRDFLNRCLEMDVEKR 260
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
463-710 2.50e-24

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: 102.72  E-value: 2.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG-DVAVKMLNVTAptpqQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQlAIVTQWCEGSSLYHHL 541
Cdd:cd14068     2 LGDGGFGSVYRAVYRGeDVAVKIFNKHT----SFRLLRQELVVLSHLHHPSLVALLAAGTAPR-MLVMELAPKGSLDALL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 542 HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL-----HEDLTVKIGDFGLAtvksRWSGSHQFEQLSGS 616
Cdd:cd14068    77 QQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIA----QYCCRMGIKTSEGT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 617 ILWMAPEVIRmqDKNPYSFQSDVYAFGIVLYELMTG--------QLPysniNNRDQIIFmvgRGYLsPDLSKVRSNCPKA 688
Cdd:cd14068   153 PGFRAPEVAR--GNVIYNQQADVYSFGLLLYDILTCgeriveglKFP----NEFDELAI---QGKL-PDPVKEYGCAPWP 222
                         250       260
                  ....*....|....*....|...
gi 1237938074 689 M-KRLMAECLKKKRDERPLFPQI 710
Cdd:cd14068   223 GvEALIKDCLKENPQCRPTSAQV 245
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
459-713 2.51e-24

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 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. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. 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: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 102.87  E-value: 2.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGK--WHGD-VAVKMLN----VTAPTPQQLqafKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQ 530
Cdd:cd14663     4 LGRTLGEGTFAKVKFARntKTGEsVAIKIIDkeqvAREGMVEQI---KREIAIMKLLRHPNIVeLHEVMATKTKIFFVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHhlhIIETKFEMIKliDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSG 606
Cdd:cd14663    81 LVTGGELFS---KIAKNGRLKE--DKARkyfqQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFRQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRmqdKNPY-SFQSDVYAFGIVLYELMTGQLPY--SNINNRDQIIFmvgrgylspdlsKVRS 683
Cdd:cd14663   156 DGLLHTTCGTPNYVAPEVLA---RRGYdGAKADIWSCGVILFVLLAGYLPFddENLMALYRKIM------------KGEF 220
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1237938074 684 NCP----KAMKRLMAECLKKKRDERPLFPQILAS 713
Cdd:cd14663   221 EYPrwfsPGAKSLIKRILDPNPSTRITVEQIMAS 254
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
443-715 2.53e-24

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: 103.51  E-value: 2.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 443 RRDSSDDWEIpdgqitvgqriGSGSFGTVYKGKWHGD--------VAVKMLNvtAPTPQQLQAFKNEVGVLRKTRHVNIL 514
Cdd:cd05092     4 RRDIVLKWEL-----------GEGAFGKVFLAECHNLlpeqdkmlVAVKALK--EATESARQDFQREAELLTVLQHQHIV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 515 LFMGYSTKPQ-LAIVTQWCEGSSLYHHL-------HIIET-------KFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKS 579
Cdd:cd05092    71 RFYGVCTEGEpLIMVFEYMRHGDLNRFLrshgpdaKILDGgegqapgQLTLGQMLQIASQIASGMVYLASLHFVHRDLAT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 580 NNIFLHEDLTVKIGDFGLatvkSRWSGSHQFEQLSGS----ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQL 654
Cdd:cd05092   151 RNCLVGQGLVVKIGDFGM----SRDIYSTDYYRVGGRtmlpIRWMPPESILYRK---FTTESDIWSFGVVLWEIFTyGKQ 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 655 PYSNINNRDQI-IFMVGRgylspDLSKVRSnCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05092   224 PWYQLSNTEAIeCITQGR-----ELERPRT-CPPEVYAIMQGCWQREPQQRHSIKDIHSRLQ 279
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
463-708 3.36e-24

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: 102.45  E-value: 3.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG----KWHGDVAVKMLN-VTAPTPQQLQAfkNEVGVLRKTRHVNILLFMGYS-TKPQLAIVTQWCEGSS 536
Cdd:cd14120     1 IGHGAFAVVFKGrhrkKPDLPVAIKCITkKNLSKSQNLLG--KEIKILKELSHENVVALLDCQeTSSSVYLVMEYCNGGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIETKFE-MIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFL-HE--------DLTVKIGDFGLAtvksrwsg 606
Cdd:cd14120    79 LADYLQAKGTLSEdTIRVF--LQQIAAAMKALHSKGIVHRDLKPQNILLsHNsgrkpspnDIRLKIADFGFA-------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 shQFEQ-------LSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPdls 679
Cdd:cd14120   149 --RFLQdgmmaatLCGSPMYMAPEVIMSLQ---YDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNANLRP--- 220
                         250       260
                  ....*....|....*....|....*....
gi 1237938074 680 KVRSNCPKAMKRLMAECLKKKRDERPLFP 708
Cdd:cd14120   221 NIPSGTSPALKDLLLGLLKRNPKDRIDFE 249
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
453-704 3.41e-24

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: 103.21  E-value: 3.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQ-ITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ---- 524
Cdd:cd14030    22 PDGRfLKFDIEIGRGSFKTVYKGldtETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVkgkk 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 -LAIVTQWCEGSSLYHHLhiieTKFEMIKLIDI---ARQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDL-TVKIGDFGL 597
Cdd:cd14030   102 cIVLVTELMTSGTLKTYL----KRFKVMKIKVLrswCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 ATVKSrwsgSHQFEQLSGSILWMAPEVIrmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPD 677
Cdd:cd14030   178 ATLKR----ASFAKSVIGTPEFMAPEMY----EEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPAS 249
                         250       260
                  ....*....|....*....|....*..
gi 1237938074 678 LSKVRsnCPKaMKRLMAECLKKKRDER 704
Cdd:cd14030   250 FDKVA--IPE-VKEIIEGCIRQNKDER 273
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
450-715 3.45e-24

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: 104.33  E-value: 3.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG----------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMG 518
Cdd:cd05100     7 WELSRTRLTLGKPLGEGCFGQVVMAEAIGidkdkpnkpvTVAVKMLKDDA-TDKDLSDLVSEMEMMKMIgKHKNIINLLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKP-QLAIVTQWCEGSSLYHHLH---------------IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNI 582
Cdd:cd05100    86 ACTQDgPLYVLVEYASKGNLREYLRarrppgmdysfdtckLPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 583 FLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNInN 661
Cdd:cd05100   166 LVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALF---DRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-P 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 662 RDQIIFMVGRGYlspDLSKvRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05100   242 VEELFKLLKEGH---RMDK-PANCTHELYMIMRECWHAVPSQRPTFKQLVEDLD 291
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
461-666 3.52e-24

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: 102.83  E-value: 3.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTaPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSS 536
Cdd:cd14046    12 QVLGKGAFGQVVKVRNKLDgryYAIKKIKLR-SESKNNSRILREVMLLSRLNHQHVVRYYQaWIERANLYIQMEYCEKST 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLH--IIETKFEMIKLIdiaRQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT------------VKS 602
Cdd:cd14046    91 LRDLIDsgLFQDTDRLWRLF---RQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATsnklnvelatqdINK 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 603 RWSGSHQFEQLS----GSILWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMtgqLPYSNINNRDQII 666
Cdd:cd14046   168 STSAALGSSGDLtgnvGTALYVAPEVQSGTKST-YNEKVDMYSLGIIFFEMC---YPFSTGMERVQIL 231
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
445-717 3.86e-24

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: 105.48  E-value: 3.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 445 DSSddWEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTPQQlQAFKNEVGVLRKT-RHVNILL 515
Cdd:cd05107    29 DSA--WEMPRDNLVLGRTLGSGAFGRVVEATAHGlshsqstmKVAVKMLKSTARSSEK-QALMSELKIMSHLgPHLNIVN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 516 FMGYSTK-PQLAIVTQWCEGSSLYHHLHIIETKF---------------------------------------------- 548
Cdd:cd05107   106 LLGACTKgGPIYIITEYCRYGDLVDYLHRNKHTFlqyyldknrddgslisggstplsqrkshvslgsesdggymdmskde 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 549 --------EM---IKLIDI----------------------------------------ARQTAQGMDYLHAKSIIHRDL 577
Cdd:cd05107   186 sadyvpmqDMkgtVKYADIessnyespydqylpsapertrrdtlinespalsymdlvgfSYQVANGMEFLASKNCVHRDL 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 578 KSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPY 656
Cdd:cd05107   266 AARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIF---NNLYTTLSDVWSFGILLWEIFTlGGTPY 342
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 657 SNINNRDQIIFMVGRGYlspDLSKvRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05107   343 PELPMNEQFYNAIKRGY---RMAK-PAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDL 399
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
453-678 4.08e-24

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: 103.27  E-value: 4.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLqaFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIV 528
Cdd:cd06654    18 PKKKYTRFEKIGQGASGTVYTAmdvATGQEVAIRQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL-ATVKSRWSgs 607
Cdd:cd06654    96 MEYLAGGSLTDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQS-- 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 608 hQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDL 678
Cdd:cd06654   172 -KRSTMVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG--TPEL 236
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
451-723 4.77e-24

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: 103.59  E-value: 4.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVY---KGKWHGDVAVKMLNVTAP-TPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLA 526
Cdd:cd06635    21 EDPEKLFSDLREIGHGSFGAVYfarDVRTSEVVAIKKMSYSGKqSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 -IVTQWCEGSSlYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrws 605
Cdd:cd06635   101 wLVMEYCLGSA-SDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIAS--- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 gshQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDLSKvrSNC 685
Cdd:cd06635   177 ---PANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNE--SPTLQS--NEW 249
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1237938074 686 PKAMKRLMAECLKKKRDERPLFPQILASIELLaRSLPK 723
Cdd:cd06635   250 SDYFRNFVDSCLQKIPQDRPTSEELLKHMFVL-RERPE 286
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
463-663 5.76e-24

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: 101.58  E-value: 5.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG---DVAVKMLNVTAPTPQQLqafKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLy 538
Cdd:cd14006     1 LGRGRFGVVKRCIEKAtgrEFAAKFIPKRDKKKEAV---LREISILNQLQHPRIIqLHEAYESPTELVLILELCSGGEL- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 hhLHIIETKFEMI--KLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE--DLTVKIGDFGLATvksRWSGSHQFEQLS 614
Cdd:cd14006    77 --LDRLAERGSLSeeEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKIIDFGLAR---KLNPGEELKEIF 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1237938074 615 GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRD 663
Cdd:cd14006   152 GTPEFVAPEIVN---GEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQE 197
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
457-722 5.97e-24

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: 102.71  E-value: 5.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKGKWHGD------VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK------PQ 524
Cdd:cd14204     9 LSLGKVLGEGEFGSVMEGELQQPdgtnhkVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEvgsqriPK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 LAIVTQWCEGSSLyhHLHIIETKFEM----------IK-LIDIArqtaQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIG 593
Cdd:cd14204    89 PMVILPFMKYGDL--HSFLLRSRLGSgpqhvplqtlLKfMIDIA----LGMEYLSSRNFLHRDLAARNCMLRDDMTVCVA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 594 DFGLAtvKSRWSGSH--QFEQLSGSILWMAPEviRMQDKnPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFM-V 669
Cdd:cd14204   163 DFGLS--KKIYSGDYyrQGRIAKMPVKWIAVE--SLADR-VYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYDYLlH 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 670 GRGYLSPDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLP 722
Cdd:cd14204   238 GHRLKQPE------DCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLESLP 284
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
463-705 6.49e-24

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: 102.03  E-value: 6.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG---DVAVKMLNVTapTPQQLQAFKNEVGVLRK-TRHVNILLFMG---YSTKPQLA--IVTQWCE 533
Cdd:cd13985     8 LGEGGFSYVYLAHDVNtgrRYALKRMYFN--DEEQLRVAIKEIEIMKRlCGHPNIVQYYDsaiLSSEGRKEvlLLMEYCP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSsLYHhlhIIE----TKFEMIKLIDIARQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDLTVKIGDFGLATVKS----R 603
Cdd:cd13985    86 GS-LVD---ILEksppSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHypleR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQFE---QLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFmvGRgYLSPDlsk 680
Cdd:cd13985   162 AEEVNIIEeeiQKNTTPMYRAPEMIDLYSKKPIGEKADIWALGCLLYKLCFFKLPFDE-SSKLAIVA--GK-YSIPE--- 234
                         250       260
                  ....*....|....*....|....*
gi 1237938074 681 vRSNCPKAMKRLMAECLKKKRDERP 705
Cdd:cd13985   235 -QPRYSPELHDLIRHMLTPDPAERP 258
RBD_CRAF cd17135
Ras-binding domain (RBD) found in RAF proto-oncogene serine/threonine-protein kinase RAF1/CRAF; ...
157-227 6.73e-24

Ras-binding domain (RBD) found in RAF proto-oncogene serine/threonine-protein kinase RAF1/CRAF; RAF1/CRAF, also termed proto-oncogene c-RAF (cRaf), or Raf-1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. RAF1/CRAF is an important effector of Ras-mediated signaling and is a critical regulator of the MAPK/ERK pathway.


Pssm-ID: 340655  Cd Length: 77  Bit Score: 95.69  E-value: 6.73e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 157 VRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKP---IGWDTDISWLTGEELHVEVL 227
Cdd:cd17135     4 IRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKkarLDWNTDAASLIGEELQVDFL 77
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
459-711 7.96e-24

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: 101.48  E-value: 7.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQQL-QAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCE 533
Cdd:cd14186     5 VLNLLGKGSFACVYRARslhTGLEVAIKMIDKKAMQKAGMvQRVRNEVEIHCQLKHPSILeLYNYFEDSNYVYLVLEMCH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQfeQL 613
Cdd:cd14186    85 NGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHF--TM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 SGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSncpkamKRLM 693
Cdd:cd14186   163 CGTPNYISPEIA---TRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREA------QDLI 233
                         250
                  ....*....|....*...
gi 1237938074 694 AECLKKKRDERPLFPQIL 711
Cdd:cd14186   234 HQLLRKNPADRLSLSSVL 251
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
463-721 9.06e-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: 101.57  E-value: 9.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK--GKWHGDVAVkMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG--YSTKpQLAIVTQWCEGSSLY 538
Cdd:cd14221     1 LGKGCFGQAIKvtHRETGEVMV-MKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGvlYKDK-RLNFITEYIKGGTLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA--TVKSRWSGSHQFEQLS-- 614
Cdd:cd14221    79 GIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlMVDEKTQPEGLRSLKKpd 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 --------GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSpdlSKVRSNCP 686
Cdd:cd14221   159 rkkrytvvGNPYWMAPEMI---NGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFGLNVRGFLD---RYCPPNCP 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1237938074 687 KAMKRLMAECLKKKRDERPLFPQILASIELLARSL 721
Cdd:cd14221   233 PSFFPIAVLCCDLDPEKRPSFSKLEHWLETLRMHL 267
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
460-656 1.14e-23

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: 101.16  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVY-------KGKWHGDVAVKMLNVTaptPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLA-IVTQW 531
Cdd:cd14187    12 GRFLGKGGFAKCYeitdadtKEVFAGKIVPKSLLLK---PHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVyVVLEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHhLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvKSRWSGSHQfE 611
Cdd:cd14187    89 CRRRSLLE-LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLAT-KVEYDGERK-K 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1237938074 612 QLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14187   166 TLCGTPNYIAPEVL---SKKGHSFEVDIWSIGCIMYTLLVGKPPF 207
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
462-656 1.15e-23

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: 101.99  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTV--YKGKWHG-DVAVKMLNVTapTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd06659    28 KIGEGSTGVVciAREKHSGrQVAVKMMDLR--KQQRRELLFNEVVIMRDYQHPNVVeMYKSYLVGEELWVLMEYLQGGAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwsGSHQFEQLSGSI 617
Cdd:cd06659   106 TDI--VSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISK--DVPKRKSLVGTP 181
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1237938074 618 LWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd06659   182 YWMAPEVI---SRCPYGTEVDIWSLGIMVIEMVDGEPPY 217
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
462-712 1.17e-23

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: 100.77  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKWHGD---VAVKMlnVTAPTPQQLQAFKnEVGVLRK----TRHVNI---LLFMGYSTKPQLAIVTQW 531
Cdd:cd05118     6 KIGEGAFGTVWLARDKVTgekVAIKK--IKNDFRHPKAALR-EIKLLKHlndvEGHPNIvklLDVFEHRGGNHLCLVFEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CeGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL-TVKIGDFGLAtvksRWSGSHQF 610
Cdd:cd05118    83 M-GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADFGLA----RSFTSPPY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 EQLSGSILWMAPEVIrMQDKnPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRgyLSPDLskvrsncpkaMK 690
Cdd:cd05118   158 TPYVATRWYRAPEVL-LGAK-PYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRL--LGTPE----------AL 223
                         250       260
                  ....*....|....*....|..
gi 1237938074 691 RLMAECLKKKRDERPLFPQILA 712
Cdd:cd05118   224 DLLSKMLKYDPAKRITASQALA 245
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
463-666 1.28e-23

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: 100.79  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKwHGDV----AVKMLN-VTAPTPQQLQAFKNEVGVLRKTRH---VNilLFMGYSTKPQLAIVTQWCEG 534
Cdd:cd05578     8 IGKGSFGKVCIVQ-KKDTkkmfAMKYMNkQKCIEKDSVRNVLNELEILQELEHpflVN--LWYSFQDEEDMYMVVDLLLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLhIIETKF--EMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSHQFEQ 612
Cdd:cd05578    85 GDLRYHL-QQKVKFseETVKFY--ICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATK---LTDGTLATS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 613 LSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINN--RDQII 666
Cdd:cd05578   159 TSGTKPYMAPEVFMRAG---YSFAVDWWSLGVTAYEMLRGKRPYEIHSRtsIEEIR 211
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
451-710 1.74e-23

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: 101.59  E-value: 1.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKGKWHG-----------------DVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNI 513
Cdd:cd05097     1 EFPRQQLRLKEKLGEGQFGEVHLCEAEGlaeflgegapefdgqpvLVAVKMLRADV-TKTARNDFLKEIKIMSRLKNPNI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 514 LLFMGYSTKPQ-LAIVTQWCEGSSLYHHL--HIIETKF---------EMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNN 581
Cdd:cd05097    80 IRLLGVCVSDDpLCMITEYMENGDLNQFLsqREIESTFthannipsvSIANLLYMAVQIASGMKYLASLNFVHRDLATRN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 582 IFLHEDLTVKIGDFGLatvkSRWSGSHQFEQLSGS----ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT--GQLP 655
Cdd:cd05097   160 CLVGNHYTIKIADFGM----SRNLYSGDYYRIQGRavlpIRWMAWESILL---GKFTTASDVWAFGVTLWEMFTlcKEQP 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 656 YSNINNrDQII-----FMVGRG---YLS-PDLskvrsnCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05097   233 YSLLSD-EQVIentgeFFRNQGrqiYLSqTPL------CPSPVFKLMMRCWSRDIKDRPTFNKI 289
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
450-711 2.03e-23

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: 101.98  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMGYS 520
Cdd:cd05102     2 WEFPRDRLRLGKVLGHGAFGKVVEASAFGidksssceTVAVKMLKEGA-TASEHKALMSELKILIHIgNHLNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 521 TKPQ--LAIVTQWCEGSSLYHHLH----------------------IIE------------------------------- 545
Cdd:cd05102    81 TKPNgpLMVIVEFCKYGNLSNFLRakregfspyrersprtrsqvrsMVEavradrrsrqgsdrvasftestsstnqprqe 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 546 ------TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGS--I 617
Cdd:cd05102   161 vddlwqSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLA--RDIYKDPDYVRKGSARlpL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 618 LWMAPEVIRmqDKnPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQII--FMVGRGYLSPDLSKvrsncpKAMKRLMA 694
Cdd:cd05102   239 KWMAPESIF--DK-VYTTQSDVWSFGVLLWEIFSlGASPYPGVQINEEFCqrLKDGTRMRAPEYAT------PEIYRIML 309
                         330
                  ....*....|....*..
gi 1237938074 695 ECLKKKRDERPLFPQIL 711
Cdd:cd05102   310 SCWHGDPKERPTFSDLV 326
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
463-704 2.09e-23

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: 100.57  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG----KWHgDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-----YSTKPQLAIVTQWCE 533
Cdd:cd14031    18 LGRGAFKTVYKGldteTWV-EVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDswesvLKGKKCIVLVTELMT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLhiieTKFEMIK---LIDIARQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDL-TVKIGDFGLATV-KSRWSG 606
Cdd:cd14031    97 SGTLKTYL----KRFKVMKpkvLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLmRTSFAK 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 ShqfeqLSGSILWMAPEVIrmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSncp 686
Cdd:cd14031   173 S-----VIGTPEFMAPEMY----EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTD--- 240
                         250
                  ....*....|....*...
gi 1237938074 687 KAMKRLMAECLKKKRDER 704
Cdd:cd14031   241 PEVKEIIEGCIRQNKSER 258
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
456-710 2.33e-23

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: 101.04  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWH---GDVAVKMlnvtapTPQQLQaFKN-EVGVLRKTRHVNI--LLFMGYST-----KPQ 524
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAKLLetgEVVAIKK------VLQDKR-YKNrELQIMRRLKHPNIvkLKYFFYSSgekkdEVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 LAIVTQwCEGSSLY---HHLHIIETKFEM--IKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFL-HEDLTVKIGDFGLA 598
Cdd:cd14137    78 LNLVME-YMPETLYrviRHYSKNKQTIPIiyVKLY--SYQLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDFGSA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 T--VKSRWSGSHQfeqlsGSILWMAPEVI-RMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ---IIFMVGrg 672
Cdd:cd14137   155 KrlVPGEPNVSYI-----CSRYYRAPELIfGATD---YTTAIDIWSAGCVLAELLLGQPLFPGESSVDQlveIIKVLG-- 224
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1237938074 673 ylSPDLSKVRSNCPKAMKrlmaeclkkkrderPLFPQI 710
Cdd:cd14137   225 --TPTREQIKAMNPNYTE--------------FKFPQI 246
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
450-715 3.84e-23

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: 101.90  E-value: 3.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTPQQlQAFKNEVGVLRKT-RHVNILLFMGYS 520
Cdd:cd05104    30 WEFPRDRLRFGKTLGAGAFGKVVEATAYGlakadsamTVAVKMLKPSAHSTER-EALMSELKVLSYLgNHINIVNLLGAC 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 521 T--KPQLAIVTQWCEG-----------------------SSLYHHL----------------------HIIETK------ 547
Cdd:cd05104   109 TvgGPTLVITEYCCYGdllnflrrkrdsficpkfedlaeAALYRNLlhqremacdslneymdmkpsvsYVVPTKadkrrg 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 548 ------------FEMIK----------LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA---TVKS 602
Cdd:cd05104   189 vrsgsyvdqdvtSEILEedelaldtedLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLArdiRNDS 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RW--SGSHQFeqlsgSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGY--LSPD 677
Cdd:cd05104   269 NYvvKGNARL-----PVKWMAPESIF---ECVYTFESDVWSYGILLWEIFSlGSSPYPGMPVDSKFYKMIKEGYrmDSPE 340
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1237938074 678 LSkvrsncPKAMKRLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd05104   341 FA------PSEMYDIMRSCWDADPLKRPTFKQIVQLIE 372
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
463-720 4.01e-23

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: 99.27  E-value: 4.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG-----KWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd05116     3 LGSGNFGTVKKGyyqmkKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAESWMLVMEMAELGPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHL----HIIETKfemikLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQfEQL 613
Cdd:cd05116    83 NKFLqknrHVTEKN-----ITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYK-AQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 SGS--ILWMAPEVIrmqdkNPYSF--QSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFM-VGRGYLSPdlskvrSNCPK 687
Cdd:cd05116   157 HGKwpVKWYAPECM-----NYYKFssKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIeKGERMECP------AGCPP 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1237938074 688 AMKRLMAECLKKKRDERPLFpqilASIELLARS 720
Cdd:cd05116   226 EMYDLMKLCWTYDVDERPGF----AAVELRLRN 254
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
453-711 4.82e-23

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: 99.74  E-value: 4.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIV 528
Cdd:cd06640     2 PEELFTKLERIGKGSFGEVFKGidnRTQQVVAIKIIDLEE-AEDEIEDIQQEITVLSQCDSPYVTKYYGsYLKGTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHiiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSH 608
Cdd:cd06640    81 MEYLGGGSALDLLR--AGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLT--DTQI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRgYLSPDLSkvrSNCPKA 688
Cdd:cd06640   157 KRNTFVGTPFWMAPEVIQ---QSAYDSKADIWSLGITAIELAKGEPPNSDMHPM-RVLFLIPK-NNPPTLV---GDFSKP 228
                         250       260
                  ....*....|....*....|...
gi 1237938074 689 MKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd06640   229 FKEFIDACLNKDPSFRPTAKELL 251
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
463-663 5.86e-23

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK 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: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 98.75  E-value: 5.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKwH----GDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd14072     8 IGKGNFAKVKLAR-HvltgREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVkLFEVIETEKTLYLVMEYASGGEV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHL--H-IIETKFEMIKLidiaRQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvkSRWSGSHQFEQLS 614
Cdd:cd14072    87 FDYLvaHgRMKEKEARAKF----RQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFS---NEFTPGNKLDTFC 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1237938074 615 GSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRD 663
Cdd:cd14072   160 GSPPYAAPEL--FQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKE 206
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
461-696 6.02e-23

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: 99.73  E-value: 6.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD-VAVKMLNvtapTPQQLQAFK-NEVGVLRKTRHVNILLFM-----GYSTKPQLAIVTQWCE 533
Cdd:cd14220     1 RQIGKGRYGEVWMGKWRGEkVAVKVFF----TTEEASWFReTEIYQTVLMRHENILGFIaadikGTGSWTQLYLITDYHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIieTKFEMIKLIDIARQTAQGMDYLHAK--------SIIHRDLKSNNIFLHEDLTVKIGDFGLAtVKSRwS 605
Cdd:cd14220    77 NGSLYDFLKC--TTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLA-VKFN-S 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 GSHQFE----QLSGSILWMAPEVIRmQDKNPYSFQ----SDVYAFGIVLYEL----MTG------QLPYSNINNRD---- 663
Cdd:cd14220   153 DTNEVDvplnTRVGTKRYMAPEVLD-ESLNKNHFQayimADIYSFGLIIWEMarrcVTGgiveeyQLPYYDMVPSDpsye 231
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1237938074 664 ---QIIFMVGrgyLSPDLSKvRSN---CPKAMKRLMAEC 696
Cdd:cd14220   232 dmrEVVCVKR---LRPTVSN-RWNsdeCLRAVLKLMSEC 266
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
460-712 6.90e-23

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: 98.85  E-value: 6.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYK------GKWHgdvAVKML-NVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY-STKPQLAIVTQW 531
Cdd:cd14189     6 GRLLGKGGFARCYEmtdlatNKTY---AVKVIpHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHfEDAENIYIFLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHIIETKFEMiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvkSRWSGSHQFE 611
Cdd:cd14189    83 CSRKSLAHIWKARHTLLEP-EVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLA---ARLEPPEQRK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 612 Q-LSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPdlskvrSNCPKAMK 690
Cdd:cd14189   159 KtICGTPNYLAPEVLLRQGHGP---ESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLP------ASLSLPAR 229
                         250       260
                  ....*....|....*....|..
gi 1237938074 691 RLMAECLKKKRDERPLFPQILA 712
Cdd:cd14189   230 HLLAGILKRNPGDRLTLDQILE 251
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
463-707 9.09e-23

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: 98.86  E-value: 9.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG-----KWHGDVAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd05115    12 LGSGNFGCVKKGvykmrKKQIDVAIKVLKQGNEKAVRDEMMR-EAQIMHQLDNPYIVRMIGVCEAEALMLVMEMASGGPL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGS- 616
Cdd:cd05115    91 NKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLS--KALGADDSYYKARSAGk 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 617 --ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGYLSpdlskVRSNCPKAMKRLM 693
Cdd:cd05115   169 wpLKWYAPECINFRK---FSSRSDVWSYGVTMWEAFSyGQKPYKKMKGPEVMSFIEQGKRMD-----CPAECPPEMYALM 240
                         250
                  ....*....|....
gi 1237938074 694 AECLKKKRDERPLF 707
Cdd:cd05115   241 SDCWIYKWEDRPNF 254
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
463-695 9.55e-23

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: 98.45  E-value: 9.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQA-FKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd05572     1 LGVGGFGRVELVQLKSKgrtFALKCVKKRHIVQTRQQEhIFSEKEILEECNSPFIVkLYRTFKDKKYLYMLMEYCLGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHiietkfeMIKLIDiaRQTAQ--------GMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQ 609
Cdd:cd05572    81 WTILR-------DRGLFD--EYTARfytacvvlAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKTWT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 610 FeqlSGSILWMAPEVIrmQDKNpYSFQSDVYAFGIVLYELMTGQLPYSNINNRD-----QIIFMVGRgYLSPdlSKVRSN 684
Cdd:cd05572   152 F---CGTPEYVAPEII--LNKG-YDFSVDYWSLGILLYELLTGRPPFGGDDEDPmkiynIILKGIDK-IEFP--KYIDKN 222
                         250
                  ....*....|.
gi 1237938074 685 CPKAMKRLMAE 695
Cdd:cd05572   223 AKNLIKQLLRR 233
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
463-712 1.01e-22

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: 98.98  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKgKWHGD----VAVKMLNVTAPTPQQLQaFKNEVGVLRKTRH-VNILLFMGystkpqlAIVTqwcEG--- 534
Cdd:cd06616    14 IGRGAFGTVNK-MLHKPsgtiMAVKRIRSTVDEKEQKR-LLMDLDVVMRSSDcPYIVKFYG-------ALFR---EGdcw 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 ----------SSLYHHLHIIETKF--EMIkLIDIARQTAQGMDYLHAK-SIIHRDLKSNNIFLHEDLTVKIGDFGLatvk 601
Cdd:cd06616    82 icmelmdislDKFYKYVYEVLDSVipEEI-LGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGI---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 602 srwSGshqfeQLSGSIL---------WMAPEVIR-MQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGR 671
Cdd:cd06616   157 ---SG-----QLVDSIAktrdagcrpYMAPERIDpSASRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLTQVVK 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 672 G---YLSPDLSKVRSNCpkaMKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd06616   229 GdppILSNSEEREFSPS---FVNFVNLCLIKDESKRPKYKELLK 269
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
458-710 1.11e-22

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: 98.01  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLQAF-KNEVGVLRKTRHVNILLFMGY--STKPQLAIVTQW 531
Cdd:cd14164     3 TLGTTIGEGSFSKVKLAtsqKYCCKVAIKIVDRRRASPDFVQKFlPRELSILRRVNHPNIVQMFECieVANGRLYIVMEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSL--YHHLHIIETKFEMikliDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH-EDLTVKIGDFGLATVKSRWSG-S 607
Cdd:cd14164    83 AATDLLqkIQEVHHIPKDLAR----DMFAQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVEDYPElS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFeqlSGSILWMAPEVIRMQDKNPYSFqsDVYAFGIVLYELMTGQLPYSNINNRdqIIFMVGRGYLSPDLSKVRSNCpk 687
Cdd:cd14164   159 TTF---CGSRAYTPPEVILGTPYDPKKY--DVWSLGVVLYVMVTGTMPFDETNVR--RLRLQQRGVLYPSGVALEEPC-- 229
                         250       260
                  ....*....|....*....|...
gi 1237938074 688 amKRLMAECLKKKRDERPLFPQI 710
Cdd:cd14164   230 --RALIRTLLQFNPSTRPSIQQV 250
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
458-653 1.13e-22

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: 98.76  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKnEVGVLRK-TRHVNIL-LFMGYSTKPQLAIVTQWC 532
Cdd:cd07830     2 KVIKQLGDGTFGSVYLARNKETgelVAIKKMKKKFYSWEECMNLR-EVKSLRKlNEHPNIVkLKEVFRENDELYFVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSsLYHhlhIIET----KFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA---------T 599
Cdd:cd07830    81 EGN-LYQ---LMKDrkgkPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAreirsrppyT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 600 --VKSRWsgshqfeqlsgsilWMAPEVIrMQDKNpYSFQSDVYAFGIVLYELMTGQ 653
Cdd:cd07830   157 dyVSTRW--------------YRAPEIL-LRSTS-YSSPVDIWALGCIMAELYTLR 196
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
463-663 1.31e-22

