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Conserved domains on  [gi|568937340|ref|XP_006530458|]
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kinase suppressor of Ras 2 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
293-562 0e+00

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: 591.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14153    1 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISGVLQAGRRDDKLRI 452
Cdd:cd14153   81 RTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFTISGVLQAGRREDKLRI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 453 QNGWLCHLAPEIIRQLSPDTEEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEIS 532
Cdd:cd14153  161 QSGWLCHLAPEIIRQLSPETEEDKLPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNLSQIGMGKEIS 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 568937340 533 DILLFCWAFEQEERPTFTKLMDMLEKLPKR 562
Cdd:cd14153  241 DILLFCWAYEQEERPTFSKLMEMLEKLPKR 270
C1_KSR2 cd20873
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and ...
36-92 6.12e-34

protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and similar proteins; 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. 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: 410423  Cd Length: 57  Bit Score: 122.88  E-value: 6.12e-34
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340  36 GNSIKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLIIHRG 92
Cdd:cd20873    1 GNSIKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLIIHRG 57
 
Name Accession Description Interval E-value
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
293-562 0e+00

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: 591.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14153    1 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISGVLQAGRRDDKLRI 452
Cdd:cd14153   81 RTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFTISGVLQAGRREDKLRI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 453 QNGWLCHLAPEIIRQLSPDTEEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEIS 532
Cdd:cd14153  161 QSGWLCHLAPEIIRQLSPETEEDKLPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNLSQIGMGKEIS 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 568937340 533 DILLFCWAFEQEERPTFTKLMDMLEKLPKR 562
Cdd:cd14153  241 DILLFCWAYEQEERPTFSKLMEMLEKLPKR 270
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
294-556 1.96e-47

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 166.52  E-value: 1.96e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  294 LEIGELIGKGRFGQVYHGRWHG-------EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGegentkiKVAVKTLK-EGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  367 TSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFsisgvlQAGR 445
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVkISDFGLS------RDIY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  446 RDDKLRIQNG------WlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTG- 517
Cdd:pfam07714 154 DDDYYRKRGGgklpikW---MAPESLKDGK---------FTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEFLEDGy 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 568937340  518 --MKPNlsqiGMGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:pfam07714 222 rlPQPE----NCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
295-553 5.24e-41

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 148.83  E-value: 5.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKtgkLVAIKVIKKKKIKKDR-ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   372 GRTLYSVVRDAKIvLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGRRDDKL 450
Cdd:smart00220  81 GGDLFDLLKKRGR-LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDeDGHVKLADFGL---ARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   451 RiqnGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNL--SQIGMG 528
Cdd:smart00220 157 V---GTPEYMAPEVLLG---------KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFppPEWDIS 224
                          250       260
                   ....*....|....*....|....*
gi 568937340   529 KEISDILLFCWAFEQEERPTFTKLM 553
Cdd:smart00220 225 PEAKDLIRKLLVKDPEKRLTAEEAL 249
C1_KSR2 cd20873
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and ...
36-92 6.12e-34

protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and similar proteins; 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. 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: 410423  Cd Length: 57  Bit Score: 122.88  E-value: 6.12e-34
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340  36 GNSIKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLIIHRG 92
Cdd:cd20873    1 GNSIKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLIIHRG 57
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
295-547 3.61e-32

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 129.75  E-value: 3.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIER-DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:COG0515   10 RILRLLGRGGMGVVYLARDLRlgrPVALKVLRPELaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsisgvlqAGRRDDK 449
Cdd:COG0515   90 EGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTpDGRVKLIDFGI--------ARALGGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIQNGWLC----HLAPEIIRQLSPDTeedklpfskHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI 525
Cdd:COG0515  161 TLTQTGTVVgtpgYMAPEQARGEPVDP---------RSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSEL 231
                        250       260
                 ....*....|....*....|....
gi 568937340 526 GMG--KEISDILLFCWAFEQEERP 547
Cdd:COG0515  232 RPDlpPALDAIVLRALAKDPEERY 255
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
294-502 1.44e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 65.99  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHGRWHGEVAIRLIDIerdnedqLKafKREVMAYRQTRHEN-------------VVLFMGACMSP 360
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKC-------LK--KREILKMKQVQHVAqeksilmelshpfIVNMMCSFQDE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 361 PHLAIITSLCKGRTLYSVVRDA-KIVLDVNKTrqIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsis 438
Cdd:PTZ00263  91 NRVYFLLEFVVGGELFTHLRKAgRFPNDVAKF--YHAELVLAFEYLHSKDIIYRDLKPENLLLDNkGHVKVTDFGF---- 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 439 gvlqAGRRDDKLRIQNGWLCHLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPF 502
Cdd:PTZ00263 165 ----AKKVPDRTFTLCGTPEYLAPEVIQSKGHG---------KAVDWWTMGVLLYEFIAGYPPF 215
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
295-434 1.54e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 63.66  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHG---RWHGEVAIRLI--DIERDNEDQLKaFKREVMAYRQTRHENVV-------------LFMga 356
Cdd:NF033483  10 EIGERIGRGGMAEVYLAkdtRLDRDVAVKVLrpDLARDPEFVAR-FRREAQSAASLSHPNIVsvydvgedggipyIVM-- 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 357 cmspphlaiitSLCKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:NF033483  87 -----------EYVDGRTLKDYIRE-HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITkDGRVKVTDFGI 153
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
41-83 1.84e-06

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: 45.15  E-value: 1.84e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568937340    41 HRFSTKYW-MSQTCTVCGK----GMLFGLKCKNCKLKCHNKCTKEAPP 83
Cdd:smart00109   1 HKHVFRTFtKPTFCCVCRKsiwgSFKQGLRCSECKVKCHKKCADKVPK 48
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
41-84 5.64e-06

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: 43.58  E-value: 5.64e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568937340   41 HRFSTK-YWMSQTCTVCGKGMLF----GLKCKNCKLKCHNKCTKEAPPC 84
Cdd:pfam00130   1 HHFVHRnFKQPTFCDHCGEFLWGlgkqGLKCSWCKLNVHKRCHEKVPPE 49
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
397-434 2.96e-04

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 42.20  E-value: 2.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568937340  397 EIVKGMGY----LHAKGILHKDLKSKNVFYDNGKVVITDFGL 434
Cdd:TIGR03724  94 ELAREIGRlvgkLHKAGIVHGDLTTSNIIVRDDKVYLIDFGL 135
 
Name Accession Description Interval E-value
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
293-562 0e+00

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: 591.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14153    1 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISGVLQAGRRDDKLRI 452
Cdd:cd14153   81 RTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFTISGVLQAGRREDKLRI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 453 QNGWLCHLAPEIIRQLSPDTEEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEIS 532
Cdd:cd14153  161 QSGWLCHLAPEIIRQLSPETEEDKLPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNLSQIGMGKEIS 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 568937340 533 DILLFCWAFEQEERPTFTKLMDMLEKLPKR 562
Cdd:cd14153  241 DILLFCWAYEQEERPTFSKLMEMLEKLPKR 270
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
293-562 0e+00

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: 517.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14063    1 ELEIKEVIGKGRFGRVHRGRWHGDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISGVLQAGRRDDKLRI 452
Cdd:cd14063   81 RTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVVITDFGLFSLSGLLQPGRREDTLVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 453 QNGWLCHLAPEIIRQLSPDTE-EDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEI 531
Cdd:cd14063  161 PNGWLCYLAPEIIRALSPDLDfEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGKKQSLSQLDIGREV 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 532 SDILLFCWAFEQEERPTFTKLMDMLEKLPKR 562
Cdd:cd14063  241 KDILMQCWAYDPEKRPTFSDLLRMLERLPKK 271
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
293-569 5.89e-176

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: 498.34  E-value: 5.89e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14152    1 QIELGELIGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISGVLQAGRRDDKLRI 452
Cdd:cd14152   81 RTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVQEGRRENELKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 453 QNGWLCHLAPEIIRQLSPDTEEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGT--GMKPNLSQIGMGKE 530
Cdd:cd14152  161 PHDWLCYLAPEIVREMTPGKDEDCLPFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSgeGMKQVLTTISLGKE 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 531 ISDILLFCWAFEQEERPTFTKLMDMLEKLPKRNRRLSHP 569
Cdd:cd14152  241 VTEILSACWAFDLEERPSFTLLMDMLEKLPKLNRRLSHP 279
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
300-556 6.02e-91

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: 279.81  E-value: 6.02e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG-EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSV 378
Cdd:cd13999    1 IGSGSFGEVYKGKWRGtDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 379 VRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGVLQagrrdDKLRIQNGWL 457
Cdd:cd13999   81 LHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDeNFTVKIADFGLSRIKNSTT-----EKMTGVVGTP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 458 CHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEISDILLF 537
Cdd:cd13999  156 RWMAPEVLR---------GEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKR 226
                        250
                 ....*....|....*....
gi 568937340 538 CWAFEQEERPTFTKLMDML 556
Cdd:cd13999  227 CWNEDPEKRPSFSEIVKRL 245
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
300-557 1.62e-64

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: 211.48  E-value: 1.62e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGaCMSPPHLAIITSLCKGRTLYSVV 379
Cdd:cd14062    1 IGSGSFGTVYKGRWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMG-YMTKPQLAIVTQWCEGSSLYKHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 380 RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-YDNGKVVITDFGLFSISGVLQAGRRDDKLriqNGWLC 458
Cdd:cd14062   80 HVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFlHEDLTVKIGDFGLATVKTRWSGSQQFEQP---TGSIL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 459 HLAPEIIRQlspdteEDKLPFSKHSDVFALGTIWYELHAREWPFK-TQPAEAIIWQMGTG-MKPNLSQI--GMGKEISDI 534
Cdd:cd14062  157 WMAPEVIRM------QDENPYSFQSDVYAFGIVLYELLTGQLPYShINNRDQILFMVGRGyLRPDLSKVrsDTPKALRRL 230
                        250       260
                 ....*....|....*....|...
gi 568937340 535 LLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd14062  231 MEDCIKFQRDERPLFPQILASLE 253
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
300-561 5.31e-56

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: 189.84  E-value: 5.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGAcMSPPHLAIITSLCKGRTLYSVV 379
Cdd:cd14150    8 IGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGF-MTRPNFAIITQWCEGSSLYRHL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 380 RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSISGVLQAGRrddKLRIQNGWLC 458
Cdd:cd14150   87 HVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVkIGDFGLATVKTRWSGSQ---QVEQPSGSIL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 459 HLAPEIIRQlspdteEDKLPFSKHSDVFALGTIWYELHAREWPFKT-QPAEAIIWQMGTG-MKPNLSQIGMG--KEISDI 534
Cdd:cd14150  164 WMAPEVIRM------QDTNPYSFQSDVYAYGVVLYELMSGTLPYSNiNNRDQIIFMVGRGyLSPDLSKLSSNcpKAMKRL 237
                        250       260
                 ....*....|....*....|....*..
gi 568937340 535 LLFCWAFEQEERPTFTKLMDMLEKLPK 561
Cdd:cd14150  238 LIDCLKFKREERPLFPQILVSIELLQR 264
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
286-561 1.77e-55

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: 188.73  E-value: 1.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACmSPPHLAI 365
Cdd:cd14151    2 DWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS-TKPQLAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-YDNGKVVITDFGLFSISGVLQAG 444
Cdd:cd14151   81 VTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFlHEDLTVKIGDFGLATVKSRWSGS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 RRDDKLriqNGWLCHLAPEIIRQlspdteEDKLPFSKHSDVFALGTIWYELHAREWPFKT-QPAEAIIWQMGTG-MKPNL 522
Cdd:cd14151  161 HQFEQL---SGSILWMAPEVIRM------QDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGyLSPDL 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568937340 523 SQI--GMGKEISDILLFCWAFEQEERPTFTKLMDMLEKLPK 561
Cdd:cd14151  232 SKVrsNCPKAMKRLMAECLKKKRDERPLFPQILASIELLAR 272
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
287-564 9.08e-48

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: 168.29  E-value: 9.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGAcMSPPHLAII 366
Cdd:cd14149    7 WEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSISGVLQAGR 445
Cdd:cd14149   86 TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVkIGDFGLATVKSRWSGSQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 RDDKLriqNGWLCHLAPEIIRQlspdteEDKLPFSKHSDVFALGTIWYELHAREWPF-KTQPAEAIIWQMGTG-MKPNLS 523
Cdd:cd14149  166 QVEQP---TGSILWMAPEVIRM------QDNNPFSFQSDVYSYGIVLYELMTGELPYsHINNRDQIIFMVGRGyASPDLS 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568937340 524 QI--GMGKEISDILLFCWAFEQEERPTFTKLMDMLE----KLPKRNR 564
Cdd:cd14149  237 KLykNCPKAMKRLVADCIKKVKEERPLFPQILSSIEllqhSLPKINR 283
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
294-556 1.96e-47

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 166.52  E-value: 1.96e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  294 LEIGELIGKGRFGQVYHGRWHG-------EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGegentkiKVAVKTLK-EGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  367 TSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFsisgvlQAGR 445
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVkISDFGLS------RDIY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  446 RDDKLRIQNG------WlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTG- 517
Cdd:pfam07714 154 DDDYYRKRGGgklpikW---MAPESLKDGK---------FTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEFLEDGy 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 568937340  518 --MKPNlsqiGMGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:pfam07714 222 rlPQPE----NCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
295-553 5.24e-41

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 148.83  E-value: 5.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKtgkLVAIKVIKKKKIKKDR-ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   372 GRTLYSVVRDAKIvLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGRRDDKL 450
Cdd:smart00220  81 GGDLFDLLKKRGR-LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDeDGHVKLADFGL---ARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   451 RiqnGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNL--SQIGMG 528
Cdd:smart00220 157 V---GTPEYMAPEVLLG---------KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFppPEWDIS 224
                          250       260
                   ....*....|....*....|....*
gi 568937340   529 KEISDILLFCWAFEQEERPTFTKLM 553
Cdd:smart00220 225 PEAKDLIRKLLVKDPEKRLTAEEAL 249
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
294-556 4.54e-40

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 146.52  E-value: 4.54e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   294 LEIGELIGKGRFGQVYHGRWHG-------EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGkggkkkvEVAVKTLK-EDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   367 TSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfSisgvlQAGR 445
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVkISDFGL-S-----RDLY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   446 RDDKLRIQNG-----WlchLAPEIIRQLSpdteedklpFSKHSDVFALG-TIWyELHAR-EWPFKTQPAEAIIWQMGTGM 518
Cdd:smart00219 154 DDDYYRKRGGklpirW---MAPESLKEGK---------FTSKSDVWSFGvLLW-EIFTLgEQPYPGMSNEEVLEYLKNGY 220
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 568937340   519 KpnLSQI-GMGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:smart00219 221 R--LPQPpNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
300-556 1.27e-38

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: 141.25  E-value: 1.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG---EVAIRLIDIErDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd00180    1 LGKGSFGKVYKARDKEtgkKVAVKVIPKE-KLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGRRDDKLRIQNG 455
Cdd:cd00180   80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDsDGTVKLADFGL---AKDLDSDDSLLKTTGGTT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 456 WLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELharewpfktqpaeaiiwqmgtgmkpnlsqigmgKEISDIL 535
Cdd:cd00180  157 PPYYAPPELLGGRY---------YGPKVDIWSLGVILYEL---------------------------------EELKDLI 194
                        250       260
                 ....*....|....*....|.
gi 568937340 536 LFCWAFEQEERPTFTKLMDML 556
Cdd:cd00180  195 RRMLQYDPKKRPSAKELLEHL 215
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
294-556 1.42e-38

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: 142.30  E-value: 1.42e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   294 LEIGELIGKGRFGQVYHGRWHG-------EVAIRLIDIERDnEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGkgdgkevEVAVKTLKEDAS-EQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   367 TSLCKGRTLYSVVRDAK-IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfSisgvlQAG 444
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRpKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVkISDFGL-S-----RDL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340   445 RRDDKLRIQNG-----WlchLAPEIIRQLSpdteedklpFSKHSDVFALG-TIWyELHAR-EWPFKTQPAEAIIWQMGTG 517
Cdd:smart00221 154 YDDDYYKVKGGklpirW---MAPESLKEGK---------FTSKSDVWSFGvLLW-EIFTLgEEPYPGMSNAEVLEYLKKG 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 568937340   518 ---MKPNlsqiGMGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:smart00221 221 yrlPKPP----NCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
298-557 9.66e-38