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: 98.06  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY--KGKWHGDV-AVKMLNvtaptPQQLQaFKNEVGVLRKTRhvNILLF--------MGYS--TKPQLAIVT 529
Cdd:cd05579     1 ISRGAYGRVYlaKKKSTGDLyAIKVIK-----KRDMI-RKNQVDSVLAER--NILSQaqnpfvvkLYYSfqGKKNLYLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIIETKFEmikliDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV----- 600
Cdd:cd05579    73 EYLPGGDLYSLLENVGALDE-----DVARiyiaEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVglvrr 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 601 --------KSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLP---------YSNINNRD 663
Cdd:cd05579   148 qiklsiqkKSNGAPEKEDRRIVGTPDYLAPEILL---GQGHGKTVDWWSLGVILYEFLVGIPPfhaetpeeiFQNILNGK 224
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
463-721 1.42e-22

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: 97.59  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMGYSTKP-QLAIVTQWCEGSSLYHHL 541
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKIVR-EISLLQKLSHPNIVRYLGICVKDeKLHPILEYVSGGCLEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 542 HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVK---IGDFGLATVKSRWSGSHQFEQLS--GS 616
Cdd:cd14156    80 AREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVGEMPANDPERKLSlvGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 617 ILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMtGQLPYSninnrDQIIFMVGRGYLSPDLSKVRSN-CPKAMKRLMAE 695
Cdd:cd14156   160 AFWMAPEMLRGE---PYDRKVDVFSFGIVLCEIL-ARIPAD-----PEVLPRTGDFGLDVQAFKEMVPgCPEPFLDLAAS 230
                         250       260
                  ....*....|....*....|....*.
gi 1237938074 696 CLKKKRDERPLFPQILASIELLARSL 721
Cdd:cd14156   231 CCRMDAFKRPSFAELLDELEDIAETL 256
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
463-656 1.70e-22

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: 97.41  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVyKGKWHG----DVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd14075    10 LGSGNFSQV-KLGIHQltkeKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIrLYEVVETLSKLHLVMEYASGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFeqlSGSI 617
Cdd:cd14075    89 YTKIST-EGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNTF---CGSP 164
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1237938074 618 LWMAPEVIRmqDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14075   165 PYAAPELFK--DEHYIGIYVDIWALGVLLYFMVTGVMPF 201
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
481-698 2.28e-22

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: 97.42  E-value: 2.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 481 AVKMLNVTAPTPQQ------LQAFKNEVGVLRK-TRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLYHHLHII------ET 546
Cdd:cd14093    32 AVKIIDITGEKSSEneaeelREATRREIEILRQvSGHPNIIeLHDVFESPTFIFLVFELCRKGELFDYLTEVvtlsekKT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 547 KFEMiklidiaRQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwsgSHQFEQLSGSILWMAPEVIR 626
Cdd:cd14093   112 RRIM-------RQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDE---GEKLRELCGTPGYLAPEVLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 627 --MQDKNP-YSFQSDVYAFGIVLYELMTGQLPYSninNRDQIIF----MVGR-GYLSPDLSKVrSNCPKAM--------- 689
Cdd:cd14093   182 csMYDNAPgYGKEVDMWACGVIMYTLLAGCPPFW---HRKQMVMlrniMEGKyEFGSPEWDDI-SDTAKDLiskllvvdp 257
                         250
                  ....*....|.
gi 1237938074 690 -KRLMA-ECLK 698
Cdd:cd14093   258 kKRLTAeEALE 268
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
450-711 4.52e-22

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: 98.13  E-value: 4.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMGYS 520
Cdd:cd05103     2 WEFPRDRLKLGKPLGRGAFGQVIEADAFGidktatcrTVAVKMLKEGA-THSEHRALMSELKILIHIgHHLNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 521 TKP--QLAIVTQWCEGSSLYHHLHIIETKFEMIK---------------------------------------------- 552
Cdd:cd05103    81 TKPggPLMVIVEFCKFGNLSAYLRSKRSEFVPYKtkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveekslsd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 553 --------------------LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQ 612
Cdd:cd05103   161 veeeeagqedlykdfltledLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGSILWMAPEVIRmqDKnPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRG--YLSPDLSKVRsncpkaM 689
Cdd:cd05103   241 ARLPLKWMAPETIF--DR-VYTIQSDVWSFGVLLWEIFSlGASPYPGVKIDEEFCRRLKEGtrMRAPDYTTPE------M 311
                         330       340
                  ....*....|....*....|..
gi 1237938074 690 KRLMAECLKKKRDERPLFPQIL 711
Cdd:cd05103   312 YQTMLDCWHGEPSQRPTFSELV 333
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
463-657 5.32e-22

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: 96.75  E-value: 5.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNV-TAPTPQQLQAFKNEVGVLRKTRHVNILLFMgySTKPQLAIVT--------- 529
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTgeyVAIKKCRQeLSPSDKNRERWCLEVQIMKKLNHPNVVSAR--DVPPELEKLSpndlpllam 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIIETKFEM--IKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE---DLTVKIGDFGLATVKSRW 604
Cdd:cd13989    79 EYCSGGDLRKVLNQPENCCGLkeSEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQgggRVIYKLIDLGYAKELDQG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 605 SGSHQFeqlSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd13989   159 SLCTSF---VGTLQYLAPELFESK---KYTCTVDYWSFGTLAFECITGYRPFL 205
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
463-702 6.50e-22

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: 96.23  E-value: 6.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGK------WhgDVAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGS 535
Cdd:cd14201    14 VGHGAFAVVFKGRhrkktdW--EVAIKSINKKNLSKSQILLGK-EIKILKELQHENIVALYDVQEMPNsVFLVMEYCNGG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIKLIdIARQTAQGMDYLHAKSIIHRDLKSNNIFLH---------EDLTVKIGDFGLAtvksRWSG 606
Cdd:cd14201    91 DLADYLQAKGTLSEDTIRV-FLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFA----RYLQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQF-EQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSkvRSNC 685
Cdd:cd14201   166 SNMMaATLCGSPMYMAPEVIMSQH---YDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIP--RETS 240
                         250
                  ....*....|....*..
gi 1237938074 686 PKAMKRLMAECLKKKRD 702
Cdd:cd14201   241 PYLADLLLGLLQRNQKD 257
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
492-711 9.49e-22

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: 95.46  E-value: 9.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 492 PQQLQAFKNEVGVLRKTRHVNILLFMGY-STKPQLAIVTQWCEGSSLYHHLHI--IETKFEMIKLIdiaRQTAQGMDYLH 568
Cdd:cd14188    42 PHQREKIDKEIELHRILHHKHVVQFYHYfEDKENIYILLEYCSRRSMAHILKArkVLTEPEVRYYL---RQIVSGLKYLH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 569 AKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYE 648
Cdd:cd14188   119 EQEILHRDLKLGNFFINENMELKVGDFGLAARLE--PLEHRRRTICGTPNYLSPEVL---NKQGHGCESDIWALGCVMYT 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 649 LMTGQLPYSNINNRDQIIFMVGRGYLSPdlskvrSNCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd14188   194 MLLGRPPFETTNLKETYRCIREARYSLP------SSLLAPAKHLIASMLSKNPEDRPSLDEII 250
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
445-711 1.55e-21

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation 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: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 95.46  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 445 DSSDDWEIPdgqitvgQRIGSGSFGTVYK--GKWHGD-VAVKMLNVTAPTPQQLQAFKNEVGVLrkTRHVNILLFMGYST 521
Cdd:cd06638    15 DPSDTWEII-------ETIGKGTYGKVFKvlNKKNGSkAAVKILDPIHDIDEEIEAEYNILKAL--SDHPNVVKFYGMYY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 522 KP------QLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIA---RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKI 592
Cdd:cd06638    86 KKdvkngdQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAyilHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 593 GDFGLATVKSrwSGSHQFEQLSGSILWMAPEVI--RMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVG 670
Cdd:cd06638   166 VDFGVSAQLT--STRLRRNTSVGTPFWMAPEVIacEQQLDSTYDARCDVWSLGITAIELGDGDPPLADLHPM-RALFKIP 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1237938074 671 RG----YLSPDLSKVRSNcpkamkRLMAECLKKKRDERPLFPQIL 711
Cdd:cd06638   243 RNppptLHQPELWSNEFN------DFIRKCLTKDYEKRPTVSDLL 281
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
451-710 1.56e-21

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: 95.83  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVYKGKWHGD-------------------VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHV 511
Cdd:cd05095     1 EFPRKLLTFKEKLGEGQFGEVHLCEAEGMekfmdkdfalevsenqpvlVAVKMLRADA-NKNARNDFLKEIKIMSRLKDP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 512 NILLFMGYS-TKPQLAIVTQWCEGSSLYHHL--HIIETKFEMI---------KLIDIARQTAQGMDYLHAKSIIHRDLKS 579
Cdd:cd05095    80 NIIRLLAVCiTDDPLCMITEYMENGDLNQFLsrQQPEGQLALPsnaltvsysDLRFMAAQIASGMKYLSSLNFVHRDLAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 580 NNIFLHEDLTVKIGDFGLAtvKSRWSGShqFEQLSGS----ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT--GQ 653
Cdd:cd05095   160 RNCLVGKNYTIKIADFGMS--RNLYSGD--YYRIQGRavlpIRWMSWESILL---GKFTTASDVWAFGVTLWETLTfcRE 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 654 LPYSNINNrDQII-----FMVGRG---YL-SPDLskvrsnCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05095   233 QPYSQLSD-EQVIentgeFFRDQGrqtYLpQPAL------CPDSVYKLMLSCWRRDTKDRPSFQEI 291
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
461-657 1.83e-21

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: 94.28  E-value: 1.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD----VAVKM-----LNVTApTPQQLQafknEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQ 530
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGarevVAVKCvskssLNKAS-TENLLT----EIELLKKLKHPHIVELKDFQWDEEhIYLIME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIIETKFEMIKLIdIARQTAQGMDYLHAKSIIHRDLKSNNIFL--HEDLTVKIGDFGLATVKSRWSGSH 608
Cdd:cd14121    76 YCSGGDLSRFIRSRRTLPESTVRR-FLQQLASALQFLREHNISHMDLKPQNLLLssRYNPVLKLADFGFAQHLKPNDEAH 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1237938074 609 qfeQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd14121   155 ---SLRGSPLYMAPEMILKKK---YDARVDLWSVGVILYECLFGRAPFA 197
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
458-666 2.22e-21

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: 94.77  E-value: 2.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTV---YKGKWHGDVAVKMLN---VTAPTPQQLQA---FKNEVGVLRKTRHVNILLFMGYSTKPQ-LAI 527
Cdd:cd14084     9 IMSRTLGSGACGEVklaYDKSTCKKVAIKIINkrkFTIGSRREINKprnIETEIEILKKLSHPCIIKIEDFFDAEDdYYI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCEGSSLYH------HLHIIETKFemiklidIARQTAQGMDYLHAKSIIHRDLKSNNIFL--HEDLT-VKIGDFGLa 598
Cdd:cd14084    89 VLELMEGGELFDrvvsnkRLKEAICKL-------YFYQMLLAVKYLHSNGIIHRDLKPENVLLssQEEEClIKITDFGL- 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 599 tvkSRWSGSHQF-EQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLP----YSNINNRDQII 666
Cdd:cd14084   161 ---SKILGETSLmKTLCGTPTYLAPEVLRSFGTEGYTRAVDCWSLGVILFICLSGYPPfseeYTQMSLKEQIL 230
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
451-710 2.64e-21

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: 95.39  E-value: 2.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQRIGSGSFGTVY--------------------KGKwHGDVAVKMLNVTApTPQQLQAFKNEVGVLRKTRH 510
Cdd:cd05096     1 KFPRGHLLFKEKLGEGQFGEVHlcevvnpqdlptlqfpfnvrKGR-PLLVAVKILRPDA-NKNARNDFLKEVKILSRLKD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 511 VNILLFMG--YSTKPqLAIVTQWCEGSSLYHHL--HIIETKFE----------------MIKLIDIARQTAQGMDYLHAK 570
Cdd:cd05096    79 PNIIRLLGvcVDEDP-LCMITEYMENGDLNQFLssHHLDDKEEngndavppahclpaisYSSLLHVALQIASGMKYLSSL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 571 SIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSG--SILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYE 648
Cdd:cd05096   158 NFVHRDLATRNCLVGENLTIKIADFGMS--RNLYAGDYYRIQGRAvlPIRWMAWECILM---GKFTTASDVWAFGVTLWE 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 649 LMT--GQLPYSNINNrDQIIFMVGRGYLSPDLSKVRSN---CPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd05096   233 ILMlcKEQPYGELTD-EQVIENAGEFFRDQGRQVYLFRpppCPQGLYELMLQCWSRDCRERPSFSDI 298
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
459-712 2.75e-21

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: 94.32  E-value: 2.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVY------KGKwhgDVAVKMLNV---TAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ---LA 526
Cdd:cd06653     6 LGKLLGRGAFGEVYlcydadTGR---ELAVKQVPFdpdSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEekkLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLHIIETKFEMIKLiDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKSRWS 605
Cdd:cd06653    83 IFVEYMPGGSVKDQLKAYGALTENVTR-RYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrIQTICM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 GSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYLSPDLSK-VRSN 684
Cdd:cd06653   162 SGTGIKSVTGTPYWMSPEVISGEG---YGRKADVWSVACTVVEMLTEKPPWAEYEAM-AAIFKIATQPTKPQLPDgVSDA 237
                         250       260
                  ....*....|....*....|....*...
gi 1237938074 685 CPKAMKRLMAEclkKKRdeRPLFPQILA 712
Cdd:cd06653   238 CRDFLRQIFVE---EKR--RPTAEFLLR 260
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
463-656 3.46e-21

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: 93.44  E-value: 3.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK------GKwhgDVAVKMlnVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd14103     1 LGRGKFGTVYRcvekatGK---ELAAKF--IKCRKAKDREDVRNEIEIMNQLRHPRLLqLYDAFETPREMVLVMEYVAGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHlhIIETKFEMIKL--IDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHeDLT---VKIGDFGLAtvkSRWSGSHQF 610
Cdd:cd14103    76 ELFER--VVDDDFELTERdcILFMRQICEGVQYMHKQGILHLDLKPENILCV-SRTgnqIKIIDFGLA---RKYDPDKKL 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1237938074 611 EQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14103   150 KVLFGTPEFVAPEVVNYE---PISYATDMWSVGVICYVLLSGLSPF 192
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
460-713 4.90e-21

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: 93.63  E-value: 4.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRI--GSGSFGTVYKGKwhgD------VAVKmlNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQ 530
Cdd:cd06624    11 GERVvlGKGTFGVVYAAR---DlstqvrIAIK--EIPERDSREVQPLHEEIALHSRLSHKNIVQYLGsVSEDGFFKIFME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHhlhIIETKFEMIK-----LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE-DLTVKIGDFGlaTVKsRW 604
Cdd:cd06624    86 QVPGGSLSA---LLRSKWGPLKdnentIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFG--TSK-RL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SG-SHQFEQLSGSILWMAPEVIrmqDKNP--YSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKV 681
Cdd:cd06624   160 AGiNPCTETFTGTLQYMAPEVI---DKGQrgYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFKVGMFKIHPEIPES 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1237938074 682 RSncpKAMKRLMAECLKKKRDERPLFPQILAS 713
Cdd:cd06624   237 LS---EEAKSFILRCFEPDPDKRATASDLLQD 265
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
463-712 6.32e-21

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: 93.11  E-value: 6.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFG-TVYKGKWHGDVAVKMLNVTAP-TPQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQWCEGSSLYH 539
Cdd:cd08219     8 VGEGSFGrALLVQHVNSDQKYAMKEIRLPkSSSAVEDSRKEAVLLAKMKHPNIVAFKeSFEADGHLYIVMEYCDGGDLMQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 540 HLHIIETK-FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwSGSHQFEQLsGSIL 618
Cdd:cd08219    88 KIKLQRGKlFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTS-PGAYACTYV-GTPY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 619 WMAPEVirmQDKNPYSFQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGRGYLSPdlskVRSNCPKAMKRLMAECLK 698
Cdd:cd08219   166 YVPPEI---WENMPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGSYKP----LPSHYSYELRSLIKQMFK 237
                         250
                  ....*....|....
gi 1237938074 699 KKRDERPLFPQILA 712
Cdd:cd08219   238 RNPRSRPSATTILS 251
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
463-704 7.86e-21

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: 94.30  E-value: 7.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY------KGKWHgdvAVKMLNvtaptpQQLQAFKNEVG-------VLRKTRHVNIL-LFMGYSTKPQLAIV 528
Cdd:cd05595     3 LGKGTFGKVIlvrekaTGRYY---AMKILR------KEVIIAKDEVAhtvtesrVLQNTRHPFLTaLKYAFQTHDRLCFV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLhiietKFEMIKLIDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRW 604
Cdd:cd05595    74 MEYANGGELFFHL-----SRERVFTEDRARfygaEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLC--KEGI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRD--QIIFMvgrgylsPDLSKVR 682
Cdd:cd05595   147 TDGATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERlfELILM-------EEIRFPR 216
                         250       260
                  ....*....|....*....|..
gi 1237938074 683 SNCPKAmKRLMAECLKKKRDER 704
Cdd:cd05595   217 TLSPEA-KSLLAGLLKKDPKQR 237
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
459-657 9.30e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 96.79  E-value: 9.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGK---WHGDVAVKMLNvtaptpQQLQA-------FKNE---VGVLRktrH---VNIllfmgYST- 521
Cdd:NF033483   11 IGERIGRGGMAEVYLAKdtrLDRDVAVKVLR------PDLARdpefvarFRREaqsAASLS---HpniVSV-----YDVg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 522 --KPQLAIVTQWCEGSSL------YHHLHIIETkfemiklIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIG 593
Cdd:NF033483   77 edGGIPYIVMEYVDGRTLkdyireHGPLSPEEA-------VEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVT 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 594 DFGLAtvksRWSGSHQFEQlSGSIL----WMAPEVIR--MQDKnpysfQSDVYAFGIVLYELMTGQLPYS 657
Cdd:NF033483  150 DFGIA----RALSSTTMTQ-TNSVLgtvhYLSPEQARggTVDA-----RSDIYSLGIVLYEMLTGRPPFD 209
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
463-669 1.20e-20

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: 92.33  E-value: 1.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK--GKWHG-DVAVKMLNVTAPtpQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLY 538
Cdd:cd14192    12 LGGGRFGQVHKctELSTGlTLAAKIIKVKGA--KEREEVKNEINIMNQLNHVNLIqLYDAFESKTNLTLIMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHlhIIETKFEMIKL--IDIARQTAQGMDYLHAKSIIHRDLKSNNIFL--HEDLTVKIGDFGLAtvkSRWSGSHQFEQLS 614
Cdd:cd14192    90 DR--ITDESYQLTELdaILFTRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQIKIIDFGLA---RRYKPREKLKVNF 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 615 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMV 669
Cdd:cd14192   165 GTPEFLAPEVV---NYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIV 216
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
462-711 1.41e-20

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: 92.34  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGT-VYKGKWHG-DVAVK-MLnvtaptPQQLQAFKNEVGVLRKT-RHVNILLFMGYSTKPQ-LAIVTQWCEgSS 536
Cdd:cd13982     8 VLGYGSEGTiVFRGTFDGrPVAVKrLL------PEFFDFADREVQLLRESdEHPNVIRYFCTEKDRQfLYIALELCA-AS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHhlhIIE-------TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL-----HEDLTVKIGDFGLAtvKSRW 604
Cdd:cd13982    81 LQD---LVEspresklFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstpnaHGNVRAMISDFGLC--KKLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 SGSHQFEQLS---GSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIfMVGRGYLSPDLSK 680
Cdd:cd13982   156 VGRSSFSRRSgvaGTSGWIAPEMLSGSTKRRQTRAVDIFSLGCVFYYVLSgGSHPFGDKLEREANI-LKGKYSLDKLLSL 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 681 VrsNCPKAMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd13982   235 G--EHGPEAQDLIERMIDFDPEKRPSAEEVL 263
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
463-714 1.66e-20

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: 92.03  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD-----VAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMGY-STKPQLAIVTQWCEGS 535
Cdd:cd05047     3 IGEGNFGQVLKARIKKDglrmdAAIKRMKEYA-SKDDHRDFAGELEVLCKLgHHPNIINLLGAcEHRGYLYLAIEYAPHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLH---IIETKFEMIK------------LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV 600
Cdd:cd05047    82 NLLDFLRksrVLETDPAFAIanstastlssqqLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 601 KSRWsgshqFEQLSGS--ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGYlspD 677
Cdd:cd05047   162 QEVY-----VKKTMGRlpVRWMAIESL---NYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCA-ELYEKLPQGY---R 229
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1237938074 678 LSKVRsNCPKAMKRLMAECLKKKRDERPLFPQILASI 714
Cdd:cd05047   230 LEKPL-NCDDEVYDLMRQCWREKPYERPSFAQILVSL 265
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
463-656 1.90e-20

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: 91.60  E-value: 1.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTV--YKGKWHGD---VAVKMLNVTAPTPQQLQAFK---NEVGVLRKTRHVNIL--LFMGYSTKPQLAIVTQWC 532
Cdd:cd13994     1 IGKGATSVVriVTKKNPRSgvlYAVKEYRRRDDESKRKDYVKrltSEYIISSKLHHPNIVkvLDLCQDLHGKWCLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYhhlhiieTKFEMIKLIDIA------RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV-KSRW- 604
Cdd:cd13994    81 PGGDLF-------TLIEKADSLSLEekdcffKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVfGMPAe 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 605 SGSHQFEQLSGSILWMAPEVIRMQDKNPYSfqSDVYAFGIVLYELMTGQLPY 656
Cdd:cd13994   154 KESPMSAGLCGSEPYMAPEVFTSGSYDGRA--VDVWSCGIVLFALFTGRFPW 203
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
459-712 2.01e-20

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: 91.63  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYK------GKwhgDVAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQW 531
Cdd:cd14184     5 IGKVIGDGNFAVVKEcverstGK---EFALKIID-KAKCCGKEHLIENEVSILRRVKHPNIIMLIEeMDTPAELYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE----DLTVKIGDFGLATVKsrwsgS 607
Cdd:cd14184    81 VKGGDLFDAI-TSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLATVV-----E 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIF---MVGR-GYLSPdlskVRS 683
Cdd:cd14184   155 GPLYTVCGTPTYVAPEIIA---ETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFdqiLLGKlEFPSP----YWD 227
                         250       260
                  ....*....|....*....|....*....
gi 1237938074 684 NCPKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd14184   228 NITDSAKELISHMLQVNVEARYTAEQILS 256
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
459-649 2.24e-20

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: 91.95  E-value: 2.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTR---HVNILLFMGYSTKPQ------LA 526
Cdd:cd07838     3 EVAEIGEGAYGTVYKARDLQDgrfVALKKVRVPLSEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHGPRtdrelkLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEgSSLYHHL-HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrws 605
Cdd:cd07838    83 LVFEHVD-QDLATYLdKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYS--- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1237938074 606 gshqFEQLSGSI---LWM-APEVIrMQDknPYSFQSDVYAFGIVLYEL 649
Cdd:cd07838   159 ----FEMALTSVvvtLWYrAPEVL-LQS--SYATPVDMWSVGCIFAEL 199
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
459-695 2.87e-20

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: 91.26  E-value: 2.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVY------KGKwhgDVAVKMLNVTAPTPQ---QLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ---LA 526
Cdd:cd06652     6 LGKLLGQGAFGRVYlcydadTGR---ELAVKQVQFDPESPEtskEVNALECEIQLLKNLLHERIVQYYGCLRDPQertLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLHIIETKFEMIKLiDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG----LATVKS 602
Cdd:cd06652    83 IFMEYMPGGSIKDQLKSYGALTENVTR-KYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGaskrLQTICL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RWSGshqFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYLSPDL-SKV 681
Cdd:cd06652   162 SGTG---MKSVTGTPYWMSPEVISGEG---YGRKADIWSVGCTVVEMLTEKPPWAEFEAM-AAIFKIATQPTNPQLpAHV 234
                         250
                  ....*....|....
gi 1237938074 682 RSNCPKAMKRLMAE 695
Cdd:cd06652   235 SDHCRDFLKRIFVE 248
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
463-711 2.95e-20

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: 90.95  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFG--TVYKGKWHGDVAV-KMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLy 538
Cdd:cd08221     8 LGRGAFGeaVLYRKTEDNSLVVwKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNhFLDGESLFIEMEYCNGGNL- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 hHLHIIETKFEMIKLIDIA---RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQLSG 615
Cdd:cd08221    87 -HDKIAQQKNQLFPEEVVLwylYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLD--SESSMAESIVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGRGYLSPDLSKVRSNcpkaMKRLMAE 695
Cdd:cd08221   164 TPYYMSPELVQ---GVKYNFKSDIWAVGCVLYELLTLKRTF-DATNPLRLAVKIVQGEYEDIDEQYSEE----IIQLVHD 235
                         250
                  ....*....|....*.
gi 1237938074 696 CLKKKRDERPLFPQIL 711
Cdd:cd08221   236 CLHQDPEDRPTAEELL 251
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
463-656 3.06e-20

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: 91.43  E-value: 3.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY------KGKWHgdvAVKMLNVTAPTPQQLQAFK-NEVGVLRKTrHVNILLFMGYS--TKPQLAIVTQWCE 533
Cdd:cd05577     1 LGRGGFGEVCacqvkaTGKMY---ACKKLDKKRIKKKKGETMAlNEKIILEKV-SSPFIVSLAYAfeTKDKLCLVLTLMN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHL-HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGSHQFEQ 612
Cdd:cd05577    77 GGDLKYHIyNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAV---EFKGGKKIKG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 613 LSGSILWMAPEVIrmQDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05577   154 RVGTHGYMAPEVL--QKEVAYDFSVDWFALGCMLYEMIAGRSPF 195
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
450-711 3.30e-20

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: 92.76  E-value: 3.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMGYS 520
Cdd:cd14207     2 WEFARERLKLGKSLGRGAFGKVVQASAFGikksptcrVVAVKMLKEGA-TASEYKALMTELKILIHIgHHLNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 521 TKP--QLAIVTQWCEGSSLYHHL-----------------HIIETKFE-------------------------------- 549
Cdd:cd14207    81 TKSggPLMVIVEYCKYGNLSNYLkskrdffvtnkdtslqeELIKEKKEaeptggkkkrlesvtssesfassgfqedksls 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 550 ------------------MIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFE 611
Cdd:cd14207   161 dveeeeedsgdfykrpltMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 612 QLSGSILWMAPEVIRmqDKnPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRG--YLSPDLSKvrsncpKA 688
Cdd:cd14207   241 DARLPLKWMAPESIF--DK-IYSTKSDVWSYGVLLWEIFSlGASPYPGVQIDEDFCSKLKEGirMRAPEFAT------SE 311
                         330       340
                  ....*....|....*....|...
gi 1237938074 689 MKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd14207   312 IYQIMLDCWQGDPNERPRFSELV 334
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
450-717 3.57e-20

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: 93.55  E-value: 3.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTPQQlQAFKNEVGVLRKT-RHVNILLFMGYS 520
Cdd:cd05105    32 WEFPRDGLVLGRILGSGAFGKVVEGTAYGlsrsqpvmKVAVKMLKPTARSSEK-QALMSELKIMTHLgPHLNIVNLLGAC 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 521 TKP-QLAIVTQWCEGSSLYHHLH--------------------------------------------------------- 542
Cdd:cd05105   111 TKSgPIYIITEYCFYGDLVNYLHknrdnflsrhpekpkkdldifginpadestrsyvilsfenkgdymdmkqadttqyvp 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 543 IIETK-----------------------------------FEMIKLIDI---ARQTAQGMDYLHAKSIIHRDLKSNNIFL 584
Cdd:cd05105   191 MLEIKeaskysdiqrsnydrpasykgsndsevknllsddgSEGLTTLDLlsfTYQVARGMEFLASKNCVHRDLAARNVLL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 585 HEDLTVKIGDFGLATvksrwSGSHQFEQLS-GS----ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPYSN 658
Cdd:cd05105   271 AQGKIVKICDFGLAR-----DIMHDSNYVSkGStflpVKWMAPESIF---DNLYTTLSDVWSYGILLWEIFSlGGTPYPG 342
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 659 INNRDQIIFMVGRGY--LSPDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd05105   343 MIVDSTFYNKIKSGYrmAKPD------HATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESL 397
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
449-660 3.82e-20

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: 90.97  E-value: 3.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 449 DWEIpdgqitvGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKT-------------RHVN 512
Cdd:cd14077     2 NWEF-------VKTIGAGSMGKVKLAKHIRTgekCAIKIIPRASNAGLKKEREKRLEKEISRDirtireaalssllNHPH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 513 IL-LFMGYSTKPQLAIVTQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVK 591
Cdd:cd14077    75 ICrLRDFLRTPNHYYMLFEYVDGGQLLDYI-ISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 592 IGDFGLATVKSRWSGSHQFeqlSGSILWMAPEVIrmqDKNPYSF-QSDVYAFGIVLYELMTGQLPYSNIN 660
Cdd:cd14077   154 IIDFGLSNLYDPRRLLRTF---CGSLYFAAPELL---QAQPYTGpEVDVWSFGVVLYVLVCGKVPFDDEN 217
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
462-658 3.89e-20

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: 91.64  E-value: 3.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTV------YKGKwhgDVAVKMLNVTapTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 534
Cdd:cd06658    29 KIGEGSTGIVciatekHTGK---QVAVKKMDLR--KQQRRELLFNEVVIMRDYHHENVVdMYNSYLVGDELWVVMEFLEG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQfeQLS 614
Cdd:cd06658   104 GALTDI--VTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRK--SLV 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 615 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSN 658
Cdd:cd06658   180 GTPYWMAPEVI---SRLPYGTEVDIWSLGIMVIEMIDGEPPYFN 220
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
463-660 4.76e-20

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: 90.52  E-value: 4.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKwH---GD-VAVKMLNVTAPTPQqLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd14078    11 IGSGGFAKVKLAT-HiltGEkVAIKIMDKKALGDD-LPRVKTEIEALKNLSHQHICrLYHVIETDNKIFMVLEYCPGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvKSRWSGSHQFEQLSGSI 617
Cdd:cd14078    89 FDYI-VAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCA-KPKGGMDHHLETCCGSP 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1237938074 618 LWMAPEVIrmQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNIN 660
Cdd:cd14078   167 AYAAPELI--QGKPYIGSEADVWSMGVLLYALLCGFLPFDDDN 207
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
463-706 5.03e-20

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: 90.79  E-value: 5.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTV-YKGKWHGD-VAVKML---------NVTAPTP-QQLQA---------FKNEVGVLRKTRHVNILLFMGYST 521
Cdd:cd14067     1 LGQGGSGTViYRARYQGQpVAVKRFhikkckkrtDGSADTMlKHLRAadamknfseFRQEASMLHSLQHPCIVYLIGISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 522 KP-----QLA-------IVTQWCEGSSLYHHLHIIETKfemiklidIARQTAQGMDYLHAKSIIHRDLKSNNIFL----- 584
Cdd:cd14067    81 HPlcfalELAplgslntVLEENHKGSSFMPLGHMLTFK--------IAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldv 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 585 HEDLTVKIGDFGLatvkSRWSGSHQFEQLSGSILWMAPEVirmQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQ 664
Cdd:cd14067   153 QEHINIKLSDYGI----SRQSFHEGALGVEGTPGYQAPEI---RPRIVYDEKVDMFSYGMVLYELLSGQRPSLG-HHQLQ 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 665 IIFMVGRGyLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPL 706
Cdd:cd14067   225 IAKKLSKG-IRPVLGQPEEVQFFRLQALMMECWDTKPEKRPL 265
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
448-712 9.74e-20

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 94.42  E-value: 9.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  448 DDWEIPDGQITVGQRIGSGSFGTVYKGK---------WHgdvAVKMLNVTAPTPQQLQAfknEVGVLRKTRHVNILLFMG 518
Cdd:PTZ00266     6 DDGESRLNEYEVIKKIGNGRFGEVFLVKhkrtqeffcWK---AISYRGLKEREKSQLVI---EVNVMRELKHKNIVRYID 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  519 Y---STKPQLAIVTQWCEGSSLYHHLHIIETKFEMIK---LIDIARQTAQGMDYLH-------AKSIIHRDLKSNNIFLH 585
Cdd:PTZ00266    80 RflnKANQKLYILMEFCDAGDLSRNIQKCYKMFGKIEehaIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074  586 EDL-----------------TVKIGDFGLATVKSRWSGSHQfeqLSGSILWMAPEVIRMQDKNpYSFQSDVYAFGIVLYE 648
Cdd:PTZ00266   160 TGIrhigkitaqannlngrpIAKIGDFGLSKNIGIESMAHS---CVGTPYYWSPELLLHETKS-YDDKSDMWALGCIIYE 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074  649 LMTGQLPYSNINNRDQIIFMVGRGylsPDLS-KVRSncpKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:PTZ00266   236 LCSGKTPFHKANNFSQLISELKRG---PDLPiKGKS---KELNILIKNLLNLSAKERPSALQCLG 294
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
500-710 9.97e-20

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: 90.08  E-value: 9.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 500 NEVGVLRK--TRHVnILLFMGYSTKPQLAIVTQWCEGSSL-YHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRD 576
Cdd:cd05630    49 NEKQILEKvnSRFV-VSLAYAYETKDALCLVLTLMNGGDLkFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 577 LKSNNIFLHEDLTVKIGDFGLA-------TVKSRwsgshqfeqlSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYEL 649
Cdd:cd05630   128 LKPENILLDDHGHIRISDLGLAvhvpegqTIKGR----------VGTVGYMAPEVVKNER---YTFSPDWWALGCLLYEM 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 650 MTGQLPYSNIN---NRDQIIFMVGRG------YLSPDlskVRSNCPKAMKRLMAECL------KKKRDERPLFPQI 710
Cdd:cd05630   195 IAGQSPFQQRKkkiKREEVERLVKEVpeeyseKFSPQ---ARSLCSMLLCKDPAERLgcrgggAREVKEHPLFKKL 267
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
456-665 1.35e-19

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: 89.01  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQW 531
Cdd:cd14082     4 QIFPDEVLGSGQFGIVYGGKHRKtgrDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECmFETPERVFVVMEK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEG-------SSLYHHLHIIETKFeMIKLIDIArqtaqgMDYLHAKSIIHRDLKSNNIFL--HEDL-TVKIGDFGLAtvk 601
Cdd:cd14082    84 LHGdmlemilSSEKGRLPERITKF-LVTQILVA------LRYLHSKNIVHCDLKPENVLLasAEPFpQVKLCDFGFA--- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 602 sRWSGSHQFEQ-LSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYS---NINnrDQI 665
Cdd:cd14082   154 -RIIGEKSFRRsVVGTPAYLAPEVLR---NKGYNRSLDMWSVGVIIYVSLSGTFPFNedeDIN--DQI 215
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
564-712 1.57e-19

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: 89.74  E-value: 1.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 564 MDYLHAK-SIIHRDLKSNNIFLHEDLTVKIGDFGLAtvkSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAF 642
Cdd:cd06618   127 LHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGIS---GRLVDSKAKTRSAGCAAYMAPERIDPPDNPKYDIRADVWSL 203
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 643 GIVLYELMTGQLPYSNINNRDQIIFMV---------GRGYLSPDLskvrsncpkamKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd06618   204 GISLVELATGQFPYRNCKTEFEVLTKIlneeppslpPNEGFSPDF-----------CSFVDLCLTKDHRYRPKYRELLQ 271
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
461-705 2.01e-19

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: 89.16  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNIL-LFMGYSTKPQ-----------L 525
Cdd:cd14048    12 QCLGRGGFGVVFEAKNKVDdcnYAVKRIRLPNNELAREKVLR-EVRALAKLDHPGIVrYFNAWLERPPegwqekmdevyL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLYHHLHIIET--KFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT---- 599
Cdd:cd14048    91 YIQMQLCRKENLKDWMNRRCTmeSRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVTamdq 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 600 ------VKSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMtgqLPYSNINNRDQIIFMVGRGY 673
Cdd:cd14048   171 gepeqtVLTPMPAYAKHTGQVGTRLYMSPEQIH---GNQYSEKVDIFALGLILFELI---YSFSTQMERIRTLTDVRKLK 244
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1237938074 674 LSPDLSKvrsNCPKAMKrLMAECLKKKRDERP 705
Cdd:cd14048   245 FPALFTN---KYPEERD-MVQQMLSPSPSERP 272
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
458-656 2.14e-19

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: 89.55  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQ----LQAFKnEVGVLRKTRHVNIL-LFMGYSTKPQLAIVT 529
Cdd:cd07841     3 EKGKKLGEGTYAVVYKARDKETgriVAIKKIKLGERKEAKdginFTALR-EIKLLQELKHPNIIgLLDVFGHKSNINLVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSslyhhL-HIIETKFEMIKLIDI---ARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT------ 599
Cdd:cd07841    82 EFMETD-----LeKVIKDKSIVLTPADIksyMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARsfgspn 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 600 ------VKSRWsgshqfeqlsgsilWMAPEVI---RMqdknpYSFQSDVYAFGIVLYELMTgQLPY 656
Cdd:cd07841   157 rkmthqVVTRW--------------YRAPELLfgaRH-----YGVGVDMWSVGCIFAELLL-RVPF 202
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
463-704 2.16e-19

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK 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: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 90.07  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNvtaptpQQLQAFKNEV-------GVLRKTRHVNILLFMGYS--TKPQLAIVTQ 530
Cdd:cd05575     3 IGKGSFGKVLLARHKAEgklYAVKVLQ------KKAILKRNEVkhimaerNVLLKNVKHPFLVGLHYSfqTKDKLYFVLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQF 610
Cdd:cd05575    77 YVNGGELFFHLQR-ERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLC--KEGIEPSDTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 611 EQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGqLP--YSniNNRDQIIfmvgRGYLSPDLsKVRSNCPKA 688
Cdd:cd05575   154 STFCGTPEYLAPEVLR---KQPYDRTVDWWCLGAVLYEMLYG-LPpfYS--RDTAEMY----DNILHKPL-RLRTNVSPS 222
                         250
                  ....*....|....*.
gi 1237938074 689 MKRLMAECLKKKRDER 704
Cdd:cd05575   223 ARDLLEGLLQKDRTKR 238
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
463-656 2.23e-19

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK 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: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 88.22  E-value: 2.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKwH----GDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd14071     8 IGKGNFAVVKLAR-HritkTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIkLYQVMETKDMLYLVTEYASNGEI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHL----HIIETKfemiklidiAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSHQ 609
Cdd:cd14071    87 FDYLaqhgRMSEKE---------ARkkfwQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNF---FKPGEL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 610 FEQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14071   155 LKTWCGSPPYAAPEV--FEGKEYEGPQLDIWSLGVVLYVLVCGALPF 199
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
458-713 2.27e-19

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: 88.13  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGD---VAVKmlnvtaptpQQLQAFKNEVGVLRKTR----------HVNILLF-MGYSTKP 523
Cdd:cd14050     4 TILSKLGEGSFGEVFKVRSREDgklYAVK---------RSRSRFRGEKDRKRKLEeverheklgeHPNCVRFiKAWEEKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCeGSSLYHHLHIIETKFEMiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLaTVKSR 603
Cdd:cd14050    75 ILYIQTELC-DTSLQQYCEETHSLPES-EVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGL-VVELD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHqfEQLSGSILWMAPEVIRmqdkNPYSFQSDVYAFGIVLYELMTG-QLPySNINNRDQIifmvGRGYLSPDLSKVR 682
Cdd:cd14050   152 KEDIH--DAQEGDPRYMAPELLQ----GSFTKAADIFSLGITILELACNlELP-SGGDGWHQL----RQGYLPEEFTAGL 220
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 683 SncpKAMKRLMAECLKKKRDERPLFPQILAS 713
Cdd:cd14050   221 S---PELRSIIKLMMDPDPERRPTAEDLLAL 248
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
455-661 2.73e-19

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: 88.09  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 455 GQITVGQRIGSGSFGTVYKGKwHG----DVAVKMLNVTAPTPQQLQA-FKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIV 528
Cdd:cd14079     2 GNYILGKTLGVGSFGKVKLAE-HEltghKVAVKILNRQKIKSLDMEEkIRREIQILKLFRHPHIIrLYEVIETPTDIFMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHlhIIET-KFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwsgS 607
Cdd:cd14079    81 MEYVSGGELFDY--IVQKgRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMR----D 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 608 HQFEQLS-GSILWMAPEVIrmqDKNPYSF-QSDVYAFGIVLYELMTGQLPY--SNINN 661
Cdd:cd14079   155 GEFLKTScGSPNYAAPEVI---SGKLYAGpEVDVWSCGVILYALLCGSLPFddEHIPN 209
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
461-669 2.98e-19

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: 88.41  E-value: 2.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD-----VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGY--STKPQLaIVTQWCE 533
Cdd:cd05042     1 QEIGNGWFGKVLLGEIYSGtsvaqVVVKELKASA-NPKEQDTFLKEGQPYRILQHPNILQCLGQcvEAIPYL-LVMEFCD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKFEMIK----LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQ 609
Cdd:cd05042    79 LGDLKAYLRSEREHERGDSdtrtLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKEDYIET 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 610 FEQLSGSILWMAPEVI-RMQDK---NPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMV 669
Cdd:cd05042   159 DDKLWFPLRWTAPELVtEFHDRllvVDQTKYSNIWSLGVTLWELFEnGAQPYSNLSDLDVLAQVV 223
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
455-724 3.39e-19

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: 88.63  E-value: 3.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 455 GQITVGQRIGSGSFGTVYKGKWHGD---VAVKMLNvTAPTPQ-QLQAFKnEVGVLRKTRHVNILLFMGYSTKPQ---LAI 527
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTktiFALKTIT-TDPNPDvQKQILR-ELEINKSCASPYIVKYYGAFLDEQdssIGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCEGSSLYHHLHIIETKFEMIK---LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA--TVKs 602
Cdd:cd06621    79 AMEYCEGGSLDSIYKKVKKKGGRIGekvLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSgeLVN- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 rwSGSHQFeqlSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY--SNINNRDQIIFMvgrGYLSPDLSK 680
Cdd:cd06621   158 --SLAGTF---TGTSYYMAPERIQGG---PYSITSDVWSLGLTLLEVAQNRFPFppEGEPPLGPIELL---SYIVNMPNP 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 681 VRSNCP-------KAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKI 724
Cdd:cd06621   227 ELKDEPengikwsESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKV 277
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
463-656 3.53e-19

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: 89.23  E-value: 3.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY------KGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd05620     3 LGKGSFGKVLlaelkgKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGS 616
Cdd:cd05620    83 LMFHIQD-KGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMC--KENVFGDNRASTFCGT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1237938074 617 ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05620   160 PDYIAPEILQGLK---YTFSVDWWSFGVLLYEMLIGQSPF 196
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
459-656 4.50e-19

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: 88.40  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVY--KGKWHGD-VAVKMLNVTAPTPQ-QLQAFKNEVGVLRKTRH---VNilLFMGYSTKPQLAIVTQW 531
Cdd:cd05580     5 FLKTLGTGSFGRVRlvKHKDSGKyYALKILKKAKIIKLkQVEHVLNEKRILSEVRHpfiVN--LLGSFQDDRNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHIiETKFEmiklIDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKSR-WS 605
Cdd:cd05580    83 VPGGELFSLLRR-SGRFP----NDVAKfyaaEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKrVKDRtYT 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 606 gshqfeqLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05580   158 -------LCGTPEYLAPEIILSK---GHGKAVDWWALGILIYEMLAGYPPF 198
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
463-656 6.17e-19

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: 87.28  E-value: 6.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK--GKWHG-DVAVKMlnVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLY 538
Cdd:cd14193    12 LGGGRFGQVHKceEKSSGlKLAAKI--IKARSQKEKEEVKNEIEVMNQLNHANLIqLYDAFESRNDIVLVMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHlhIIETKFEMIKL--IDIARQTAQGMDYLHAKSIIHRDLKSNNIFL--HEDLTVKIGDFGLAtvkSRWSGSHQFEQLS 614
Cdd:cd14193    90 DR--IIDENYNLTELdtILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLA---RRYKPREKLRVNF 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 615 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14193   165 GTPEFLAPEVV---NYEFVSFPTDMWSLGVIAYMLLSGLSPF 203
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
457-722 6.53e-19

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: 87.79  E-value: 6.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKGKWHGD--------VAVKMLNVTAPTPQQlqAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAI 527
Cdd:cd05093     7 IVLKRELGEGAFGKVFLAECYNLcpeqdkilVAVKTLKDASDNARK--DFHREAELLTNLQHEHIVKFYGVCVEGDpLIM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCEGSSLYHHLHI------------IETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDF 595
Cdd:cd05093    85 VFEYMKHGDLNKFLRAhgpdavlmaegnRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 596 GLatvkSRWSGSHQFEQLSG----SILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNrDQIIFMVG 670
Cdd:cd05093   165 GM----SRDVYSTDYYRVGGhtmlPIRWMPPESIMYRK---FTTESDVWSLGVVLWEIFTyGKQPWYQLSN-NEVIECIT 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 671 RGYLspdLSKVRSnCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLP 722
Cdd:cd05093   237 QGRV---LQRPRT-CPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASP 284
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
463-661 6.68e-19

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: 87.39  E-value: 6.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY---KGKWHGDVAVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLY 538
Cdd:cd14167    11 LGTGAFSEVVlaeEKRTQKLVAIKCIAKKALEGKE-TSIENEIAVLHKIKHPNIVALDDiYESGGHLYLIMQLVSGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHlhIIETKFEMIKliDIARQTAQGMD---YLHAKSIIHRDLKSNNIF---LHEDLTVKIGDFGLATVKSrwSGShQFEQ 612
Cdd:cd14167    90 DR--IVEKGFYTER--DASKLIFQILDavkYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIEG--SGS-VMST 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1237938074 613 LSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINN 661
Cdd:cd14167   163 ACGTPGYVAPEVLA---QKPYSKAVDCWSIGVIAYILLCGYPPFYDEND 208
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
463-660 6.87e-19

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: 87.20  E-value: 6.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAptpQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLY 538
Cdd:cd14087     9 IGRGSFSRVVRVEHRVTrqpYAIKMIETKC---RGREVCESELNVLRRVRHTNIIQLIEvFETKERVYMVMELATGGELF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE---DLTVKIGDFGLATVKSRwSGSHQFEQLSG 615
Cdd:cd14087    86 DRI-IAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHpgpDSKIMITDFGLASTRKK-GPNCLMKTTCG 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1237938074 616 SILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNIN 660
Cdd:cd14087   164 TPEYIAPEILL---RKPYTQSVDMWAVGVIAYILLSGTMPFDDDN 205
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
450-716 6.89e-19

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: 87.75  E-value: 6.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEipdgQITVGQRIGSGSFGTVYKGKWHGD-----VAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMGY-STK 522
Cdd:cd05089     1 WE----DIKFEDVIGEGNFGQVIKAMIKKDglkmnAAIKMLKEFA-SENDHRDFAGELEVLCKLgHHPNIINLLGAcENR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 523 PQLAIVTQWCEGSSLYHHLH---IIETKFEMIK------------LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED 587
Cdd:cd05089    76 GYLYIAIEYAPYGNLLDFLRksrVLETDPAFAKehgtastltsqqLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGEN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 588 LTVKIGDFGLATVKSRWsgshqFEQLSGS--ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQ 664
Cdd:cd05089   156 LVSKIADFGLSRGEEVY-----VKKTMGRlpVRWMAIESL---NYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGMTCA-E 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 665 IIFMVGRGYlspDLSKVRsNCPKAMKRLMAECLKKKRDERPLFPQIlaSIEL 716
Cdd:cd05089   227 LYEKLPQGY---RMEKPR-NCDDEVYELMRQCWRDRPYERPPFSQI--SVQL 272
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
455-656 6.93e-19

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 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: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 87.15  E-value: 6.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 455 GQITVGQRIGSGSFGTVYKGkWHGD---------VAVKM-LNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKP 523
Cdd:cd14076     1 GPYILGRTLGEGEFGKVKLG-WPLPkanhrsgvqVAIKLiRRDTQQENCQTSKIMREINILKGLTHPNIVrLLDVLKTKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEGSSLYHHLhiieTKFEMIKLIDIARQTAQ---GMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV 600
Cdd:cd14076    80 YIGIVLEFVSGGELFDYI----LARRRLKDSVACRLFAQlisGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANT 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 601 KSRWSGShQFEQLSGSILWMAPEVIRMqdKNPYS-FQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14076   156 FDHFNGD-LMSTSCGSPCYAAPELVVS--DSMYAgRKADIWSCGVILYAMLAGYLPF 209
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
459-656 7.32e-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: 87.39  E-value: 7.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHGD---VAVKMLNV-TAPTPQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQWCE 533
Cdd:cd08228     6 IEKKIGRGQFSEVYRATCLLDrkpVALKKVQIfEMMDAKARQDCVKEIDLLKQLNHPNVIKYLdSFIEDNELNIVLELAD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKFEMIKLIDIAR---QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKSRWSGSHq 609
Cdd:cd08228    86 AGDLSQMIKYFKKQKRLIPERTVWKyfvQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRfFSSKTTAAH- 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 610 feQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd08228   165 --SLVGTPYYMSPERIH---ENGYNFKSDIWSLGCLLYEMAALQSPF 206
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
461-660 7.52e-19

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: 86.67  E-value: 7.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHG---DVAVKMLNVTA-PTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd14073     7 ETLGKGTYGKVKLAIERAtgrEVAIKSIKKDKiEDEQDMVRIRREIEIMSSLNHPHIIrIYEVFENKDKIVIVMEYASGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHiietkfEMIKLID-----IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSHQF 610
Cdd:cd14073    87 ELYDYIS------ERRRLPErearrIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNL---YSKDKLL 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 611 EQLSGSILWMAPEVIRMQdknPYSF-QSDVYAFGIVLYELMTGQLPYSNIN 660
Cdd:cd14073   158 QTFCGSPLYASPEIVNGT---PYQGpEVDCWSLGVLLYTLVYGTMPFDGSD 205
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
456-712 8.51e-19

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: 86.88  E-value: 8.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGD--VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRH-VNILLFMGY--STKPQLAIVTQ 530
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVLNPKKkiYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIQLYDYevTDEDDYLYMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYhhlHIIETKFEM-IKLIDIA---RQTAQGMDYLHAKSIIHRDLKSNNiFLHEDLTVKIGDFGLATVKSRWSG 606
Cdd:cd14131    82 ECGEIDLA---TILKKKRPKpIDPNFIRyywKQMLEAVHTIHEEGIVHSDLKPAN-FLLVKGRLKLIDFGIAKAIQNDTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQLSGSILWMAPE-VIRMQ----DKNPY--SFQSDVYAFGIVLYELMTGQLPYSNI-----------NNRDQIIFm 668
Cdd:cd14131   158 SIVRDSQVGTLNYMSPEaIKDTSasgeGKPKSkiGRPSDVWSLGCILYQMVYGKTPFQHItnpiaklqaiiDPNHEIEF- 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 669 vgrgylsPDLSkvrsncPKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd14131   237 -------PDIP------NPDLIDVMKRCLQRDPKKRPSIPELLN 267
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
450-656 8.65e-19

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: 86.93  E-value: 8.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQItvGQRIGSGSFGTVYKGKWHGDVAVKMLNV-------TAPTPQQLqafKNEVGVLRKTRHVNILLFMGY-ST 521
Cdd:cd14116     2 WALEDFEI--GRPLGKGKFGNVYLAREKQSKFILALKVlfkaqleKAGVEHQL---RREVEIQSHLRHPNILRLYGYfHD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 522 KPQLAIVTQWCEGSSLYHHLHIIeTKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGlatvk 601
Cdd:cd14116    77 ATRVYLILEYAPLGTVYRELQKL-SKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG----- 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 602 srWS---GSHQFEQLSGSILWMAPEVI--RMQDKnpysfQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14116   151 --WSvhaPSSRRTTLCGTLDYLPPEMIegRMHDE-----KVDLWSLGVLCYEFLVGKPPF 203
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
463-675 9.23e-19

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: 87.84  E-value: 9.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY-----KGKWHGDV-AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd05582     3 LGQGSFGKVFlvrkiTGPDAGTLyAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVkLHYAFQTEGKLYLILDFLRGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHL--HIIET----KFEMIKLidiarqtAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQ 609
Cdd:cd05582    83 DLFTRLskEVMFTeedvKFYLAEL-------ALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLS--KESIDHEKK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 610 FEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYLS 675
Cdd:cd05582   154 AYSFCGTVEYMAPEVV---NRRGHTQSADWWSFGVLMFEMLTGSLPFQG-KDRKETMTMILKAKLG 215
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
463-648 9.41e-19

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: 87.09  E-value: 9.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK---GKWHGDV-AVKMLNVTAPTPQQLQAFKNEVGVLRKTR---HVNILLFM-GYSTKPQLAIVTQWCEG 534
Cdd:cd14052     8 IGSGEFSQVYKvseRVPTGKVyAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIdSWEYHGHLYIQTELCEN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLhiieTKFEMIKLIDIAR------QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSH 608
Cdd:cd14052    88 GSLDVFL----SELGLLGRLDEFRvwkilvELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATV---WPLIR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 609 QFEqLSGSILWMAPEVI--RMQDKnpysfQSDVYAFGIVLYE 648
Cdd:cd14052   161 GIE-REGDREYIAPEILseHMYDK-----PADIFSLGLILLE 196
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
463-710 1.10e-18

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: 86.16  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVykgKWHGD------VAVKMLNVT--APTPQQLQAFKNEVGVLRKTRHVNI--LL-FMGYSTKPQLAIVTQW 531
Cdd:cd14119     1 LGEGSYGKV---KEVLDtetlcrRAVKILKKRklRRIPNGEANVKREIQILRRLNHRNVikLVdVLYNEEKQKLYMVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFE 611
Cdd:cd14119    78 CVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFAEDDTCT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 612 QLSGSILWMAPEVIRMQDKnpYS-FQSDVYAFGIVLYELMTGQLPYsninnRDQIIFM----VGRG-YLSPDlskvrsNC 685
Cdd:cd14119   158 TSQGSPAFQPPEIANGQDS--FSgFKVDIWSAGVTLYNMTTGKYPF-----EGDNIYKlfenIGKGeYTIPD------DV 224
                         250       260
                  ....*....|....*....|....*
gi 1237938074 686 PKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd14119   225 DPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
463-658 1.12e-18

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: 88.21  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY------KGKWHgdvAVKMLNVTAPTPQQLQAFK-NEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 534
Cdd:cd05593    23 LGKGTFGKVIlvrekaSGKYY---AMKILKKEVIIAKDEVAHTlTESRVLKNTRHPFLTsLKYSFQTKDRLCFVMEYVNG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLS 614
Cdd:cd05593   100 GELFFHLSR-ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC--KEGITDAATMKTFC 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 615 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSN 658
Cdd:cd05593   177 GTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 217
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
461-669 1.30e-18

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: 86.58  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHG-----DVAVKMLNVTAPTPQQLQaFKNEVGVLRKTRHVNILLFMGYSTK--PQLaIVTQWCE 533
Cdd:cd05087     3 KEIGHGWFGKVFLGEVNSglsstQVVVKELKASASVQDQMQ-FLEEAQPYRALQHTNLLQCLAQCAEvtPYL-LVMEFCP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKFEM----IKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQ 609
Cdd:cd05087    81 LGDLKGYLRSCRAAESMapdpLTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKEDYFVT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 610 FEQLSGSILWMAPEVIRMQDKN----PYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMV 669
Cdd:cd05087   161 ADQLWVPLRWIAPELVDEVHGNllvvDQTKQSNVWSLGVTIWELFElGNQPYRHYSDRQVLTYTV 225
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
461-712 1.30e-18

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: 86.29  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTV----YKGKwHGDVAVKMLNV---------------TAPTPQQLQAFknevgvLRKTRHVNIL-LFMGYS 520
Cdd:cd14004     6 KEMGEGAYGQVnlaiYKSK-GKEVVIKFIFKerilvdtwvrdrklgTVPLEIHILDT------LNKRSHPNIVkLLDFFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 521 TKPQLAIVTQwCEGSSL----YHHLHIIETKFEMIKLIdiaRQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG 596
Cdd:cd14004    79 DDEFYYLVME-KHGSGMdlfdFIERKPNMDEKEAKYIF---RQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 597 LATvksrWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQS-DVYAFGIVLYELMTGQLPYSNInnrDQIifmvgrgyLS 675
Cdd:cd14004   155 SAA----YIKSGPFDTFVGTIDYAAPEVLR---GNPYGGKEqDIWALGVLLYTLVFKENPFYNI---EEI--------LE 216
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1237938074 676 PDLsKVRSNCPKAMKRLMAECLKKKRDERPLFPQILA 712
Cdd:cd14004   217 ADL-RIPYAVSEDLIDLISRMLNRDVGDRPTIEELLT 252
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
463-656 1.34e-18

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: 87.75  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLN---VTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd05616     8 LGKGSFGKVMLAERKGTdelYAVKILKkdvVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIeTKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvKSRWSGSHQfEQLSGS 616
Cdd:cd05616    88 LMYHIQQV-GRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK-ENIWDGVTT-KTFCGT 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1237938074 617 ILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05616   165 PDYIAPEIIAYQ---PYGKSVDWWAFGVLLYEMLAGQAPF 201
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
462-658 1.39e-18

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: 87.00  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTV------YKGKWhgdVAVKMLNVTapTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 534
Cdd:cd06657    27 KIGEGSTGIVciatvkSSGKL---VAVKKMDLR--KQQRRELLFNEVVIMRDYQHENVVeMYNSYLVGDELWVVMEFLEG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwsGSHQFEQLS 614
Cdd:cd06657   102 GALTDI--VTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK--EVPRRKSLV 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 615 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSN 658
Cdd:cd06657   178 GTPYWMAPELI---SRLPYGPEVDIWSLGIMVIEMVDGEPPYFN 218
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
450-721 1.71e-18

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: 87.73  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVgQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP--- 523
Cdd:cd07851    11 WEVPDRYQNL-SPVGSGAYGQVCSAFDTKtgrKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPAssl 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 ----QLAIVTQWCeGSSLYHhlhIIETKfemiKLID-----IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGD 594
Cdd:cd07851    90 edfqDVYLVTHLM-GADLNN---IVKCQ----KLSDdhiqfLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 595 FGLAT---------VKSRWsgshqfeqlsgsilWMAPEVI--RMQdknpYSFQSDVYAFGIVLYELMTGQ--LPYSN-IN 660
Cdd:cd07851   162 FGLARhtddemtgyVATRW--------------YRAPEIMlnWMH----YNQTVDIWSVGCIMAELLTGKtlFPGSDhID 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 661 NRDQIIFMVGrgylSPD---LSKVRSNCPKAMKRLMAEclKKKRDERPLFPQilAS---IELLARSL 721
Cdd:cd07851   224 QLKRIMNLVG----TPDeelLKKISSESARNYIQSLPQ--MPKKDFKEVFSG--ANplaIDLLEKML 282
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
459-665 1.83e-18

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: 85.83  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYK------GK-WHGDVavkmlnVTAPTPQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQ 530
Cdd:cd14191     6 IEERLGSGKFGQVFRlvekktKKvWAGKF------FKAYSAKEKENIRQEISIMNCLHHPKLVQCVdAFEEKANIVMVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHlhIIETKFEMIK--LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL--HEDLTVKIGDFGLAtvkSRWSG 606
Cdd:cd14191    80 MVSGGELFER--IIDEDFELTEreCIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLA---RRLEN 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 665
Cdd:cd14191   155 AGSLKVLFGTPEFVAPEVINYE---PIGYATDMWSIGVICYILVSGLSPFMGDNDNETL 210
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
455-657 2.27e-18

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: 85.64  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 455 GQITVGQRIGSGSFGTVYKGkWHG----DVAVKMLNVTAPTPQQ--LQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAI 527
Cdd:cd14070     2 GSYLIGRKLGEGSFAKVREG-LHAvtgeKVAIKVIDKKKAKKDSyvTKNLRREGRIQQMIRHPNITqLLDILETENSYYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGS 607
Cdd:cd14070    81 VMELCPGGNLMHRIYD-KKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQLSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd14070   160 DPFSTQCGSPAYAAPELLARKKYGP---KVDVWSIGVNMYAMLTGTLPFT 206
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
456-696 2.31e-18

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: 86.64  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGD-VAVKMLNVTaptpQQLQAFK-NEVGVLRKTRHVNILLFM-----GYSTKPQLAIV 528
Cdd:cd14219     6 QIQMVKQIGKGRYGEVWMGKWRGEkVAVKVFFTT----EEASWFReTEIYQTVLMRHENILGFIaadikGTGSWTQLYLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHiiETKFEMIKLIDIARQTAQGMDYLHAK--------SIIHRDLKSNNIFLHEDLTVKIGDFGLAT- 599
Cdd:cd14219    82 TDYHENGSLYDYLK--STTLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNGTCCIADLGLAVk 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 600 -VKSRWSGSHQFEQLSGSILWMAPEVIRmQDKNPYSFQS----DVYAFGIVLYEL----MTG------QLPYSNINNRD- 663
Cdd:cd14219   160 fISDTNEVDIPPNTRVGTKRYMPPEVLD-ESLNRNHFQSyimaDMYSFGLILWEVarrcVSGgiveeyQLPYHDLVPSDp 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1237938074 664 ---QIIFMVGRGYLSPDLSKVRSN--CPKAMKRLMAEC 696
Cdd:cd14219   239 syeDMREIVCIKRLRPSFPNRWSSdeCLRQMGKLMTEC 276
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
469-710 2.62e-18

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: 85.54  E-value: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 469 GTVYKGKWhgdVAVKMLNVtAPTPQQLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLYHHLHIIETK 547
Cdd:cd14043    18 GVAYEGDW---VWLKKFPG-GSHTELRPSTKNVFSKLRELRHENVNLFLGlFVDCGILAIVSEHCSRGSLEDLLRNDDMK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 548 FE-MIK---LIDIARqtaqGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVkSRWSGSHQFEQLSGSILWMAPE 623
Cdd:cd14043    94 LDwMFKsslLLDLIK----GMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYNEI-LEAQNLPLPEPAPEELLWTAPE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 624 VIRMQD-KNPYSFQSDVYAFGIVLYELMTGQLPYSninnrdqiifMVGrgyLSPD--LSKVRSncPKAMKR--------- 691
Cdd:cd14043   169 LLRDPRlERRGTFPGDVFSFAIIMQEVIVRGAPYC----------MLG---LSPEeiIEKVRS--PPPLCRpsvsmdqap 233
                         250       260
                  ....*....|....*....|....
gi 1237938074 692 -----LMAECLKKKRDERPLFPQI 710
Cdd:cd14043   234 leciqLMKQCWSEAPERRPTFDQI 257
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
463-653 3.19e-18

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: 85.69  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG--KWHGD-VAVKMLN---------VTAptpqqlqafKNEVGVLRKTRHVNILLFMG-------YSTKP 523
Cdd:cd07840     7 IGEGTYGQVYKArnKKTGElVALKKIRmenekegfpITA---------IREIKLLQKLDHPNVVRLKEivtskgsAKYKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEG--SSLYHHlhiIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVk 601
Cdd:cd07840    78 SIYMVFEYMDHdlTGLLDN---PEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARP- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 602 srWSGSHQFEQLSGSI-LWM-APEVIrMQDKNpYSFQSDVYAFGIVLYELMTGQ 653
Cdd:cd07840   154 --YTKENNADYTNRVItLWYrPPELL-LGATR-YGPEVDMWSVGCILAELFTGK 203
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
461-711 3.67e-18