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: 140.37  E-value: 9.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHG------EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGgdgktvDVAVKTLK-EDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVLDVNKTR--------QIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsisgvlq 442
Cdd:cd00192   80 GGDLLDFLRKSRPVFPSPEPStlslkdllSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVkISDFGL-------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 aGRR-DDKLRIQNGwlcHLAPEIIRQLSPDTEEDKLpFSKHSDVFALG-TIWyEL--HAREwPFKTQPAEAIIWQMGTGM 518
Cdd:cd00192  152 -SRDiYDDDYYRKK---TGGKLPIRWMAPESLKDGI-FTSKSDVWSFGvLLW-EIftLGAT-PYPGLSNEEVLEYLRKGY 224
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 519 KPNLSQiGMGKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd00192  225 RLPKPE-NCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
300-557 2.85e-34

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: 130.34  E-value: 2.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGE-VAIRLIdieRDN----EDQLKAFKREVMAYRQTRHENVVLFMGACMS-PPHLAIITSLCKGR 373
Cdd:cd14064    1 IGSGSFGKVYKGRCRNKiVAIKRY---RANtycsKSDVDMFCREVSILCRLNHPCVIQFVGACLDdPSQFAIVTQYVSGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLH--AKGILHKDLKSKNVF-YDNGKVVITDFGLfsiSGVLQAgRRDDKL 450
Cdd:cd14064   78 SLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILlYEDGHAVVADFGE---SRFLQS-LDEDNM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 451 RIQNGWLCHLAPEIIRQLSpdteedklPFSKHSDVFALGTIWYELHAREWPFK-TQPAEAIIWQMGTGMKPNLSqIGMGK 529
Cdd:cd14064  154 TKQPGNLRWMAPEVFTQCT--------RYSIKADVFSYALCLWELLTGEIPFAhLKPAAAAADMAYHHIRPPIG-YSIPK 224
                        250       260
                 ....*....|....*....|....*...
gi 568937340 530 EISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd14064  225 PISSLLMRGWNAEPESRPSFVEIVALLE 252
C1_KSR2 cd20873
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and ...
36-92 6.12e-34

protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and similar proteins; 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. 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: 410423  Cd Length: 57  Bit Score: 122.88  E-value: 6.12e-34
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340  36 GNSIKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLIIHRG 92
Cdd:cd20873    1 GNSIKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLIIHRG 57
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
299-559 8.64e-33

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: 126.35  E-value: 8.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRWHG-EVAIR--LIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTL 375
Cdd:cd14061    1 VIGVGGFGKVYRGIWRGeEVAVKaaRQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 376 YSVVRDAKIVLDV--NKTRQIAqeivKGMGYLHAKG---ILHKDLKSKNVF---------YDNGKVVITDFGL----FSI 437
Cdd:cd14061   81 NRVLAGRKIPPHVlvDWAIQIA----RGMNYLHNEApvpIIHRDLKSSNILileaienedLENKTLKITDFGLarewHKT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 438 SGVLQAGrrddklriQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWqmGTG 517
Cdd:cd14061  157 TRMSAAG--------TYAW---MAPEVIKSST---------FSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAY--GVA 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 518 MK------PNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14061  215 VNkltlpiPSTCP----EPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
295-548 3.05e-32

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: 125.01  E-value: 3.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY---HGRWHGEVAIRLIDIE-RDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14014    3 RLVRLLGRGGMGEVYrarDTLLGRPVAIKVLRPElAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIvLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsisgvlqAGRRDDK 449
Cdd:cd14014   83 EGGSLADLLRERGP-LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTeDGRVKLTDFGI--------ARALGDS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIQNGWLC----HLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI 525
Cdd:cd14014  154 GLTQTGSVLgtpaYMAPEQARGGPVD---------PRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPL 224
                        250       260
                 ....*....|....*....|....*
gi 568937340 526 --GMGKEISDILLFCWAFEQEERPT 548
Cdd:cd14014  225 npDVPPALDAIILRALAKDPEERPQ 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
295-547 3.61e-32

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 129.75  E-value: 3.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIER-DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:COG0515   10 RILRLLGRGGMGVVYLARDLRlgrPVALKVLRPELaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsisgvlqAGRRDDK 449
Cdd:COG0515   90 EGESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTpDGRVKLIDFGI--------ARALGGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIQNGWLC----HLAPEIIRQLSPDTeedklpfskHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI 525
Cdd:COG0515  161 TLTQTGTVVgtpgYMAPEQARGEPVDP---------RSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSEL 231
                        250       260
                 ....*....|....*....|....
gi 568937340 526 GMG--KEISDILLFCWAFEQEERP 547
Cdd:COG0515  232 RPDlpPALDAIVLRALAKDPEERY 255
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
295-505 1.36e-31

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


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 123.01  E-value: 1.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRwH---GE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14003    3 ELGKTLGEGSFGKVKLAR-HkltGEkVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISgvlqagRRDDK 449
Cdd:cd14003   82 SGGELFDYIV-NNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDkNGNLKIIDFGLSNEF------RGGSL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 450 LRIQNGWLCHLAPEIIRQLSPDTEEdklpfskhSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14003  155 LKTFCGTPAYAAPEVLLGRKYDGPK--------ADVWSLGVILYAMLTGYLPFDDD 202
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
290-548 1.07e-30

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: 120.57  E-value: 1.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVYHGRWHGE-VAIRLIDIERDNEDQLKAFKREVMAYRqTRHENVVLFMGA--CMSPPHLA-I 365
Cdd:cd13979    1 DWEPLRLQEPLGSGGFGSVYKATYKGEtVAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVRVLAAetGTDFASLGlI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL-FSISGVLQA 443
Cdd:cd13979   80 IMEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILIsEQGVCKLCDFGCsVKLGEGNEV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 GRRDDKLRiqnGWLCHLAPEIIRQLSPdteedklpfSKHSDVFALG-TIWyELHAREWPFKTQPAEAIIWQMGTGMKPNL 522
Cdd:cd13979  160 GTPRSHIG---GTYTYRAPELLKGERV---------TPKADIYSFGiTLW-QMLTRELPYAGLRQHVLYAVVAKDLRPDL 226
                        250       260
                 ....*....|....*....|....*....
gi 568937340 523 SQIG---MGKEISDILLFCWAFEQEERPT 548
Cdd:cd13979  227 SGLEdseFGQRLRSLISRCWSAQPAERPN 255
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
317-561 3.00e-30

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: 120.01  E-value: 3.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 317 VAIRliDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC-KGrTLYSVVRDAKIVLD-------V 388
Cdd:cd14042   33 VAIK--KVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCpKG-SLQDILENEDIKLDwmfryslI 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 389 NktrqiaqEIVKGMGYLHAKGI-LHKDLKSKNVFYDNGKVV-ITDFGLFSIsgvlqagRRDDKLRIQNGWLCH----LAP 462
Cdd:cd14042  110 H-------DIVKGMHYLHDSEIkSHGNLKSSNCVVDSRFVLkITDFGLHSF-------RSGQEPPDDSHAYYAkllwTAP 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 463 EIIRQLSPDTeedklPFSKHSDVFALGTIWYELHAREWPFKTQ-----PAEAIIWQMGTGMK----PNLSQIGMGKEISD 533
Cdd:cd14042  176 ELLRDPNPPP-----PGTQKGDVYSFGIILQEIATRQGPFYEEgpdlsPKEIIKKKVRNGEKppfrPSLDELECPDEVLS 250
                        250       260
                 ....*....|....*....|....*...
gi 568937340 534 ILLFCWAFEQEERPTFTKLMDMLEKLPK 561
Cdd:cd14042  251 LMQRCWAEDPEERPDFSTLRNKLKKLNK 278
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
300-556 6.89e-30

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: 118.32  E-value: 6.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd13978    1 LGSGGFGTVSKARhvsWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLDVNKTRQIAQEIVKGMGYLH--AKGILHKDLKSKNVFYDNG-KVVITDFGLFSISGVLQAGRRDDKLRIQ 453
Cdd:cd13978   81 SLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHfHVKISDFGLSKLGMKSISANRRRGTENL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 NGWLCHLAPEIIRQLSpdteedKLPFSKHsDVFALGTIWYELHAREWPFKTQPAEAIIWQ-MGTGMKPNLSQIG------ 526
Cdd:cd13978  161 GGTPIYMAPEAFDDFN------KKPTSKS-DVYSFAIVIWAVLTRKEPFENAINPLLIMQiVSKGDRPSLDDIGrlkqie 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 568937340 527 MGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd13978  234 NVQELISLMIRCWDGNPDARPTFLECLDRL 263
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
297-569 8.60e-30

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: 118.01  E-value: 8.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHGRWH---GEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd06606    5 GELLGKGSFGSVYLALNLdtgELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGVLQAGRRDDKLRI 452
Cdd:cd06606   85 SLASLLKKFG-KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVkLADFGC---AKRLAEIATGEGTKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 453 QNG---WlchLAPEIIRQLSPDTEedklpfskhSDVFALG-TIwYELHA--REWPFKTQPAeAIIWQMGTGMKP-----N 521
Cdd:cd06606  161 LRGtpyW---MAPEVIRGEGYGRA---------ADIWSLGcTV-IEMATgkPPWSELGNPV-AALFKIGSSGEPppipeH 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 522 LSQIGMgkeisDILLFCWAFEQEERPTFTKLmdmleklpkrnrrLSHP 569
Cdd:cd06606  227 LSEEAK-----DFLRKCLQRDPKKRPTADEL-------------LQHP 256
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
288-556 5.38e-29

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: 116.30  E-value: 5.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEQLEIGELIGKGRFGQVYHGRWHG-EVAIRLI--DIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd14145    2 EIDFSELVLEEIIGIGGFGKVYRAIWIGdEVAVKAArhDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKIVLD--VNKTRQIAqeivKGMGYLHAKGI---LHKDLKSKNVF----YDNGKVV-----IT 430
Cdd:cd14145   82 LVMEFARGGPLNRVLSGKRIPPDilVNWAVQIA----RGMNYLHCEAIvpvIHRDLKSSNILilekVENGDLSnkilkIT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 431 DFGLfsisgvLQAGRRDDKLRIQnGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAI 510
Cdd:cd14145  158 DFGL------AREWHRTTKMSAA-GTYAWMAPEVIRSSM---------FSKGSDVWSYGVLLWELLTGEVPFRGIDGLAV 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568937340 511 IWqmGTGMK------PNLSQIGMGKEISDillfCWAFEQEERPTFTKLMDML 556
Cdd:cd14145  222 AY--GVAMNklslpiPSTCPEPFARLMED----CWNPDPHSRPPFTNILDQL 267
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
287-559 2.91e-28

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: 113.60  E-value: 2.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHGE-VAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAI 365
Cdd:cd05039    1 WAINKKDLKLGELIGKGEFGDVMLGDYRGQkVAVKCL---KDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLdVNKTRQI--AQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSISGVLQ 442
Cdd:cd05039   78 VTEYMAKGSLVDYLRSRGRAV-ITRKDQLgfALDVCEGMEYLESKKFVHRDLAARNVLVsEDNVAKVSDFGLAKEASSNQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGrrdDKLRIQngWlchLAPEIIRqlspdteeDKLpFSKHSDVFALGTIWYELHA--REwPFKTQPAEAIIWQMGTGMK- 519
Cdd:cd05039  157 DG---GKLPIK--W---TAPEALR--------EKK-FSTKSDVWSFGILLWEIYSfgRV-PYPRIPLKDVVPHVEKGYRm 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568937340 520 --PNlsqiGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05039  219 eaPE----GCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
291-505 3.79e-28

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: 113.54  E-value: 3.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIgelIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd13996    8 FEEIEL---LGSGGFGSVYKVRNKVdgvTYAIKKIRLTEKSSASEKVL-REVKALAKLNHPNIVRYYTAWVEEPPLYIQM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVLDVNKT--RQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV--ITDFGL--------- 434
Cdd:cd13996   84 ELCEGGTLRDWIDRRNSSSKNDRKlaLELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQvkIGDFGLatsignqkr 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 435 FSISGVLQAGRRDDKLRIQNGWLCHLAPEiirqlspdtEEDKLPFSKHSDVFALGTIWYE-LHarewPFKTQ 505
Cdd:cd13996  164 ELNNLNNNNNGNTSNNSVGIGTPLYASPE---------QLDGENYNEKADIYSLGIILFEmLH----PFKTA 222
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
295-553 6.03e-28

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: 112.68  E-value: 6.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRwH----GEVAIRLIDIErdNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd05122    3 EILEKIGKGGFGVVYKAR-HkktgQIVAIKKINLE--SKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-FYDNGKVVITDFGLfsiSGVLQAGRRDDK 449
Cdd:cd05122   80 SGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANIlLTSDGEVKLIDFGL---SAQLSDGKTRNT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 lriQNGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI-GMG 528
Cdd:cd05122  157 ---FVGTPYWMAPEVIQG---------KPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPkKWS 224
                        250       260
                 ....*....|....*....|....*
gi 568937340 529 KEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd05122  225 KEFKDFLKKCLQKDPEKRPTAEQLL 249
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
299-559 1.57e-27

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: 111.62  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRWHGE-VAIRLI--DIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTL 375
Cdd:cd14148    1 IIGVGGFGKVYKGLWRGEeVAVKAArqDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 376 YSVVRDAKI---VLdVNKTRQIAqeivKGMGYLHAKG---ILHKDLKSKNVF---------YDNGKVVITDFGLfsisgv 440
Cdd:cd14148   81 NRALAGKKVpphVL-VNWAVQIA----RGMNYLHNEAivpIIHRDLKSSNILilepienddLSGKTLKITDFGL------ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 LQAGRRDDKLRIQnGWLCHLAPEIIRqLSpdteedklPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWqmGTGM-K 519
Cdd:cd14148  150 AREWHKTTKMSAA-GTYAWMAPEVIR-LS--------LFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAY--GVAMnK 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568937340 520 PNLSQIGMGKE-ISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14148  218 LTLPIPSTCPEpFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
300-557 2.62e-27

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: 110.28  E-value: 2.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGE-VAIRLIDIERDNEdqlkafkreVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSV 378
Cdd:cd14059    1 LGSGAQGAVFLGKFRGEeVAVKKVRDEKETD---------IKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 379 VRDAKIV---LDVNKTRQIAQeivkGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSisgvlQAGRRDDKLRIQn 454
Cdd:cd14059   72 LRAGREItpsLLVDWSKQIAS----GMNYLHLHKIIHRDLKSPNVLVTYNDVLkISDFGTSK-----ELSEKSTKMSFA- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 455 GWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEISDI 534
Cdd:cd14059  142 GTVAWMAPEVIRN---------EPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQLPVPSTCPDGFKLL 212
                        250       260
                 ....*....|....*....|...
gi 568937340 535 LLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd14059  213 MKQCWNSKPRNRPSFRQILMHLD 235
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
292-504 7.80e-27

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: 109.26  E-value: 7.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHGE---VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTgqvVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRtLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL---FSISGVLqag 444
Cdd:cd14002   81 YAQGE-LFQILEDDG-TLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGkGGVVKLCDFGFaraMSCNTLV--- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 rrddkLRIQNGWLCHLAPEIIRqlspdtEEdklPFSKHSDVFALGTIWYELHAREWPFKT 504
Cdd:cd14002  156 -----LTSIKGTPLYMAPELVQ------EQ---PYDHTADLWSLGCILYELFVGQPPFYT 201
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
295-505 1.33e-26

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: 109.03  E-value: 1.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGR---WHGEVAIRLIDIER-DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14663    3 ELGRTLGEGTFAKVKFARntkTGESVAIKIIDKEQvAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsiSGVLQAGRRDDK 449
Cdd:cd14663   83 TGGELFSKIAKNG-RLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEdGNLKISDFGL---SALSEQFRQDGL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 450 LRIQNGWLCHLAPEIIRQLSPDteedklpfSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14663  159 LHTTCGTPNYVAPEVLARRGYD--------GAKADIWSCGVILFVLLAGYLPFDDE 206
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
300-559 1.43e-26

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: 108.68  E-value: 1.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG-EVAIRLIDIERDNedqlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSV 378
Cdd:cd14058    1 VGRGSFGVVCKARWRNqIVAVKIIESESEK----KAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 379 VRDAKIVLDVNKTRQI--AQEIVKGMGYLHA---KGILHKDLKSKNVF-YDNGKVV-ITDFGLfsiSGVLQAGRRDDKlr 451
Cdd:cd14058   77 LHGKEPKPIYTAAHAMswALQCAKGVAYLHSmkpKALIHRDLKPPNLLlTNGGTVLkICDFGT---ACDISTHMTNNK-- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 452 iqnGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFK--TQPAEAIIWQMGTGMKPNLSQiGMGK 529
Cdd:cd14058  152 ---GSAAWMAPEVFEGSK---------YSEKCDVFSWGIILWEVITRRKPFDhiGGPAFRIMWAVHNGERPPLIK-NCPK 218
                        250       260       270
                 ....*....|....*....|....*....|
gi 568937340 530 EISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14058  219 PIESLMTRCWSKDPEKRPSMKEIVKIMSHL 248
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
299-556 4.39e-26

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: 107.82  E-value: 4.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRWHG-EVAIRLI--DIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTL 375
Cdd:cd14146    1 IIGVGGFGKVYRATWKGqEVAVKAArqDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 376 YSVVRDAKIVLDVNKTRQI--------AQEIVKGMGYLHAKG---ILHKDLKSKNVF------YD---NGKVVITDFGLf 435
Cdd:cd14146   81 NRALAAANAAPGPRRARRIpphilvnwAVQIARGMLYLHEEAvvpILHRDLKSSNILllekieHDdicNKTLKITDFGL- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 436 sisgvLQAGRRDDKLRIQnGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMG 515
Cdd:cd14146  160 -----AREWHRTTKMSAA-GTYAWMAPEVIKSSL---------FSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVA 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568937340 516 TGmKPNLSQIGMGKE-ISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd14146  225 VN-KLTLPIPSTCPEpFAKLMKECWEQDPHIRPSFALILEQL 265
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
286-557 5.49e-26

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: 107.49  E-value: 5.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRWHG--EVAIRLIDIERDNEdqlKAFKREVMAYRQTRHENVVLFMGACMSPPHL 363
Cdd:cd05068    2 QWEIDRKSLKLLRKLGSGQFGEVWEGLWNNttPVAVKTLKPGTMDP---EDFLREAQIMKKLRHPKLIQLYAVCTLEEPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL---FSISG 439
Cdd:cd05068   79 YIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVgENNICKVADFGLarvIKVED 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 440 VLQAgRRDDKLRIQngWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYEL--HAReWPFKTQPAEAIIWQMGTG 517
Cdd:cd05068  159 EYEA-REGAKFPIK--W---TAPEAANYNR---------FSIKSDVWSFGILLTEIvtYGR-IPYPGMTNAEVLQQVERG 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568937340 518 MK-PNLSqiGMGKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05068  223 YRmPCPP--NCPPQLYDIMLECWKADPMERPTFETLQWKLE 261
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
295-502 6.63e-26

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: 106.78  E-value: 6.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY------HGRwhgEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd08215    3 EKIRVIGKGSFGSAYlvrrksDGK---LYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAKIVLDVNKTRQI----AQeIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGlfsISGVLQa 443
Cdd:cd08215   80 YADGGDLAQKIKKQKKKGQPFPEEQIldwfVQ-ICLALKYLHSRKILHRDLKTQNIFLTKDGVVkLGDFG---ISKVLE- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 444 gRRDDKLRIQNGWLCHLAPEIIrqlspdteEDKlPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd08215  155 -STTDLAKTVVGTPYYLSPELC--------ENK-PYNYKSDIWALGCVLYELCTLKHPF 203
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
300-559 8.03e-26

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: 106.97  E-value: 8.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGE--VAIRLIDIERDNEDqLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYS 377
Cdd:cd14066    1 IGSGGFGTVYKGVLENGtvVAVKRLNEMNCAAS-KKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 V--VRDAKIVLDVnKTRQ-IAQEIVKGMGYLHAKG---ILHKDLKSKNVFYDNGKV-VITDFGLFSISGVLQAGRRDDKL 450
Cdd:cd14066   80 RlhCHKGSPPLPW-PQRLkIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEpKLTDFGLARLIPPSESVSKTSAV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 451 RiqnGWLCHLAPEIIRqlspdteeDKLPfSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGM--- 527
Cdd:cd14066  159 K---GTIGYLAPEYIR--------TGRV-STKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEWVESKGKEELEdil 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340 528 --------GKEISDIL------LFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14066  227 dkrlvdddGVEEEEVEallrlaLLCTRSDPSLRPSMKEVVQMLEKL 272
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
287-556 8.95e-26

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: 106.75  E-value: 8.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRW--HGEVAIRLidIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd05148    1 WERPREEFTLERKLGSGYFGEVWEGLWknRVRVAIKI--LKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAK-IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSI--SGV 440
Cdd:cd05148   79 IITELMEKGSLLAFLRSPEgQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCkVADFGLARLikEDV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 LQAgrrDDKlRIQNGWlchLAPE-IIRQLspdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGM 518
Cdd:cd05148  159 YLS---SDK-KIPYKW---TAPEaASHGT----------FSTKSDVWSFGILLYEMFTYgQVPYPGMNNHEVYDQITAGY 221
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 519 K-PNLSQIgmGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd05148  222 RmPCPAKC--PQEIYKIMLECWAAEPEDRPSFKALREEL 258
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
301-559 9.69e-26

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: 106.19  E-value: 9.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 301 GKGRFGQVYHGRW---HGEVAIRlidierdnedQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYS 377
Cdd:cd14060    2 GGGSFGSVYRAIWvsqDKEVAVK----------KLLKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 VVRDAKI-VLDVNKTRQIAQEIVKGMGYLHAKG---ILHKDLKSKN-VFYDNGKVVITDFG---LFSISGVLQAgrrddk 449
Cdd:cd14060   72 YLNSNESeEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNvVIAADGVLKICDFGasrFHSHTTHMSL------ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 lriqNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQ-MGTGMKPNLSQIGMG 528
Cdd:cd14060  146 ----VGTFPWMAPEVIQ---------SLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLvVEKNERPTIPSSCPR 212
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 529 KeISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14060  213 S-FAELMRRCWEADVKERPSFKQIIGILESM 242
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
298-556 1.51e-25

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: 105.89  E-value: 1.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE------VAIRLIDIER-DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPhLAIITSLC 370
Cdd:cd05040    1 EKLGDGSFGVVRRGEWTTPsgkviqVAVKCLKSDVlSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSP-LMMVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-YDNGKVVITDFGLFSISGVlqagrRDD- 448
Cdd:cd05040   80 PLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILlASKDKVKIGDFGLMRALPQ-----NEDh 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 -----KLRIQNGWlChlAPEIIRQLSpdteedklpFSKHSDVFALG-TIWYELHAREWPFK----TQPAEAIIWQMGTGM 518
Cdd:cd05040  155 yvmqeHRKVPFAW-C--APESLKTRK---------FSHASDVWMFGvTLWEMFTYGEEPWLglngSQILEKIDKEGERLE 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568937340 519 KPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd05040  223 RPDDCP----QDIYNVMLQCWAHKPADRPTFVALRDFL 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
296-553 2.12e-25

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: 105.38  E-value: 2.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHG--RWHGE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd06627    4 LGDLIGRGAFGSVYKGlnLNTGEfVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRD-----AKIVldvnkTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlfsISGVLQAGRR 446
Cdd:cd06627   84 GSLASIIKKfgkfpESLV-----AVYIYQ-VLEGLAYLHEQGVIHRDIKGANILTtKDGLVKLADFG---VATKLNEVEK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 DDKLRIqnG---WlchLAPEIIrQLSPDTEEdklpfskhSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLS 523
Cdd:cd06627  155 DENSVV--GtpyW---MAPEVI-EMSGVTTA--------SDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPPLP 220
                        250       260       270
                 ....*....|....*....|....*....|
gi 568937340 524 QiGMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06627  221 E-NISPELRDFLLQCFQKDPTLRPSAKELL 249
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
295-554 2.30e-25

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: 105.19  E-value: 2.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGR--WHGEV-AIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd08529    3 EILNKLGKGSFGVVYKVVrkVDGRVyALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVV-RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGlfsISGVLQagrrddk 449
Cdd:cd08529   83 NGDLHSLIkSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGdNVKIGDLG---VAKILS------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 lriQNGWLCHLAPEIIRQLSPDTEEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQiGMGK 529
Cdd:cd08529  153 ---DTTNFAQTIVGTPYYLSPELCEDK-PYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPISA-SYSQ 227
                        250       260
                 ....*....|....*....|....*
gi 568937340 530 EISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd08529  228 DLSQLIDSCLTKDYRQRPDTTELLR 252
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
293-562 3.56e-25

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: 105.19  E-value: 3.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRW--HGE-----VAIRLIdieRDNEDQ--LKAFKREVMAYRQTRHENVVLFMGACMSPPHl 363
Cdd:cd05057    8 ELEKGKVLGSGAFGTVYKGVWipEGEkvkipVAIKVL---REETGPkaNEEILDEAYVMASVDHPHLVRLLGICLSSQV- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRDAKIVLD----VNKTRQIAqeivKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSIs 438
Cdd:cd05057   84 QLITQLMPLGCLLDYVRNHRDNIGsqllLNWCVQIA----KGMSYLEEKRLVHRDLAARNVLVKTPNHVkITDFGLAKL- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 439 gvlqAGRRDDKLRIQNG-----WlchLAPEIIRQLSpdteedklpFSKHSDVFALG-TIWYELHAREWPFKTQPAEAIIW 512
Cdd:cd05057  159 ----LDVDEKEYHAEGGkvpikW---MALESIQYRI---------YTHKSDVWSYGvTVWELMTFGAKPYEGIPAVEIPD 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 513 QMGTGMK---PNLSQIgmgkEISDILLFCWAFEQEERPTFTKLMDMLEKL---PKR 562
Cdd:cd05057  223 LLEKGERlpqPPICTI----DVYMVLVKCWMIDAESRPTFKELANEFSKMardPQR 274
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
295-517 6.17e-25

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


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 104.10  E-value: 6.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd05117    3 ELGKVLGRGSFGVVRLAVHKKtgeEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSvvrdaKIV----LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLfsiSGVLQA 443
Cdd:cd05117   83 GGELFD-----RIVkkgsFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskdPDSPIKIIDFGL---AKIFEE 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 444 GrrdDKLRIQNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTG 517
Cdd:cd05117  155 G---EKLKTVCGTPYYVAPEVLK---------GKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKG 216
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
290-559 6.57e-25

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: 104.77  E-value: 6.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVYHGRW------HGE-VAIRLIDIERdNEDQLKAFKREVMAYRQTRHENVVLFMGACMSP-- 360
Cdd:cd05038    2 EERHLKFIKQLGEGHFGSVELCRYdplgdnTGEqVAVKSLQPSG-EEQHMSDFKREIEILRTLDHEYIVKYKGVCESPgr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 361 PHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSG 439
Cdd:cd05038   81 RSLRLIMEYLPSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVkISDFGL---AK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 440 VLQA------GRRDDKLRIQngWlchLAPEIIRqlspdteEDKlpFSKHSDVFALGTIWYELHAREWPFKTQPAE----- 508
Cdd:cd05038  158 VLPEdkeyyyVKEPGESPIF--W---YAPECLR-------ESR--FSSASDVWSFGVTLYELFTYGDPSQSPPALflrmi 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 509 ------AIIWQMGTGMKPN--LSQ-IGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05038  224 giaqgqMIVTRLLELLKSGerLPRpPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRL 283
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
297-553 9.86e-25

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 103.77  E-value: 9.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHG--RWHGEV-AIRLIDIERD---NEDQ----LKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:cd06628    5 GALIGSGSFGSVYLGmnASSGELmAVKQVELPSVsaeNKDRkksmLDALQREIALLRELQHENIVQYLGSSSDANHLNIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGlfsISGVLQAGR 445
Cdd:cd06628   85 LEYVPGGSVATLL-NNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNkGGIKISDFG---ISKKLEANS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 RDDKLRIQ----NGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPN 521
Cdd:cd06628  161 LSTKNNGArpslQGSVFWMAPEVVKQTS---------YTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPT 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568937340 522 LSQIgMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06628  232 IPSN-ISSEARDFLEKTFEIDHNKRPTADELL 262
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
297-554 1.23e-24

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: 103.62  E-value: 1.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHGR--WHGEV-AIRLIDI-----ERDNEDQ---LKAFKREVMAYRQTRHENVVLFMGACMSPPHLAI 365
Cdd:cd06629    6 GELIGKGTYGRVYLAMnaTTGEMlAVKQVELpktssDRADSRQktvVDALKSEIDTLKDLDHPNIVQYLGFEETEDYFSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRD-AKIVLDVnkTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGVLQA 443
Cdd:cd06629   86 FLEYVPGGSIGSCLRKyGKFEEDL--VRFFTRQILDGLAYLHSKGILHRDLKADNILVDlEGICKISDFGISKKSDDIYG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 GRRDDKLRIQNGWlchLAPEIIrqlspdtEEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMK--PN 521
Cdd:cd06629  164 NNGATSMQGSVFW---MAPEVI-------HSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSapPV 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568937340 522 LSQIGMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd06629  234 PEDVNLSPEALDFLNACFAIDPRDRPTAAELLS 266
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
300-498 1.34e-24

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: 102.95  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRwHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVV 379
Cdd:cd14065    1 LGKGFFGEVYKVT-HRETGKVMVMKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 380 RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF---YDNGK-VVITDFGLFSISGVLQAGRRDDKLRIQN- 454
Cdd:cd14065   80 KSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLvreANRGRnAVVADFGLAREMPDEKTKKPDRKKRLTVv 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568937340 455 GWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAR 498
Cdd:cd14065  160 GSPYWMAPEMLR---------GESYDEKVDVFSFGIVLCEIIGR 194
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
291-559 6.13e-24

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: 101.64  E-value: 6.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIGELIGKGRFGQVYHGRWHGE-VAIRLIDIERDNEDQLKA--FKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14147    2 FQELRLEEVIGIGGFGKVYRGSWRGElVAVKAARQDPDEDISVTAesVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKI---VLdVNKTRQIAqeivKGMGYLHAKGI---LHKDLKSKNVF---------YDNGKVVITDF 432
Cdd:cd14147   82 EYAAGGPLSRALAGRRVpphVL-VNWAVQIA----RGMHYLHCEALvpvIHRDLKSNNILllqpienddMEHKTLKITDF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 433 GLfsisgvLQAGRRDDKLRIQnGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIW 512
Cdd:cd14147  157 GL------AREWHKTTQMSAA-GTYAWMAPEVIKAST---------FSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAY 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 513 QMGTGmKPNLSQIGMGKE-ISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14147  221 GVAVN-KLTLPIPSTCPEpFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
297-549 7.22e-24

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: 101.31  E-value: 7.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHgrwhgeVAIRLIDIERDNEDQLKafkREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd13992   14 PKYVKKVGVYGGRT------VAIKHITFSRTEKRTIL---QELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLDVNKTRQIAQEIVKGMGYLH-AKGILHKDLKSKNVFYDNGKVV-ITDFGLFSI-SGVLQAGRRDDKLRIQ 453
Cdd:cd13992   85 DVLLNREIKMDWMFKSSFIKDIVKGMNYLHsSSIGYHGRLKSSNCLVDSRWVVkLTDFGLRNLlEEQTNHQLDEDAQHKK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 NGWlchLAPEIIRQlsPDTEEDKLPfskHSDVFALGTIWYELHAREWPFKTQPAEAI-IWQMGTGMKPNLSQIGMGK--- 529
Cdd:cd13992  165 LLW---TAPELLRG--SLLEVRGTQ---KGDVYSFAIILYEILFRSDPFALEREVAIvEKVISGGNKPFRPELAVLLdef 236
                        250       260
                 ....*....|....*....|..
gi 568937340 530 --EISDILLFCWAFEQEERPTF 549
Cdd:cd13992  237 ppRLVLLVKQCWAENPEKRPSF 258
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
287-559 9.80e-24