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: 85.57  E-value: 3.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMG--YSTKPQLAIVTQWCEGS 535
Cdd:cd06620    11 KDLGAGNGGSVSKVLHIPTgtiMAKKVIHIDAKSSVRKQILR-ELQILHECHSPYIVSFYGafLNENNNIIICMEYMDCG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLyHHLHIIETKFEMIKLIDIARQTAQGMDYLHAK-SIIHRDLKSNNIFLHEDLTVKIGDFGLatvksrwSGshqfeQLS 614
Cdd:cd06620    90 SL-DKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGV-------SG-----ELI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSI--------LWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY--SNINNRDQIIFMvgrGYL---------- 674
Cdd:cd06620   157 NSIadtfvgtsTYMSPERIQ---GGKYSVKSDVWSLGLSIIELALGEFPFagSNDDDDGYNGPM---GILdllqrivnep 230
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1237938074 675 SPDLSKVRSnCPKAMKRLMAECLKKKRDERPlFPQIL 711
Cdd:cd06620   231 PPRLPKDRI-FPKDLRDFVDRCLLKDPRERP-SPQLL 265
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
461-656 4.84e-18

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: 84.73  E-value: 4.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd14083     9 EVLGTGAFSEVVLAEDKATgklVAIKCIDKKALKGKE-DSLENEIAVLRKIKHPNIVqLLDIYESKSHLYLVMELVTGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHlhIIE----TKFEMIKLIdiaRQTAQGMDYLHAKSIIHRDLKSNNIFLH---EDLTVKIGDFGLatvkSRWSGSHQ 609
Cdd:cd14083    88 LFDR--IVEkgsyTEKDASHLI---RQVLEAVDYLHSLGIVHRDLKPENLLYYspdEDSKIMISDFGL----SKMEDSGV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 610 FEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14083   159 MSTACGTPGYVAPEVLA---QKPYGKAVDCWSIGVISYILLCGYPPF 202
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
461-663 5.50e-18

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: 85.14  E-value: 5.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVY-------KGKWHGDVAVKMLNVTApTPQQLQAF----KNEVGVLRKTRHVNILLFMGYSTKP--QLAI 527
Cdd:cd14001     5 KKLGYGTGVNVYlmkrsprGGSSRSPWAVKKINSKC-DKGQRSLYqerlKEEAKILKSLNHPNIVGFRAFTKSEdgSLCL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCE---GSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLH-AKSIIHRDLKSNNIFLHEDL-TVKIGDFGLA---- 598
Cdd:cd14001    84 AMEYGGkslNDLIEERYEAGLGPFPAATILKVALSIARALEYLHnEKKILHGDIKSGNVLIKGDFeSVKLCDFGVSlplt 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 599 ---TVKSRWSGshqfeQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRD 663
Cdd:cd14001   164 enlEVDSDPKA-----QYVGTEPWKAKEA--LEEGGVITDKADIFAYGLVLWEMMTLSVPHLNLLDIE 224
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
459-667 7.74e-18

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: 84.28  E-value: 7.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNILLFMGYSTKP-QLAIVTQWCEG 534
Cdd:cd14183    10 VGRTIGDGNFAVVKECVERStgrEYALKIINKSKCRGKE-HMIQNEVSILRRVKHPNIVLLIEEMDMPtELYLVMELVKG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE----DLTVKIGDFGLATVKsrwsgSHQF 610
Cdd:cd14183    89 GDLFDAI-TSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhqdgSKSLKLGDFGLATVV-----DGPL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 611 EQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIF 667
Cdd:cd14183   163 YTVCGTPTYVAPEIIA---ETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLF 216
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
463-663 7.95e-18

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: 85.10  E-value: 7.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY--KGKWHGDV-AVKMLNvtaptpQQLQAFKNEVG-------VLRKTRHvNILLFMGYS--TKPQLAIVTQ 530
Cdd:cd05571     3 LGKGTFGKVIlcREKATGELyAIKILK------KEVIIAKDEVAhtltenrVLQNTRH-PFLTSLKYSfqTNDRLCFVME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIiETKFEMikliDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSG 606
Cdd:cd05571    76 YVNGGELFFHLSR-ERVFSE----DRTRfygaEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLC--KEEISY 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 607 SHQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYsniNNRD 663
Cdd:cd05571   149 GATTKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPF---YNRD 199
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
461-688 9.14e-18

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: 84.23  E-value: 9.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD-----VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK--PQLaIVTQWCE 533
Cdd:cd14206     3 QEIGNGWFGKVILGEIFSDytpaqVVVKELRVSA-GPLEQRKFISEAQPYRSLQHPNILQCLGLCTEtiPFL-LIMEFCQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHI----------IETKfEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR 603
Cdd:cd14206    81 LGDLKRYLRAqrkadgmtpdLPTR-DLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHNNYK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 WSGSHQFEQLSGSILWMAPEVIRMQDKN----PYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGYLSpdL 678
Cdd:cd14206   160 EDYYLTPDRLWIPLRWVAPELLDELHGNlivvDQSKESNVWSLGVTIWELFEfGAQPYRHLSDEEVLTFVVREQQMK--L 237
                         250
                  ....*....|
gi 1237938074 679 SKVRSNCPKA 688
Cdd:cd14206   238 AKPRLKLPYA 247
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
462-667 9.72e-18

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: 84.29  E-value: 9.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKG--KWHGD-VAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMGY-STKPQLAIVTQWCEgSSL 537
Cdd:cd07871    12 KLGEGTYATVFKGrsKLTENlVALKEIRLEHEEGAPCTAIR-EVSLLKNLKHANIVTLHDIiHTERCLTLVFEYLD-SDL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSgsi 617
Cdd:cd07871    90 KQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSNEVVT--- 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 618 LWMAPEVIrMQDKNPYSFQSDVYAFGIVLYELMTGQ--LPYSNINNRDQIIF 667
Cdd:cd07871   167 LWYRPPDV-LLGSTEYSTPIDMWGVGCILYEMATGRpmFPGSTVKEELHLIF 217
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
459-705 1.10e-17

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: 83.40  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTpqQLQAFKnEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 534
Cdd:cd14107     6 VKEEIGRGTFGFVKRVTHKGNgecCAAKFIPLRSST--RARAFQ-ERDILARLSHRRLTcLLDQFETRKTLILILELCSS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHI--IETKFEMIKLIdiaRQTAQGMDYLHAKSIIHRDLKSNNIFL----HEDLtvKIGDFGLAtvKSRWSGSH 608
Cdd:cd14107    83 EELLDRLFLkgVVTEAEVKLYI---QQVLEGIGYLHGMNILHLDIKPDNILMvsptREDI--KICDFGFA--QEITPSEH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQLsGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIfMVGRGYLS---PDLSKVRSNC 685
Cdd:cd14107   156 QFSKY-GSPEFVAPEIVH---QEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLL-NVAEGVVSwdtPEITHLSEDA 230
                         250       260
                  ....*....|....*....|
gi 1237938074 686 PKAMKRLmaecLKKKRDERP 705
Cdd:cd14107   231 KDFIKRV----LQPDPEKRP 246
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
463-663 1.19e-17

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: 84.98  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNvtaptpQQLQAFKNEVGVLRKTRHVNIL---------LFMGYSTKPQLAIVTQ 530
Cdd:cd05619    13 LGKGSFGKVFLAELKGTnqfFAIKALK------KDVVLMDDDVECTMVEKRVLSLawehpflthLFCTFQTKENLFFVME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIIEtKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQF 610
Cdd:cd05619    87 YLNGGDLMFHIQSCH-KFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMC--KENMLGDAKT 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 611 EQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRD 663
Cdd:cd05619   164 STFCGTPDYIAPEILLGQK---YNTSVDWWSFGVLLYEMLIGQSPFHGQDEEE 213
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
463-658 1.32e-17

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: 84.63  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY--KGKWHGDV-AVKML--NVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd05604     4 IGKGSFGKVLlaKRKRDGKYyAVKVLqkKVILNRKEQKHIMAERNVLLKNVKHPFLVgLHYSFQTTDKLYFVLDFVNGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGS 616
Cdd:cd05604    84 LFFHLQR-ERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLC--KEGISNSDTTTTFCGT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 617 ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSN 658
Cdd:cd05604   161 PEYLAPEVIR---KQPYDNTVDWWCLGSVLYEMLYGLPPFYC 199
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
462-669 1.35e-17

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: 83.90  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMGY-STKPQLAIVTQWCEgSSL 537
Cdd:cd07873     9 KLGEGTYATVYKGRsklTDNLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIiHTEKSLTLVFEYLD-KDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSgsi 617
Cdd:cd07873    87 KQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVT--- 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 618 LWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMTGQ--LPYSNINNRDQIIFMV 669
Cdd:cd07873   164 LWYRPPDILLGSTD-YSTQIDMWGVGCIFYEMSTGRplFPGSTVEEQLHFIFRI 216
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
453-701 1.43e-17

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: 84.13  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYK---GKWHGDVAVKMLNV---TAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQL 525
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRcihRETGQQFAVKIVDVakfTSSPGLSTEDLKREASICHMLKHPHIVeLLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLYhhlhiietkFEMIKLIDIA------------RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT---V 590
Cdd:cd14094    81 YMVFEFMDGADLC---------FEIVKRADAGfvyseavashymRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 591 KIGDFGLATvksrwsgshqfeQLSGSIL----------WMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNIN 660
Cdd:cd14094   152 KLGGFGVAI------------QLGESGLvaggrvgtphFMAPEVVK---REPYGKPVDVWGCGVILFILLSGCLPFYGTK 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1237938074 661 NRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKR 701
Cdd:cd14094   217 ERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAER 257
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
450-670 1.54e-17

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: 84.71  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDgQITVGQRIGSGSFGTV---YKGKWHGDVAVKMLnvTAPTPQQLQAFKN--EVGVLRKTRHVNILLFMGYSTKpq 524
Cdd:cd07877    13 WEVPE-RYQNLSPVGSGAYGSVcaaFDTKTGLRVAVKKL--SRPFQSIIHAKRTyrELRLLKHMKHENVIGLLDVFTP-- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 laiVTQWCEGSSLYHHLHIIETKFEMI----KLID-----IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDF 595
Cdd:cd07877    88 ---ARSLEEFNDVYLVTHLMGADLNNIvkcqKLTDdhvqfLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 596 GLAtvksrwsgSHQFEQLSGSIL---WMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPY---SNINNRDQIIFMV 669
Cdd:cd07877   165 GLA--------RHTDDEMTGYVAtrwYRAPEI--MLNWMHYNQTVDIWSVGCIMAELLTGRTLFpgtDHIDQLKLILRLV 234

                  .
gi 1237938074 670 G 670
Cdd:cd07877   235 G 235
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
457-722 1.63e-17

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: 83.52  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKGKWHGD--------VAVKMLNvtAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAI 527
Cdd:cd05094     7 IVLKRELGEGAFGKVFLAECYNLsptkdkmlVAVKTLK--DPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDpLIM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCEGSSLYHHLHI-------------IETKFEM--IKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKI 592
Cdd:cd05094    85 VFEYMKHGDLNKFLRAhgpdamilvdgqpRQAKGELglSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 593 GDFGLatvkSRWSGSHQFEQLSG----SILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQI-I 666
Cdd:cd05094   165 GDFGM----SRDVYSTDYYRVGGhtmlPIRWMPPESIMYRK---FTTESDVWSFGVILWEIFTyGKQPWFQLSNTEVIeC 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 667 FMVGRGYLSPDLskvrsnCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLP 722
Cdd:cd05094   238 ITQGRVLERPRV------CPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGKATP 287
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
476-713 2.51e-17

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: 82.41  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 476 WHGDVAVKMLNVTAPTP--------QQLQAFKNEVGVLRKTRHVNILLFMGYSTKP-------QLAIVTQWCEGSSLYHH 540
Cdd:cd14012    15 VVLDNSKKPGKFLTSQEyfktsngkKQIQLLEKELESLKKLRHPNLVSYLAFSIERrgrsdgwKVYLLTEYAPGGSLSEL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 541 LHIIETkfemIKLIDIARQTAQ---GMDYLHAKSIIHRDLKSNNIFLHEDL---TVKIGDFGLATVKSRwSGSHQFEQLS 614
Cdd:cd14012    95 LDSVGS----VPLDTARRWTLQlleALEYLHRNGVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTLLD-MCSRGSLDEF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSILWMAPEVIRMqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNinnrdqiifmvgrgYLSPDLSKVRSNCPKAMKRLMA 694
Cdd:cd14012   170 KQTYWLPPELAQG--SKSPTRKTDVWDLGLLFLQMLFGLDVLEK--------------YTSPNPVLVSLDLSASLQDFLS 233
                         250
                  ....*....|....*....
gi 1237938074 695 ECLKKKRDERPLFPQILAS 713
Cdd:cd14012   234 KCLSLDPKKRPTALELLPH 252
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
500-656 2.61e-17

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: 82.79  E-value: 2.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 500 NEVGVLRK--TRHVnILLFMGYSTKPQLAIVTQWCEGSSLYHHLH-IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRD 576
Cdd:cd05605    49 NEKQILEKvnSRFV-VSLAYAYETKDALCLVLTIMNGGDLKFHIYnMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 577 LKSNNIFLHEDLTVKIGDFGLA-------TVKSRwsgshqfeqlSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYEL 649
Cdd:cd05605   128 LKPENILLDDHGHVRISDLGLAveipegeTIRGR----------VGTVGYMAPEVV---KNERYTFSPDWWGLGCLIYEM 194

                  ....*..
gi 1237938074 650 MTGQLPY 656
Cdd:cd05605   195 IEGQAPF 201
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
481-700 2.68e-17

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 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). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. 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 PhKG2 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: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 82.71  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 481 AVKMLNVTAP--TPQQLQAFKN----EVGVLRKTR-HVNIL-LFMGYSTKPQLAIVTQWCEGSSLYHHLHiietkfEMIK 552
Cdd:cd14181    39 AVKIIEVTAErlSPEQLEEVRSstlkEIHILRQVSgHPSIItLIDSYESSTFIFLVFDLMRRGELFDYLT------EKVT 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 553 LID-----IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGSHQFEQLSGSILWMAPEVIR- 626
Cdd:cd14181   113 LSEketrsIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSC---HLEPGEKLRELCGTPGYLAPEILKc 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 627 -MQDKNP-YSFQSDVYAFGIVLYELMTGQLPYSninNRDQIIF----MVGR-GYLSPDLSKVRSNCPKAMKRLMAECLKK 699
Cdd:cd14181   190 sMDETHPgYGKEVDLWACGVILFTLLAGSPPFW---HRRQMLMlrmiMEGRyQFSSPEWDDRSSTVKDLISRLLVVDPEI 266

                  .
gi 1237938074 700 K 700
Cdd:cd14181   267 R 267
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
459-693 2.76e-17

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: 82.35  E-value: 2.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTV---YKGKWHGDVAVKMLNVTAPTPQQLQAF-KNEVGVLRKTRHVNILLF--MGYSTKPQLAIVTQWC 532
Cdd:cd14163     4 LGKTIGEGTYSKVkeaFSKKHQRKVAIKIIDKSGGPEEFIQRFlPRELQIVERLDHKNIIHVyeMLESADGKIYLVMELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLY----HHLHIIETKFEMIklidiARQTAQGMDYLHAKSIIHRDLKSNNIFLhEDLTVKIGDFGLATV--KSRWSG 606
Cdd:cd14163    84 EDGDVFdcvlHGGPLPEHRAKAL-----FRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQlpKGGREL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFeqlSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYLSPDLSKVRSNCP 686
Cdd:cd14163   158 SQTF---CGSTAYAAPEV--LQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDD-TDIPKMLCQQQKGVSLPGHLGVSRTCQ 231

                  ....*..
gi 1237938074 687 KAMKRLM 693
Cdd:cd14163   232 DLLKRLL 238
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
458-661 2.83e-17

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: 82.63  E-value: 2.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCE 533
Cdd:cd14169     6 ELKEKLGEGAFSEVVLAQERGSqrlVALKCIPKKALRGKE-AMVENEIAVLRRINHENIVsLEDIYESPTHLYLAMELVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHlhIIE----TKFEMIKLIdiaRQTAQGMDYLHAKSIIHRDLKSNNIFLH---EDLTVKIGDFGLatvkSRWSG 606
Cdd:cd14169    85 GGELFDR--IIErgsyTEKDASQLI---GQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGL----SKIEA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 607 SHQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINN 661
Cdd:cd14169   156 QGMLSTACGTPGYVAPELL---EQKPYGKAVDVWAIGVISYILLCGYPPFYDEND 207
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
463-715 3.07e-17

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: 82.62  E-value: 3.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHG-DVAVKMLNVTAPTpqQLQA----FKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGSS 536
Cdd:cd14160     1 IGEGEIFEVYRVRIGNrSYAVKLFKQEKKM--QWKKhwkrFLSELEVLLLFQHPNILELAAYFTETEkFCLVYPYMQNGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLH--IIETKFEMIKLIDIARQTAQGMDYLHAK---SIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwsgshQFE 611
Cdd:cd14160    79 LFDRLQchGVTKPLSWHERINILIGIAKAIHYLHNSqpcTVICGNISSANILLDDQMQPKLTDFALAHFRP------HLE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 612 QLSGSI---------LWMAPEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQL----PYSNINNRDQIIFMVGRGYLSPDL 678
Cdd:cd14160   153 DQSCTInmttalhkhLWYMPEEYIRQGK--LSVKTDVYSFGIVIMEVLTGCKvvldDPKHLQLRDLLHELMEKRGLDSCL 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 679 S---KVRSNCPKAMK----RLMAECLKKKRDERPLFPQILASIE 715
Cdd:cd14160   231 SfldLKFPPCPRNFSaklfRLAGRCTATKAKLRPDMDEVLQRLE 274
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
463-656 3.23e-17

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 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: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 83.31  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG--KWHGD-VAVKMLN-VTAPTPQQLQafKNEVGVLRKTRHVNILLFMGY---STKPQLAIVTQWCEGS 535
Cdd:cd13988     1 LGQGATANVFRGrhKKTGDlYAVKVFNnLSFMRPLDVQ--MREFEVLKKLNHKNIVKLFAIeeeLTTRHKVLVMELCPCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIK--LIDIARQTAQGMDYLHAKSIIHRDLKSNNI--FLHEDLTV--KIGDFGLAtvkSRWSGSHQ 609
Cdd:cd13988    79 SLYTVLEEPSNAYGLPEseFLIVLRDVVAGMNHLRENGIVHRDIKPGNImrVIGEDGQSvyKLTDFGAA---RELEDDEQ 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 610 FEQLSGSILWMAPE-----VIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd13988   156 FVSLYGTEEYLHPDmyeraVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
466-649 3.25e-17

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) 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. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors 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. The ACVR2a 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: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 82.78  E-value: 3.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 466 GSFGTVYKGKWHGD-VAVKMLNVtaptpQQLQAFKNEVGV--LRKTRHVNILLFMGYSTK-----PQLAIVTQWCEGSSL 537
Cdd:cd14141     6 GRFGCVWKAQLLNEyVAVKIFPI-----QDKLSWQNEYEIysLPGMKHENILQFIGAEKRgtnldVDLWLITAFHEKGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIIETKFEmiKLIDIARQTAQGMDYLHAK----------SIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGS 607
Cdd:cd14141    81 TDYLKANVVSWN--ELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSA 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1237938074 608 HQFEQLSGSILWMAPEVIrmqdKNPYSFQS------DVYAFGIVLYEL 649
Cdd:cd14141   159 GDTHGQVGTRRYMAPEVL----EGAINFQRdaflriDMYAMGLVLWEL 202
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
453-656 4.23e-17

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: 81.79  E-value: 4.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVY--KGKWHGDVAvkMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVT 529
Cdd:cd14111     1 PQKPYTFLDEKARGRFGVIRrcRENATGKNF--PAKIVPYQAEEKQGVLQEYEILKSLHHERIMaLHEAYITPRYLVLIA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSgSHQ 609
Cdd:cd14111    79 EFCSGKELLHSL-IDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLS-LRQ 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 610 FEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14111   157 LGRRTGTLEYMAPEMVK---GEPVGPPADIWSIGVLTYIMLSGRSPF 200
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
461-680 5.58e-17

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: 82.10  E-value: 5.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKG----KWHGDVAVKM-----LNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQ 530
Cdd:cd14096     7 NKIGEGAFSNVYKAvplrNTGKPVAIKVvrkadLSSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEyYYIVLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHlhIIE-TKFEMikliDIAR----QTAQGMDYLHAKSIIHRDLKSNNIF---------------LHEDLT- 589
Cdd:cd14096    87 LADGGEIFHQ--IVRlTYFSE----DLSRhvitQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkADDDETk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 590 -----------------VKIGDFGLAtvKSRWsgSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTG 652
Cdd:cd14096   161 vdegefipgvggggigiVKLADFGLS--KQVW--DSNTKTPCGTVGYTAPEVVK---DERYSKKVDMWALGCVLYTLLCG 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1237938074 653 QLPYSNiNNRDQIIFMVGRGY---LSP---DLSK 680
Cdd:cd14096   234 FPPFYD-ESIETLTEKISRGDytfLSPwwdEISK 266
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
463-657 6.21e-17

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: 82.07  E-value: 6.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY--KGKWHGD-VAVKMLNVTAPTP-QQLQAFKNEVGVLRKTRHVNiLLFMGYSTK--PQLAIVTQWCEGSS 536
Cdd:cd14209     9 LGTGSFGRVMlvRHKETGNyYAMKILDKQKVVKlKQVEHTLNEKRILQAINFPF-LVKLEYSFKdnSNLYMVMEYVPGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIEtKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKSR-WSgshqfeqLS 614
Cdd:cd14209    88 MFSHLRRIG-RFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKrVKGRtWT-------LC 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1237938074 615 GSILWMAPEVIrmQDKnPYSFQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd14209   160 GTPEYLAPEII--LSK-GYNKAVDWWALGVLIYEMAAGYPPFF 199
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
461-704 6.44e-17

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: 81.09  E-value: 6.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYK--GKWHGDV-AVKMLNVtaPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd14114     8 EELGTGAFGVVHRctERATGNNfAAKFIMT--PHESDKETVRKEIQIMNQLHHPKLInLHDAFEDDNEMVLILEFLSGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH--EDLTVKIGDFGLATvksRWSGSHQFEQLS 614
Cdd:cd14114    86 LFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLAT---HLDPKESVKVTT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYLSPDLSKVRSNCPKAmKRLMA 694
Cdd:cd14114   163 GTAEFAAPEIV---EREPVGFYTDMWAVGVLSYVLLSGLSPFAG-ENDDETLRNVKSCDWNFDDSAFSGISEEA-KDFIR 237
                         250
                  ....*....|
gi 1237938074 695 ECLKKKRDER 704
Cdd:cd14114   238 KLLLADPNKR 247
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
461-656 6.87e-17

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: 81.70  E-value: 6.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYK--GKWHGDV-AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd14086     7 EELGKGAFSVVRRcvQKSTGQEfAAKIINTKKLSARDHQKLEREARICRLLKHPNIVrLHDSISEEGFHYLVFDLVTGGE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LyhhlhiietkFEMIklidIAR-------------QTAQGMDYLHAKSIIHRDLKSNNIFL---HEDLTVKIGDFGLATV 600
Cdd:cd14086    87 L----------FEDI----VARefyseadashciqQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 601 ----KSRWSGshqfeqLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14086   153 vqgdQQAWFG------FAGTPGYLSPEVLR---KDPYGKPVDIWACGVILYILLVGYPPF 203
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
235-280 8.44e-17

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 74.79  E-value: 8.44e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 235 HNFVRKTFFTLAFCDFCRKLL----FQGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLwglgKQGLKCSWCKLNVHKRCHEKVPPEC 50
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
462-724 9.04e-17

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: 81.59  E-value: 9.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYK------GKWhgdVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEg 534
Cdd:cd07833     8 VVGEGAYGVVLKcrnkatGEI---VAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVnLKEAFRRKGRLYLVFEYVE- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLyhhLHIIETK-----FEMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT---------- 599
Cdd:cd07833    84 RTL---LELLEASpgglpPDAVRSY--IWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARaltarpaspl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 600 ---VKSRWsgshqfeqlsgsilWMAPEVIrMQDKNpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQiifmvgrgylsp 676
Cdd:cd07833   159 tdyVATRW--------------YRAPELL-VGDTN-YGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQ------------ 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1237938074 677 dLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILaSIELLARSLPKI 724
Cdd:cd07833   211 -LYLIQKCLGPLPPSHQELFSSNPRFAGVAFPEPS-QPESLERRYPGK 256
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
515-657 9.77e-17

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: 82.05  E-value: 9.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 515 LFMGYSTKPQLAIVTQWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGD 594
Cdd:cd05592    61 LFCTFQTESHLFFVMEYLNGGDLMFHIQQ-SGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIAD 139
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 595 FGLAtvKSRWSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd05592   140 FGMC--KENIYGENKASTFCGTPDYIAPEILKGQK---YNQSVDWWSFGVLLYEMLIGQSPFH 197
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
549-690 1.29e-16

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: 80.45  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 549 EMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHE-DLT-VKIGDFGLatvkSRWSGShQFEQLSGSILWMAPEVIR 626
Cdd:cd13987    91 ERVKRC--AAQLASALDFMHSKNLVHRDIKPENVLLFDkDCRrVKLCDFGL----TRRVGS-TVKRVSGTIPYTAPEVCE 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 627 MQDKNPYSFQ--SDVYAFGIVLYELMTGQLPYSNINNRDQII--FMVGRGYLSPDL-SKVRSNCPKAMK 690
Cdd:cd13987   164 AKKNEGFVVDpsIDVWAFGVLLFCCLTGNFPWEKADSDDQFYeeFVRWQKRKNTAVpSQWRRFTPKALR 232
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
440-656 1.39e-16

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 81.79  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 440 TLGRRDSSDdWEIPDGQItvGQRIGSGSFGTVY--KGKWHGD-VAVKMLNVTAPTP-QQLQAFKNEVGVLRKTRHVNILL 515
Cdd:PTZ00263    6 MFTKPDTSS-WKLSDFEM--GETLGTGSFGRVRiaKHKGTGEyYAIKCLKKREILKmKQVQHVAQEKSILMELSHPFIVN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 516 FM-GYSTKPQLAIVTQWCEGSSLYHHLHIiETKFEMikliDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTV 590
Cdd:PTZ00263   83 MMcSFQDENRVYFLLEFVVGGELFTHLRK-AGRFPN----DVAKfyhaELVLAFEYLHSKDIIYRDLKPENLLLDNKGHV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 591 KIGDFGLAT-VKSRwsgshQFeQLSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPY 656
Cdd:PTZ00263  158 KVTDFGFAKkVPDR-----TF-TLCGTPEYLAPEVIQSKGHGK---AVDWWTMGVLLYEFIAGYPPF 215
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
471-710 1.46e-16

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: 80.29  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 471 VYKGKwhgDVAVKMLNVTAPTPQQlqAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEGSSLYHHLHIIETKFE 549
Cdd:cd14045    27 IYDGR---TVAIKKIAKKSFTLSK--RIRKEVKQVRELDHPNLCKFIGGCIEvPNVAIITEYCPKGSLNDVLLNEDIPLN 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 550 MIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR--WSGSHQFEQLSGSIlWMAPEVIRM 627
Cdd:cd14045   102 WGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEdgSENASGYQQRLMQV-YLPPENHSN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 628 QDKNPySFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLF 707
Cdd:cd14045   181 TDTEP-TQATDVYSYAIILLEIATRNDPVPEDDYSLDEAWCPPLPELISGKTENSCPCPADYVELIRRCRKNNPAQRPTF 259

                  ...
gi 1237938074 708 PQI 710
Cdd:cd14045   260 EQI 262
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
515-658 1.52e-16

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: 80.72  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 515 LFMGYSTKPQLAIVTQWCEGSSL-YHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIG 593
Cdd:cd05607    67 LAYAFETKTHLCLVMSLMNGGDLkYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLS 146
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 594 DFGLATvksRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSN 658
Cdd:cd05607   147 DLGLAV---EVKEGKPITQRAGTNGYMAPEILK---EESYSYPVDWFAMGCSIYEMVAGRTPFRD 205
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
461-738 1.57e-16

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: 80.60  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKG--KWHGD-VAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGS- 535
Cdd:cd07836     6 EKLGEGTYATVYKGrnRTTGEiVALKEIHLDAEEGTPSTAIR-EISLMKELKHENIVrLHDVIHTENKLMLVFEYMDKDl 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRWSG--SHQFEQL 613
Cdd:cd07836    85 KKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLA----RAFGipVNTFSNE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 SGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI--IFMVgRGYLSPDLSKVRSNCPKaMKR 691
Cdd:cd07836   161 VVTLWYRAPDV--LLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLlkIFRI-MGTPTESTWPGISQLPE-YKP 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 692 LMAEClkKKRDERPLFPQILA-SIELLARSL---PKIHRSASEpSLNRAGF 738
Cdd:cd07836   237 TFPRY--PPQDLQQLFPHADPlGIDLLHRLLqlnPELRISAHD-ALQHPWF 284
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
519-656 1.60e-16

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: 81.28  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKPQLAIVTQWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd05587    66 FQTMDRLYFVMEYVNGGDLMYHIQQ-VGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMC 144
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 599 tvKSRWSGSHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05587   145 --KEGIFGGKTTRTFCGTPDYIAPEIIAYQ---PYGKSVDWWAYGVLLYEMLAGQPPF 197
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
463-656 1.63e-16

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: 81.17  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQA-FKNEVGVLRKTRHVNILLFMGYS--TKPQLAIVTQWCEGSS 536
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDgkfYAVKVLQKKTILKKKEQNhIMAERNVLLKNLKHPFLVGLHYSfqTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksrwSGSHQFEQLS-- 614
Cdd:cd05603    83 LFFHLQR-ERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCK-----EGMEPEETTStf 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1237938074 615 -GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05603   157 cGTPEYLAPEVLR---KEPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
460-657 1.82e-16

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: 80.13  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVY------KGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY---STKPQLAIVTQ 530
Cdd:cd06651    12 GKLLGQGAFGRVYlcydvdTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNLQHERIVQYYGClrdRAEKTLTIFME 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIIETKFEMIKLiDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG----LATVKSRWSG 606
Cdd:cd06651    92 YMPGGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrLQTICMSGTG 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 607 shqFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd06651   171 ---IRSVTGTPYWMSPEVISGEG---YGRKADVWSLGCTVVEMLTEKPPWA 215
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
463-704 2.38e-16

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: 81.23  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTV--YKGKWHGDV-AVKMLNvtaptpQQLQAFKNEVG-------VLRKTRHvNILLFMGYS--TKPQLAIVTQ 530
Cdd:cd05594    33 LGKGTFGKVilVKEKATGRYyAMKILK------KEVIVAKDEVAhtltenrVLQNSRH-PFLTALKYSfqTHDRLCFVME 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHA-KSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQ 609
Cdd:cd05594   106 YANGGELFFHLSR-ERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLC--KEGIKDGAT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 610 FEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVgrgyLSPDLSKVRSNCPKAm 689
Cdd:cd05594   183 MKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELI----LMEEIRFPRTLSPEA- 253
                         250
                  ....*....|....*
gi 1237938074 690 KRLMAECLKKKRDER 704
Cdd:cd05594   254 KSLLSGLLKKDPKQR 268
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
492-663 2.75e-16

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: 79.19  E-value: 2.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 492 PQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAK 570
Cdd:cd14110    40 PEDKQLVLREYQVLRRLSHPRIAqLHSAYLSPRHLVLIEELCSGPELLYNL-AERNSYSEAEVTDYLWQILSAVDYLHSR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 571 SIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwSGSHQFEQLSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELM 650
Cdd:cd14110   119 RILHLDLRSENMIITEKNLLKIVDLGNAQPFNQ-GKVLMTDKKGDYVETMAPELLEGQGAGP---QTDIWAIGVTAFIML 194
                         170
                  ....*....|...
gi 1237938074 651 TGQLPYSNINNRD 663
Cdd:cd14110   195 SADYPVSSDLNWE 207
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
559-717 2.82e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 82.37  E-value: 2.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 559 QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvkSRWSGSHQFEQLS---GSILWMAPEVirmQDKNPYSF 635
Cdd:PTZ00267  177 QIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFS---KQYSDSVSLDVASsfcGTPYYLAPEL---WERKRYSK 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 636 QSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYLSPDLSKVRSncpkAMKRLMAECLKKKRDERPLFPQILASiE 715
Cdd:PTZ00267  251 KADMWSLGVILYELLTLHRPFKGPSQR-EIMQQVLYGKYDPFPCPVSS----GMKALLDPLLSKNPALRPTTQQLLHT-E 324