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: 100.83  E-value: 9.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG-EVAIRLIDierdNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPP-HLA 364
Cdd:cd05082    1 WALNMKELKLLQTIGKGEFGDVMLGDYRGnKVAVKCIK----NDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKgGLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRD-AKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSisgvlQ 442
Cdd:cd05082   77 IVTEYMAKGSLVDYLRSrGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAkVSDFGLTK-----E 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGRRDDKLRIQNGWlchLAPEIIRqlspdteEDKlpFSKHSDVFALGTIWYELHA-REWPFKTQPAEAIIWQMGTGMKPN 521
Cdd:cd05082  152 ASSTQDTGKLPVKW---TAPEALR-------EKK--FSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPRVEKGYKMD 219
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568937340 522 lSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05082  220 -APDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLEHI 256
C1_KSR1 cd20872
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and ...
39-84 1.54e-23

protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and similar proteins; 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. 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: 410422  Cd Length: 47  Bit Score: 93.57  E-value: 1.54e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340  39 IKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPC 84
Cdd:cd20872    1 VTHRFSTKSWLSQTCQVCQKSMMFGVKCKHCRLKCHNKCTKEAPAC 46
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
293-556 5.12e-23

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: 98.67  E-value: 5.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHG--EVAIRLIDIERDNEDQlkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd05059    5 ELTFLKELGSGQFGVVHLGKWRGkiDVAIKMIKEGSMSEDD---FIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSIsgVLqagrrDDK 449
Cdd:cd05059   82 ANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVgEQNVVKVSDFGLARY--VL-----DDE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIQNG------WlchLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAR-EWPFK----TQPAEAIiwQMGTGM 518
Cdd:cd05059  155 YTSSVGtkfpvkW---SPPEVF---------MYSKFSSKSDVWSFGVLMWEVFSEgKMPYErfsnSEVVEHI--SQGYRL 220
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 519 -KPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd05059  221 yRPHLAP----TEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
293-559 7.45e-23

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: 98.93  E-value: 7.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWH------GEVaIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSP--PHLA 364
Cdd:cd14205    5 HLKFLQQLGKGNFGSVEMCRYDplqdntGEV-VAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAgrRNLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsiSGVLQA 443
Cdd:cd14205   84 LIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENeNRVKIGDFGL---TKVLPQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 GRRDDKLRiQNG-----WlchLAPEIIrqlspdTEEDklpFSKHSDVFALGTIWYELHAREWPFKTQPAE---------- 508
Cdd:cd14205  161 DKEYYKVK-EPGespifW---YAPESL------TESK---FSVASDVWSFGVVLYELFTYIEKSKSPPAEfmrmigndkq 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 509 --AIIWQMGTGMKPN--LSQI-GMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14205  228 gqMIVFHLIELLKNNgrLPRPdGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
298-556 1.10e-22

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: 97.51  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHG---EVAIRLIDIErDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPdntEVAVKTCRET-LPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL--------FSISGvlqaGR 445
Cdd:cd05041   80 LLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVgENNVLKISDFGMsreeedgeYTVSD----GL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 RddklRIQNGWLchlAPEIIRQLSpdteedklpFSKHSDVFALGTIWYElharewpfktqpaeaiIWQMGTGMKPNLS-- 523
Cdd:cd05041  156 K----QIPIKWT---APEALNYGR---------YTSESDVWSFGILLWE----------------IFSLGATPYPGMSnq 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568937340 524 ----QI----------GMGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd05041  204 qtreQIesgyrmpapeLCPEAVYRLMLQCWAYDPENRPSFSEIYNEL 250
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
290-554 3.07e-22

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: 96.18  E-value: 3.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDqlkaFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:cd06612    1 PEEVFDILEKLGEGSYGSVYKAIHKEtgqVVAIKVVPVEEDLQE----IIKEISILKQCDSPYIVKYYGSYFKNTDLWIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRDAKIVLDvnkTRQIA---QEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGlfsISGVLQ 442
Cdd:cd06612   77 MEYCGAGSVSDIMKITNKTLT---EEEIAailYQTLKGLEYLHSNKKIHRDIKAGNILLNEeGQAKLADFG---VSGQLT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGRRDDKLRIqnGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNL 522
Cdd:cd06612  151 DTMAKRNTVI--GTPFWMAPEVIQ---------EIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTL 219
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568937340 523 SQIG-MGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd06612  220 SDPEkWSPEFNDFVKKCLVKDPEERPSAIQLLQ 252
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
291-504 3.10e-22

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: 96.67  E-value: 3.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEigeLIGKGRFGQVYH------GRWHgevAIRLIDIeRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd14046    8 FEELQ---VLGKGAFGQVVKvrnkldGRYY---AIKKIKL-RSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL--------- 434
Cdd:cd14046   81 IQMEYCEKSTLRDLIDS-GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDsNGNVKIGDFGLatsnklnve 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 435 -------FSISgvlQAGRRDDKLRIQNGWLCHLAPEIIRQLSPdTEEDKLpfskhsDVFALGTIWYELHareWPFKT 504
Cdd:cd14046  160 latqdinKSTS---AALGSSGDLTGNVGTALYVAPEVQSGTKS-TYNEKV------DMYSLGIIFFEMC---YPFST 223
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
39-83 3.67e-22

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: 89.31  E-value: 3.67e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568937340  39 IKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPP 83
Cdd:cd20812    1 IKHRFSKKLFMRQTCDYCHKQMFFGLKCKDCKYKCHKKCAKKAPP 45
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
287-559 3.91e-22

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: 97.17  E-value: 3.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLI-DIERDNEDQLKAFKREVMAYRQTrHENVVLFMGAC 357
Cdd:cd05055   30 WEFPRNNLSFGKTLGAGAFGKVVEATAYGlsksdavmKVAVKMLkPTAHSSEREALMSELKIMSHLGN-HENIVNLLGAC 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 358 -MSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGL- 434
Cdd:cd05055  109 tIGGPILVITEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVkICDFGLa 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 435 ---FSISGVLQAGrrddKLRIQNGWlchLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREW-PFKTQPAEAI 510
Cdd:cd05055  189 rdiMNDSNYVVKG----NARLPVKW---MAPESIFNCVYTFE---------SDVWSYGILLWEIFSLGSnPYPGMPVDSK 252
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 511 IWQM---GTGM-KPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05055  253 FYKLikeGYRMaQPEHAP----AEIYDIMKTCWDADPLKRPTFKQIVQLIGKQ 301
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
292-509 5.48e-22

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: 95.86  E-value: 5.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVflaVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSvvrdaKIVLDVNKTRQIAQ----EIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISgvlqa 443
Cdd:cd14069   81 YASGGELFD-----KIEPDVGMPEDVAQfyfqQLMAGLKYLHSCGITHRDIKPENLLLDeNDNLKISDFGLATVF----- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 444 gRRDDKLRIQN---GWLCHLAPEIIRQLSPDTEEdklpfskhSDVFALGTIWYELHAREWPFKtQPAEA 509
Cdd:cd14069  151 -RYKGKERLLNkmcGTLPYVAPELLAKKKYRAEP--------VDVWSCGIVLFAMLAGELPWD-QPSDS 209
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
297-552 1.12e-21

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: 94.69  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLK-AFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTL 375
Cdd:cd05085    1 GELLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKiKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 376 YSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL--------FSISGVLQagrr 446
Cdd:cd05085   81 LSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVgENNALKISDFGMsrqeddgvYSSSGLKQ---- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 ddklrIQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALGT-IWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQi 525
Cdd:cd05085  157 -----IPIKW---TAPEALNYGR---------YSSESDVWSFGIlLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQ- 218
                        250       260
                 ....*....|....*....|....*..
gi 568937340 526 GMGKEISDILLFCWAFEQEERPTFTKL 552
Cdd:cd05085  219 RCPEDIYKIMQRCWDYNPENRPKFSEL 245
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
287-558 1.70e-21

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: 94.17  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHGE-VAIRliDIERDNEDQlkAFKREVMAYRQTRHENVVLFMGACMSPPHLAI 365
Cdd:cd05083    1 WLLNLQKLTLGEIIGEGEFGAVLQGEYMGQkVAVK--NIKCDVTAQ--AFLEETAVMTKLQHKNLVRLLGVILHNGLYIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSISgvlqaG 444
Cdd:cd05083   77 MELMSKGNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVsEDGVAKISDFGLAKVG-----S 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 RRDDKLRIQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTG--MKPN 521
Cdd:cd05083  152 MGVDNSRLPVKW---TAPEALKNKK---------FSSKSDVWSYGVLLWEVFSYgRAPYPKMSVKEVKEAVEKGyrMEPP 219
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568937340 522 LSQIGMgkeISDILLFCWAFEQEERPTFTKLMDMLEK 558
Cdd:cd05083  220 EGCPPD---VYSIMTSCWEAEPGKRPSFKKLREKLEK 253
Pkinase pfam00069
Protein kinase domain;
294-555 1.92e-21

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 93.08  E-value: 1.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  294 LEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYkakHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  371 KGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMgylhakgilhKDLKSKNVFydngkvVITDFglfsisgvlqagrrddkl 450
Cdd:pfam00069  81 EGGSLFDLLSE-KGAFSEREAKFIMKQILEGL----------ESGSSLTTF------VGTPW------------------ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  451 riqngwlcHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGM------KPNLSq 524
Cdd:pfam00069 126 --------YMAPEVLGG---------NPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPyafpelPSNLS- 187
                         250       260       270
                  ....*....|....*....|....*....|.
gi 568937340  525 igmgKEISDILLFCWAFEQEERPTFTKLMDM 555
Cdd:pfam00069 188 ----EEAKDLLKKLLKKDPSKRLTATQALQH 214
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
300-559 2.16e-21

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: 93.74  E-value: 2.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVV 379
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKIV-REISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 380 RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY---DNGK-VVITDFGLFSISGVLQAGRRDDKLRIQnG 455
Cdd:cd14156   80 AREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrvtPRGReAVVTDFGLAREVGEMPANDPERKLSLV-G 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 456 WLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHARewpfktQPAEAIIW----------QMGTGMKPnlsqi 525
Cdd:cd14156  159 SAFWMAPEMLR---------GEPYDRKVDVFSFGIVLCEILAR------IPADPEVLprtgdfgldvQAFKEMVP----- 218
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568937340 526 GMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14156  219 GCPEPFLDLAASCCRMDAFKRPSFAELLDELEDI 252
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
298-555 2.77e-21

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: 94.08  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRwHGE----VAIRLIDIERDnEDQLKAFKREVMAYRQTRH---ENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd06917    7 ELVGRGSYGAVYRGY-HVKtgrvVALKVLNLDTD-DDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIvldvnKTRQIA---QEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGlfsISGVLQAGRR 446
Cdd:cd06917   85 EGGSIRTLMRAGPI-----AERYIAvimREVLVALKFIHKDGIIHRDIKAANILVTNtGNVKLCDFG---VAASLNQNSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 ddKLRIQNGWLCHLAPEIIRqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIG 526
Cdd:cd06917  157 --KRSTFVGTPYWMAPEVIT--------EGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRLEGNG 226
                        250       260
                 ....*....|....*....|....*....
gi 568937340 527 MGKEISDILLFCWAFEQEERPTFTKLMDM 555
Cdd:cd06917  227 YSPLLKEFVAACLDEEPKDRLSADELLKS 255
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
297-554 3.41e-21

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: 93.24  E-value: 3.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHGrWHGEVA-------IRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd06632    5 GQLLGSGSFGSVYEG-FNGDTGdffavkeVSLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDV---NKTRQIaqeiVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGR 445
Cdd:cd06632   84 VPGGSIHKLLQRYGAFEEPvirLYTRQI----LSGLAYLHSRNTVHRDIKGANILVDtNGVVKLADFGM---AKHVEAFS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 RDDKLRiqnGWLCHLAPEIIRQLSPdteedklPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTgmKPNLSQI 525
Cdd:cd06632  157 FAKSFK---GSPYWMAPEVIMQKNS-------GYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGN--SGELPPI 224
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 526 --GMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd06632  225 pdHLSPDAKDFIRLCLQRDPEDRPTASQLLE 255
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
298-562 3.53e-21

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: 93.32  E-value: 3.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRwhGEVAIRLIDIERDNEDQLKAfKREVMAYRQTRHENVVLFMGA------CMSP----------P 361
Cdd:cd14047   12 ELIGSGGFGQVFKAK--HRIDGKTYAIKRVKLNNEKA-EREVKALAKLDHPNIVRYNGCwdgfdyDPETsssnssrsktK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCKGRTLYS-VVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLF-SIS 438
Cdd:cd14047   89 CLFIQMEFCEKGTLESwIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLvDTGKVKIGDFGLVtSLK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 439 GVLQAGRRddklriqNGWLCHLAPEiirQLSPDTeedklpFSKHSDVFALGTIWYELHareWPFKTQPAEAIIWQmgtgm 518
Cdd:cd14047  169 NDGKRTKS-------KGTLSYMSPE---QISSQD------YGKEVDIYALGLILFELL---HVCDSAFEKSKFWT----- 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568937340 519 kpNLSqigmGKEISDIllFCWAFEQEErptfTKLMDMLEKLPKR 562
Cdd:cd14047  225 --DLR----NGILPDI--FDKRYKIEK----TIIKKMLSKKPED 256
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
297-554 4.10e-21

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: 93.27  E-value: 4.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFK------REVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd06631    6 GNVLGKGAYGTVYCGLTSTGQLIAVKQVELDTSDKEKAEKeyeklqEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-FYDNGKVVITDFGLFS-ISGVLQAGRRDD 448
Cdd:cd06631   86 PGGSIASILARFG-ALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNImLMPNGVIKLIDFGCAKrLCINLSSGSQSQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 KLRIQNGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMK--PNLSQiG 526
Cdd:cd06631  165 LLKSMRGTPYWMAPEVINETG---------HGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKpvPRLPD-K 234
                        250       260
                 ....*....|....*....|....*...
gi 568937340 527 MGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd06631  235 FSPEARDFVHACLTRDQDERPSAEQLLK 262
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
286-557 4.41e-21

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: 93.03  E-value: 4.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRW--HGEVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHL 363
Cdd:cd05067    1 EWEVPRETLKLVERLGAGQFGEVWMGYYngHTKVAIKSL---KQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFS-ISGVL 441
Cdd:cd05067   78 IITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVsDTLSCKIADFGLARlIEDNE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAGRRDDKLRIQngWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYEL--HAR-EWPFKTQPAEAIIWQMGTGM 518
Cdd:cd05067  158 YTAREGAKFPIK--W---TAPEAINYGT---------FTIKSDVWSFGILLTEIvtHGRiPYPGMTNPEVIQNLERGYRM 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568937340 519 -KPNlsqiGMGKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05067  224 pRPD----NCPEELYQLMRLCWKERPEDRPTFEYLRSVLE 259
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
300-557 7.81e-21

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: 91.96  E-value: 7.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG--EVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL-CKGRTLY 376
Cdd:cd05034    3 LGAGQFGEVWMGVWNGttKVAVKTL---KPGTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELmSKGSLLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGVLQAG----RRDDKLR 451
Cdd:cd05034   80 YLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCkVADFGL---ARLIEDDeytaREGAKFP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 452 IQngWLchlAPEIIRQLSpdteedklpFSKHSDVFALGTIWYEL--HAREwPFKTQPAEAIIWQMGTG--M-KPNlsqiG 526
Cdd:cd05034  157 IK--WT---APEAALYGR---------FTIKSDVWSFGILLYEIvtYGRV-PYPGMTNREVLEQVERGyrMpKPP----G 217
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 527 MGKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05034  218 CPDELYDIMLQCWKKEPEERPTFEYLQSFLE 248
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
302-559 1.43e-20

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: 91.84  E-value: 1.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 302 KGRFGQ--VYHGRwhgEVAIRLIDIERDNEDqlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVV 379
Cdd:cd14045   19 KKPFTQtgIYDGR---TVAIKKIAKKSFTLS--KRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 380 RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGlfsisgvLQAGRRDDKLRIQNGWLC 458
Cdd:cd14045   94 LNEDIPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCkIADYG-------LTTYRKEDGSENASGYQQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 459 HL-----APEIirQLSPDTEEDKLpfskhSDVFALGTIWYELHAREWPFktqPAEAiiWQMGTGMKPNLSQIGMGK---- 529
Cdd:cd14045  167 RLmqvylPPEN--HSNTDTEPTQA-----TDVYSYAIILLEIATRNDPV---PEDD--YSLDEAWCPPLPELISGKtens 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568937340 530 -----EISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14045  235 cpcpaDYVELIRRCRKNNPAQRPTFEQIKKTLHKI 269
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
297-554 1.91e-20

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: 91.21  E-value: 1.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHG--RWHGEV-AIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd06626    5 GNKIGEGTFGKVYTAvnLDTGELmAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVRDAKIvLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlfSISGVLQAGRRDDKLRI 452
Cdd:cd06626   85 TLEELLRHGRI-LDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDsNGLIKLGDFG--SAVKLKNNTTTMAPGEV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 453 QN--GWLCHLAPEIIRQlspDTEEDKLpfsKHSDVFALGTIWYELHA--REWPFKTQPAeAIIWQMGTGMKP------NL 522
Cdd:cd06626  162 NSlvGTPAYMAPEVITG---NKGEGHG---RAADIWSLGCVVLEMATgkRPWSELDNEW-AIMYHVGMGHKPpipdslQL 234
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568937340 523 SQIGMgkeisDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd06626  235 SPEGK-----DFLSRCLESDPKKRPTASELLD 261
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
298-552 3.28e-20

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: 90.35  E-value: 3.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQLKafkREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd06614    6 EKIGEGASGEVYKATDRAtgkEVAIKKMRLRKQNKELII---NEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVLdvnKTRQIA---QEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsisgVLQAGRRDDKL 450
Cdd:cd06614   83 LTDIITQNPVRM---NESQIAyvcREVLQGLEYLHSQNVIHRDIKSDNILLSkDGSVKLADFGF-----AAQLTKEKSKR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 451 RIQNG---WlchLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI-G 526
Cdd:cd06614  155 NSVVGtpyW---MAPEVIKRKDYGPK---------VDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPeK 222
                        250       260
                 ....*....|....*....|....*.
gi 568937340 527 MGKEISDILLFCWAFEQEERPTFTKL 552
Cdd:cd06614  223 WSPEFKDFLNKCLVKDPEKRPSAEEL 248
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
297-553 1.32e-19

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: 88.57  E-value: 1.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVY------HGRwhgEVAIRLIDIERDNED---QLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd06625    5 GKLLGQGAFGQVYlcydadTGR---ELAVKQVEIDPINTEaskEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlfsISGVLQAGRR 446
Cdd:cd06625   82 EYMPGGSVKDEIK-AYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDsNGNVKLGDFG---ASKRLQTICS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 DDKLRIQNGWLCHLAPEIIRQlspdteEDklpFSKHSDVFALG-TI---------WYELHAREWPFK--TQPAEAIiwqm 514
Cdd:cd06625  158 STGMKSVTGTPYWMSPEVING------EG---YGRKADIWSVGcTVvemlttkppWAEFEPMAAIFKiaTQPTNPQ---- 224
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 515 gtgMKPNLSQIGmgkeiSDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06625  225 ---LPPHVSEDA-----RDFLSLIFVRNKKQRPSAEELL 255
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
298-573 1.41e-19

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: 88.89  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE---VAIRLIDIERDNEdqlkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd14010    6 DEIGRGKHSVVYKGRRKGTiefVAIKCVDKSKRPE-----VLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL-----------FSISGVLQ 442
Cdd:cd14010   81 LETLLR-QDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDgNGTLKLSDFGLarregeilkelFGQFSDEG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGRRDDKLRIQNGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFK----TQPAEAIIwqmgtGM 518
Cdd:cd14010  160 NVNKVSKKQAKRGTPYYMAPELFQG---------GVHSFASDLWALGCVLYEMFTGKPPFVaesfTELVEKIL-----NE 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 519 KPNLSQIGMGKEISdillfcwafeqeerPTFTKLMD-MLEKLP-KR---NRRLSHPghFW 573
Cdd:cd14010  226 DPPPPPPKVSSKPS--------------PDFKSLLKgLLEKDPaKRlswDELVKHP--FW 269
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
296-507 1.86e-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: 88.70  E-value: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHGrWHG---------EVAIRLIdiERD---NEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHL 363
Cdd:cd14076    5 LGRTLGEGEFGKVKLG-WPLpkanhrsgvQVAIKLI--RRDtqqENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGVLQ 442
Cdd:cd14076   82 GIVLEFVSGGELFDYILARRRLKDSVACRLFAQ-LISGVAYLHKKGVVHRDLKLENLLLDkNRNLVITDFGFANTFDHFN 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 443 AgrrdDKLRIQNGWLCHLAPEIIRQLSPDTeedklpfSKHSDVFALGTIWYELHAREWPFKTQPA 507
Cdd:cd14076  161 G----DLMSTSCGSPCYAAPELVVSDSMYA-------GRKADIWSCGVILYAMLAGYLPFDDDPH 214
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
300-498 2.22e-19

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: 88.33  E-value: 2.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQ---VYHgRWHGEVAIrLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd14154    1 LGKGFFGQaikVTH-RETGEVMV-MKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGK-VVITDFGLfsiSGVLQAGRRDDKLRIQNG 455
Cdd:cd14154   79 DVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKtVVVADFGL---ARLIVEERLPSGNMSPSE 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 456 WLCHL------------------APEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAR 498
Cdd:cd14154  156 TLRHLkspdrkkrytvvgnpywmAPEMLNGRSYD---------EKVDIFSFGIVLCEIIGR 207
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
292-495 2.68e-19

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: 88.07  E-value: 2.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDnEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRtnqVVAIKVIDLEEA-EDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlfsISGvlQAGRRD 447
Cdd:cd06609   80 YCGGGSVLDLLKPGP--LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLsEEGDVKLADFG---VSG--QLTSTM 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568937340 448 DKLRIQNG---WlchLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYEL 495
Cdd:cd06609  153 SKRNTFVGtpfW---MAPEVIKQSGYDEK---------ADIWSLGITAIEL 191
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
290-554 2.91e-19

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: 88.13  E-value: 2.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVYHGRwHGE----VAIRLIDIERDNEDQLKAFKREVMAYRQtrHENVVLFMGACMSPPH--- 362
Cdd:cd06608    4 PAGIFELVEVIGEGTYGKVYKAR-HKKtgqlAAIKIMDIIEDEEEEIKLEINILRKFSN--HPNIATFYGAFIKKDPpgg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 ---LAIITSLCKGRtlySVVRDAKIVLDVNKT---RQIA---QEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDF 432
Cdd:cd06608   81 ddqLWLVMEYCGGG---SVTDLVKGLRKKGKRlkeEWIAyilRETLRGLAYLHENKVIHRDIKGQNILLtEEAEVKLVDF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 433 GLfsiSGVLQA--GRRDDKLriqnGWLCHLAPEIIR-QLSPDTEEDklpfsKHSDVFALGTIWYELHAREWPFKTQPAEA 509
Cdd:cd06608  158 GV---SAQLDStlGRRNTFI----GTPYWMAPEVIAcDQQPDASYD-----ARCDVWSLGITAIELADGKPPLCDMHPMR 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340 510 IIWQMGTGMKPNLSQ-IGMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd06608  226 ALFKIPRNPPPTLKSpEKWSKEFNDFISECLIKNYEQRPFTEELLE 271
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
292-498 2.98e-19

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: 88.65  E-value: 2.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHGE-VAIRLIDiERDNedqlKAFKREVMAYRQT--RHENVVLFMGACM----SPPHLA 364
Cdd:cd14142    5 RQITLVECIGKGRYGEVWRGQWQGEsVAVKIFS-SRDE----KSWFRETEIYNTVllRHENILGFIASDMtsrnSCTQLW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAK--------GILHKDLKSKNVFY-DNGKVVITDFGLf 435
Cdd:cd14142   80 LITHYHENGSLYDYLQRT--TLDHQEMLRLALSAASGLVHLHTEifgtqgkpAIAHRDLKSKNILVkSNGQCCIADLGL- 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 436 sisGVLQAgRRDDKLRIQN----GWLCHLAPEII-RQLSPDTEEDklpfSKHSDVFALGTIWYELHAR 498
Cdd:cd14142  157 ---AVTHS-QETNQLDVGNnprvGTKRYMAPEVLdETINTDCFES----YKRVDIYAFGLVLWEVARR 216
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
287-557 3.50e-19

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: 87.78  E-value: 3.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGAC- 357
Cdd:cd05032    1 WELPREKITLIRELGQGSFGMVYEGLAKGvvkgepetRVAIKTVN-ENASMRERIEFLNEASVMKEFNCHHVVRLLGVVs 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 358 MSPPHLAIITSLCKGrTLYSVVR---------DAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKN-VFYDNGKV 427
Cdd:cd05032   80 TGQPTLVVMELMAKG-DLKSYLRsrrpeaennPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNcMVAEDLTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 428 VITDFGLfsisgvlqagRRD----DKLRIQNGwlcHLAPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHA-REWPF 502
Cdd:cd05032  159 KIGDFGM----------TRDiyetDYYRKGGK---GLLP--VRWMAPESLKDGV-FTTKSDVWSFGVVLWEMATlAEQPY 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 503 KTQPAEAIIWQMGTG--MKPnlsQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05032  223 QGLSNEEVLKFVIDGghLDL---PENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
300-560 4.37e-19

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: 87.02  E-value: 4.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRW----HGEVAIRLIDIERDNEDQLKA-FKREVMAYRQTRHENVVLFMGACMSPPhLAIITSLCKGRT 374
Cdd:cd05060    3 LGHGNFGSVRKGVYlmksGKEVEVAVKTLKQEHEKAGKKeFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAPLGP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVLDVNKTrQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsiSGVLQAGrrDDKLRIQ 453
Cdd:cd05060   82 LLKYLKKRREIPVSDLK-ELAHQVAMGMAYLESKHFVHRDLAARNVLLVNrHQAKISDFGM---SRALGAG--SDYYRAT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 NG--W-LCHLAPEIIRQLSpdteedklpFSKHSDVFALG-TIWYELHAREWPFKTQPAEAIIWQMGTGM---KPNLSQIg 526
Cdd:cd05060  156 TAgrWpLKWYAPECINYGK---------FSSKSDVWSYGvTLWEAFSYGAKPYGEMKGPEVIAMLESGErlpRPEECPQ- 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568937340 527 mgkEISDILLFCWAFEQEERPTFTKLMDMLEKLP 560
Cdd:cd05060  226 ---EIYSIMLSCWKYRPEDRPTFSELESTFRRDP 256
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
295-555 4.42e-19

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: 87.56  E-value: 4.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHGE----VAIRLIDIE-----RDNEDQLKAFK---REVMAYR-QTRHENVVLFMGACMSPP 361
Cdd:cd08528    3 AVLELLGSGAFGCVYKVRKKSNgqtlLALKEINMTnpafgRTEQERDKSVGdiiSEVNIIKeQLRHPNIVRYYKTFLEND 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCKG---RTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLH-AKGILHKDLKSKNVFY-DNGKVVITDFGLFS 436
Cdd:cd08528   83 RLYIVMELIEGaplGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLgEDDKVTITDFGLAK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 437 isgvlQAGRRDDKLRIQNGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGT 516
Cdd:cd08528  163 -----QKGPESSKMTSVVGTILYSCPEIVQN---------EPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVE 228
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 517 GMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMDM 555
Cdd:cd08528  229 AEYEPLPEGMYSDDITFVIRSCLTPDPEARPDIVEVSSM 267
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
292-553 5.93e-19

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: 87.03  E-value: 5.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRW---HGEVAIRLIDIERDNEDqLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYClpkKEKVAIKRIDLEKCQTS-MDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDA--KIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlfsISGVLQAGr 445
Cdd:cd06610   80 LLSGGSLLDIMKSSypRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGeDGSVKIADFG---VSASLATG- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 RDDKLRIQN---GWLCHLAPEIIRQLSPDTEEdklpfskhSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNL 522
Cdd:cd06610  156 GDRTRKVRKtfvGTPCWMAPEVMEQVRGYDFK--------ADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSL 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568937340 523 ----SQIGMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06610  228 etgaDYKKYSKSFRKMISLCLQKDPSKRPTAEELL 262
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
287-557 6.19e-19

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: 87.02  E-value: 6.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG--EVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd05072    2 WEIPRESIKLVKKLGAGQFGEVWMGYYNNstKVAVKTL---KPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITS-LCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFS-ISGVL 441
Cdd:cd05072   79 IITEyMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCkIADFGLARvIEDNE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAGRRDDKLRIQngWLchlAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR---EWPFKTQPAEAIIWQMGTGM 518
Cdd:cd05072  159 YTAREGAKFPIK--WT---APEAINFGS---------FTIKSDVWSFGILLYEIVTYgkiPYPGMSNSDVMSALQRGYRM 224
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 519 kPNLSQIGmgKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05072  225 -PRMENCP--DELYDIMKTCWKEKAEERPTFDYLQSVLD 260
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
297-510 8.11e-19

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: 86.45  E-value: 8.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHG-------RWhgevAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14097    6 GRKLGQGSFGVVIEAthketqtKW----AIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY--------DNGKVVITDFGLfsisGVL 441
Cdd:cd14097   82 CEDGELKELL-LRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnnDKLNIKVTDFGL----SVQ 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 442 QAGRRDDKLRIQNGWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAI 510
Cdd:cd14097  157 KYGLGEDMLQETCGTPIYMAPEVI---------SAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKL 216
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
300-557 8.95e-19

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: 86.09  E-value: 8.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGE--VAIRLIDIERDNEDQlkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYS 377
Cdd:cd05113   12 LGTGQFGVVKYGKWRGQydVAIKMIKEGSMSEDE---FIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 VVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSIsgVLqagrrDDKLRIQNG- 455
Cdd:cd05113   89 YLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNdQGVVKVSDFGLSRY--VL-----DDEYTSSVGs 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 456 -----WlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGM---KPNLSQig 526
Cdd:cd05113  162 kfpvrW---SPPEVLMYSK---------FSSKSDVWAFGVLMWEVYSLgKMPYERFTNSETVEHVSQGLrlyRPHLAS-- 227
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 527 mgKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05113  228 --EKVYTIMYSCWHEKADERPTFKILLSNIL 256
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
298-498 9.21e-19

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: 86.94  E-value: 9.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE-VAIRlIDIERDNEdqlkAFKREVMAYrQT---RHENVVLFMGACM----SPPHLAIITSL 369
Cdd:cd14056    1 KTIGKGRYGEVWLGKYRGEkVAVK-IFSSRDED----SWFRETEIY-QTvmlRHENILGFIAADIkstgSWTQLWLITEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAK--------GILHKDLKSKNVFY-DNGKVVITDFGLfSISGV 440
Cdd:cd14056   75 HEHGSLYDYLQRN--TLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVkRDGTCCIADLGL-AVRYD 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 441 LQAGRRDDKLRIQNGWLCHLAPEIIR-QLSPDTeedklpFS--KHSDVFALGTIWYELHAR 498
Cdd:cd14056  152 SDTNTIDIPPNPRVGTKRYMAPEVLDdSINPKS------FEsfKMADIYSFGLVLWEIARR 206
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
295-510 1.36e-18

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: 85.68  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIER-DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14099    4 RRGKFLGKGGFAKCYEVTDMStgkVYAGKVVPKSSlTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQagRRDDK 449
Cdd:cd14099   84 SNGSLMELLKRRK-ALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDeNMNVKIGDFGL---AARLE--YDGER 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 450 LRIqngwLC----HLAPEIIrqlspdteEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAI 510
Cdd:cd14099  158 KKT----LCgtpnYIAPEVL--------EKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKET 210
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
287-553 1.62e-18

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 85.95  E-value: 1.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIpfeqleIGELiGKGRFGQVYHGRwHGE----VAIRLIDIErdNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPH 362
Cdd:cd06611    7 WEI------IGEL-GDGAFGKVYKAQ-HKEtglfAAAKIIQIE--SEEELEDFMVEIDILSECKHPNIVGLYEAYFYENK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 LAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-FYDNGKVVITDFGLfSISGVL 441
Cdd:cd06611   77 LWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNIlLTLDGDVKLADFGV-SAKNKS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAGRRDDKLriqnGWLCHLAPEIIRqlspdTEEDK-LPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKP 520
Cdd:cd06611  156 TLQKRDTFI----GTPYWMAPEVVA-----CETFKdNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPP 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568937340 521 NLSQI-GMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06611  227 TLDQPsKWSSSFNDFLKSCLVKDPDDRPTAAELL 260
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
295-502 1.70e-18

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: 85.43  E-value: 1.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRW--HG-EVAIRLIDIERDNEDQLKAF-KREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14162    3 IVGKTLGHGSYAVVKKAYStkHKcKVAIKIVSKKKAPEDYLQKFlPREIEVIKGLKHPNLICFYEAIETTSRVYIIMELA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGVLQAGRRddK 449
Cdd:cd14162   83 ENGDLLDYIR-KNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDkNNNLKITDFGFARGVMKTKDGKP--K 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 450 L-RIQNGWLCHLAPEIIRQLSPDteedklPFskHSDVFALGTIWYE-LHAReWPF 502
Cdd:cd14162  160 LsETYCGSYAYASPEILRGIPYD------PF--LSDIWSMGVVLYTmVYGR-LPF 205
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
290-553 1.96e-18