                  ..
gi 1237938074 716 LL 717
Cdd:PTZ00267  325 FL 326
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
463-705 2.87e-16

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: 79.23  E-value: 2.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG---KWHGDVAVKML-NVTAPTPQQLqafkNEVGVLR------KTRHVNILLFMGYST-KPQLAIVTQW 531
Cdd:cd14133     7 LGKGTFGQVVKCydlLTGEEVALKIIkNNKDYLDQSL----DEIRLLEllnkkdKADKYHIVRLKDVFYfKNHLCIVFEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CeGSSLYHHLHIIETKFEMIKLI-DIARQTAQGMDYLHAKSIIHRDLKSNNIFL--HEDLTVKIGDFGLATVKSRwsGSH 608
Cdd:cd14133    83 L-SQNLYEFLKQNKFQYLSLPRIrKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGSSCFLTQ--RLY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 QFEQlsgSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVG-RGYLSPDLSKVRSNCPK 687
Cdd:cd14133   160 SYIQ---SRYYRAPEVIL---GLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGtIGIPPAHMLDQGKADDE 233
                         250
                  ....*....|....*...
gi 1237938074 688 AMKRLMAECLKKKRDERP 705
Cdd:cd14133   234 LFVDFLKKLLEIDPKERP 251
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
480-690 3.44e-16

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. 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. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 80.30  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 480 VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLI-DIA 557
Cdd:cd08226    28 VTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMtHWTVFTEGSWLWVISPFMAYGSARGLLKTYFPEGMNEALIgNIL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 558 RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKI----GDFGLATVKSRWSGSHQFEQLSGSIL-WMAPEVIRmQDKNP 632
Cdd:cd08226   108 YGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLsglsHLYSMVTNGQRSKVVYDFPQFSTSVLpWLSPELLR-QDLHG 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 633 YSFQSDVYAFGIVLYELMTGQLPYSNInNRDQIIFMVGRGYL-SPDLSKVRSNCPKAMK 690
Cdd:cd08226   187 YNVKSDIYSVGITACELARGQVPFQDM-RRTQMLLQKLKGPPySPLDIFPFPELESRMK 244
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
479-656 3.59e-16

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 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). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. 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 PhKG1 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: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 79.57  E-value: 3.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 479 DVAVKMLNVTA---PTPQQLQAFKN----EVGVLRKTR-HVNIL-LFMGYSTKPQLAIVTQWCEGSSLYHHL--HIIETK 547
Cdd:cd14182    30 EYAVKIIDITGggsFSPEEVQELREatlkEIDILRKVSgHPNIIqLKDTYETNTFFFLVFDLMKKGELFDYLteKVTLSE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 548 FEMIKLIdiaRQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGSHQFEQLSGSILWMAPEVIR- 626
Cdd:cd14182   110 KETRKIM---RALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSC---QLDPGEKLREVCGTPGYLAPEIIEc 183
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1237938074 627 -MQDKNP-YSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14182   184 sMDDNHPgYGKEVDMWSTGVIMYTLLAGSPPF 215
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
461-661 4.24e-16

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: 79.23  E-value: 4.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKG--KWHGD-VAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMGY-STKPQLAIVTQWCE--- 533
Cdd:cd07870     6 EKLGEGSYATVYKGisRINGQlVALKVISMKTEEGVPFTAIR-EASLLKGLKHANIVLLHDIiHTKETLTFVFEYMHtdl 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHH---LHIIETKFEMIKLIdiarqtaQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQF 610
Cdd:cd07870    85 AQYMIQHpggLHPYNVRLFMFQLL-------RGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSS 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 611 EQLSgsiLWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMTGQLPYSNINN 661
Cdd:cd07870   158 EVVT---LWYRPPDVLLGATD-YSSALDIWGAGCIFIEMLQGQPAFPGVSD 204
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
456-711 4.28e-16

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: 79.25  E-value: 4.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGD---VAVKMLNVtaPTPQQLQAFKNEVGVLRK-TRHVNILLFMGYSTKP------QL 525
Cdd:cd14037     4 HVTIEKYLAEGGFAHVYLVKTSNGgnrAALKRVYV--NDEHDLNVCKREIEIMKRlSGHKNIVGYIDSSANRsgngvyEV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLYH----HLHIIETKFEMIKlidIARQTAQGMDYLHA--KSIIHRDLKSNNIFLHEDLTVKIGDFGLAT 599
Cdd:cd14037    82 LLLMEYCKGGGVIDlmnqRLQTGLTESEILK---IFCDVCEAVAAMHYlkPPLIHRDLKVENVLISDSGNYKLCDFGSAT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 600 VKSRWSGSHQ-FEQLSGSIL------WMAPEVIRMQDKNPYSFQSDVYAFGIVLYEL--------MTGQLPYSNINnrdq 664
Cdd:cd14037   159 TKILPPQTKQgVTYVEEDIKkyttlqYRAPEMIDLYRGKPITEKSDIWALGCLLYKLcfyttpfeESGQLAILNGN---- 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 665 iifmvgrgYLSPDLSKVRSNcpkaMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd14037   235 --------FTFPDNSRYSKR----LHKLIRYMLEEDPEKRPNIYQVS 269
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
463-711 4.30e-16

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: 78.90  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPqqlqafkNEVGVLRKTRHVNILLFMGYSTKPQ-LAIVTQWCEGSSLY 538
Cdd:cd13995    12 IPRGAFGKVYLAqdtKTKKRMACKLIPVEQFKP-------SDVEIQACFRHENIAELYGALLWEEtVHLFMEAGEGGSVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKFEMiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIgDFGLaTVKSRwSGSHQFEQLSGSIL 618
Cdd:cd13995    85 EKLESCGPMREF-EIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGL-SVQMT-EDVYVPKDLRGTEI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 619 WMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRD---QIIFMVGRGylSPDLSKVRSNCPKAMKRLMAE 695
Cdd:cd13995   161 YMSPEVILCRG---HNTKADIYSLGATIIHMQTGSPPWVRRYPRSaypSYLYIIHKQ--APPLEDIAQDCSPAMRELLEA 235
                         250
                  ....*....|....*.
gi 1237938074 696 CLKKKRDERPLFPQIL 711
Cdd:cd13995   236 ALERNPNHRSSAAELL 251
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
466-651 4.31e-16

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) 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. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors 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. The ACVR2b 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: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 79.69  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 466 GSFGTVYKGKWHGD-VAVKMLNVtaptpQQLQAFKNEVGVLRK--TRHVNILLFM-----GYSTKPQLAIVTQWCEGSSL 537
Cdd:cd14140     6 GRFGCVWKAQLMNEyVAVKIFPI-----QDKQSWQSEREIFSTpgMKHENLLQFIaaekrGSNLEMELWLITAFHDKGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLhiietKFEMI---KLIDIARQTAQGMDYLHAK-----------SIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR 603
Cdd:cd14140    81 TDYL-----KGNIVswnELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEP 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 604 WSGSHQFEQLSGSILWMAPEVIrmqdKNPYSFQS------DVYAFGIVLYELMT 651
Cdd:cd14140   156 GKPPGDTHGQVGTRRYMAPEVL----EGAINFQRdsflriDMYAMGLVLWELVS 205
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
461-656 4.35e-16

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: 78.84  E-value: 4.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGDVAVKMLNVTAPT---PQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd14161     9 ETLGKGTYGRVKKARDSSGRLVAIKSIRKDRikdEQDLLHIRREIEIMSSLNHPHIIsVYEVFENSSKIVIVMEYASRGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHiietkfEMIKLIDIA-----RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSHQFE 611
Cdd:cd14161    89 LYDYIS------ERQRLSELEarhffRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNL---YNQDKFLQ 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1237938074 612 QLSGSILWMAPEVIrmqDKNPYSF-QSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14161   160 TYCGSPLYASPEIV---NGRPYIGpEVDSWSLGVLLYILVHGTMPF 202
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
463-720 4.38e-16

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: 79.48  E-value: 4.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK---GKWHGDVAVKMLnvTAPTPQQLQAFKNEVGVLRKTR-HVNILLFMGYST---------KPQLAIVT 529
Cdd:cd14036     8 IAEGGFAFVYEaqdVGTGKEYALKRL--LSNEEEKNKAIIQEINFMKKLSgHPNIVQFCSAASigkeesdqgQAEYLLLT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSsLYHHLHIIETK--FEMIKLIDIARQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDLTVKIGDFGLATVKS--- 602
Cdd:cd14036    86 ELCKGQ-LVDFVKKVEAPgpFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAhyp 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 --RWSgSHQFEQLSGSI------LWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIfmVGRGYL 674
Cdd:cd14036   165 dySWS-AQKRSLVEDEItrnttpMYRTPEMIDLYSNYPIGEKQDIWALGCILYLLCFRKHPFED-GAKLRII--NAKYTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1237938074 675 SPDLSKVrsncpKAMKRLMAECLKKKRDERPLFPQILASIELLARS 720
Cdd:cd14036   241 PPNDTQY-----TVFHDLIRSTLKVNPEERLSITEIVEQLQELAAA 281
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
463-657 4.39e-16

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK 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: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 78.97  E-value: 4.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY-----KGKWHGDV-AVKMLNVTAPTPQQ--LQAFKNEVGVLRKTRHVNIL--LFMGYSTKPQLAIVTQWC 532
Cdd:cd05583     2 LGTGAYGKVFlvrkvGGHDAGKLyAMKVLKKATIVQKAktAEHTMTERQVLEAVRQSPFLvtLHYAFQTDAKLHLILDYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLHIIETKFEMIKLIDIARQTAqGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT--VKSRWSGSHQF 610
Cdd:cd05583    82 NGGELFTHLYQREHFTESEVRIYIGEIVL-ALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKefLPGENDRAYSF 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 611 eqlSGSILWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd05583   161 ---CGTIEYMAPEVVRGGSDG-HDKAVDWWSLGVLTYELLTGASPFT 203
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
459-693 4.56e-16

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: 78.84  E-value: 4.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGK-WHGD--VAVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 534
Cdd:cd14185     4 IGRTIGDGNFAVVKECRhWNENqeYAMKIIDKSKLKGKE-DMIESEILIIKSLSHPNIVkLFEVYETEKEIYLILEYVRG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHlhIIET-KF----EMIKLIDIArqtaQGMDYLHAKSIIHRDLKSNNIFLHED----LTVKIGDFGLATVKSRws 605
Cdd:cd14185    83 GDLFDA--IIESvKFtehdAALMIIDLC----EALVYIHSKHIVHRDLKPENLLVQHNpdksTTLKLADFGLAKYVTG-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 gshQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPY-SNINNRDQIIFMVGRG---YLSPDLSKV 681
Cdd:cd14185   155 ---PIFTVCGTPTYVAPEIL---SEKGYGLEVDMWAAGVILYILLCGFPPFrSPERDQEELFQIIQLGhyeFLPPYWDNI 228
                         250
                  ....*....|..
gi 1237938074 682 RSNCPKAMKRLM 693
Cdd:cd14185   229 SEAAKDLISRLL 240
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
459-656 4.82e-16

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: 78.91  E-value: 4.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAPTPQQL----QAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQ 530
Cdd:cd14194     9 TGEELGSGQFAVVKKCREKStglQYAAKFIKKRRTKSSRRgvsrEDIEREVSILKEIQHPNVItLHEVYENKTDVILILE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIIETKFEMiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT----VKIGDFGLAtvkSRWSG 606
Cdd:cd14194    89 LVAGGELFDFLAEKESLTEE-EATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLA---HKIDF 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14194   165 GNEFKNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 211
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
463-656 5.52e-16

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: 78.88  E-value: 5.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY------KGKWHGDVAVKMLNVTAPTpqqlqAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGS 535
Cdd:cd14166    11 LGSGAFSEVYlvkqrsTGKLYALKCIKKSPLSRDS-----SLENEIAVLKRIKHENIVTLEDiYESTTHYYLVMQLVSGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHlhIIE----TKFEMIKLIdiaRQTAQGMDYLHAKSIIHRDLKSNNIFL---HEDLTVKIGDFGLatvkSRWSGSH 608
Cdd:cd14166    86 ELFDR--ILErgvyTEKDASRVI---NQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGL----SKMEQNG 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1237938074 609 QFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14166   157 IMSTACGTPGYVAPEVLA---QKPYSKAVDCWSIGVITYILLCGYPPF 201
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
460-711 6.11e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 79.87  E-value: 6.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGS 535
Cdd:PLN00034   79 VNRIGSGAGGTVYKVIHRPTgrlYALKVIYGNHEDTVRRQICR-EIEILRDVNHPNVVKCHDmFDHNGEIQVLLEFMDGG 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHlHIIETKFemikLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG----LATVKSRWSGShqfe 611
Cdd:PLN00034  158 SLEGT-HIADEQF----LADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGvsriLAQTMDPCNSS---- 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 612 qlSGSILWMAPEVIRMQ-DKNPYS-FQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPdlSKVRSNCPKAM 689
Cdd:PLN00034  229 --VGTIAYMSPERINTDlNHGAYDgYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQP--PEAPATASREF 304
                         250       260
                  ....*....|....*....|..
gi 1237938074 690 KRLMAECLKKKRDERPLFPQIL 711
Cdd:PLN00034  305 RHFISCCLQREPAKRWSAMQLL 326
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
459-659 6.17e-16

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: 78.28  E-value: 6.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTV---YKGKWHGDVAVKMLNvTAPTPQQ-LQAF-KNEVGVLRKTRHVNIL----LFMGYSTKpqLAIVT 529
Cdd:cd14165     5 LGINLGEGSYAKVksaYSERLKCNVAIKIID-KKKAPDDfVEKFlPRELEILARLNHKSIIktyeIFETSDGK--VYIVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLyhhLHIIETKFEMIKliDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWS 605
Cdd:cd14165    82 ELGVQGDL---LEFIKLRGALPE--DVARkmfhQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDE 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 606 G-----SHQFeqlSGSILWMAPEVIRMQDKNPYsfQSDVYAFGIVLYELMTGQLPY--SNI 659
Cdd:cd14165   157 NgrivlSKTF---CGSAAYAAPEVLQGIPYDPR--IYDIWSLGVILYIMVCGSMPYddSNV 212
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
461-663 6.20e-16

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: 78.75  E-value: 6.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTV-----YKGKWHGDVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNILLFMGY--STKPQLaIVTQWCE 533
Cdd:cd05086     3 QEIGNGWFGKVllgeiYTGTSVARVVVKELKASA-NPKEQDDFLQQGEPYYILQHPNILQCVGQcvEAIPYL-LVFEFCD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKF----EMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQ 609
Cdd:cd05086    81 LGDLKTYLANQQEKLrgdsQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFSRYKEDYIET 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 610 FEQLSGSILWMAPE-VIRMQDKNPYSFQ---SDVYAFGIVLYELM-TGQLPYSNINNRD 663
Cdd:cd05086   161 DDKKYAPLRWTAPElVTSFQDGLLAAEQtkySNIWSLGVTLWELFeNAAQPYSDLSDRE 219
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
460-706 6.35e-16

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: 78.30  E-value: 6.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVY--KGKW-HGDVAVKmlNVTAPTPQQLQAFKNEVGVLRK-TRHVNILLFMG------YS--TKPQLAI 527
Cdd:cd13975     5 GRELGRGQYGVVYacDSWGgHFPCALK--SVVPPDDKHWNDLALEFHYTRSlPKHERIVSLHGsvidysYGggSSIAVLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQwcegsSLYHHLHI-IETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSG 606
Cdd:cd13975    83 IME-----RLHRDLYTgIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 ShqfeqLSGSILWMAPEVIrmqdKNPYSFQSDVYAFGIVLYELMTG--QLP--YSNINNRDQIIFMVGRGYLSPDLSKVR 682
Cdd:cd13975   158 S-----IVGTPIHMAPELF----SGKYDNSVDVYAFGILFWYLCAGhvKLPeaFEQCASKDHLWNNVRKGVRPERLPVFD 228
                         250       260
                  ....*....|....*....|....
gi 1237938074 683 SNCpkamKRLMAECLKKKRDERPL 706
Cdd:cd13975   229 EEC----WNLMEACWSGDPSQRPL 248
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
463-730 7.74e-16

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: 79.49  E-value: 7.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTV---YKGKWHGDVAVKMLNvtaptpqqlQAFKN---------EVGVLRKTRHVNIL----LF--MGYSTKPQ 524
Cdd:cd07834     8 IGSGAYGVVcsaYDKRTGRKVAIKKIS---------NVFDDlidakrilrEIKILRHLKHENIIglldILrpPSPEEFND 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 525 LAIVTQwcegssLYHH-LH-IIETKfemIKLIDIARQ--TAQ---GMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL 597
Cdd:cd07834    79 VYIVTE------LMETdLHkVIKSP---QPLTDDHIQyfLYQilrGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 ATVKsrwSGSHQFEQLSGSIL--WM-APEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ---IIFMVGr 671
Cdd:cd07834   150 ARGV---DPDEDKGFLTEYVVtrWYrAPELLLSSKK--YTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQlnlIVEVLG- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 672 gylSP---DLSKVRSncPKAMKRLMAECLKKKRDERPLFPQI--LAsIELLARSL---PKIHRSASE 730
Cdd:cd07834   224 ---TPseeDLKFISS--EKARNYLKSLPKKPKKPLSEVFPGAspEA-IDLLEKMLvfnPKKRITADE 284
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
494-740 7.94e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 80.04  E-value: 7.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 494 QLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSII 573
Cdd:PHA03212  126 QRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAA-KRNIAICDILAIERSVLRAIQYLHENRII 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 574 HRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSgSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQ 653
Cdd:PHA03212  205 HRDIKAENIFINHPGDVCLGDFGAACFPVDIN-ANKYYGWAGTIATNAPELLA---RDPYGPAVDIWSAGIVLFEMATCH 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 654 LPY-------SNINNRDQIIFMVGRGYLSPdlSKVRSNCPKAMKRLMAECLKK---KRDERPLFPQILA---SIELL--- 717
Cdd:PHA03212  281 DSLfekdgldGDCDSDRQIKLIIRRSGTHP--NEFPIDAQANLDEIYIGLAKKssrKPGSRPLWTNLYElpiDLEYLick 358
                         250       260
                  ....*....|....*....|...
gi 1237938074 718 ARSLPKIHRSASEPSLNRAGFQT 740
Cdd:PHA03212  359 MLAFDAHHRPSAEALLDFAAFQD 381
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
462-656 8.42e-16

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: 78.63  E-value: 8.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTP-QQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd05612     8 TIGTGTFGRVHLVRDRISehyYALKVMAIPEVIRlKQEQHVHNEKRVLKEVSHPFIIrLFWTEHDQRFLYMLMEYVPGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT--VKSRWSgshqfeqLS 614
Cdd:cd05612    88 LFSYLRN-SGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKklRDRTWT-------LC 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 615 GSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05612   160 GTPEYLAPEVIQSKGHNK---AVDWWALGILIYEMLVGYPPF 198
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
556-712 8.49e-16

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: 78.62  E-value: 8.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 556 IARQTAQGMDYLHAK-SIIHRDLKSNNIFLHEDLTVKIGDFGLA------TVKSRWSGSHQFeqlsgsilwMAPEVIRMQ 628
Cdd:cd06617   108 IAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISgylvdsVAKTIDAGCKPY---------MAPERINPE 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 629 -DKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGyLSPDLSKVRSNcpKAMKRLMAECLKKKRDERPLF 707
Cdd:cd06617   179 lNQKGYDVKSDVWSLGITMIELATGRFPYDSWKTPFQQLKQVVEE-PSPQLPAEKFS--PEFQDFVNKCLKKNYKERPNY 255

                  ....*
gi 1237938074 708 PQILA 712
Cdd:cd06617   256 PELLQ 260
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
463-652 9.19e-16

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. 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. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 78.74  E-value: 9.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG---KWHGDVAVKMLNVTAPTpqQLQAfKNEVGVLRKTRH---------VNIL---LFMGYstkpqLAI 527
Cdd:cd14210    21 LGKGSFGQVVKCldhKTGQLVAIKIIRNKKRF--HQQA-LVEVKILKHLNDndpddkhniVRYKdsfIFRGH-----LCI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTqwcE--GSSLYHHLHIieTKF-----EMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT--VKIGDFGla 598
Cdd:cd14210    93 VF---EllSINLYELLKS--NNFqglslSLIRKF--AKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFG-- 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 599 tvKSRWSG--SHQFEQlsgSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTG 652
Cdd:cd14210   164 --SSCFEGekVYTYIQ---SRFYRAPEVIL---GLPYDTAIDMWSLGCILAELYTG 211
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
458-700 9.49e-16

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: 78.33  E-value: 9.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAptpqQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCE 533
Cdd:cd14085     6 EIESELGRGATSVVYRCRQKGtqkPYAVKKLKKTV----DKKIVRTEIGVLLRLSHPNIIkLKEIFETPTEISLVLELVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHlhIIETKFEMIK-LIDIARQTAQGMDYLHAKSIIHRDLKSNNIF---LHEDLTVKIGDFGLATVKsrwsgSHQ 609
Cdd:cd14085    82 GGELFDR--IVEKGYYSERdAADAVKQILEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGLSKIV-----DQQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 610 --FEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFM----VGRGYLSPDLSKVRS 683
Cdd:cd14085   155 vtMKTVCGTPGYCAPEILRGC---AYGPEVDMWSVGVITYILLCGFEPFYD-ERGDQYMFKrilnCDYDFVSPWWDDVSL 230
                         250
                  ....*....|....*..
gi 1237938074 684 NCPKAMKRLMAECLKKK 700
Cdd:cd14085   231 NAKDLVKKLIVLDPKKR 247
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
462-653 1.10e-15

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. 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 CDKL1/4 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: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 78.18  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKwHGD----VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd07847     8 KIGEGSYGVVFKCR-NREtgqiVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVnLIEVFRRKRKLHLVFEYCDHTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LyHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT------------VKSRW 604
Cdd:cd07847    87 L-NELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARiltgpgddytdyVATRW 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 605 sgshqfeqlsgsilWMAPEVI--RMQdknpYSFQSDVYAFGIVLYELMTGQ 653
Cdd:cd07847   166 --------------YRAPELLvgDTQ----YGPPVDVWAIGCVFAELLTGQ 198
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
463-714 1.13e-15

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: 78.50  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGK-----WHGDVAVKMLNVTAPTPQQlQAFKNEVGVL-RKTRHVNILLFMGYST-KPQLAIVTQWCEGS 535
Cdd:cd05088    15 IGEGNFGQVLKARikkdgLRMDAAIKRMKEYASKDDH-RDFAGELEVLcKLGHHPNIINLLGACEhRGYLYLAIEYAPHG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLH---IIET------------KFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV 600
Cdd:cd05088    94 NLLDFLRksrVLETdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 601 KSRWsgshqFEQLSGS--ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQIIFMVGRGY-LSP 676
Cdd:cd05088   174 QEVY-----VKKTMGRlpVRWMAIESL---NYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCA-ELYEKLPQGYrLEK 244
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1237938074 677 DLskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASI 714
Cdd:cd05088   245 PL-----NCDDEVYDLMRQCWREKPYERPSFAQILVSL 277
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
462-669 1.30e-15

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: 77.81  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNI-LLFMGYSTKPQLAIVTQWCE---- 533
Cdd:cd07844     7 KLGEGSYATVYKGRSKLTgqlVALKEIRLEHEEGAPFTAIR-EASLLKDLKHANIvTLHDIIHTKKTLTLVFEYLDtdlk 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 ------GSSLYHHlhiiETKFEMIKLIdiarqtaQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGS 607
Cdd:cd07844    86 qymddcGGGLSMH----NVRLFLFQLL-------RGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSKT 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 608 HQFEQLSgsiLWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMTGQLPY---SNINNRDQIIFMV 669
Cdd:cd07844   155 YSNEVVT---LWYRPPDVLLGSTE-YSTSLDMWGVGCIFYEMATGRPLFpgsTDVEDQLHKIFRV 215
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
463-656 1.38e-15

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: 77.39  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK------GKwhgDVAVKMLNVTAPTPQQLQAFKNEVGVLR----KTRHVNilLFMGYSTKPQLAIVTQWC 532
Cdd:cd14106    16 LGRGKFAVVRKcihketGK---EYAAKFLRKRRRGQDCRNEILHEIAVLElckdCPRVVN--LHEVYETRSELILILELA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL-----HEDLtvKIGDFGLATVKSrwSGS 607
Cdd:cd14106    91 AGGELQTLL-DEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtsefpLGDI--KLCDFGISRVIG--EGE 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1237938074 608 HQFEQLsGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14106   166 EIREIL-GTPDYVAPEILSYE---PISLATDMWSIGVLTYVLLTGHSPF 210
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
458-705 1.45e-15

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: 77.30  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVYKGKWHGD---VAVKmlnvTAPTPQQLQAFKNEVGVLRKT---RHVniLLFMGYSTKPQLA-IVTQ 530
Cdd:cd14017     3 KVVKKIGGGGFGEIYKVRDVVDgeeVAMK----VESKSQPKQVLKMEVAVLKKLqgkPHF--CRLIGCGRTERYNyIVMT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCeGSSLYHHLHII-ETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH----EDLTVKIGDFGLAtvksrws 605
Cdd:cd14017    77 LL-GPNLAELRRSQpRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGrgpsDERTVYILDFGLA------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 gsHQFEQLSGSILWMAPEV-----------IRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMvGRGYL 674
Cdd:cd14017   149 --RQYTNKDGEVERPPRNAagfrgtvryasVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLKDKEEVGKM-KEKID 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 675 SPDLSKvrsNCPKAMKRLMAECLKKKRDERP 705
Cdd:cd14017   226 HEELLK---GLPKEFFQILKHIRSLSYFDTP 253
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
558-710 1.86e-15

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; 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). 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 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: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 77.40  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 558 RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGlatVKSRWSGSHQF-EQLSGSILWMAPEVIRmQDKNPYSFQ 636
Cdd:cd14118   122 RDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG---VSNEFEGDDALlSSTAGTPAFMAPEALS-ESRKKFSGK 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 637 S-DVYAFGIVLYELMTGQLPYSNINN-------RDQIIFMVGRGYLSPDLskvrsncpkamKRLMAECLKKKRDERPLFP 708
Cdd:cd14118   198 AlDIWAMGVTLYCFVFGRCPFEDDHIlglhekiKTDPVVFPDDPVVSEQL-----------KDLILRMLDKNPSERITLP 266

                  ..
gi 1237938074 709 QI 710
Cdd:cd14118   267 EI 268
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
463-656 1.88e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. 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 GRK1 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: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 77.61  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY------KGKWHgdvAVKMLNvtaptPQQLQAFKNEVGVLRKTR-----HVNILLFMGYS--TKPQLAIVT 529
Cdd:cd05608     9 LGKGGFGEVSacqmraTGKLY---ACKKLN-----KKRLKKRKGYEGAMVEKRilakvHSRFIVSLAYAfqTKTDLCLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIIETK---FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSG 606
Cdd:cd05608    81 TIMNGGDLRYHIYNVDEEnpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELK--DG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05608   159 QTKTKGYAGTPGFMAPELLLGEE---YDYSVDYFTLGVTLYEMIAARGPF 205
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
459-656 2.17e-15

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: 76.97  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAPTPQQL----QAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQ 530
Cdd:cd14195     9 MGEELGSGQFAIVRKCREKGtgkEYAAKFIKKRRLSSSRRgvsrEEIEREVNILREIQHPNIITLHDiFENKTDVVLILE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIIETKFEMiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT----VKIGDFGLAtvkSRWSG 606
Cdd:cd14195    89 LVSGGELFDFLAEKESLTEE-EATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIA---HKIEA 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14195   165 GNEFKNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 211
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
459-656 2.21e-15

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: 76.76  E-value: 2.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAPTPQQL----QAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQ 530
Cdd:cd14105     9 IGEELGSGQFAVVKKCREKStglEYAAKFIKKRRSKASRRgvsrEDIEREVSILRQVLHPNIItLHDVFENKTDVVLILE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIIETKFEMiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT----VKIGDFGLAtvkSRWSG 606
Cdd:cd14105    89 LVAGGELFDFLAEKESLSEE-EATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLA---HKIED 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14105   165 GNEFKNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 211
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
463-656 2.28e-15

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: 76.88  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK--GKWHG-DVAVKMLNvtAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLY 538
Cdd:cd14190    12 LGGGKFGKVHTctEKRTGlKLAAKVIN--KQNSKDKEMVLLEIQVMNQLNHRNLIqLYEAIETPNEIVLFMEYVEGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL--HEDLTVKIGDFGLAtvkSRWSGSHQFEQLSGS 616
Cdd:cd14190    90 ERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLA---RRYNPREKLKVNFGT 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1237938074 617 ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14190   167 PEFLSPEVVNYDQ---VSFPTDMWSMGVITYMLLSGLSPF 203
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
463-710 2.76e-15

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: 77.64  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTV----YKGKwhGDV-AVKMLN-VTAPTPQQLQAFKNEVGVLRKTRHVNIL--LFMGYSTKPQLAIVTQWCEG 534
Cdd:cd05570     3 LGKGSFGKVmlaeRKKT--DELyAIKVLKkEVIIEDDDVECTMTEKRVLALANRHPFLtgLHACFQTEDRLYFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLS 614
Cdd:cd05570    81 GDLMFHIQR-ARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMC--KEGIWGGNTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLP---------YSNINNrDQIIFMVgrgYLSPD-------- 677
Cdd:cd05570   158 GTPDYIAPEILREQD---YGFSVDWWALGVLLYEMLAGQSPfegddedelFEAILN-DEVLYPR---WLSREavsilkgl 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1237938074 678 LSKVRSN---C-PKAMKRLMA---------ECLKKKRDERPLFPQI 710
Cdd:cd05570   231 LTKDPARrlgCgPKGEADIKAhpffrnidwDKLEKKEVEPPFKPKV 276
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
463-656 3.03e-15

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: 77.73  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLN---VTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd05615    18 LGKGSFGKVMLAERKGSdelYAIKILKkdvVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIeTKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGS 616
Cdd:cd05615    98 LMYHIQQV-GKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMC--KEHMVEGVTTRTFCGT 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1237938074 617 ILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05615   175 PDYIAPEIIAYQ---PYGRSVDWWAYGVLLYEMLAGQPPF 211
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
463-665 3.19e-15

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: 77.51  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG---KWHGDVAVKMLNVTapTPQQLQAFKNEVGVLRKTRHVNILLF---MGYSTKPQLAIVTQWCEGSS 536
Cdd:cd07854    13 LGCGSNGLVFSAvdsDCDKRVAVKKIVLT--DPQSVKHALREIKIIRRLDHDNIVKVyevLGPSGSDLTEDVGSLTELNS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIETKF-----------EMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLH-EDLTVKIGDFGLA-TVKSR 603
Cdd:cd07854    91 VYIVQEYMETDLanvleqgplseEHARLF--MYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLArIVDPH 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 604 WSGSHQFEQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 665
Cdd:cd07854   169 YSHKGYLSEGLVTKWYRSPRL--LLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQM 228
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
456-713 3.24e-15