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: 85.51  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVYHG---RWHGEVAIRLIDIErDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:cd06641    2 PEELFTKLEKIGKGSFGEVFKGidnRTQKVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsisgvlqAGR 445
Cdd:cd06641   81 MEYLGGGSALDLLEPGP--LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLsEHGEVKLADFGV--------AGQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 RDDKLRIQNGWLCH---LAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGmKPNL 522
Cdd:cd06641  151 LTDTQIKRN*FVGTpfwMAPEVIKQSAYDSK---------ADIWSLGITAIELARGEPPHSELHPMKVLFLIPKN-NPPT 220
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 523 SQIGMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06641  221 LEGNYSKPLKEFVEACLNKEPSFRPTAKELL 251
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
292-503 2.18e-18

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: 85.34  E-value: 2.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHG---EVAIRLID---IERDNEDQLKAFKREVMAYrqTRHENVVLFMGACMSPPHLAI 365
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKEtgkEYAIKVLDkrhIIKEKKVKYVTIEKEVLSR--LAHPGIVKLYYTFQDESKLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFG--------LFS 436
Cdd:cd05581   79 VLEYAPNGDLLEYIRKYG-SLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDeDMHIKITDFGtakvlgpdSSP 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 437 ISGVLQAGRRDDKLRIQNGWLC----HLAPEIIrqlspdteEDKlPFSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd05581  158 ESTKGDADSQIAYNQARAASFVgtaeYVSPELL--------NEK-PAGKSSDLWALGCIIYQMLTGKPPFR 219
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
298-498 2.36e-18

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: 85.57  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE-VAIRLIDIERDnedqlKAFKREVMAYRQT--RHENVVLFMGACMSPPHLA----IIT--- 367
Cdd:cd13998    1 EVIGKGRFGEVWKASLKNEpVAVKIFSSRDK-----QSWFREKEIYRTPmlKHENILQFIAADERDTALRtelwLVTafh 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 ---SLCKGRTLYsvvrdakiVLDVNKTRQIAQEIVKGMGYLHAK---------GILHKDLKSKNVFY-DNGKVVITDFGL 434
Cdd:cd13998   76 pngSL*DYLSLH--------TIDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVkNDGTCCIADFGL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 435 ---FSisgvlQAGRRDDKLRI-QNGWLCHLAPEIIrqlspdteEDKLPFS-----KHSDVFALGTIWYELHAR 498
Cdd:cd13998  148 avrLS-----PSTGEEDNANNgQVGTKRYMAPEVL--------EGAINLRdfesfKRVDIYAMGLVLWEMASR 207
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
295-554 2.39e-18

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: 85.22  E-value: 2.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYH------GRWHgevAIRLIDIER--DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:cd14098    3 QIIDRLGSGTFAEVKKavevetGKMR---AIKQIVKRKvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKN--VFYDNGKVV-ITDFGLFSISGvlqa 443
Cdd:cd14098   80 MEYVEGGDLMDFIMAWG-AIPEQHARELTKQILEAMAYTHSMGITHRDLKPENilITQDDPVIVkISDFGLAKVIH---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 grRDDKLRIQNGWLCHLAPEIIRqlSPDTEEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKP--- 520
Cdd:cd14098  155 --TGTFLVTFCGTMAYLAPEILM--SKEQNLQG-GYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTqpp 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568937340 521 ----NLSQigMGKEISDILLfcwAFEQEERPTFTKLMD 554
Cdd:cd14098  230 lvdfNISE--EAIDFILRLL---DVDPEKRMTAAQALD 262
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
300-554 2.71e-18

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: 85.15  E-value: 2.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR-WHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSV 378
Cdd:cd06624   16 LGKGTFGVVYAARdLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSAL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 379 VRDAKIVLDVNKTRQI--AQEIVKGMGYLHAKGILHKDLKSKNVFYD--NGKVVITDFGLF-----------SISGVLQa 443
Cdd:cd06624   96 LRSKWGPLKDNENTIGyyTKQILEGLKYLHDNKIVHRDIKGDNVLVNtySGVVKISDFGTSkrlaginpcteTFTGTLQ- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 grrddklriqngwlcHLAPEIIrqlspdteeDKLP--FSKHSDVFALGTIWYELHAREWPF-KTQPAEAIIWQMGT-GMK 519
Cdd:cd06624  175 ---------------YMAPEVI---------DKGQrgYGPPADIWSLGCTIIEMATGKPPFiELGEPQAAMFKVGMfKIH 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568937340 520 PNLSQIgMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd06624  231 PEIPES-LSEEAKSFILRCFEPDPDKRATASDLLQ 264
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
316-502 2.96e-18

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: 85.10  E-value: 2.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 316 EVAIRLIDIERDN------EDQLKAFKREVMAYRQ-TRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVrDAKIVLDV 388
Cdd:cd14093   30 EFAVKIIDITGEKsseneaEELREATRREIEILRQvSGHPNIIELHDVFESPTFIFLVFELCRKGELFDYL-TEVVTLSE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 389 NKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlFSIsgVLQAGrrdDKLRIQNGWLCHLAPEIIRQ 467
Cdd:cd14093  109 KKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDdNLNVKISDFG-FAT--RLDEG---EKLRELCGTPGYLAPEVLKC 182
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568937340 468 lspDTEEDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14093  183 ---SMYDNAPGYGKEVDMWACGVIMYTLLAGCPPF 214
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
295-520 3.10e-18

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 84.66  E-value: 3.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGR--WHGE-VAIRLIDIERDneDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd06613    3 ELIQRIGSGTYGDVYKARniATGElAAVKVIKLEPG--DDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTlysvVRDAKIVLDVNKTRQIA---QEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlfsISGVLQA--GR 445
Cdd:cd06613   81 GGS----LQDIYQVTGPLSELQIAyvcRETLKGLAYLHSTGKIHRDIKGANILLtEDGDVKLADFG---VSAQLTAtiAK 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 446 RddKLRIqnGWLCHLAPEIIrqlspdTEEDKLPFSKHSDVFALGTIWYELHAREWP-FKTQPAEAiIWQMG-TGMKP 520
Cdd:cd06613  154 R--KSFI--GTPYWMAPEVA------AVERKGGYDGKCDIWALGITAIELAELQPPmFDLHPMRA-LFLIPkSNFDP 219
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
295-553 3.28e-18

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


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 84.62  E-value: 3.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHGE---VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd08225    3 EIIKKIGEGSFGKIYLAKAKSDsehCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVV-RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVviTDFGLFSISGVLqagrrDDK 449
Cdd:cd08225   83 GGDLMKRInRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSkNGMV--AKLGDFGIARQL-----NDS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIqnGWLCHLAPeiiRQLSPDTEEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTG----MKPNLSqi 525
Cdd:cd08225  156 MEL--AYTCVGTP---YYLSPEICQNR-PYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGyfapISPNFS-- 227
                        250       260
                 ....*....|....*....|....*...
gi 568937340 526 gmgKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd08225  228 ---RDLRSLISQLFKVSPRDRPSITSIL 252
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
300-553 3.51e-18

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: 84.40  E-value: 3.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYhgrwhgevaiRLIDIERDNEDQLKAFKR----------EVMAYRQTR------HENVVLFMGACMSPPHL 363
Cdd:cd08222    8 LGSGNFGTVY----------LVSDLKATADEELKVLKEisvgelqpdeTVDANREAKllskldHPAIVKFHDSFVEKESF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQ---EIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGlfsISGV 440
Cdd:cd08222   78 CIVTEYCEGGDLDDKISEYKKSGTTIDENQILDwfiQLLLAVQYMHERRILHRDLKAKNIFLKNNVIKVGDFG---ISRI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 LQAgrRDDKLRIQNGWLCHLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKP 520
Cdd:cd08222  155 LMG--TSDLATTFTGTPYYMSPEVLKHEGYNSK---------SDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETP 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568937340 521 NLSQIgMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd08222  224 SLPDK-YSKELNAIYSRMLNKDPALRPSAAEIL 255
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
294-559 4.17e-18

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: 84.51  E-value: 4.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHGRWH------GEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACM------SPP 361
Cdd:cd05035    1 LKLGKILGEGEFGSVMEAQLKqddgsqLKVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFtasdlnKPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCK-----GRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKN-VFYDNGKVVITDFGLf 435
Cdd:cd05035   81 SPMVILPFMKhgdlhSYLLYSRLGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNcMLDENMTVCVADFGL- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 436 siSGVLQAGrrdDKLRiQNgwlcHLAPEIIRQLSPDTEEDKLpFSKHSDVFALG-TIWYELHAREWPFKTQPAEAIIWQM 514
Cdd:cd05035  160 --SRKIYSG---DYYR-QG----RISKMPVKWIALESLADNV-YTSKSDVWSFGvTMWEIATRGQTPYPGVENHEIYDYL 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568937340 515 GTGMKPNLSQIGMgKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05035  229 RNGNRLKQPEDCL-DEVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
294-553 4.42e-18

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: 84.67  E-value: 4.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHGRwH---GEVA-IRLIDIERDNEDQLKAfkrEV-MAYRQTRHENVVLFMGACM--SPP----H 362
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGR-HvktGQLAaIKVMDVTEDEEEEIKL---EInMLKKYSHHRNIATYYGAFIkkSPPghddQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 LAIITSLCKGRTLYSVVRDAK-IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlfsISGV 440
Cdd:cd06636   94 LWLVMEFCGAGSVTDLVKNTKgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLtENAEVKLVDFG---VSAQ 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 LQ--AGRRDDKLriqnGWLCHLAPEIIR-QLSPDTEEDklpfsKHSDVFALGTIWYELHAREWPF-KTQPAEAiIWQMGT 516
Cdd:cd06636  171 LDrtVGRRNTFI----GTPYWMAPEVIAcDENPDATYD-----YRSDIWSLGITAIEMAEGAPPLcDMHPMRA-LFLIPR 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568937340 517 GMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06636  241 NPPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLL 277
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
288-556 4.78e-18

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: 85.08  E-value: 4.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEQLEIGELIGKGRFGQV---------------YHGRW-HGEVAIRLIDIERD--NEDQLKAFKREVMAYRQTRHEN 349
Cdd:cd05051    1 EFPREKLEFVEKLGEGQFGEVhlceanglsdltsddFIGNDnKDEPVLVAVKMLRPdaSKNAREDFLKEVKIMSQLKDPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 350 VVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQ-----------IAQEIVKGMGYLHAKGILHKDLKSK 418
Cdd:cd05051   81 IVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNsktlsygtllyMATQIASGMKYLESLNFVHRDLATR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 419 NVFYDNG-KVVITDFGlfsISGVLQAGrrdDKLRIQNGwlchlAPEIIRQLSpdTEEDKLP-FSKHSDVFALG-TIW--Y 493
Cdd:cd05051  161 NCLVGPNyTIKIADFG---MSRNLYSG---DYYRIEGR-----AVLPIRWMA--WESILLGkFTTKSDVWAFGvTLWeiL 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 494 ELhAREWPFKTQPAEAIIWQMG-----TGMKPNLSQI-GMGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd05051  228 TL-CKEQPYEHLTDEQVIENAGeffrdDGMEVYLSRPpNCPKEIYELMLECWRRDEEDRPTFREIHLFL 295
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
300-559 4.94e-18

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: 84.24  E-value: 4.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQ---VYHgRWHGEVAIRLIDIERDNEDQlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd14221    1 LGKGCFGQaikVTH-RETGEVMVMKELIRFDEETQ-RTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSI--------SGVLQAGRRD 447
Cdd:cd14221   79 GIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVrENKSVVVADFGLARLmvdektqpEGLRSLKKPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 448 DKLR---IQNGWLchLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGT-GMKPNLS 523
Cdd:cd14221  159 RKKRytvVGNPYW--MAPEMINGRSYD---------EKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFGLNVrGFLDRYC 227
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568937340 524 QIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14221  228 PPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETL 263
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
293-559 5.46e-18

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: 84.63  E-value: 5.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHG---RWHG-----EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd05045    1 NLVLGKTLGEGEFGKVVKAtafRLKGragytTVAVKMLK-ENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKIV-----------------------LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF 421
Cdd:cd05045   80 LIVEYAKYGSLRSFLRESRKVgpsylgsdgnrnssyldnpderaLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 422 YDNGKVV-ITDFGLFSISGVLQAGRRDDKLRIQNGWlchlapeiirqLSPDTEEDKLpFSKHSDVFALGTIWYELHAREW 500
Cdd:cd05045  160 VAEGRKMkISDFGLSRDVYEEDSYVKRSKGRIPVKW-----------MAIESLFDHI-YTTQSDVWSFGVLLWEIVTLGG 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 501 -PFKTQPAEAIIWQMGTGMKPNLSQiGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05045  228 nPYPGIAPERLFNLLKTGYRMERPE-NCSEEMYNLMLTCWKQEPDKRPTFADISKELEKM 286
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
289-558 6.72e-18

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: 84.05  E-value: 6.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 289 IPFEQLEIGELIGKGRFGQVYHGRWHGE--------VAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACM-S 359
Cdd:cd05046    2 FPRSNLQEITTLGRGEFGEVFLAKAKGIeeeggetlVLVKALQ-KTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCReA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 360 PPHLAIITslckgrtlYSVVRDAKIVLDVNKTRQ---------------IAQEIVKGMGYLHAKGILHKDLKSKN--VFY 422
Cdd:cd05046   81 EPHYMILE--------YTDLGDLKQFLRATKSKDeklkppplstkqkvaLCTQIALGMDHLSNARFVHRDLAARNclVSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 423 DNgKVVItdfglfSISGVLQAGRRDDKLRIQNGW--LCHLAPEIIRqlspdtEEDklpFSKHSDVFALG-TIWYELHARE 499
Cdd:cd05046  153 QR-EVKV------SLLSLSKDVYNSEYYKLRNALipLRWLAPEAVQ------EDD---FSTKSDVWSFGvLMWEVFTQGE 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 500 WPFKTQPAEAIIWQMGTGmKPNLSQI-GMGKEISDILLFCWAFEQEERPTFTKLMDMLEK 558
Cdd:cd05046  217 LPFYGLSDEEVLNRLQAG-KLELPVPeGCPSRLYKLMTRCWAVNPKDRPSFSELVSALGE 275
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
303-550 7.14e-18

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: 83.70  E-value: 7.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 303 GRFGQVY--HGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVR 380
Cdd:cd14027    4 GGFGKVSlcFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 381 DAKIVLDVnKTRQIAqEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGL--FSISGVLQAGRRDDKLRIQN--- 454
Cdd:cd14027   84 KVSVPLSV-KGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDfHIKIADLGLasFKMWSKLTKEEHNEQREVDGtak 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 455 ---GWLCHLAPEIIRQLSPDTEEDklpfskhSDVFALGTIWYELHAREWPFKTQPAE-AIIWQMGTGMKPNLSQI--GMG 528
Cdd:cd14027  162 knaGTLYYMAPEHLNDVNAKPTEK-------SDVYSFAIVLWAIFANKEPYENAINEdQIIMCIKSGNRPDVDDIteYCP 234
                        250       260
                 ....*....|....*....|..
gi 568937340 529 KEISDILLFCWAFEQEERPTFT 550
Cdd:cd14027  235 REIIDLMKLCWEANPEARPTFP 256
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
300-498 8.39e-18

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: 83.29  E-value: 8.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVY---HgRWHGEVAIRLIDIERDNEDQLKafkREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd14155    1 IGSGFFSEVYkvrH-RTSGQVMALKMNTLSSNRANML---REVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY---DNG-KVVITDFGLfsISGVLQAGRRDDKLRI 452
Cdd:cd14155   77 QLL-DSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGyTAVVGDFGL--AEKIPDYSDGKEKLAV 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 453 QNG--WlchLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAR 498
Cdd:cd14155  154 VGSpyW---MAPEVLRG---------EPYNEKADVFSYGIILCEIIAR 189
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
298-502 8.46e-18

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: 83.89  E-value: 8.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVY------HGRWHGEVAIRLIDIERDnedqlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14166    9 EVLGSGAFSEVYlvkqrsTGKLYALKCIKKSPLSRD-----SSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVLDVNKTRQIaQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFSISgvlqagrrd 447
Cdd:cd14166   84 GGELFDRILERGVYTEKDASRVI-NQVLSAVKYLHENGIVHRDLKPENLLYltpdENSKIMITDFGLSKME--------- 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 448 dklriQNGWL---C----HLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14166  154 -----QNGIMstaCgtpgYVAPEVLAQ---------KPYSKAVDCWSIGVITYILLCGYPPF 201
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
299-559 8.95e-18

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: 83.79  E-value: 8.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRWH------GE-VAIRliDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSP--PHLAIITSL 369
Cdd:cd05081   11 QLGKGNFGSVELCRYDplgdntGAlVAVK--QLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPgrRSLRLVMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFSisgvLQAGRRDD 448
Cdd:cd05081   89 LPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESeAHVKIADFGLAK----LLPLDKDY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 KLRIQNGWlchlAPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELH---------AREW-----PFKTQPAEAIIWQM 514
Cdd:cd05081  165 YVVREPGQ----SP--IFWYAPESLSDNI-FSRQSDVWSFGVVLYELFtycdkscspSAEFlrmmgCERDVPALCRLLEL 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568937340 515 GTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05081  238 LEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
297-552 9.43e-18

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: 83.06  E-value: 9.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHGRWHGEVAIRLIDIERDN-EDQLKA-FKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd05084    1 GERIGRGNFGEVFSGRLRADNTPVAVKSCRETlPPDLKAkFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGL--------FSISGVLQagr 445
Cdd:cd05084   81 FLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLkISDFGMsreeedgvYAATGGMK--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 rddklRIQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYE---LHAREWPFKT-QPAEAIIWQMGTGMKPN 521
Cdd:cd05084  158 -----QIPVKW---TAPEALNYGR---------YSSESDVWSFGILLWEtfsLGAVPYANLSnQQTREAVEQGVRLPCPE 220
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 522 LSQigmgKEISDILLFCWAFEQEERPTFTKL 552
Cdd:cd05084  221 NCP----DEVYRLMEQCWEYDPRKRPSFSTV 247
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
286-559 1.19e-17

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: 83.62  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRWHG---------EVAIRLIDIERdNEDQLKAFKREV-MAYRQTRHENVVLFMG 355
Cdd:cd05053    6 EWELPRDRLTLGKPLGEGAFGQVVKAEAVGldnkpnevvTVAVKMLKDDA-TEKDLSDLVSEMeMMKMIGKHKNIINLLG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 356 ACMSPPHLAIITSLCKGRTLYSVVR-------DAKIVLDVNKTRQIAQ--------EIVKGMGYLHAKGILHKDLKSKNV 420
Cdd:cd05053   85 ACTQDGPLYVVVEYASKGNLREFLRarrppgeEASPDDPRVPEEQLTQkdlvsfayQVARGMEYLASKKCIHRDLAARNV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 421 FYDNGKVV-ITDFGLfsisgvlqagRRD----DKLR-IQNGWLchlaPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYE 494
Cdd:cd05053  165 LVTEDNVMkIADFGL----------ARDihhiDYYRkTTNGRL----P--VKWMAPEALFDRV-YTHQSDVWSFGVLLWE 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 495 LhareWPFKTQPAEAI-IWQM------GTGM-KPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05053  228 I----FTLGGSPYPGIpVEELfkllkeGHRMeKPQNCT----QELYMLMRDCWHEVPSQRPTFKQLVEDLDRI 292
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
285-554 1.29e-17

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 83.54  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 285 QEWDIpfeqleIGELiGKGRFGQVYHG--RWHGEVAIRLIdIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPH 362
Cdd:cd06644   12 EVWEI------IGEL-GDGAFGKVYKAknKETGALAAAKV-IETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 LAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfSISGVL 441
Cdd:cd06644   84 LWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTlDGDIKLADFGV-SAKNVK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAGRRDDKLriqnGWLCHLAPEIIRqlsPDTEEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPN 521
Cdd:cd06644  163 TLQRRDSFI----GTPYWMAPEVVM---CETMKDT-PYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPT 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568937340 522 LSQIGM-GKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd06644  235 LSQPSKwSMEFRDFLKTALDKHPETRPSAAQLLE 268
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
295-502 1.44e-17

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: 82.58  E-value: 1.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDqlkAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14087    4 DIKALIGRGSFSRVVrveHRVTRQPYAIKMIETKCRGRE---VCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVV--------RDAKIVLdvnktrqiaQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFSisg 439
Cdd:cd14087   81 GGELFDRIiakgsfteRDATRVL---------QMVLDGVKYLHGLGITHRDLKPENLLYyhpgPDSKIMITDFGLAS--- 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 440 vLQAGRRDDKLRIQNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14087  149 -TRKKGPNCLMKTTCGTPEYIAPEILL---------RKPYTQSVDMWAVGVIAYILLSGTMPF 201
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
300-511 1.66e-17

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: 82.65  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWH--GEV-AIRLI---DIERDNE-DQLKAfKREVMAyrQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd05579    1 ISRGAYGRVYLAKKKstGDLyAIKVIkkrDMIRKNQvDSVLA-ERNILS--QAQNPFVVKLYYSFQGKKNLYLVMEYLPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfSISGVLqagRRDDKLR 451
Cdd:cd05579   78 GDLYSLLENVG-ALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDaNGHLKLTDFGL-SKVGLV---RRQIKLS 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 452 IQNGWLC--------------HLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAII 511
Cdd:cd05579  153 IQKKSNGapekedrrivgtpdYLAPEILL---------GQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIF 217
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
298-565 1.71e-17

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 82.80  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHG---RWHGEVAIRLIDIErDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd06642   10 ERIGKGSFGEVYKGidnRTKEVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsisgvlqAGRRDDKLRIQ 453
Cdd:cd06642   89 ALDLLKPGP--LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLsEQGDVKLADFGV--------AGQLTDTQIKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 NGWLCH---LAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLsQIGMGKE 530
Cdd:cd06642  159 NTFVGTpfwMAPEVIKQSAYDFK---------ADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTL-EGQHSKP 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568937340 531 ISDILLFCWAFEQEERPT------------FTKLMDMLEKLPKRNRR 565
Cdd:cd06642  229 FKEFVEACLNKDPRFRPTakellkhkfitrYTKKTSFLTELIDRYKR 275
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
287-557 1.96e-17

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: 82.38  E-value: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRW--HGEVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd05073    6 WEIPRESLKLEKKLGAGQFGEVWMATYnkHTKVAVKTM---KPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSI-SGVLQ 442
Cdd:cd05073   83 ITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCkIADFGLARViEDNEY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGRRDDKLRIQngWLchlAPEIIRQLSpdteedklpFSKHSDVFALGTIWYEL--HAREwPFKTQPAEAIIWQMGTGMKP 520
Cdd:cd05073  163 TAREGAKFPIK--WT---APEAINFGS---------FTIKSDVWSFGILLMEIvtYGRI-PYPGMSNPEVIRALERGYRM 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568937340 521 NLSQiGMGKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05073  228 PRPE-NCPEELYNIMMRCWKNRPEERPTFEYIQSVLD 263
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
287-557 2.63e-17

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: 82.43  E-value: 2.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG--EVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd05071    4 WEIPRESLRLEVKLGQGCFGEVWMGTWNGttRVAIKTL---KPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFS-ISGVLQ 442
Cdd:cd05071   81 VTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVgENLVCKVADFGLARlIEDNEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGRRDDKLRIQngWLchlAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGMK-P 520
Cdd:cd05071  161 TARQGAKFPIK--WT---APEAALYGR---------FTIKSDVWSFGILLTELTTKgRVPYPGMVNREVLDQVERGYRmP 226
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568937340 521 NLSQIGmgKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05071  227 CPPECP--ESLHDLMCQCWRKEPEERPTFEYLQAFLE 261
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
287-553 2.79e-17

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: 82.38  E-value: 2.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIpfeqleIGELiGKGRFGQVYHGRwHGEVAI----RLIDIErdNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPH 362
Cdd:cd06643    7 WEI------VGEL-GDGAFGKVYKAQ-NKETGIlaaaKVIDTK--SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 LAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-FYDNGKVVITDFGLfSISGVL 441
Cdd:cd06643   77 LWILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNIlFTLDGDIKLADFGV-SAKNTR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAGRRDDKLriqnGWLCHLAPEIIRqlsPDTEEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPN 521
Cdd:cd06643  156 TLQRRDSFI----GTPYWMAPEVVM---CETSKDR-PYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPT 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568937340 522 LSQIGM-GKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06643  228 LAQPSRwSPEFKDFLRKCLEKNVDARWTTSQLL 260
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
292-557 2.79e-17

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: 82.08  E-value: 2.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHG------EVAIRLIDIERDNEDQLKaFKREVMAYRQTRHENVVLFMGACMSPPhLAI 365
Cdd:cd05056    6 EDITLGRCIGEGQFGDVYQGVYMSpenekiAVAVKTCKNCTSPSVREK-FLQEAYIMRQFDHPHIVKLIGVITENP-VWI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL---FSISGVL 441
Cdd:cd05056   84 VMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVsSPDCVKLGDFGLsryMEDESYY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAGRrdDKLRIQngWLchlAPEII--RQlspdteedklpFSKHSDVFALGT-IWYELHAREWPFKTQPAEAIIWQMGTGM 518
Cdd:cd05056  164 KASK--GKLPIK--WM---APESInfRR-----------FTSASDVWMFGVcMWEILMLGVKPFQGVKNNDVIGRIENGE 225
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 519 KPNLSQiGMGKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05056  226 RLPMPP-NCPPTLYSLMTKCWAYDPSKRPRFTELKAQLS 263
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
292-556 2.82e-17

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: 81.92  E-value: 2.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHG--EVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd05112    4 SELTFVQEIGSGQFGLVHLGYWLNkdKVAIKTI---REGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSIsgVLqagrrDD 448
Cdd:cd05112   81 MEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVkVSDFGMTRF--VL-----DD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 KLRIQNG------WlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTG---M 518
Cdd:cd05112  154 QYTSSTGtkfpvkW---SSPEVFSFSR---------YSSKSDVWSFGVLMWEVFSEgKIPYENRSNSEVVEDINAGfrlY 221
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568937340 519 KPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd05112  222 KPRLAS----THVYEIMNHCWKERPEDRPSFSLLLRQL 255
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
299-557 2.85e-17

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: 82.08  E-value: 2.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHG---------RWHGEVAIRliDIERDNEDQLKA-FKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd05044    2 FLGSGAFGEVFEGtakdilgdgSGETKVAVK--TLRKGATDQEKAeFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAKIV------LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-----YDNGKVVITDFGLfsi 437
Cdd:cd05044   80 LMEGGDLLSYLRAARPTaftpplLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLvsskdYRERVVKIGDFGL--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 438 sgvlqagRRD----DKLRIQNGwlcHLAPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHArewpFKTQPAEA---- 509
Cdd:cd05044  157 -------ARDiyknDYYRKEGE---GLLP--VRWMAPESLVDGV-FTTQSDVWAFGVLMWEILT----LGQQPYPArnnl 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568937340 510 -IIWQMGTGMKpnLSQIGM-GKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05044  220 eVLHFVRAGGR--LDQPDNcPDDLYELMLRCWSTDPEERPSFARILEQLQ 267
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
287-559 3.31e-17

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: 81.70  E-value: 3.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRW---HGEVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHL 363
Cdd:cd05052    1 WEIERTDITMKHKLGGGQYGEVYEGVWkkyNLTVAVKTL---KEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITS-LCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSIsgvl 441
Cdd:cd05052   78 YIITEfMPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVgENHLVKVADFGLSRL---- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 qagRRDDKLRIQNG------WlchLAPEiirQLSPDTeedklpFSKHSDVFALGTiwyelharewpfktqpaeaIIWQMG 515
Cdd:cd05052  154 ---MTGDTYTAHAGakfpikW---TAPE---SLAYNK------FSIKSDVWAFGV-------------------LLWEIA 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 516 T-GMKP----NLSQI--------------GMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05052  200 TyGMSPypgiDLSQVyellekgyrmerpeGCPPKVYELMRACWQWNPSDRPSFAEIHQALETM 262
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
293-553 3.73e-17

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: 81.28  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSdnqVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKivldvNKTRQIAQE--------IVKGMGYLHAKGILHKDLKSKNVF-YDNGKVVITDFGlfsISGV 440
Cdd:cd08530   81 APFGDLSKLISKRK-----KKRRLFPEDdiwrifiqMLRGLKALHDQKILHRDLKSANILlSAGDLVKIGDLG---ISKV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 LQAGRrddkLRIQNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKP 520
Cdd:cd08530  153 LKKNL----AKTQIGTPLYAAPEVWK---------GRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFP 219
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568937340 521 NLSQIgMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd08530  220 PIPPV-YSQDLQQIIRSLLQVNPKKRPSCDKLL 251
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
298-498 4.64e-17

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: 81.72  E-value: 4.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE-VAIRlIDIERDNedqlKAFKREVMAYrQT---RHENVVLFMGA----CMSPPHLAIITSL 369
Cdd:cd14143    1 ESIGKGRFGEVWRGRWRGEdVAVK-IFSSREE----RSWFREAEIY-QTvmlRHENILGFIAAdnkdNGTWTQLWLVSDY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRdaKIVLDVNKTRQIAQEIVKGMGYLHAK--------GILHKDLKSKNVFY-DNGKVVITDFGLfsisgv 440
Cdd:cd14143   75 HEHGSLFDYLN--RYTVTVEGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVkKNGTCCIADLGL------ 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 441 lqAGRRD---DKLRIQN----GWLCHLAPEIIRqlspDTEEDKLPFS-KHSDVFALGTIWYELHAR 498
Cdd:cd14143  147 --AVRHDsatDTIDIAPnhrvGTKRYMAPEVLD----DTINMKHFESfKRADIYALGLVFWEIARR 206
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
286-559 4.67e-17

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: 82.15  E-value: 4.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLI-DIERDNEDqlKAFKREV-MAYRQTRHENVVLFMG 355
Cdd:cd05054    1 KWEFPRDRLKLGKPLGRGAFGKVIQASAFGidksatcrTVAVKMLkEGATASEH--KALMTELkILIHIGHHLNVVNLLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 356 ACMSPPH-LAIITSLCK----------GRTLYSVVRD--AKIVLDVNKTRQIAQE-------------IVKGMGYLHAKG 409
Cdd:cd05054   79 ACTKPGGpLMVIVEFCKfgnlsnylrsKREEFVPYRDkgARDVEEEEDDDELYKEpltledlicysfqVARGMEFLASRK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 410 ILHKDLKSKNVFYDNGKVV-ITDFGLfsisgvlqagRRD-----DKLRIQNGWLchlaPeiIRQLSPDTEEDKLpFSKHS 483
Cdd:cd05054  159 CIHRDLAARNILLSENNVVkICDFGL----------ARDiykdpDYVRKGDARL----P--LKWMAPESIFDKV-YTTQS 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 484 DVFALGTIWYE---LHAREWPfKTQPAEAIIWQMGTGM---KPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05054  222 DVWSFGVLLWEifsLGASPYP-GVQMDEEFCRRLKEGTrmrAPEYTT----PEIYQIMLDCWHGEPKERPTFSELVEKLG 296

                 ..
gi 568937340 558 KL 559
Cdd:cd05054  297 DL 298
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
300-502 4.83e-17

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: 80.77  E-value: 4.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQLKafkREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd14006    1 LGRGRFGVVKRCIEKAtgrEFAAKFIPKRDKKKEAVL---REISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG---KVVITDFGLfsisgvLQAGRRDDKLRIQ 453
Cdd:cd14006   78 DRLAE-RGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRpspQIKIIDFGL------ARKLNPGEELKEI 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568937340 454 NGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14006  151 FGTPEFVAPEIVNG---------EPVSLATDMWSIGVLTYVLLSGLSPF 190
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
287-557 5.80e-17

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: 81.27  E-value: 5.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG--EVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd05070    4 WEIPRESLQLIKRLGNGQFGEVWMGTWNGntKVAIKTL---KPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFS-ISGVLQ 442
Cdd:cd05070   81 VTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICkIADFGLARlIEDNEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGRRDDKLRIQngWLchlAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGMKPN 521
Cdd:cd05070  161 TARQGAKFPIK--WT---APEAALYGR---------FTIKSDVWSFGILLTELVTKgRVPYPGMNNREVLEQVERGYRMP 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568937340 522 LSQiGMGKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05070  227 CPQ-DCPISLHELMIHCWKKDPEERPTFEYLQGFLE 261
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
290-553 6.19e-17