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: 76.12  E-value: 3.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGKWHGD---VAVK---------MLNVTAPTPQQLqafknEVGVLRKTRHVNIllfmgystkP 523
Cdd:cd14005     1 QYEVGDLLGKGGFGTVYSGVRIRDglpVAVKfvpksrvteWAMINGPVPVPL-----EIALLLKASKPGV---------P 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAIVTQWCEGSSlyHHLHIIE------TKFEMIK---------LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH-ED 587
Cdd:cd14005    67 GVIRLLDWYERPD--GFLLIMErpepcqDLFDFITergalsenlARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 588 LTVKIGDFGLATVKSRwsgsHQFEQLSGSILWMAPEVIRMQDKNPYSfqSDVYAFGIVLYELMTGQLPYsniNNRDQIIF 667
Cdd:cd14005   145 GEVKLIDFGCGALLKD----SVYTDFDGTRVYSPPEWIRHGRYHGRP--ATVWSLGILLYDMLCGDIPF---ENDEQILR 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1237938074 668 mvGRGYLSPDLSkvrsncpKAMKRLMAECLKKKRDERPLFPQILAS 713
Cdd:cd14005   216 --GNVLFRPRLS-------KECCDLISRCLQFDPSKRPSLEQILSH 252
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
463-704 3.58e-15

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: 77.36  E-value: 3.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQA-FKNEVGVLRKTRHVNILLFMGYS--TKPQLAIVTQWCEGSS 536
Cdd:cd05602    15 IGKGSFGKVLLARHKSDekfYAVKVLQKKAILKKKEEKhIMSERNVLLKNVKHPFLVGLHFSfqTTDKLYFVLDYINGGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQfeQLSGS 616
Cdd:cd05602    95 LFYHLQR-ERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTS--TFCGT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 617 ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYlspdlsKVRSNCPKAMKRLMAEC 696
Cdd:cd05602   172 PEYLAPEVLH---KQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPL------QLKPNITNSARHLLEGL 242

                  ....*...
gi 1237938074 697 LKKKRDER 704
Cdd:cd05602   243 LQKDRTKR 250
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
463-691 3.85e-15

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K 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: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 77.06  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKgkwhgdvaVKMLnvTAPTPQQLQAFKnevgVLRK---------TRHV----NIL----------LFMGY 519
Cdd:cd05584     4 LGKGGYGKVFQ--------VRKT--TGSDKGKIFAMK----VLKKasivrnqkdTAHTkaerNILeavkhpfivdLHYAF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 520 STKPQLAIVTQWCEGSSLYHHLhiiETkfEMIKLIDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDF 595
Cdd:cd05584    70 QTGGKLYLILEYLSGGELFMHL---ER--EGIFMEDTACfylaEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 596 GLAtvKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRG--- 672
Cdd:cd05584   145 GLC--KESIHDGTVTHTFCGTIEYMAPEILTRSGHGK---AVDWWSLGALMYDMLTGAPPFTA-ENRKKTIDKILKGkln 218
                         250       260
                  ....*....|....*....|..
gi 1237938074 673 ---YLSPDlskVRSNCPKAMKR 691
Cdd:cd05584   219 lppYLTNE---ARDLLKKLLKR 237
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
461-730 4.12e-15

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: 77.23  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP--QLAIVTQwCEGS 535
Cdd:cd07856    16 QPVGMGAFGLVCSARdqlTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPleDIYFVTE-LLGT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHI--IETKFEMIKLIDIARqtaqGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrwsgshQFEQL 613
Cdd:cd07856    95 DLHRLLTSrpLEKQFIQYFLYQILR----GLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI--------QDPQM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 614 SGSI---LWMAPEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ---IIFMVGrgylSPDLSKVRSNCPK 687
Cdd:cd07856   163 TGYVstrYYRAPEIMLTWQK--YDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQfsiITELLG----TPPDDVINTICSE 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 688 AMKRLMAEClkKKRDERPL---FPQILA-SIELLARSL---PKIHRSASE 730
Cdd:cd07856   237 NTLRFVQSL--PKRERVPFsekFKNADPdAIDLLEKMLvfdPKKRISAAE 284
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
459-657 4.62e-15

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; 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: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 76.30  E-value: 4.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTV------YKGKWHgdvAVKMLNvTAPTPQQLQAFKnEVGVLRKTR-HVNILLFMGY-STKPQLAIVTQ 530
Cdd:cd14090     6 TGELLGEGAYASVqtcinlYTGKEY---AVKIIE-KHPGHSRSRVFR-EVETLHQCQgHPNILQLIEYfEDDERFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHIIETkFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL-HED--LTVKIGDFGLAT----VKSR 603
Cdd:cd14090    81 KMRGGPLLSHIEKRVH-FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCeSMDkvSPVKICDFDLGSgiklSSTS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 604 WSGSHQFEQLS--GSILWMAPEVIR--MQDKNPYSFQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd14090   160 MTPVTTPELLTpvGSAEYMAPEVVDafVGEALSYDKRCDLWSLGVILYIMLCGYPPFY 217
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
459-665 5.96e-15

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: 75.76  E-value: 5.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHG---DVAVKMLNvtaptPQQLQA---------FKNEVGVLRKTRHVNILLFMG-YSTKPQL 525
Cdd:cd14196     9 IGEELGSGQFAIVKKCREKStglEYAAKFIK-----KRQSRAsrrgvsreeIEREVSILRQVLHPNIITLHDvYENRTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEGSSLYHHLHIIETKFEMiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT----VKIGDFGLAtvk 601
Cdd:cd14196    84 VLILELVSGGELFDFLAQKESLSEE-EATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLA--- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 602 SRWSGSHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 665
Cdd:cd14196   160 HEIEDGVEFKNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPFLGDTKQETL 220
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
461-667 6.50e-15

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: 76.18  E-value: 6.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEgSS 536
Cdd:cd07872    12 EKLGEGTYATVFKGRsklTENLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDiVHTDKSLTLVFEYLD-KD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSgs 616
Cdd:cd07872    90 LKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVT-- 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 617 iLWMAPEVIrMQDKNPYSFQSDVYAFGIVLYELMTGQ--LPYSNINNRDQIIF 667
Cdd:cd07872   168 -LWYRPPDV-LLGSSEYSTQIDMWGVGCIFFEMASGRplFPGSTVEDELHLIF 218
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
457-711 6.98e-15

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: 75.21  E-value: 6.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKGKWH--GDVAVKMLNVT-----APTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVT 529
Cdd:cd05037     1 ITFHEHLGQGTFTNIYDGILRevGDGRVQEVEVLlkvldSDHRDISESFFETASLMSQISHKHLVKLYGVCVADENIMVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED------LTVKIGDFGLA-TVKS 602
Cdd:cd05037    81 EYVRYGPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREgldgypPFIKLSDPGVPiTVLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 RwsgshqfEQLSGSILWMAPEVIRMQDKNPySFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGYL-SPDlsk 680
Cdd:cd05037   161 R-------EERVDRIPWIAPECLRNLQANL-TIAADKWSFGTTLWEICSgGEEPLSALSSQEKLQFYEDQHQLpAPD--- 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 681 vrsnCPKaMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd05037   230 ----CAE-LAELIMQCWTYEPTKRPSFRAIL 255
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
462-670 8.72e-15

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: 75.87  E-value: 8.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKwhgD------VA---VKMLNVTAPTPqqLQAFKnEVGVLRKTRHVNILLFMGYSTKPQLA---IVT 529
Cdd:cd07845    14 RIGEGTYGIVYRAR---DttsgeiVAlkkVRMDNERDGIP--ISSLR-EITLLLNLRHPNIVELKEVVVGKHLDsifLVM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEgSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRWSGSHQ 609
Cdd:cd07845    88 EYCE-QDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLA----RTYGLPA 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 610 fEQLSGSI--LWM-APEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQ--LP-YSNINNRDQIIFMVG 670
Cdd:cd07845   163 -KPMTPKVvtLWYrAPELLLGCTT--YTTAIDMWAVGCILAELLAHKplLPgKSEIEQLDLIIQLLG 226
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
461-669 9.36e-15

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-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 PFTAIRE-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: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 75.88  E-value: 9.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKnEVGVLRKTRHVNILLFMGY-STKPQLAIVTQWCEGSS 536
Cdd:cd07869    11 EKLGEGSYATVYKGKSKVNgklVALKVIRLQEEEGTPFTAIR-EASLLKGLKHANIVLLHDIiHTKETLTLVFEYVHTDL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHH------LHIIETKFEMIKLIdiarqtaQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQF 610
Cdd:cd07869    90 CQYMdkhpggLHPENVKLFLFQLL-------RGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSN 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 611 EQLSgsiLWMAPEVIrMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINN-RDQI--IFMV 669
Cdd:cd07869   163 EVVT---LWYRPPDV-LLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDiQDQLerIFLV 220
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
500-656 1.10e-14

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: 75.78  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 500 NEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLYHHLHII-ETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDL 577
Cdd:cd05632    51 NEKQILEKVNSQFVVnLAYAYETKDALCLVLTIMNGGDLKFHIYNMgNPGFEEERALFYAAEILCGLEDLHRENTVYRDL 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 578 KSNNIFLHEDLTVKIGDFGLATvksRWSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05632   131 KPENILLDDYGHIRISDLGLAV---KIPEGESIRGRVGTVGYMAPEVLNNQR---YTLSPDYWGLGCLIYEMIEGQSPF 203
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
462-656 1.31e-14

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: 75.00  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKgkWHG-----DVAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNI---------LLFMGYSTKPQLAI 527
Cdd:cd14038     1 RLGTGGFGNVLR--WINqetgeQVAIKQCR-QELSPKNRERWCLEIQIMKRLNHPNVvaardvpegLQKLAPNDLPLLAM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 vtQWCEGSSLYHHLHIIETKFEMIK--LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED---LTVKIGDFGLATVKS 602
Cdd:cd14038    78 --EYCQGGDLRKYLNQFENCCGLREgaILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGeqrLIHKIIDLGYAKELD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 603 RWSGSHQFeqlSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14038   156 QGSLCTSF---VGTLQYLAPELLEQQK---YTVTVDYWSFGTLAFECITGFRPF 203
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
457-740 2.23e-14

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 75.18  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLQAFKN------------EVGVLRKTRHVNIllfMG--- 518
Cdd:PTZ00024   11 IQKGAHLGEGTYGKVEKAydtLTGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfttlrELKIMNEIKHENI---MGlvd 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 -YSTKPQLAIVTQWCEgsslYHHLHIIETKfemIKLID-----IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKI 592
Cdd:PTZ00024   88 vYVEGDFINLVMDIMA----SDLKKVVDRK---IRLTEsqvkcILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 593 GDFGLA--TVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNP--------YSFQSDVYAFGIVLYELMTGQLPYSNINNR 662
Cdd:PTZ00024  161 ADFGLArrYGYPPYSDTLSKDETMQRREEMTSKVVTLWYRAPellmgaekYHFAVDMWSVGCIFAELLTGKPLFPGENEI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 663 DQ---IIFMVGrgylSPDlskvRSNCPKAMK-RLMAECLK-KKRDERPLFPQILA-SIELLARSL---PKIHRSASEpSL 733
Cdd:PTZ00024  241 DQlgrIFELLG----TPN----EDNWPQAKKlPLYTEFTPrKPKDLKTIFPNASDdAIDLLQSLLklnPLERISAKE-AL 311

                  ....*..
gi 1237938074 734 NRAGFQT 740
Cdd:PTZ00024  312 KHEYFKS 318
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
500-705 2.87e-14

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: 73.80  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 500 NEVGVLRKT----RHVNilLFMGYSTKPQLAIVTQWCEGSSLYHH----LHIIETKFEMIKLIdiaRQTAQGMDYLHAKS 571
Cdd:cd14198    56 HEIAVLELAksnpRVVN--LHEVYETTSEIILILEYAAGGEIFNLcvpdLAEMVSENDIIRLI---RQILEGVYYLHQNN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 572 IIHRDLKSNNIFLHE-----DltVKIGDFGLAtvkSRWSGSHQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVL 646
Cdd:cd14198   131 IVHLDLKPQNILLSSiyplgD--IKIVDFGMS---RKIGHACELREIMGTPEYLAPEIL---NYDPITTATDMWNIGVIA 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 647 YELMTGQLPYSNINNRDQI--IFMVGRGYLSPDLSKVRSNCPKAMKRLmaecLKKKRDERP 705
Cdd:cd14198   203 YMLLTHESPFVGEDNQETFlnISQVNVDYSEETFSSVSQLATDFIQKL----LVKNPEKRP 259
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
496-704 2.88e-14

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: 73.52  E-value: 2.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 496 QAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIH 574
Cdd:cd14088    44 KAAKNEINILKMVKHPNILQLVDvFETRKEYFIFLELATGREVFDWI-LDQGYYSERDTSNVIRQVLEAVAYLHSLKIVH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 575 RDLKSNNIFLHEDL---TVKIGDFGLATVKSRWsgshqFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT 651
Cdd:cd14088   123 RNLKLENLVYYNRLknsKIVISDFHLAKLENGL-----IKEPCGTPEYLAPEVVGRQR---YGRPVDCWAIGVIMYILLS 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 652 GQLPY------SNINNRDQIIFmvgRGYLSPDL---SKVRSNCPKAMKRLMAECLKKKRDER 704
Cdd:cd14088   195 GNPPFydeaeeDDYENHDKNLF---RKILAGDYefdSPYWDDISQAAKDLVTRLMEVEQDQR 253
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
459-656 3.07e-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: 73.91  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKW---HGDVAVKMLNVTAPTPQQLQA-FKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCE 533
Cdd:cd08229    28 IEKKIGRGQFSEVYRATClldGVPVALKKVQIFDLMDAKARAdCIKEIDLLKQLNHPNVIKYYAsFIEDNELNIVLELAD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKFEMIKLIDIAR---QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKSRWSGSHq 609
Cdd:cd08229   108 AGDLSRMIKHFKKQKRLIPEKTVWKyfvQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRfFSSKTTAAH- 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 610 feQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd08229   187 --SLVGTPYYMSPERIH---ENGYNFKSDIWSLGCLLYEMAALQSPF 228
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
500-656 3.15e-14

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: 73.87  E-value: 3.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 500 NEVGVLRK--TRHVnILLFMGYSTKPQLAIVTQWCEGSSLYHHLHII-ETKFEMIKLIDIARQTAQGMDYLHAKSIIHRD 576
Cdd:cd05631    49 NEKRILEKvnSRFV-VSLAYAYETKDALCLVLTIMNGGDLKFHIYNMgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 577 LKSNNIFLHEDLTVKIGDFGLA-------TVKSRwsgshqfeqlSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYEL 649
Cdd:cd05631   128 LKPENILLDDRGHIRISDLGLAvqipegeTVRGR----------VGTVGYMAPEVINNEK---YTFSPDWWGLGCLIYEM 194

                  ....*..
gi 1237938074 650 MTGQLPY 656
Cdd:cd05631   195 IQGQSPF 201
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
235-280 3.17e-14

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 67.49  E-value: 3.17e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1237938074  235 HNFVRKTFFTLAFCDFCRKLLF----QGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWgsfkQGLRCSECKVKCHKKCADKVPKAC 50
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
235-280 3.44e-14

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 67.16  E-value: 3.44e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 235 HNFVRKTFFTLAFCDFCRKLLF----QGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWglfkQGLKCSDCGLVCHKKCLDKAPSPC 50
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
450-729 3.87e-14

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein 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 p38beta 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: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 74.32  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVgQRIGSGSFGTV---YKGKWHGDVAVKMLnvTAPTPQQLQAFKN--EVGVLRKTRHVNILLFMGYSTKP- 523
Cdd:cd07878    11 WEVPERYQNL-TPVGSGAYGSVcsaYDTRLRQKVAVKKL--SRPFQSLIHARRTyrELRLLKHMKHENVIGLLDVFTPAt 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 ------QLAIVTQWCeGSSLYHHLHIIETKFEMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL 597
Cdd:cd07878    88 sienfnEVYLVTNLM-GADLNNIVKCQKLSDEHVQFL--IYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 AT---------VKSRWsgshqfeqlsgsilWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQiifm 668
Cdd:cd07878   165 ARqaddemtgyVATRW--------------YRAPEI--MLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQ---- 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 669 vgrgyLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQilasiellaRSLPKIHRSAS 729
Cdd:cd07878   225 -----LKRIMEVVGTPSPEVLKKISSEHARKYIQSLPHMPQ---------QDLKKIFRGAN 271
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
497-661 4.61e-14

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: 73.54  E-value: 4.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 497 AFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSSLYHHlhIIETKFEMIK-LIDIARQTAQGMDYLHAKSIIH 574
Cdd:cd14168    54 SIENEIAVLRKIKHENIVALEDiYESPNHLYLVMQLVSGGELFDR--IVEKGFYTEKdASTLIRQVLDAVYYLHRMGIVH 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 575 RDLKSNNIFLH---EDLTVKIGDFGLATVKSRwsgSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT 651
Cdd:cd14168   132 RDLKPENLLYFsqdEESKIMISDFGLSKMEGK---GDVMSTACGTPGYVAPEVLA---QKPYSKAVDCWSIGVIAYILLC 205
                         170
                  ....*....|
gi 1237938074 652 GQLPYSNINN 661
Cdd:cd14168   206 GYPPFYDEND 215
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
562-713 4.90e-14

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; 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). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 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: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 73.46  E-value: 4.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 562 QGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGlatVKSRWSGSHQF-EQLSGSILWMAPEVIRMQDKNpYSFQS-DV 639
Cdd:cd14199   137 KGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFG---VSNEFEGSDALlTNTVGTPAFMAPETLSETRKI-FSGKAlDV 212
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 640 YAFGIVLYELMTGQLPYSNinnrDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILAS 713
Cdd:cd14199   213 WAMGVTLYCFVFGQCPFMD----ERILSLHSKIKTQPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLH 282
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
463-693 5.05e-14

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: 72.83  E-value: 5.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVyKGKWH---GD-VAVKMLNVT----APTPQQLQafknEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCE 533
Cdd:cd14074    11 LGRGHFAVV-KLARHvftGEkVAVKVIDKTklddVSKAHLFQ----EVRCMKLVQHPNVVrLYEVIDTQTKLYLILELGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL-TVKIGDFGLAtvkSRWSGSHQFEQ 612
Cdd:cd14074    86 GGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFS---NKFQPGEKLET 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 LSGSILWMAPEVIRMQDKNPYSFqsDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDlsKVRSNCPKAMKRL 692
Cdd:cd14074   163 SCGSLAYSAPEILLGDEYDAPAV--DIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPA--HVSPECKDLIRRM 238

                  .
gi 1237938074 693 M 693
Cdd:cd14074   239 L 239
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
535-650 5.22e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 74.14  E-value: 5.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKsrwSGSHQFEQLS 614
Cdd:PHA03209  141 SDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFP---VVAPAFLGLA 217
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1237938074 615 GSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELM 650
Cdd:PHA03209  218 GTVETNAPEVLA---RDKYNSKADIWSAGIVLFEML 250
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
456-705 6.87e-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: 72.60  E-value: 6.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKGkWHGD----VAVKM--LNVTAPTPQQLQAfknEVGVLRKTRHVNILLFMG-YSTKPQLAIV 528
Cdd:cd06619     2 DIQYQEILGHGNGGTVYKA-YHLLtrriLAVKVipLDITVELQKQIMS---ELEILYKCDSPYIIGFYGaFFVENRISIC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 529 TQWCEGSSLYHHLHIIETKfemikLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksrwsgsh 608
Cdd:cd06619    78 TEFMDGGSLDVYRKIPEHV-----LGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVST--------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 609 qfeQLSGSI--------LWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNrdqiifmvGRGYLSP-DLS 679
Cdd:cd06619   144 ---QLVNSIaktyvgtnAYMAPERISGEQ---YGIHSDVWSLGISFMELALGRFPYPQIQK--------NQGSLMPlQLL 209
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1237938074 680 K--VRSNCP--------KAMKRLMAECLKKKRDERP 705
Cdd:cd06619   210 QciVDEDPPvlpvgqfsEKFVHFITQCMRKQPKERP 245
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
558-710 7.25e-14

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: 72.67  E-value: 7.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 558 RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvksrwsgSHQFE----QLS---GSILWMAPEVIRMQDK 630
Cdd:cd14200   131 RDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGV---------SNQFEgndaLLSstaGTPAFMAPETLSDSGQ 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 631 NPYSFQSDVYAFGIVLYELMTGQLPYSNinnrDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQI 710
Cdd:cd14200   202 SFSGKALDVWAMGVTLYCFVYGKCPFID----EFILALHNKIKNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEI 277
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
459-665 8.07e-14

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: 72.59  E-value: 8.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd14104     4 IAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILrLHESFESHEELVMIFEFISGVDI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 YHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNI--FLHEDLTVKIGDFGLAtvkSRWSGSHQFEQLSG 615
Cdd:cd14104    84 FERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIiyCTRRGSYIKIIEFGQS---RQLKPGDKFRLQYT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 616 SILWMAPEVirmQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 665
Cdd:cd14104   161 SAEFYAPEV---HQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTI 207
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
463-675 9.51e-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: 72.28  E-value: 9.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK------GKwhgDVAVKMLNVTAPTPQQlqafknEVGVL-RKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 534
Cdd:cd14091     8 IGKGSYSVCKRcihkatGK---EYAVKIIDKSKRDPSE------EIEILlRYGQHPNIItLRDVYDDGNSVYLVTELLRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHlhIIETKF-------EMIKLIdiarqtAQGMDYLHAKSIIHRDLKSNNIFLHEDL----TVKIGDFGLAtvksr 603
Cdd:cd14091    79 GELLDR--ILRQKFfsereasAVMKTL------TKTVEYLHSQGVVHRDLKPSNILYADESgdpeSLRICDFGFA----- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 604 wsgshqfEQLSGS--IL--------WMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINN--RDQIIFMVGR 671
Cdd:cd14091   146 -------KQLRAEngLLmtpcytanFVAPEVLKKQG---YDAACDIWSLGVLLYTMLAGYTPFASGPNdtPEVILARIGS 215

                  ....
gi 1237938074 672 GYLS 675
Cdd:cd14091   216 GKID 219
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
466-662 1.15e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 73.34  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 466 GSFGTVYKGKWHGDVAVKMLNVTAPTPQQlqAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQW--CEgssLYHHLH 542
Cdd:PHA03207  103 GSEGEVFVCTKHGDEQRKKVIVKAVTGGK--TPGREIDILKTISHRAIInLIHAYRWKSTVCMVMPKykCD---LFTYVD 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 543 IIETkFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAP 622
Cdd:PHA03207  178 RSGP-LPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDTPQCYGWSGTLETNSP 256
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1237938074 623 EVIRMqdkNPYSFQSDVYAFGIVLYELMTGQLPYSNINNR 662
Cdd:PHA03207  257 ELLAL---DPYCAKTDIWSAGLVLFEMSVKNVTLFGKQVK 293
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
463-692 1.53e-13

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: 71.17  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGT--VYKGKWHGD-VAVKMLNVTAPTPQQLQafkNEVGVLRKTRHVNILLFMGYSTKP-QLAIVTQWCEGSSLY 538
Cdd:cd14665     8 IGSGNFGVarLMRDKQTKElVAVKYIERGEKIDENVQ---REIINHRSLRHPNIVRFKEVILTPtHLAIVMEYAAGGELF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHL------HIIETKFEMIKLIdiarqtaQGMDYLHAKSIIHRDLKSNNIFLHEDLT--VKIGDFGLatvkSRWSGSH-Q 609
Cdd:cd14665    85 ERIcnagrfSEDEARFFFQQLI-------SGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGY----SKSSVLHsQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 610 FEQLSGSILWMAPEVIRMQDKNpySFQSDVYAFGIVLYELMTGQLPYSNI----NNRDQIIFMVGRGYLSPDLSKVRSNC 685
Cdd:cd14665   154 PKSTVGTPAYIAPEVLLKKEYD--GKIADVWSCGVTLYVMLVGAYPFEDPeeprNFRKTIQRILSVQYSIPDYVHISPEC 231

                  ....*..
gi 1237938074 686 PKAMKRL 692
Cdd:cd14665   232 RHLISRI 238
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
463-669 1.71e-13

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: 71.93  E-value: 1.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKW-----HGDVAVKMLNvtaPTPQQLQAFK----NEVGVLRKTRHVNIL----LFMGYSTKpQLAIVT 529
Cdd:cd07842     8 IGRGTYGRVYKAKRkngkdGKEYAIKKFK---GDKEQYTGISqsacREIALLRELKHENVVslveVFLEHADK-SVYLLF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEgsslYHHLHIIetKFE-----------MIKliDIARQTAQGMDYLHAKSIIHRDLKSNNIFL----HEDLTVKIGD 594
Cdd:cd07842    84 DYAE----HDLWQII--KFHrqakrvsippsMVK--SLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 595 FGLATVksRWSGSHQFEQLSG---SILWMAPEVIrMQDKNpYSFQSDVYAFGIVLYELMTGQLPY---------SNINNR 662
Cdd:cd07842   156 LGLARL--FNAPLKPLADLDPvvvTIWYRAPELL-LGARH-YTKAIDIWAIGCIFAELLTLEPIFkgreakikkSNPFQR 231

                  ....*....
gi 1237938074 663 DQI--IFMV 669
Cdd:cd07842   232 DQLerIFEV 240
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
566-663 1.77e-13

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 73.36  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 566 YLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIV 645
Cdd:PTZ00283  158 HVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATVSDDVGRTFCGTPYYVAPEIWR---RKPYSKKADMFSLGVL 234
                          90
                  ....*....|....*...
gi 1237938074 646 LYELMTGQLPYSNINNRD 663
Cdd:PTZ00283  235 LYELLTLKRPFDGENMEE 252
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
443-661 1.89e-13

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: 71.05  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 443 RRDSSDDWEIpdgqitvGQRIGSGSFGTVY---KGKWHGDVAVKMLNVTAPTPQQLQ-AFKNEVGVLRKTRHVNILLFMG 518
Cdd:cd14117     1 RKFTIDDFDI-------GRPLGKGKFGNVYlarEKQSKFIVALKVLFKSQIEKEGVEhQLRREIEIQSHLRHPNILRLYN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 Y-STKPQLAIVTQWCEGSSLYHHLHIIEtKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGl 597
Cdd:cd14117    74 YfHDRKRIYLILEYAPRGELYKELQKHG-RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFG- 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 598 atvksrWS---GSHQFEQLSGSILWMAPEVI--RMQDKnpysfQSDVYAFGIVLYELMTGQLPYSNINN 661
Cdd:cd14117   152 ------WSvhaPSLRRRTMCGTLDYLPPEMIegRTHDE-----KVDLWCIGVLCYELLVGMPPFESASH 209
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
463-665 2.27e-13

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: 70.97  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY--KGKWHGD-VAVKMLnvtaptPQQLQAFKNEVGVLRKTRHVNIL---------LFMGYSTKPQLAIVTQ 530
Cdd:cd05611     4 ISKGAFGSVYlaKKRSTGDyFAIKVL------KKSDMIAKNQVTNVKAERAIMMIqgespyvakLYYSFQSKDYLYLVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLyhhlhiiETKFEMIKLI--DIARQ----TAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRW 604
Cdd:cd05611    78 YLNGGDC-------ASLIKTLGGLpeDWAKQyiaeVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEK 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 605 SGSHQFeqlSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYsNINNRDQI 665
Cdd:cd05611   151 RHNKKF---VGTPDYLAPETILGVGDDK---MSDWWSLGCVIFEFLFGYPPF-HAETPDAV 204
pknD PRK13184
serine/threonine-protein kinase PknD;
518-695 2.30e-13

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 74.04  E-value: 2.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 518 GYSTKPQLAIVTQwCEgsSLYHHLHIietKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL 597
Cdd:PRK13184   86 GYTLKSLLKSVWQ-KE--SLSKELAE---KTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 ATVKS-------------RWSGSHQFE---QLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSN--- 658
Cdd:PRK13184  160 AIFKKleeedlldidvdeRNICYSSMTipgKIVGTPDYMAPERLL---GVPASESTDIYALGVILYQMLTLSFPYRRkkg 236
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 659 --INNRDQIIF---MVGRGYLSPDLSKVrsncpkAMKRLMAE 695
Cdd:PRK13184  237 rkISYRDVILSpieVAPYREIPPFLSQI------AMKALAVD 272
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
450-665 2.52e-13

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: 71.91  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVgQRIGSGSFGTV---YKGKWHGDVAVKMLNvtapTPQQLQAFKN----EVGVLRKTRHVNILLFMGYSTK 522
Cdd:cd07880    11 WEVPDRYRDL-KQVGSGAYGTVcsaLDRRTGAKVAIKKLY----RPFQSELFAKrayrELRLLKHMKHENVIGLLDVFTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 523 PQ---------LAIVTQWCEGSSLYHHLHIIETKFEMIklidiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIG 593
Cdd:cd07880    86 DLsldrfhdfyLVMPFMGTDLGKLMKHEKLSEDRIQFL-----VYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKIL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 594 DFGLAtvksrwsgSHQFEQLSGSIL---WMAPEVIR--MQdknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 665
Cdd:cd07880   161 DFGLA--------RQTDSEMTGYVVtrwYRAPEVILnwMH----YTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQL 225
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
456-725 2.54e-13

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: 71.03  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKgkwhgdVAVKMLNVTAPTPQ--------QLQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLA 526
Cdd:cd06622     2 EIEVLDELGKGNYGSVYK------VLHRPTGVTMAMKEirleldesKFNQIIMELDILHKAVSPYIVDFYGaFFIEGAVY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSS---LYHHLHIIETKFEMIkLIDIARQTAQGMDYLHAK-SIIHRDLKSNNIFLHEDLTVKIGDFGLatvks 602
Cdd:cd06622    76 MCMEYMDAGSldkLYAGGVATEGIPEDV-LRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGV----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 603 rwSGshqfeQLSGSIL--------WMAPEVIR---MQDKNPYSFQSDVYAFGIVLYELMTGQLPY-----SNINNRDQII 666
Cdd:cd06622   150 --SG-----NLVASLAktnigcqsYMAPERIKsggPNQNPTYTVQSDVWSLGLSILEMALGRYPYppetyANIFAQLSAI 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 667 FMVGRGYLSPDLSkvrsncPKAmKRLMAECLKKKRDERPLFPQILASIELLARSLPKIH 725
Cdd:cd06622   223 VDGDPPTLPSGYS------DDA-QDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADVD 274
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
463-669 2.64e-13

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: 71.15  E-value: 2.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGK-WHGDVAVKMLNVTAPTPQQ---LQAFKnEVGVLRKTR---HVNILLFMGYSTKPQlaiVTQWCEGS 535
Cdd:cd07863     8 IGVGAYGTVYKARdPHSGHFVALKSVRVQTNEDglpLSTVR-EVALLKRLEafdHPNIVRLMDVCATSR---TDRETKVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHL-HIIETKFEMI--------KLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSG 606
Cdd:cd07863    84 LVFEHVdQDLRTYLDKVpppglpaeTIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARI---YSC 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 607 SHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI--IFMV 669
Cdd:cd07863   161 QMALTPVVVTLWYRAPEVLL---QSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLgkIFDL 222
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
462-668 2.98e-13

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: 71.10  E-value: 2.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKwhgD------VAVKMLNVTaptpQQLQAFK----NEVGVLRKTRHVNIL----LFMGySTKPQLAI 527
Cdd:cd07843    12 RIEEGTYGVVYRAR---DkktgeiVALKKLKME----KEKEGFPitslREINILLKLQHPNIVtvkeVVVG-SNLDKIYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCEGS--SLYHHLH----IIETKFEMIKLIDiarqtaqGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvk 601
Cdd:cd07843    84 VMEYVEHDlkSLMETMKqpflQSEVKCLMLQLLS-------GVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLA--- 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 602 sRWSGS--HQFEQLSGSILWMAPEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI--IFM 668
Cdd:cd07843   154 -REYGSplKPYTQLVVTLWYRAPELLLGAKE--YSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLnkIFK 221
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
453-656 3.53e-13

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 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: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 70.25  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 453 PDGQITVGQRIGSGSFGTVYKG-----KWHGDVAVKMLNVTAPTPQQLQAFKNevgvLRKTRHVNIL-LFMGYSTKPQLA 526
Cdd:cd14112     1 PTGRFSFGSEIFRGRFSVIVKAvdsttETDAHCAVKIFEVSDEASEAVREFES----LRTLQHENVQrLIAAFKPSNFAY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 IVTQWCEGSSLYHHLHIIETKFEMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLH--EDLTVKIGDFGLATVKSRW 604
Cdd:cd14112    77 LVMEKLQEDVFTRFSSNDYYSEEQVATT--VRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQKVSKL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 605 SGShqfeQLSGSILWMAPEVIrmQDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14112   155 GKV----PVDGDTDWASPEFH--NPETPITVQSDIWGLGVLTFCLLSGFHPF 200
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
463-656 4.49e-13

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: 70.00  E-value: 4.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQafkNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLY 538
Cdd:cd14113    15 LGRGRFSVVKKCDQRGTkraVATKFVNKKLMKRDQVT---HELGVLQSLQHPQLVgLLDTFETPTSYILVLEMADQGRLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHL----HIIETKFEMIklidiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL---TVKIGDFGLATvksRWSGSHQFE 611
Cdd:cd14113    92 DYVvrwgNLTEEKIRFY-----LREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFGDAV---QLNTTYYIH 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1237938074 612 QLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14113   164 QLLGSPEFAAPEIIL---GNPVSLTSDLWSIGVLTYVLLSGVSPF 205
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
450-665 4.84e-13

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: 71.09  E-value: 4.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 450 WEIPDGQITVGQrIGSGSFGTVYKG---KWHGDVAVKMLNvtaptpqqlQAFKNEVGVLRKTRHVNILLFMGYSTkpqla 526
Cdd:cd07879    11 WELPERYTSLKQ-VGSGAYGSVCSAidkRTGEKVAIKKLS---------RPFQSEIFAKRAYRELTLLKHMQHEN----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 527 iVTQWCE---GSSLYHHLH---------------IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL 588
Cdd:cd07879    76 -VIGLLDvftSAVSGDEFQdfylvmpymqtdlqkIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 589 TVKIGDFGLAtvksrwsgSHQFEQLSGSIL---WMAPEVIR--MQdknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRD 663
Cdd:cd07879   155 ELKILDFGLA--------RHADAEMTGYVVtrwYRAPEVILnwMH----YNQTVDIWSVGCIMAEMLTGKTLFKGKDYLD 222

                  ..
gi 1237938074 664 QI 665
Cdd:cd07879   223 QL 224
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
515-677 4.99e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST 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: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 70.13  E-value: 4.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 515 LFMGYSTKPQLAIVTQWCEG---SSLYHHlhIIETKFEMIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVK 591
Cdd:cd05609    65 MYCSFETKRHLCMVMEYVEGgdcATLLKN--IGPLPVDMARMY--FAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIK 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 592 IGDFGLATV------KSRWSGS-----HQF--EQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLP--- 655
Cdd:cd05609   141 LTDFGLSKIglmsltTNLYEGHiekdtREFldKQVCGTPEYIAPEVILRQG---YGKPVDWWAMGIILYEFLVGCVPffg 217
                         170       180
                  ....*....|....*....|....*...
gi 1237938074 656 ------YSNINNrDQIIFMVGRGYLSPD 677
Cdd:cd05609   218 dtpeelFGQVIS-DEIEWPEGDDALPDD 244
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
461-717 4.99e-13

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: 70.02  E-value: 4.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKG---KWHGDVAVKmlNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ------LAIVTQW 531
Cdd:cd13986     6 RLLGEGGFSFVYLVedlSTGRLYALK--KILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEaggkkeVYLLLPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLH---IIETKFEMIKLIDIARQTAQGMDYLHA---KSIIHRDLKSNNIFLHEDLTVKIGDFGlATVKSRW- 604
Cdd:cd13986    84 YKRGSLQDEIErrlVKGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLG-SMNPARIe 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 -SGSHQFEQLS------GSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNR-DQIIFMVGRGYLSP 676
Cdd:cd13986   163 iEGRREALALQdwaaehCTMPYRAPELFDVKSHCTIDEKTDIWSLGCTLYALMYGESPFERIFQKgDSLALAVLSGNYSF 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1237938074 677 DLSkvrSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 717
Cdd:cd13986   243 PDN---SRYSEELHQLVKSMLVVNPAERPSIDDLLSRVHDL 280
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
460-658 5.01e-13

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: 70.79  E-value: 5.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 460 GQRIGSGSFGTVYKGKWHGD-VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFmgYST---KPQLAIVTQWCE-G 534
Cdd:cd08216     7 GKCFKGGGVVHLAKHKPTNTlVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPY--VTSfvvDNDLYVVTPLMAyG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLyhhlHIIETKFE------MIKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV---KSRWS 605
Cdd:cd08216    85 SCR----DLLKTHFPeglpelAIAFI--LRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSmvkHGKRQ 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 606 GS-HQFEQLSGSIL-WMAPEVIRmQDKNPYSFQSDVYAFGIVLYELMTGQLPYSN 658
Cdd:cd08216   159 RVvHDFPKSSEKNLpWLSPEVLQ-QNLLGYNEKSDIYSVGITACELANGVVPFSD 212
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
463-657 6.71e-13

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: 70.33  E-value: 6.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY---------KGKWHgdvAVKMLNVTA--PTPQQLQAFKNEVGVLRKTRHVNILLFMGYS--TKPQLAIVT 529
Cdd:cd05614     8 LGTGAYGKVFlvrkvsghdANKLY---AMKVLRKAAlvQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAfqTDAKLHLIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT--VKSRWSGS 607
Cdd:cd05614    85 DYVSGGELFTHLYQ-RDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKefLTEEKERT 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFeqlSGSILWMAPEVIRmqDKNPYSFQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd05614   164 YSF---CGTIEYMAPEIIR--GKSGHGKAVDWWSLGILMFELLTGASPFT 208
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
479-656 6.78e-13

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; 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: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 70.06  E-value: 6.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 479 DVAVKMLNvTAPTPQQLQAFKnEVGVLRKTR-HVNIL-LFMGYSTKPQLAIVTQWCEGSSLYHHLHIiETKFEMIKLIDI 556
Cdd:cd14173    29 EYAVKIIE-KRPGHSRSRVFR-EVEMLYQCQgHRNVLeLIEFFEEEDKFYLVFEKMRGGSILSHIHR-RRHFNELEASVV 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 557 ARQTAQGMDYLHAKSIIHRDLKSNNIFL---HEDLTVKIGDFGLAT---VKSRWSGSHQFEQLS--GSILWMAPEVIRM- 627
Cdd:cd14173   106 VQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLGSgikLNSDCSPISTPELLTpcGSAEYMAPEVVEAf 185
                         170       180       190
                  ....*....|....*....|....*....|
gi 1237938074 628 -QDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14173   186 nEEASIYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
458-675 6.97e-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: 70.06  E-value: 6.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGT----VYKGKwHGDVAVKMLNVTAPTPQQlqafknEVGVLRK-TRHVNILLFMG-YSTKPQLAIVTQW 531
Cdd:cd14175     4 VVKETIGVGSYSVckrcVHKAT-NMEYAVKVIDKSKRDPSE------EIEILLRyGQHPNIITLKDvYDDGKHVYLVTEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHlhIIETKFEMIKLIDIARQT-AQGMDYLHAKSIIHRDLKSNNIFLHEDL----TVKIGDFGLATvksrwsg 606
Cdd:cd14175    77 MRGGELLDK--ILRQKFFSEREASSVLHTiCKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGFAK------- 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 607 shQFEQLSGSIL-------WMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSN--INNRDQIIFMVGRGYLS 675
Cdd:cd14175   148 --QLRAENGLLMtpcytanFVAPEVLKRQG---YDEGCDIWSLGILLYTMLAGYTPFANgpSDTPEEILTRIGSGKFT 220
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
235-280 7.81e-13

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; 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. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 63.11  E-value: 7.81e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1237938074 235 HNFVRKTFFTLAfCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:cd20812     3 HRFSKKLFMRQT-CDYCHKQMFFGLKCKDCKYKCHKKCAKKAPPSC 47
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
459-667 7.98e-13

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: 70.04  E-value: 7.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHGD---VAVK-MLNVTAPTPQQLQAFKnEVGVLRKTRHVNI--LLFMGYS-------TKPQL 525
Cdd:cd07866    12 ILGKLGEGTFGEVYKARQIKTgrvVALKkILMHNEKDGFPITALR-EIKILKKLKHPNVvpLIDMAVErpdkskrKRGSV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEgSSLYHHLHIIETKFEM--IKLIdiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV--- 600
Cdd:cd07866    91 YMVTPYMD-HDLSGLLENPSVKLTEsqIKCY--MLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPydg 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 601 ---KSRWSGSHQFEQLSGSIL--WM-APEVIrMQDKNpYSFQSDVYAFGIVLYELMTGQ--LPYSNINNRDQIIF 667
Cdd:cd07866   168 pppNPKGGGGGGTRKYTNLVVtrWYrPPELL-LGERR-YTTAVDIWGIGCVFAEMFTRRpiLQGKSDIDQLHLIF 240
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
463-705 8.01e-13

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: 69.66  E-value: 8.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLQA-----FKNEVGVLRKTRHVNIL-LFMGYSTKPQ-LAIVTQWC 532
Cdd:cd13990     8 LGKGGFSEVYKAfdlVEQRYVACKIHQLNKDWSEEKKQnyikhALREYEIHKSLDHPRIVkLYDVFEIDTDsFCTVLEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHLHIIETKFEMIKLIdIARQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDLT---VKIGDFGLATVKSRWSGS 607
Cdd:cd13990    88 DGNDLDFYLKQHKSIPEREARS-IIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVsgeIKITDFGLSKIMDDESYN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 608 HQFEQL----SGSILWMAPEVIRMQDKNP-YSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIF----MVGRGYLSPDL 678
Cdd:cd13990   167 SDGMELtsqgAGTYWYLPPECFVVGKTPPkISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILEentiLKATEVEFPSK 246
                         250       260
                  ....*....|....*....|....*..
gi 1237938074 679 SKVRSNCpkamKRLMAECLKKKRDERP 705
Cdd:cd13990   247 PVVSSEA----KDFIRRCLTYRKEDRP 269
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
462-696 8.16e-13

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: 69.67  E-value: 8.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKwHGD----VAVK-MLNVTAPTPQQLQAFKnEVGVLRKTR-HVNILLFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd07832     7 RIGEGAHGIVFKAK-DREtgetVALKkVALRKLEGGIPNQALR-EIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYMLS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSG---SHQFeq 612
Cdd:cd07832    85 SLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPrlySHQV-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 613 lsGSILWMAPEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ---IIFMVGR-------GYLS-PDLSKV 681
Cdd:cd07832   163 --ATRWYRAPELLYGSRK--YDEGVDLWAVGCIFAELLNGSPLFPGENDIEQlaiVLRTLGTpnektwpELTSlPDYNKI 238
                         250
                  ....*....|....*..
gi 1237938074 682 RS--NCPKAMKRLMAEC 696
Cdd:cd07832   239 TFpeSKGIRLEEIFPDC 255
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
448-665 8.36e-13

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 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: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 69.88  E-value: 8.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 448 DDWEIPDGQI---TVGQRIGSGSFGTVYKGkWHGD----VAVKMLNvtaptPQQLQAFKNEVGVLRKTR-HVNIL----L 515
Cdd:cd14132     8 ENLNVEWGSQddyEIIRKIGRGKYSEVFEG-INIGnnekVVIKVLK-----PVKKKKIKREIKILQNLRgGPNIVklldV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 516 FMGYSTKpQLAIVTQWCEGS---SLYHHLHIIETKFEMIKLIdiarqtaQGMDYLHAKSIIHRDLKSNNIFL-HEDLTVK 591
Cdd:cd14132    82 VKDPQSK-TPSLIFEYVNNTdfkTLYPTLTDYDIRYYMYELL-------KALDYCHSKGIMHRDVKPHNIMIdHEKRKLR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 592 IGDFGLAT-----------VKSRWsgshqfeqlsgsilWMAPEV---IRMQDknpYSFqsDVYAFGIVLYELMTGQLPYS 657
Cdd:cd14132   154 LIDWGLAEfyhpgqeynvrVASRY--------------YKGPELlvdYQYYD---YSL--DMWSLGCMLASMIFRKEPFF 214

                  ....*....
gi 1237938074 658 N-INNRDQI 665
Cdd:cd14132   215 HgHDNYDQL 223
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
463-657 8.67e-13

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: 69.64  E-value: 8.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY---------KGKWHGDVAVKMLNVT--APTPQQLqafKNEVGVLRKTRHVNILLFMGYS--TKPQLAIVT 529
Cdd:cd05613     8 LGTGAYGKVFlvrkvsghdAGKLYAMKVLKKATIVqkAKTAEHT---RTERQVLEHIRQSPFLVTLHYAfqTDTKLHLIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIIEtKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGSHQ 609
Cdd:cd05613    85 DYINGGELFTHLSQRE-RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGL----SKEFLLDE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 610 FEQ---LSGSILWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMTGQLPYS 657
Cdd:cd05613   160 NERaysFCGTIEYMAPEIVRGGDSG-HDKAVDWWSLGVLMYELLTGASPFT 209
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
556-671 9.97e-13

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: 69.91  E-value: 9.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 556 IARQTAQGMDYLHAK-SIIHRDLKSNNIFL-HEDLTVKIGDFGLATvksrWSGSH-----QFEQlsgsilWMAPEVIRmq 628
Cdd:cd14136   124 IARQVLQGLDYLHTKcGIIHTDIKPENVLLcISKIEVKIADLGNAC----WTDKHftediQTRQ------YRSPEVIL-- 191
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 629 dKNPYSFQSDVYAFGIVLYELMTGQL---PYSNIN-NRD-----QIIFMVGR 671
Cdd:cd14136   192 -GAGYGTPADIWSTACMAFELATGDYlfdPHSGEDySRDedhlaLIIELLGR 242
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
462-705 1.56e-12

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear 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. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The 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: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 68.58  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYK--GKWHGDV-AVK--MLNVTAPTPQQlQAFkNEV---GVLRKTRHVnILLFMGYSTKPQLAIVTQWCE 533
Cdd:cd14051     7 KIGSGEFGSVYKciNRLDGCVyAIKksKKPVAGSVDEQ-NAL-NEVyahAVLGKHPHV-VRYYSAWAEDDHMIIQNEYCN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHL---HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIF------------------------LHE 586
Cdd:cd14051    84 GGSLADAIsenEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFisrtpnpvsseeeeedfegeednpESN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 587 DLTVKIGDFGLATVKSrwsgSHQFEQlsGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQ-LP-----YSNIN 660
Cdd:cd14051   164 EVTYKIGDLGHVTSIS----NPQVEE--GDCRFLANEI--LQENYSHLPKADIFALALTVYEAAGGGpLPkngdeWHEIR 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1237938074 661 nrdqiifmvgRGYLsPDLskvrSNCPKAMKRLMAECLKKKRDERP 705
Cdd:cd14051   236 ----------QGNL-PPL----PQCSPEFNELLRSMIHPDPEKRP 265
PHA02988 PHA02988
hypothetical protein; Provisional
471-716 1.90e-12

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 68.62  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 471 VYKGKWHG-DVAVKMLNVTAPTPQQL-QAFKNEVGVLRKTRHVNILLFMGYSTK-----PQLAIVTQWCEGSSLYHHLHI 543
Cdd:PHA02988   36 IYKGIFNNkEVIIRTFKKFHKGHKVLiDITENEIKNLRRIDSNNILKIYGFIIDivddlPRLSLILEYCTRGYLREVLDK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 544 iETKFEMIKLIDIARQTAQGMDYLHAK-SIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSgshqfeqlSGSILWMAP 622
Cdd:PHA02988  116 -EKDLSFKTKLDMAIDCCKGLYNLYKYtNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPP--------FKNVNFMVY 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 623 EVIRMQDK--NPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDqIIFMVgrgYLSPDLSKVRSNCPKAMKRLMAECLKKK 700
Cdd:PHA02988  187 FSYKMLNDifSEYTIKDDIYSLGVVLWEIFTGKIPFENLTTKE-IYDLI---INKNNSLKLPLDCPLEIKCIVEACTSHD 262
                         250
                  ....*....|....*.
gi 1237938074 701 RDERPLFPQILASIEL 716
Cdd:PHA02988  263 SIKRPNIKEILYNLSL 278
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
555-671 1.96e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK 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: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 68.87  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 555 DIARQTAQGMDYLHAKSIIHRDLKSNNI-FLH--EDLTVKIGDFGLATVKSrwsgshQFEQLSG---SILWMAPEVIRMQ 628
Cdd:cd14092   103 RIMRQLVSAVSFMHSKGVVHRDLKPENLlFTDedDDAEIKIVDFGFARLKP------ENQPLKTpcfTLPYAAPEVLKQA 176
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 629 DKNP-YSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGR 671
Cdd:cd14092   177 LSTQgYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKR 220
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
519-704 2.06e-12

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: 68.04  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKPQLAIVTQWCEGSSLYHHlhIIETKFEMIKLIDIAR---QTAQGMDYLHAKSIIHRDLKSNNIFLHEDL---TVKI 592
Cdd:cd14197    78 YETASEMILVLEYAAGGEIFNQ--CVADREEAFKEKDVKRlmkQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKI 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 593 GDFGLATVksrWSGSHQFEQLSGSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYsnINNRDQIIFM---- 668
Cdd:cd14197   156 VDFGLSRI---LKNSEELREIMGTPEYVAPEILSYE---PISTATDMWSIGVLAYVMLTGISPF--LGDDKQETFLnisq 227
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1237938074 669 VGRGYLSPDLSKVRSNCPKAMKRLmaecLKKKRDER 704
Cdd:cd14197   228 MNVSYSEEEFEHLSESAIDFIKTL----LIKKPENR 259
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
461-675 2.16e-12

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: 68.50  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFgTVYKGKWHG----DVAVKMLNVTAPTPQQlqafknEVGVL-RKTRHVNILLFMG-YSTKPQLAIVTQWCEG 534
Cdd:cd14177    10 EDIGVGSY-SVCKRCIHRatnmEFAVKIIDKSKRDPSE------EIEILmRYGQHPNIITLKDvYDDGRYVYLVTELMKG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHlhIIETK-FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL----TVKIGDFGLATvksrwsgshQ 609
Cdd:cd14177    83 GELLDR--ILRQKfFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFAK---------Q 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 610 FEQLSGSIL-------WMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNR--DQIIFMVGRGYLS 675
Cdd:cd14177   152 LRGENGLLLtpcytanFVAPEVLMRQG---YDAACDIWSLGVLLYTMLAGYTPFANGPNDtpEEILLRIGSGKFS 223
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
459-675 2.83e-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: 68.51  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGT----VYKGKwHGDVAVKMLNVTAPTPQQlqafknEVGVL-RKTRHVNILLFMG-YSTKPQLAIVTQWC 532
Cdd:cd14176    23 VKEDIGVGSYSVckrcIHKAT-NMEFAVKIIDKSKRDPTE------EIEILlRYGQHPNIITLKDvYDDGKYVYVVTELM 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHlhIIETKF----EMIKLIDIARQTAQgmdYLHAKSIIHRDLKSNNIFLHEDL----TVKIGDFGLATvksrw 604
Cdd:cd14176    96 KGGELLDK--ILRQKFfserEASAVLFTITKTVE---YLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAK----- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 605 sgshQFEQLSGSIL-------WMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSN--INNRDQIIFMVGRGYLS 675
Cdd:cd14176   166 ----QLRAENGLLMtpcytanFVAPEVLERQG---YDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARIGSGKFS 238
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
459-658 3.47e-12

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: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKgkwhgdvavkmlnVTAPTPQQLQAFKnevgVLRK--------TRHVN----IL----------LF 516
Cdd:cd05573     5 VIKVIGRGAFGEVWL-------------VRDKDTGQVYAMK----ILRKsdmlkreqIAHVRaerdILadadspwivrLH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 517 MGYSTKPQLAIVTQWCEGSSLYHHL---HIIE---TKF---EMIKLIDiarqtaqgmdYLHAKSIIHRDLKSNNIFLHED 587
Cdd:cd05573    68 YAFQDEDHLYLVMEYMPGGDLMNLLikyDVFPeetARFyiaELVLALD----------SLHKLGFIHRDIKPDNILLDAD 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 588 LTVKIGDFGLAT-----------------------VKSRWSGSHQFEQLSGSIL----WMAPEVIRmqdKNPYSFQSDVY 640
Cdd:cd05573   138 GHIKLADFGLCTkmnksgdresylndsvntlfqdnVLARRRPHKQRRVRAYSAVgtpdYIAPEVLR---GTGYGPECDWW 214
                         250
                  ....*....|....*...
gi 1237938074 641 AFGIVLYELMTGQLPYSN 658
Cdd:cd05573   215 SLGVILYEMLYGFPPFYS 232
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
461-663 3.77e-12

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: 68.01  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVY--KGKWHGDV-AVKMLNVTAPTPQQ-LQAFKNEVGVLRKTRHVNIL--LFMGYSTKPQLAIVTQWCEG 534
Cdd:cd05590     1 RVLGKGSFGKVMlaRLKESGRLyAVKVLKKDVILQDDdVECTMTEKRILSLARNHPFLtqLYCCFQTPDRLFFVMEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLS 614
Cdd:cd05590    81 GDLMFHIQK-SRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMC--KEGIFNGKTTSTFC 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 615 GSILWMAPEVIR-MQdknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRD 663
Cdd:cd05590   158 GTPDYIAPEILQeML----YGPSVDWWAMGVLLYEMLCGHAPFEAENEDD 203
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
443-711 3.98e-12

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: 68.53  E-value: 3.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 443 RRDSS-DDWEIPDGQITVGQR------IGSGSFGTV---YKGKWHGDVAVKMLnvTAPTPQQLQAFK--NEVGVLRKTRH 510
Cdd:cd07875     5 KRDNNfYSVEIGDSTFTVLKRyqnlkpIGSGAQGIVcaaYDAILERNVAIKKL--SRPFQNQTHAKRayRELVLMKCVNH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 511 VNILLFMGYSTkPQ--------LAIVTQWCEGSSLyhhlHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNI 582
Cdd:cd07875    83 KNIIGLLNVFT-PQksleefqdVYIVMELMDANLC----QVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 583 FLHEDLTVKIGDFGLAtvksrwsgshqfeQLSGSILWMAPEVIRMQDKNP-------YSFQSDVYAFGIVLYELMTGQLP 655
Cdd:cd07875   158 VVKSDCTLKILDFGLA-------------RTAGTSFMMTPYVVTRYYRAPevilgmgYKENVDIWSVGCIMGEMIKGGVL 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 656 YSNINNRDQiifmvgrgyLSPDLSKVRSNCPKAMKRLMAeCLKKKRDERP---------LFPQIL 711
Cdd:cd07875   225 FPGTDHIDQ---------WNKVIEQLGTPCPEFMKKLQP-TVRTYVENRPkyagysfekLFPDVL 279
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
501-693 4.84e-12

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-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: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 67.65  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 501 EVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKfeMIKlIDIARQTAQ----GMDYLHAKSIIHR 575
Cdd:cd05574    51 EREILATLDHPFLPtLYASFQTSTHLCFVMDYCPGGELFRLLQKQPGK--RLP-EEVARFYAAevllALEYLHLLGFVYR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 576 DLKSNNIFLHEDLTVKIGDFGLA-------TVKSRWSGSH---------QFEQLSGSIL-----------WMAPEVIRmq 628
Cdd:cd05574   128 DLKPENILLHESGHIMLTDFDLSkqssvtpPPVRKSLRKGsrrssvksiEKETFVAEPSarsnsfvgteeYIAPEVIK-- 205
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 629 dKNPYSFQSDVYAFGIVLYELMTGQLP---------YSNINNRDqIIFmvgrgylsPDLSKVRSNCPKAMKRLM 693
Cdd:cd05574   206 -GDGHGSAVDWWTLGILLYEMLYGTTPfkgsnrdetFSNILKKE-LTF--------PESPPVSSEAKDLIRKLL 269
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
463-692 5.89e-12

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: 66.72  E-value: 5.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGT--VYKGKWHGD-VAVKMLNVTAPTPQQLQafkNEVGVLRKTRHVNILLFMGYSTKP-QLAIVTQWCEGSSLY 538
Cdd:cd14662     8 IGSGNFGVarLMRNKETKElVAVKYIERGLKIDENVQ---REIINHRSLRHPNIIRFKEVVLTPtHLAIVMEYAAGGELF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHL------HIIETKFEMIKLIdiarqtaQGMDYLHAKSIIHRDLKSNNIFLHEDLT--VKIGDFGLatvkSRWSGSH-Q 609
Cdd:cd14662    85 ERIcnagrfSEDEARYFFQQLI-------SGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGY----SKSSVLHsQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 610 FEQLSGSILWMAPEVIRMQDKNPYSfqSDVYAFGIVLYELMTGQLPYSN----INNRDQIIFMVGRGYLSPDLSKVRSNC 685
Cdd:cd14662   154 PKSTVGTPAYIAPEVLSRKEYDGKV--ADVWSCGVTLYVMLVGAYPFEDpddpKNFRKTIQRIMSVQYKIPDYVRVSQDC 231

                  ....*..
gi 1237938074 686 PKAMKRL 692
Cdd:cd14662   232 RHLLSRI 238
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
461-651 6.06e-12

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: 67.39  E-value: 6.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKG--KWHGD-VAVK---MLNVTAPTPqqLQAFKnEVGVLRKTRHVNILLF---------MGYSTKPQL 525
Cdd:cd07865    18 AKIGQGTFGEVFKArhRKTGQiVALKkvlMENEKEGFP--ITALR-EIKILQLLKHENVVNLieicrtkatPYNRYKGSI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 AIVTQWCEgSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWS 605
Cdd:cd07865    95 YLVFEFCE-HDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFSLAK 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1237938074 606 GShQFEQLSGSI--LWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMT 651
Cdd:cd07865   174 NS-QPNRYTNRVvtLWYRPPELLLGERD-YGPPIDMWGAGCIMAEMWT 219
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
545-689 7.82e-12

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 66.42  E-value: 7.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 545 ETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT-VKIGDFGLatVKSRWSGSHQfeqlSGSILWMAPE 623
Cdd:PHA03390  103 EGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDrIYLCDYGL--CKIIGTPSCY----DGTLDYFSPE 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 624 VIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSniNNRDQII---FMVGRGYLSPDLSKVRSncPKAM 689
Cdd:PHA03390  177 KIKGH---NYDVSFDWWAVGVLTYELLTGKHPFK--EDEDEELdleSLLKRQQKKLPFIKNVS--KNAN 238
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
519-669 7.83e-12

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: 67.35  E-value: 7.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKPQLAIVTQWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd05617    85 FQTTSRLFLVIEYVNGGDLMFHMQR-QRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMC 163
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 599 tvKSRWSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNIN-----NRDQIIFMV 669
Cdd:cd05617   164 --KEGLGPGDTTSTFCGTPNYIAPEILRGEE---YGFSVDWWALGVLMFEMMAGRSPFDIITdnpdmNTEDYLFQV 234
RBD cd01760
Ras-binding domain (RBD), structurally similar to a beta-grasp ubiquitin-like fold; The RBD of ...
158-225 8.16e-12

Ras-binding domain (RBD), structurally similar to a beta-grasp ubiquitin-like fold; The RBD of the serine/threonine kinase Raf is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. A Raf-like RBD is also present in Regulator of G protein Signaling (RGS12 and RGS14) members of GTPase activating proteins.


Pssm-ID: 340461  Cd Length: 71  Bit Score: 61.26  E-value: 8.16e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 158 RVFLPN-KQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRiqDGEKKPIGWDTDISWLTGEELHVE 225
Cdd:cd01760     4 RLFLPNnETSVVVAVKPGKSLHEVLMPVLERHGLQLECVDVFL--LGEKAPLDLNTDASSLIGQELRLD 70
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
456-705 8.38e-12

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: 66.33  E-value: 8.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQlqafKNEVGVLRKTR-HVNIllfmgystkPQL------ 525
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGidlKTGEEVAIKIEKKDSKHPQL----EYEAKVYKLLQgGPGI---------PRLywfgqe 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 526 ----AIVTQWCeGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL---TVKIGDFGLA 598
Cdd:cd14016    68 gdynVMVMDLL-GPSLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKnsnKVYLIDFGLA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 TV-KSRWSGSH----QFEQLSG-----SI---LWMApevirmqdknpysfQS---DVYAFGIVLYELMTGQLPYSNI--N 660
Cdd:cd14016   147 KKyRDPRTGKHipyrEGKSLTGtaryaSInahLGIE--------------QSrrdDLESLGYVLIYFLKGSLPWQGLkaQ 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1237938074 661 NRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERP 705
Cdd:cd14016   213 SKKEKYEKIGEKKMNTSPEELCKGLPKEFAKYLEYVRSLKFEEEP 257
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
461-669 9.17e-12

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: 67.01  E-value: 9.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTV------YKGKwhgDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILlfmgySTKPQLAIVTQWCEG 534
Cdd:cd07855    11 ETIGSGAYGVVcsaidtKSGQ---KVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNII-----AIRDILRPKVPYADF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIIETKFEMIklI--------DIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKS 602
Cdd:cd07855    83 KDVYVVLDLMESDLHHI--IhsdqpltlEHIRyflyQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLC 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 603 RWSGSHQF--EQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYElMTGQ---LPYSNINNRDQIIFMV 669
Cdd:cd07855   161 TSPEEHKYfmTEYVATRWYRAPEL--MLSLPEYTQAIDMWSVGCIFAE-MLGRrqlFPGKNYVHQLQLILTV 229
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
463-656 9.67e-12

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: 66.48  E-value: 9.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTV--YKGKWHGD-VAVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNIL--------LFMGYSTKPQLAIvtQW 531
Cdd:cd14039     1 LGTGGFGNVclYQNQETGEkIAIKSCRLELSVKNK-DRWCHEIQIMKKLNHPNVVkacdvpeeMNFLVNDVPLLAM--EY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 532 CEGSSLYHHLHIIET--KFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE---DLTVKIGDFGLATVKSRWSG 606
Cdd:cd14039    78 CSGGDLRKLLNKPENccGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEingKIVHKIIDLGYAKDLDQGSL 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 607 SHQFeqlSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14039   158 CTSF---VGTLQYLAPELF---ENKSYTVTVDYWSFGTMVFECIAGFRPF 201
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
535-648 1.10e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 67.61  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKSRWSGSHQFeQL 613
Cdd:PHA03211  244 SDLYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACfARGSWSTPFHY-GI 322
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1237938074 614 SGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYE 648
Cdd:PHA03211  323 AGTVDTNAPEVLA---GDPYTPSVDIWSAGLVIFE 354
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
519-663 1.48e-11

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: 66.59  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 519 YSTKPQLAIVTQWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd05618    90 FQTESRLFFVIEYVNGGDLMFHMQR-QRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMC 168
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 599 tvKSRWSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRD 663
Cdd:cd05618   169 --KEGLRPGDTTSTFCGTPNYIAPEILRGED---YGFSVDWWALGVLMFEMMAGRSPFDIVGSSD 228
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
463-704 1.58e-11

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: 65.54  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVY------KGKWHgdvAVKMLNVTAPTPQQLQAFK-NEVGVLRKTRHVNILLF---MGYS--TKPQLAIVTQ 530
Cdd:cd05606     2 IGRGGFGEVYgcrkadTGKMY---AMKCLDKKRIKMKQGETLAlNERIMLSLVSTGGDCPFivcMTYAfqTPDKLCFILD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHL--HIIETKFEMIKLidiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWS--- 605
Cdd:cd05606    79 LMNGGDLHYHLsqHGVFSEAEMRFY---AAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKpha 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 --GSHQFeqlsgsilwMAPEVIrmQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQiiFMVGRGYLSPDLSKVRS 683
Cdd:cd05606   156 svGTHGY---------MAPEVL--QKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDK--HEIDRMTLTMNVELPDS 222
                         250       260
                  ....*....|....*....|.
gi 1237938074 684 NCPKaMKRLMAECLKKKRDER 704
Cdd:cd05606   223 FSPE-LKSLLEGLLQRDVSKR 242
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
459-666 1.74e-11

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: 65.31  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGKWHG---DVAVKMLNVTAptpQQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQWCEG 534
Cdd:cd14108     6 IHKEIGRGAFSYLRRVKEKSsdlSFAAKFIPVRA---KKKTSARRELALLAELDHKSIVRFHdAFEKRRVVIIVTELCHE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLYHHLH---IIETKFEmikliDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT--VKIGDFGLAtvKSRWSGSHQ 609
Cdd:cd14108    83 ELLERITKrptVCESEVR-----SYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNA--QELTPNEPQ 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 610 FEQLsGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQII 666
Cdd:cd14108   156 YCKY-GTPEFVAPEIV---NQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLM 208
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
515-663 1.87e-11

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: 65.98  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 515 LFMGYSTKPQLAIVTQWCEGSSLYHHLHIIEtKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGD 594
Cdd:cd05591    61 LHSCFQTKDRLFFVMEYVNGGDLMFQIQRAR-KFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLAD 139
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 595 FGLAtvKSRWSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRD 663
Cdd:cd05591   140 FGMC--KEGILNGKTTTTFCGTPDYIAPEILQELE---YGPSVDWWALGVLMYEMMAGQPPFEADNEDD 203
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
235-280 2.30e-11

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410380  Cd Length: 52  Bit Score: 59.19  E-value: 2.30e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 235 HNFVRKTFFTLAFCDFCRKLLF----QGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:cd20830     1 HRFVEQSFSTLQWCDKCGKFLFglvhQGLQCQDCGLVCHRTCAATGLPKC 50
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
463-656 3.94e-11

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: 65.01  E-value: 3.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTV----YKGKwhGDV-AVKMLN----VTAPTPQQLQAFKNEVGVLRKTRH---VNilLFMGYSTKPQLAIVTQ 530
Cdd:cd05589     7 LGRGHFGKVllaeYKPT--GELfAIKALKkgdiIARDEVESLMCEKRIFETVNSARHpflVN--LFACFQTPEHVCFVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 531 WCEGSSLYHHLHiiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL-------ATVKSR 603
Cdd:cd05589    83 YAAGGDLMMHIH--EDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLckegmgfGDRTST 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237938074 604 WSGSHQFeqlsgsilwMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05589   161 FCGTPEF---------LAPEVLT---DTSYTRAVDWWGLGVLIYEMLVGESPF 201
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
457-714 5.02e-11

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: 63.80  E-value: 5.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKGK-----------WHGDVAVK-MLNVTAPTPQQLQ-AFKNEVGVLRKTRHVNILLFMGYSTKP 523
Cdd:cd05077     1 IVQGEHLGRGTRTQIYAGIlnykdddedegYSYEKEIKvILKVLDPSHRDISlAFFETASMMRQVSHKHIVLLYGVCVRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 524 QLAI-VTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT-------VKIGDF 595
Cdd:cd05077    81 VENImVEEFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLAREGIdgecgpfIKLSDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 596 GLA-TVKSRwsgshqfEQLSGSILWMAPEVIrmQDKNPYSFQSDVYAFGIVLYEL-MTGQLPYSNINNRDQIIFMVGRGY 673
Cdd:cd05077   161 GIPiTVLSR-------QECVERIPWIAPECV--EDSKNLSIAADKWSFGTTLWEIcYNGEIPLKDKTLAEKERFYEGQCM 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1237938074 674 LspdlskVRSNCpKAMKRLMAECLKKKRDERPLFPQILASI 714
Cdd:cd05077   232 L------VTPSC-KELADLMTHCMNYDPNQRPFFRAIMRDI 265
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
451-692 5.91e-11

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: 64.72  E-value: 5.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQR------IGSGSFGTV---YKGKWHGDVAVKMLnvTAPTPQQLQAFK--NEVGVLRKTRHVNILLFMGY 519
Cdd:cd07874     7 EVGDSTFTVLKRyqnlkpIGSGAQGIVcaaYDAVLDRNVAIKKL--SRPFQNQTHAKRayRELVLMKCVNHKNIISLLNV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 520 STkPQLAIVtqwcEGSSLY--------HHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVK 591
Cdd:cd07874    85 FT-PQKSLE----EFQDVYlvmelmdaNLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 592 IGDFGLAtvksrwsgshqfeQLSGSILWMAPEVIRMQDKNP-------YSFQSDVYAFGIVLYELMtgqlpysninnRDQ 664
Cdd:cd07874   160 ILDFGLA-------------RTAGTSFMMTPYVVTRYYRAPevilgmgYKENVDIWSVGCIMGEMV-----------RHK 215
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1237938074 665 IIFmVGRGYL---SPDLSKVRSNCPKAMKRL 692
Cdd:cd07874   216 ILF-PGRDYIdqwNKVIEQLGTPCPEFMKKL 245
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
462-665 6.98e-11

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: 63.83  E-value: 6.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 462 RIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFkNEVGVLRK-TRHVNILLFMG--YSTKP-QLAIVTQWCEG 534
Cdd:cd07831     6 KIGEGTFSEVLKAQSRKTgkyYAIKCMKKHFKSLEQVNNL-REIQALRRlSPHPNILRLIEvlFDRKTgRLALVFELMDM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SsLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDlTVKIGDFGLAT-----------VKSR 603
Cdd:cd07831    85 N-LYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSCRgiyskppyteyISTR 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 604 WsgshqfeqlsgsilWMAPEVIrMQDkNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 665
Cdd:cd07831   163 W--------------YRAPECL-LTD-GYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQI 208
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
463-596 7.45e-11

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: 60.53  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK--GKWHG-DVAVKMLNVTapTPQQLQAFKNEVGVLRKTR--HVNILLFMGYSTKPQ-LAIVTQWCEGSS 536
Cdd:cd13968     1 MGEGASAKVFWaeGECTTiGVAVKIGDDV--NNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGpNILLMELVKGGT 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIiETKFEmIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG 596
Cdd:cd13968    79 LIAYTQE-EELDE-KDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
433-669 8.20e-11

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 64.67  E-value: 8.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 433 EDRNRMKTLGRRDSSDDWEIPDGQIT--------VGQRIGSGSFGTVYKG---KWHGDVAVKMLnvtAPTPQqlqaFKN- 500
Cdd:PTZ00036   36 DEEERSHNNNAGEDEDEEKMIDNDINrspnksykLGNIIGNGSFGVVYEAiciDTSEKVAIKKV---LQDPQ----YKNr 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 501 EVGVLRKTRHVNILLFMGY----STKPQ-----LAIVTQWCEGSSLYHHLHIIETKFEM----IKLIdiARQTAQGMDYL 567
Cdd:PTZ00036  109 ELLIMKNLNHINIIFLKDYyyteCFKKNeknifLNVVMEFIPQTVHKYMKHYARNNHALplflVKLY--SYQLCRALAYI 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 568 HAKSIIHRDLKSNNIFLHEDL-TVKIGDFGLAtvKSRWSGSHQFEQLSgSILWMAPEVirMQDKNPYSFQSDVYAFGIVL 646
Cdd:PTZ00036  187 HSKFICHRDLKPQNLLIDPNThTLKLCDFGSA--KNLLAGQRSVSYIC-SRFYRAPEL--MLGATNYTTHIDLWSLGCII 261
                         250       260
                  ....*....|....*....|...
gi 1237938074 647 YELMTGQLPYSNINNRDQIIFMV 669
Cdd:PTZ00036  262 AEMILGYPIFSGQSSVDQLVRII 284
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
556-708 8.88e-11

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: 64.12  E-value: 8.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 556 IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvksRwSGSHQFEQLSGSIL-------WM-APEVIRM 627
Cdd:cd07852   112 IMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLA----R-SLSQLEEDDENPVLtdyvatrWYrAPEILLG 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 628 QDKnpYSFQSDVYAFGIVLYELMTGQlPY----SNINNRDQIIFMVGRgyLS-PDLSKVRSncPKAMKRLMAECLKKKRD 702
Cdd:cd07852   187 STR--YTKGVDMWSVGCILGEMLLGK-PLfpgtSTLNQLEKIIEVIGR--PSaEDIESIQS--PFAATMLESLPPSRPKS 259

                  ....*.
gi 1237938074 703 ERPLFP 708
Cdd:cd07852   260 LDELFP 265
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
235-280 1.09e-10

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. 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. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 57.28  E-value: 1.09e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 235 HNFVRKTFFTLAFCDFCRKLLF----QGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVglvrQGLVCEVCGYACHVSCADKAPQVC 50
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
461-677 1.14e-10

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: 63.29  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKG--KWHGD-VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEgSS 536
Cdd:cd07860     6 EKIGEGTYGVVYKArnKLTGEvVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVkLLDVIHTENKLYLVFEFLH-QD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHII---ETKFEMIKliDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQL 613
Cdd:cd07860    85 LKKFMDASaltGIPLPLIK--SYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237938074 614 SgsiLWM-APEVI---RMqdknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQiIFMVGRGYLSPD 677
Cdd:cd07860   163 T---LWYrAPEILlgcKY-----YSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQ-LFRIFRTLGTPD 221
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
463-652 1.18e-10

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; 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. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 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: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 63.32  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGDV-AVKMLNVTAPT-PQQLQAF-KNEVGVLRKTRHVNILLFMGYSTKPQL-AIVTQWCEGSSLY 538
Cdd:cd14157     1 ISEGTFADIYKGYRHGKQyVIKRLKETECEsPKSTERFfQTEVQICFRCCHPNILPLLGFCVESDChCLIYPYMPNGSLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 539 HHL------HIIETKfemiKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL----ATVKSRWSgSH 608
Cdd:cd14157    81 DRLqqqggsHPLPWE----QRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGLrlcpVDKKSVYT-MM 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1237938074 609 QFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTG 652
Cdd:cd14157   156 KTKVLQISLAYLPEDFVR---HGQLTEKVDIFSCGVVLAEILTG 196
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
463-661 1.26e-10

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: 63.28  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWH--GD-VAVKMLNvtapTPQQLQAFK----NEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd07864    15 IGEGTYGQVYKAKDKdtGElVALKKVR----LDNEKEGFPitaiREIKILRQLNHRSVVNLKEIVTDKQDALDFKKDKGA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 ------SLYHHLH-IIETK---FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWS 605
Cdd:cd07864    91 fylvfeYMDHDLMgLLESGlvhFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARL---YN 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 606 GSHQFEQLSGSI-LWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMTgQLPYSNINN 661
Cdd:cd07864   168 SEESRPYTNKVItLWYRPPELLLGEER-YGPAIDVWSCGCILGELFT-KKPIFQANQ 222
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
459-672 1.47e-10

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: 62.72  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGT----VYKGKwHGDVAVKMLNVTAPTPQQlqafknEVGVL-RKTRHVNILLFMG-YSTKPQLAIVTQWC 532
Cdd:cd14178     7 IKEDIGIGSYSVckrcVHKAT-STEYAVKIIDKSKRDPSE------EIEILlRYGQHPNIITLKDvYDDGKFVYLVMELM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLYHHlhIIETK-FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL----TVKIGDFGLATvksrwsgs 607
Cdd:cd14178    80 RGGELLDR--ILRQKcFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAK-------- 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 608 hQFEQLSGSIL-------WMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSN--INNRDQIIFMVGRG 672
Cdd:cd14178   150 -QLRAENGLLMtpcytanFVAPEVLKRQG---YDAACDIWSLGILLYTMLAGFTPFANgpDDTPEEILARIGSG 219
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
463-665 1.53e-10

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: 62.74  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD----VAVKMLNVTAPTPQQLQAFKNEVGVLRKTR---HVNILLFMGYSTKPQLAIVTQWcegS 535
Cdd:cd07862     9 IGEGAYGKVFKARDLKNggrfVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTVSRTDRETKL---T 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKF-----------EMIKliDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrw 604
Cdd:cd07862    86 LVFEHVDQDLTTYldkvpepgvptETIK--DMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYS-- 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237938074 605 sgshqFEQLSGSI---LWM-APEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 665
Cdd:cd07862   162 -----FQMALTSVvvtLWYrAPEVLL---QSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQL 218
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
456-664 1.62e-10

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: 63.16  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 456 QITVGQRIGSGSFGTVY------KGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS--TKPQLAI 527
Cdd:cd05633     6 DFSVHRIIGRGGFGEVYgcrkadTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAfhTPDKLCF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 528 VTQWCEGSSLYHHL--HIIETKFEMIKLidiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRws 605
Cdd:cd05633    86 ILDLMNGGDLHYHLsqHGVFSEKEMRFY---ATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK-- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 606 gsHQFEQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ 664
Cdd:cd05633   161 --KKPHASVGTHGYMAPEV--LQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 215
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
457-714 1.88e-10

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: 62.23  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 457 ITVGQRIGSGSFGTVYKGKWHGDVAVK------MLNVTAPTPQQLQ-AFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVT 529
Cdd:cd14208     1 LTFMESLGKGSFTKIYRGLRTDEEDDErcetevLLKVMDPTHGNCQeSFLEAASIMSQISHKHLVLLHGVCVGKDSIMVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QW-CEGS-SLY----HHLHIIETKFEMikliDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT------VKIGDFGL 597
Cdd:cd14208    81 EFvCHGAlDLYlkkqQQKGPVAISWKL----QVVKQLAYALNYLEDKQLVHGNVSAKKVLLSREGDkgsppfIKLSDPGV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 598 A-TVKSRwsgshqfEQLSGSILWMAPEVIRmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFMVGRGYL- 674
Cdd:cd14208   157 SiKVLDE-------ELLAERIPWVAPECLS--DPQNLALEADKWGFGATLWEIFSgGHMPLSALDPSKKLQFYNDRKQLp 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1237938074 675 SPDLSKVRSncpkamkrLMAECLKKKRDERPLFPQILASI 714
Cdd:cd14208   228 APHWIELAS--------LIQQCMSYNPLLRPSFRAIIRDL 259
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
463-711 1.92e-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: 62.44  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKwHGD----VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 537
Cdd:cd07846     9 VGEGSYGMVMKCR-HKEtgqiVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVnLIEVFRRKKRWYLVFEFVDHTVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 538 yHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT------------VKSRWs 605
Cdd:cd07846    88 -DDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtlaapgevytdyVATRW- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 606 gshqfeqlsgsilWMAPEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQ--LP--------------YSNINNRDQIIFM- 668
Cdd:cd07846   166 -------------YRAPELLVGDTK--YGKAVDVWAVGCLVTEMLTGEplFPgdsdidqlyhiikcLGNLIPRHQELFQk 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 669 --VGRGYLSPDLSKV---RSNCPK---AMKRLMAECLKKKRDERPLFPQIL 711
Cdd:cd07846   231 npLFAGVRLPEVKEVeplERRYPKlsgVVIDLAKKCLHIDPDKRPSCSELL 281
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
463-664 1.93e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein 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. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK 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: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 62.82  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTV---YKGKWHGDVAVKML-----NVTAPTpqqlQAFKnEVGVLRKTRHVNILLFMGYSTkPQlaivTQWCEG 534
Cdd:cd07850     8 IGSGAQGIVcaaYDTVTGQNVAIKKLsrpfqNVTHAK----RAYR-ELVLMKLVNHKNIIGLLNVFT-PQ----KSLEEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 535 SSLY-------HHLH-IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKsrwSG 606
Cdd:cd07850    78 QDVYlvmelmdANLCqVIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA---GT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938074 607 SHQFEQLSGSILWMAPEVIR-MqdknPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ 664
Cdd:cd07850   155 SFMMTPYVVTRYYRAPEVILgM----GYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQ 209
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
458-664 2.33e-10

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: 62.76  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 458 TVGQRIGSGSFGTVY------KGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS--TKPQLAIVT 529
Cdd:cd14223     3 SVHRIIGRGGFGEVYgcrkadTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAfhTPDKLSFIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHL--HIIETKFEMIKLidiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwsgs 607
Cdd:cd14223    83 DLMNGGDLHYHLsqHGVFSEAEMRFY---AAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSK---- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237938074 608 HQFEQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ 664
Cdd:cd14223   156 KKPHASVGTHGYMAPEV--LQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 210
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
556-656 2.60e-10

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: 61.97  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 556 IARQTAQGMDYLHAKSIIHRDLKSNNIFLH--EDLT-VKIGDFGLAT-VKSRWS----GSHQFEQLSGSILWMAPEVIRM 627
Cdd:cd14174   105 VVRDIASALDFLHTKGIAHRDLKPENILCEspDKVSpVKICDFDLGSgVKLNSActpiTTPELTTPCGSAEYMAPEVVEV 184
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1237938074 628 --QDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14174   185 ftDEATFYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
463-663 2.80e-10

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: 62.59  E-value: 2.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGD---VAVKMLN----VTAPTPQQLQAFKNEVGVLRKTRHVNilLFMGYSTKPQLAIVTQWCEGS 535
Cdd:cd05610    12 ISRGAFGKVYLGRKKNNsklYAVKVVKkadmINKNMVHQVQAERDALALSKSPFIVH--LYYSLQSANNVYLVMEYLIGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 536 SLYHHLHIIETKFEMIKLIDIArQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVK-------------- 601
Cdd:cd05610    90 DVKSLLHIYGYFDEEMAVKYIS-EVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTlnrelnmmdilttp 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 602 SRWSGSHQFEQLSGSIL-------------------------------------WMAPEVIRmqdKNPYSFQSDVYAFGI 644
Cdd:cd05610   169 SMAKPKNDYSRTPGQVLslisslgfntptpyrtpksvrrgaarvegerilgtpdYLAPELLL---GKPHGPAVDWWALGV 245
                         250       260
                  ....*....|....*....|....*...
gi 1237938074 645 VLYELMTG---------QLPYSNINNRD 663
Cdd:cd05610   246 CLFEFLTGippfndetpQQVFQNILNRD 273
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
461-705 2.85e-10

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L 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: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 62.19  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYK---GKWHGDVAVKMLNVTAPTPQQLQAfkNEVGVLR--KTRHVNILLF------------------- 516
Cdd:cd13977     6 REVGRGSYGVVYEavvRRTGARVAVKKIRCNAPENVELAL--REFWALSsiQRQHPNVIQLeecvlqrdglaqrmshgss 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 517 ------------------MGYSTKPQLAIVTQWCEGSSLyhHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLK 578
Cdd:cd13977    84 ksdlylllvetslkgercFDPRSACYLWFVMEFCDGGDM--NEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDLK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 579 SNNIFLHE---DLTVKIGDFGLATVkSRWSG----------SHQFEQLSGSILWMAPEVIrmqdKNPYSFQSDVYAFGIV 645
Cdd:cd13977   162 PDNILISHkrgEPILKVADFGLSKV-CSGSGlnpeepanvnKHFLSSACGSDFYMAPEVW----EGHYTAKADIFALGII 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 646 LYElMTGQLPYSNINNRDQI----------IFMVGRGYL-SPDLS-----KVRSNCPKAMKRLMAECLKKKRDERP 705
Cdd:cd13977   237 IWA-MVERITFRDGETKKELlgtyiqqgkeIVPLGEALLeNPKLElqiplKKKKSMNDDMKQLLRDMLAANPQERP 311
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
561-656 2.85e-10

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: 62.33  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 561 AQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvKSRWSGSHQFEQ---LSGSILWMAPEVIRMQDknpYSFQS 637
Cdd:cd05598   111 VCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWTHDSKYYLahsLVGTPNYIAPEVLLRTG---YTQLC 186
                          90
                  ....*....|....*....
gi 1237938074 638 DVYAFGIVLYELMTGQLPY 656
Cdd:cd05598   187 DWWSVGVILYEMLVGQPPF 205
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
563-664 2.86e-10

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: 62.44  E-value: 2.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 563 GMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAF 642
Cdd:cd05588   108 ALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMC--KEGLRPGDTTSTFCGTPNYIAPEILRGED---YGFSVDWWAL 182
                          90       100
                  ....*....|....*....|....*
gi 1237938074 643 GIVLYELMTGQLPY---SNINNRDQ 664
Cdd:cd05588   183 GVLMFEMLAGRSPFdivGSSDNPDQ 207
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
463-656 3.54e-10

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: 61.98  E-value: 3.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK---GKWHGDVAVKMLN--VTAPTPQQLQAFKNEVGvlrktrHVNIL-LFMGYSTKPQLAIVTQWCEGSS 536
Cdd:cd14179    15 LGEGSFSICRKclhKKTNQEYAVKIVSkrMEANTQREIAALKLCEG------HPNIVkLHEVYHDQLHTFLVMELLKGGE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHL----HIIETKFEMIklidiARQTAQGMDYLHAKSIIHRDLKSNNIFL---HEDLTVKIGDFGLATVKSrwSGSHQ 609
Cdd:cd14179    89 LLERIkkkqHFSETEASHI-----MRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKP--PDNQP 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 610 FEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd14179   162 LKTPCFTLHYAAPELL---NYNGYDESCDLWSLGVILYTMLSGQVPF 205
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
461-669 3.60e-10

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: 61.68  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEgSS 536
Cdd:cd07839     6 EKIGEGTYGTVFKAKNRETheiVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVrLYDVLHSDKKLTLVFEYCD-QD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 537 LYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSgs 616
Cdd:cd07839    85 LKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCYSAEVVT-- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 617 iLWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMTGQ---LPYSNINNRDQIIFMV 669
Cdd:cd07839   163 -LWYRPPDVLFGAKL-YSTSIDMWSAGCIFAELANAGrplFPGNDVDDQLKRIFRL 216
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
463-656 3.88e-10

Catalytic domain of Suppressor of loss of cAMP-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 Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-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: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 62.20  E-value: 3.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYKGKWHGDVAVKMLNVTAptpQQLQAFKNEVGVLRKTRhvNIL-------------LFMGYSTKPQLAIVT 529
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLS---KKVIVAKKEVAHTIGER--NILvrtaldespfivgLKFSFQTPTDLYLVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 530 QWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQ 609
Cdd:cd05586    76 DYMSGGELFWHLQK-EGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLS--KADLTDNKT 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1237938074 610 FEQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPY 656
Cdd:cd05586   153 TNTFCGTTEYLAPEV--LLDEKGYTKMVDFWSLGVLVFEMCCGWSPF 197
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
459-609 4.25e-10

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; 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. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon 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: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 61.23  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 459 VGQRIGSGSFGTVYKGK--WHGD-VAVKMLNVTAPTPQQLQAFKnevgvLRKTRH--VNILLFMGYSTKPQLAIVTQWCE 533
Cdd:cd14125     4 LGRKIGSGSFGDIYLGTniQTGEeVAIKLESVKTKHPQLLYESK-----LYKILQggVGIPNVRWYGVEGDYNVMVMDLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 534 GSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNiFL----HEDLTVKIGDFGLATvKSRWSGSHQ 609
Cdd:cd14125    79 GPSLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDN-FLmglgKKGNLVYIIDFGLAK-KYRDPRTHQ 156
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
499-710 4.38e-10

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: 61.05  E-value: 4.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 499 KNEVGVLRKTRHVNILLFMGySTKPQLAI--VTQWCEGSSLYHHLH---------IIETKFEMIKLIDIARqtaqGMDYL 567
Cdd:cd14044    51 KIELNKLLQIDYYNLTKFYG-TVKLDTMIfgVIEYCERGSLRDVLNdkisypdgtFMDWEFKISVMYDIAK----GMSYL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 568 HA-KSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwsgshqfeqlSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVL 646
Cdd:cd14044   126 HSsKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILP-----------PSKDLWTAPEHLRQAG---TSQKGDVYSYGIIA 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938074 647 YELMTGQLPY--SNINNRDQIIFMV----GRGYLSPDLSkVRSNCPKAMK--RLMAECLKKKRDERPLFPQI 710
Cdd:cd14044   192 QEIILRKETFytAACSDRKEKIYRVqnpkGMKPFRPDLN-LESAGEREREvyGLVKNCWEEDPEKRPDFKKI 262
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
234-280 6.14e-10

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 55.11  E-value: 6.14e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 234 THNFVRKTFFTLAFCDFCRKLLF----QGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:cd20827     1 PHRFEKHNFTTPTYCDYCSSLLWglvkTGMRCADCGYSCHEKCLEHVPKNC 51
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
235-280 6.31e-10

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; 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 are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 55.39  E-value: 6.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237938074 235 HNFVRKTFFTLAFCDFCRKLLF----QGFRCQTCGYKFHQRCSTEVPLMC 280
Cdd:cd20795     4 HSLFVHSYKSPTFCDFCGEMLFglvrQGLKCEGCGLNFHKRCAYKIPNNC 53
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
559-653 6.94e-10

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: 61.23  E-value: 6.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 559 QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKsrwSGSHQFEQLSGSILWM-APEVIRMQDKnpYSFQS 637
Cdd:cd07858   116 QLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTT---SEKGDFMTEYVVTRWYrAPELLLNCSE--YTTAI 190
                          90
                  ....*....|....*.
gi 1237938074 638 DVYAFGIVLYELMTGQ 653
Cdd:cd07858   191 DVWSVGCIFAELLGRK 206
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
559-721 7.89e-10

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: 61.17  E-value: 7.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 559 QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT---------------VKSRWsgshqfeqlsgsilWMAPE 623
Cdd:cd07849   114 QILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARiadpehdhtgflteyVATRW--------------YRAPE 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 624 VirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI--IFMV-GrgylSP---DLSKVRSncPKAMKRLMAECL 697
Cdd:cd07849   180 I--MLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLnlILGIlG----TPsqeDLNCIIS--LKARNYIKSLPF 251
                         170       180
                  ....*....|....*....|....*
gi 1237938074 698 KKKRDERPLFPQI-LASIELLARSL 721
Cdd:cd07849   252 KPKVPWNKLFPNAdPKALDLLDKML 276
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
463-693 1.14e-09

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: 60.91  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 463 IGSGSFGTVYK------GKwhgDVAVK-MLNVTaptpQQLQAFKN---EVGVLRKTRHVNILLFMGYSTKPQLaivtqwc 532
Cdd:cd07853     8 IGYGAFGVVWSvtdprdGK---RVALKkMPNVF----QNLVSCKRvfrELKMLCFFKHDNVLSALDILQPPHI------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 egsSLYHHLHIIE--TKFEMIKLI--------DIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA 598
Cdd:cd07853    74 ---DPFEEIYVVTelMQSDLHKIIvspqplssDHVKvflyQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 599 TVKSRWSGSHQFEQLSgSILWMAPEVIrMQDKNpYSFQSDVYAFGIVLYELMTGQLPY---SNINNRDQIIFMVGrgylS 675
Cdd:cd07853   151 RVEEPDESKHMTQEVV-TQYYRAPEIL-MGSRH-YTSAVDIWSVGCIFAELLGRRILFqaqSPIQQLDLITDLLG----T 223
                         250
                  ....*....|....*...
gi 1237938074 676 PDLSKVRSNCPKAMKRLM 693
Cdd:cd07853   224 PSLEAMRSACEGARAHIL 241
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
515-660 1.31e-09

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: 60.28  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 515 LFMGYSTKPQLAIVTQWCEGSSLYHHLHIiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGD 594
Cdd:cd05585    59 LKFSFQSPEKLYLVLAFINGGELFHHLQR-EGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCD 137
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237938074 595 FGLAtvKSRWSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNIN 660
Cdd:cd05585   138 FGLC--KLNMKDDDKTNTFCGTPEYLAPELLLGHG---YTKAVDWWTLGVLLYEMLTGLPPFYDEN 198
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
493-697 1.43e-09

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: 59.64  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 493 QQLQAFKNEVGVLRKTRHVNILLFM-GY-STKPQLAIVT------------QWCEGSSLYHH-----LHIIETKFEMIKL 553
Cdd:cd14011    44 QILELLKRGVKQLTRLRHPRILTVQhPLeESRESLAFATepvfaslanvlgERDNMPSPPPElqdykLYDVEIKYGLLQI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 554 IDiarqtaqGMDYLH-AKSIIHRDLKSNNIFLHEDLTVKIGDFGLA-TVKSRWSGSHQFEQLSGSIL--------WMAPE 623
Cdd:cd14011   124 SE-------ALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCiSSEQATDQFPYFREYDPNLPplaqpnlnYLAPE 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237938074 624 VIRmqdKNPYSFQSDVYAFGIVLYElmtgqlpysnINNRDQIIFMVGRGYLSPdlsKVRSNCPKAMKRLMAECL 697
Cdd:cd14011   197 YIL---SKTCDPASDMFSLGVLIYA----------IYNKGKPLFDCVNNLLSY---KKNSNQLRQLSLSLLEKV 254
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
512-656 1.72e-09

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: 59.78  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 512 NILLFMGYST-KPQLAIVTQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL---HED 587
Cdd:cd14171    70 NSVQFPGESSpRARLLIVMELMEGGELFDRI-SQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSED 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 588 LTVKIGDFGLATVKSRWSGSHQFeqlsgSILWMAPEVIRMQDKN------------PYSFQS--DVYAFGIVLYELMTGQ 653
Cdd:cd14171   149 APIKLCDFGFAKVDQGDLMTPQF-----TPYYVAPQVLEAQRRHrkersgiptsptPYTYDKscDMWSLGVIIYIMLCGY 223

                  ...
gi 1237938074 654 LPY 656
Cdd:cd14171   224 PPF 226
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
451-710 2.13e-09

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: 60.04  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 451 EIPDGQITVGQR------IGSGSFGTV---YKGKWHGDVAVKMLnvTAPTPQQLQAFK--NEVGVLRKTRHVNILLFMGY 519
Cdd:cd07876    11 QVADSTFTVLKRyqqlkpIGSGAQGIVcaaFDTVLGINVAVKKL--SRPFQNQTHAKRayRELVLLKCVNHKNIISLLNV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 520 STkPQLAIVtqwcEGSSLYHHLHIIETKFEMIKLIDIAR--------QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVK 591
Cdd:cd07876    89 FT-PQKSLE----EFQDVYLVMELMDANLCQVIHMELDHermsyllyQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 592 IGDFGLATVKSRwsgSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ---IIFM 668
Cdd:cd07876   164 ILDFGLARTACT---NFMMTPYVVTRYYRAPEVILGMG---YKENVDIWSVGCIMGELVKGSVIFQGTDHIDQwnkVIEQ 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1237938074 669 VGrgylSPDLskvrsncpKAMKRLMaECLKKKRDERPLFPQI 710
Cdd:cd07876   238 LG----TPSA--------EFMNRLQ-PTVRNYVENRPQYPGI 266
C1_CHN cd20806
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ...
235-281 2.38e-09

protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410356  Cd Length: 53  Bit Score: 53.47  E-value: 2.38e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 235 HNFVRKTFFTLAFCDFCRKLLF----QGFRCQTCGYKFHQRCSTEVPLMCV 281
Cdd:cd20806     2 HNFKVHTFKGPHWCDYCGNFMWgliaQGVKCEDCGFNAHKQCSKLVPHDCQ 52
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
461-646 2.70e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. 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 Wee1b 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: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 58.79  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 461 QRIGSGSFGTVYK--GKWHGDV-AVK--MLNVTAPTPQQLqAFKnEV---GVLRKTRHVnILLFMGYSTKPQLAIVTQWC 532
Cdd:cd14139     6 EKIGVGEFGSVYKciKRLDGCVyAIKrsMRPFAGSSNEQL-ALH-EVyahAVLGHHPHV-VRYYSAWAEDDHMIIQNEYC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 533 EGSSLyhHLHIIETK-----FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTV----------------- 590
Cdd:cd14139    83 NGGSL--QDAISENTksgnhFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKMQSssgvgeevsneedefls 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938074 591 -----KIGDFGLATVKSrwsgSHQFEQlsGSILWMAPEVirMQDKNPYSFQSDVYAFGIVL 646
Cdd:cd14139   161 anvvyKIGDLGHVTSIN----KPQVEE--GDSRFLANEI--LQEDYRHLPKADIFALGLTV 213
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
559-653 2.75e-09

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: 59.34  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938074 559 QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksrwSGSHQFEQLSG-------SILWMAPEVirMQDKN 631
Cdd:cd07857   113 QILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLAR-----GFSENPGENAGfmteyvaTRWYRAPEI--MLSFQ 185
                          90       100
                  ....*....|....*....|..
gi 1237938074 632 PYSFQSDVYAFGIVLYELMTGQ 653
Cdd:cd07857   186 SYTKAIDVWSVGCILAELLGRK 207
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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