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: 81.69  E-value: 6.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVYHGRW--HGEVA-IRLIDIERDNEDQLKafkREV-MAYRQTRHENVVLFMGACM--SPP-- 361
Cdd:cd06637    4 PAGIFELVELVGNGTYGQVYKGRHvkTGQLAaIKVMDVTGDEEEEIK---QEInMLKKYSHHRNIATYYGAFIkkNPPgm 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 --HLAIITSLCKGRTLYSVVRDAK-IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlfsI 437
Cdd:cd06637   81 ddQLWLVMEFCGAGSVTDLIKNTKgNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLtENAEVKLVDFG---V 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 438 SGVLQ--AGRRDDKLriqnGWLCHLAPEIIR-QLSPDTEEDklpfsKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQM 514
Cdd:cd06637  158 SAQLDrtVGRRNTFI----GTPYWMAPEVIAcDENPDATYD-----FKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLI 228
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 515 GTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06637  229 PRNPAPRLKSKKWSKKFQSFIESCLVKNHSQRPSTEQLM 267
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
295-495 7.98e-17

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: 80.49  E-value: 7.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY--HGRWHGE-VAIRLIDIE--RDNEDQLKafkREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14083    6 EFKEVLGTGAFSEVVlaEDKATGKlVAIKCIDKKalKGKEDSLE---NEIAVLRKIKHPNIVQLLDIYESKSHLYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSvvrdaKIVLDVNKTRQIAQEIVK----GMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFSI--SG 439
Cdd:cd14083   83 VTGGELFD-----RIVEKGSYTEKDASHLIRqvleAVDYLHSLGIVHRDLKPENLLYyspdEDSKIMISDFGLSKMedSG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 440 VLQAGrrddklriqngwlC----HLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYEL 495
Cdd:cd14083  158 VMSTA-------------CgtpgYVAPEVLAQ---------KPYGKAVDCWSIGVISYIL 195
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
300-557 8.36e-17

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: 80.62  E-value: 8.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRW--HGEVAIRLIdIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYS 377
Cdd:cd14664    1 IGRGGAGTVYKGVMpnGTLVAVKRL-KGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 VVR---DAKIVLDVNKTRQIAQEIVKGMGYLH---AKGILHKDLKSKNVFYDNG-KVVITDFGLfsisgvlqAGRRDDK- 449
Cdd:cd14664   80 LLHsrpESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEfEAHVADFGL--------AKLMDDKd 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 ---LRIQNGWLCHLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPFKTQPAEA----IIWQMGT------ 516
Cdd:cd14664  152 shvMSSVAGSYGYIAPEYAYTGKVS---------EKSDVYSYGVVLLELITGKRPFDEAFLDDgvdiVDWVRGLleekkv 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340 517 --GMKPNLSQIGMGKEISDIL---LFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd14664  223 eaLVDPDLQGVYKLEEVEQVFqvaLLCTQSSPMERPTMREVVRMLE 268
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
287-557 9.35e-17

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: 80.89  E-value: 9.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG--EVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd05069    7 WEIPRESLRLDVKLGQGCFGEVWMGTWNGttKVAIKTL---KPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFS-ISGVLQ 442
Cdd:cd05069   84 VTEFMGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVgDNLVCKIADFGLARlIEDNEY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGRRDDKLRIQngWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGMKPN 521
Cdd:cd05069  164 TARQGAKFPIK--W---TAPEAALYGR---------FTIKSDVWSFGILLTELVTKgRVPYPGMVNREVLEQVERGYRMP 229
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568937340 522 LSQiGMGKEISDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05069  230 CPQ-GCPESLHELMKLCWKKDPDERPTFEYIQSFLE 264
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
280-505 1.04e-16

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: 80.69  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 280 TSIFLQEwdipFEQLEIgelIGKGRFGQVYHGRW---HGEVAIRLIDIErDNEDQLKAFKREVMAYRQTRHENVVLFMGA 356
Cdd:cd14048    1 TSRFLTD----FEPIQC---LGRGGFGVVFEAKNkvdDCNYAVKRIRLP-NNELAREKVLREVRALAKLDHPGIVRYFNA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 357 CMSPP-----------HLAIITSLCKGRTLYSVVRDAKIVL--DVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD 423
Cdd:cd14048   73 WLERPpegwqekmdevYLYIQMQLCRKENLKDWMNRRCTMEsrELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 424 -NGKVVITDFGLFSISG-------VLQAGRRDDKLRIQNGWLCHLAPEiirQLSPDTEEDKLpfskhsDVFALGTIWYEL 495
Cdd:cd14048  153 lDDVVKVGDFGLVTAMDqgepeqtVLTPMPAYAKHTGQVGTRLYMSPE---QIHGNQYSEKV------DIFALGLILFEL 223
                        250
                 ....*....|
gi 568937340 496 harEWPFKTQ 505
Cdd:cd14048  224 ---IYSFSTQ 230
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
300-499 1.07e-16

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: 79.97  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYR----QTRHENVVLFMGACMSPP--HLAIITSLCkGR 373
Cdd:cd05118    7 IGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKhlndVEGHPNIVKLLDVFEHRGgnHLCLVFELM-GM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF--YDNGKVVITDFGLfsisgVLQAGRRDDKLR 451
Cdd:cd05118   86 NLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILinLELGQLKLADFGL-----ARSFTSPPYTPY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 452 IQNGWLchLAPEIIRQLSpdteedklPFSKHSDVFALGTIWYELHARE 499
Cdd:cd05118  161 VATRWY--RAPEVLLGAK--------PYGSSIDIWSLGCILAELLTGR 198
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
293-561 1.28e-16

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: 80.44  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHGE-----VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMS-------P 360
Cdd:cd05075    1 KLALGKTLGEGEFGSVMEGQLNQDdsvlkVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQntesegyP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 361 PHLAIITSLCKGRT----LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKN-VFYDNGKVVITDFGLf 435
Cdd:cd05075   81 SPVVILPFMKHGDLhsflLYSRLGDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNcMLNENMNVCVADFGL- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 436 siSGVLQAGRRDDKLRIqngwlchlAPEIIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQM 514
Cdd:cd05075  160 --SKKIYNGDYYRQGRI--------SKMPVKWIAIESLADRV-YTTKSDVWSFGVTMWEIATRgQTPYPGVENSEIYDYL 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 515 GTGMKpnLSQ-IGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKLPK 561
Cdd:cd05075  229 RQGNR--LKQpPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILK 274
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
306-559 1.38e-16

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: 79.84  E-value: 1.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 306 GQVYHGRWHG-EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDA-K 383
Cdd:cd14057    9 GELWKGRWQGnDIVAKILKVRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHEGtG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 384 IVLDVNKTRQIAQEIVKGMGYLHA--KGILHKDLKSKNVFYDNGKVVITDFGlfsisgvlqagrrDDKLRIQN------- 454
Cdd:cd14057   89 VVVDQSQAVKFALDIARGMAFLHTlePLIPRHHLNSKHVMIDEDMTARINMA-------------DVKFSFQEpgkmynp 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 455 GWlchLAPEIIRQLSPDTEedklpfSKHSDVFALGTIWYELHAREWPFktqpaeAIIWQMGTGMKPNLSQI------GMG 528
Cdd:cd14057  156 AW---MAPEALQKKPEDIN------RRSADMWSFAILLWELVTREVPF------ADLSNMEIGMKIALEGLrvtippGIS 220
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 529 KEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14057  221 PHMCKLMKICMNEDPGKRPKFDMIVPILEKM 251
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
295-502 1.79e-16

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: 79.93  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHGE---VAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14169    6 ELKEKLGEGAFSEVVLAQERGSqrlVALKCIP-KKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFSISGvlqagrrD 447
Cdd:cd14169   85 GGELFDRIIERGSYTEKDASQLIGQ-VLQAVKYLHQLGIVHRDLKPENLLYatpfEDSKIMISDFGLSKIEA-------Q 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 448 DKLRIQNGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14169  157 GMLSTACGTPGYVAPELLEQ---------KPYGKAVDVWAIGVISYILLCGYPPF 202
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
289-506 1.82e-16

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: 80.11  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 289 IPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSP 360
Cdd:cd05048    2 IPLSAVRFLEELGEGAFGKVYKGELLGpsseesaiSVAIKTLK-ENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 361 PHLAIITSLCKGRTLY---------------SVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-YDN 424
Cdd:cd05048   81 QPQCMLFEYMAHGDLHeflvrhsphsdvgvsSDDDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLvGDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 425 GKVVITDFGLFsisgvlqagrRD----DKLRIQngwlcHLAPEIIRQLSPdteEDKL--PFSKHSDVFALGTIWYELHAr 498
Cdd:cd05048  161 LTVKISDFGLS----------RDiyssDYYRVQ-----SKSLLPVRWMPP---EAILygKFTTESDVWSFGVVLWEIFS- 221

                 ....*...
gi 568937340 499 ewpFKTQP 506
Cdd:cd05048  222 ---YGLQP 226
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
300-503 2.03e-16

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: 79.26  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFG--QVYHGRWHGE-VAIRLIDI-ERDNEDqlkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTL 375
Cdd:cd14665    8 IGSGNFGvaRLMRDKQTKElVAVKYIERgEKIDEN----VQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGGEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 376 YSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG---KVVITDFGlFSISGVLQAGRRDDKlri 452
Cdd:cd14665   84 FERICNAGRFSE-DEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpapRLKICDFG-YSKSSVLHSQPKSTV--- 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568937340 453 qnGWLCHLAPEIIRQLSPDteedklpfSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd14665  159 --GTPAYIAPEVLLKKEYD--------GKIADVWSCGVTLYVMLVGAYPFE 199
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
292-502 2.28e-16

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: 79.30  E-value: 2.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd14167    3 DIYDFREVLGTGAFSEVVlaeEKRTQKLVAIKCIA-KKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAKIVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFSISGvlqag 444
Cdd:cd14167   82 LVSGGELFDRIVEKGFYTERDASKLIFQ-ILDAVKYLHDMGIVHRDLKPENLLYysldEDSKIMISDFGLSKIEG----- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 445 rRDDKLRIQNGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14167  156 -SGSVMSTACGTPGYVAPEVLAQ---------KPYSKAVDCWSIGVIAYILLCGYPPF 203
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
298-549 2.53e-16

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: 79.08  E-value: 2.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPphLAIITSLCKGRT 374
Cdd:cd14025    2 EKVGSGGFGQVYkvrHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVrdAKIVLDVNKTRQIAQEIVKGMGYLH--AKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGvlQAGRRDDKLR 451
Cdd:cd14025   80 LEKLL--ASEPLPWELRFRIIHETAVGMNFLHcmKPPLLHLDLKPANILLDaHYHVKISDFGLAKWNG--LSHSHDLSRD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 452 IQNGWLCHLAPEIIRqlspdtEEDKLPFSKHsDVFALGTIWYELHAREWPFKTQ-PAEAIIWQMGTGMKPNLSQIGMGK- 529
Cdd:cd14025  156 GLRGTIAYLPPERFK------EKNRCPDTKH-DVYSFAIVIWGILTQKKPFAGEnNILHIMVKVVKGHRPSLSPIPRQRp 228
                        250       260
                 ....*....|....*....|....
gi 568937340 530 ----EISDILLFCWAFEQEERPTF 549
Cdd:cd14025  229 secqQMICLMKRCWDQDPRKRPTF 252
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
296-553 2.57e-16

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: 79.30  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVY------HGRwhgEVAIRLIDIERDNED---QLKAFKREVMAYRQTRHENVVLFMGaCMSPPH---L 363
Cdd:cd06653    6 LGKLLGRGAFGEVYlcydadTGR---ELAVKQVPFDPDSQEtskEVNALECEIQLLKNLRHDRIVQYYG-CLRDPEekkL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFS-ISGVL 441
Cdd:cd06653   82 SIFVEYMPGGSVKDQLK-AYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSaGNVKLGDFGASKrIQTIC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAGRRDDKLRIQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTG-MKP 520
Cdd:cd06653  161 MSGTGIKSVTGTPYW---MSPEVISGEG---------YGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQpTKP 228
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568937340 521 NLSQiGMGKEISDIL--LFCWafeQEERPTFTKLM 553
Cdd:cd06653  229 QLPD-GVSDACRDFLrqIFVE---EKRRPTAEFLL 259
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
296-555 3.25e-16

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: 78.93  E-value: 3.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELiGKGRFGQVY---HgRWHGEV-AIRLIDIERDNEDQlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd06605    6 LGEL-GEGNGGVVSkvrH-RPSGQImAVKVIRLEIDEALQ-KQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAK-GILHKDLKSKNVFYDN-GKVVITDFGlfsISGVLQagrrDDK 449
Cdd:cd06605   83 GGSLDKILKEVG-RIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSrGQVKLCDFG---VSGQLV----DSL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIQNGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFK---TQPAEAIIWQMG---TGMKPNLS 523
Cdd:cd06605  155 AKTFVGTRSYMAPERISGGK---------YTVKSDIWSLGLSLVELATGRFPYPppnAKPSMMIFELLSyivDEPPPLLP 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568937340 524 QIGMGKEISDILLFCWAFEQEERPTFTKLMDM 555
Cdd:cd06605  226 SGKFSPDFQDFVSQCLQKDPTERPSYKELMEH 257
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
296-528 4.91e-16

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: 78.32  E-value: 4.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHGrWH---GE-VAIRLIDIERDNEDQ--LKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14070    6 IGRKLGEGSFAKVREG-LHavtGEkVAIKVIDKKKAKKDSyvTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGVLQAGrrdD 448
Cdd:cd14070   85 CPGGNLMHRIYDKK-RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDeNDNIKLIDFGLSNCAGILGYS---D 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 KLRIQNGWLCHLAPEII--RQLSPDTeedklpfskhsDVFALGTIWYELHAREWPFKTQP--AEAIIWQMGTG-MKPNLS 523
Cdd:cd14070  161 PFSTQCGSPAYAAPELLarKKYGPKV-----------DVWSIGVNMYAMLTGTLPFTVEPfsLRALHQKMVDKeMNPLPT 229

                 ....*
gi 568937340 524 QIGMG 528
Cdd:cd14070  230 DLSPG 234
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
299-553 5.34e-16

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: 78.24  E-value: 5.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTL 375
Cdd:cd08220    7 VVGRGAYGTVYLCRrkdDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 376 YSVVRDAK-IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV--ITDFGlfsISGVLQAgrrDDKLRI 452
Cdd:cd08220   87 FEYIQQRKgSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvkIGDFG---ISKILSS---KSKAYT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 453 QNGWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMgtgMKPNLSQIG--MGKE 530
Cdd:cd08220  161 VVGTPCYISPELC---------EGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKI---MRGTFAPISdrYSEE 228
                        250       260
                 ....*....|....*....|...
gi 568937340 531 ISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd08220  229 LRHLILSMLHLDPNKRPTLSEIM 251
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
291-502 5.61e-16

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: 78.47  E-value: 5.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIGELIGKGRFGQV---YHGRWHGEVAIRLIDI--ERDNEDQLKAFK----REVMAYRQTR-HENVVLFMGACMSP 360
Cdd:cd14181    9 YQKYDPKEVIGRGVSSVVrrcVHRHTGQEFAVKIIEVtaERLSPEQLEEVRsstlKEIHILRQVSgHPSIITLIDSYESS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 361 PHLAIITSLCKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsiSG 439
Cdd:cd14181   89 TFIFLVFDLMRRGELFDYLTE-KVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLdDQLHIKLSDFGF---SC 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 440 VLQAGrrdDKLRIQNGWLCHLAPEIIRQLSPDTEEDklpFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14181  165 HLEPG---EKLRELCGTPGYLAPEILKCSMDETHPG---YGKEVDLWACGVILFTLLAGSPPF 221
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
298-553 6.21e-16

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: 78.17  E-value: 6.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHG---RWHGEVAIRLIDIErDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd06640   10 ERIGKGSFGEVFKGidnRTQQVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsisgvlqAGRRDDKLRIQ 453
Cdd:cd06640   89 ALDLLRAGP--FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLsEQGDVKLADFGV--------AGQLTDTQIKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 NGWLCH---LAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQiGMGKE 530
Cdd:cd06640  159 NTFVGTpfwMAPEVIQQSAYDSK---------ADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVG-DFSKP 228
                        250       260
                 ....*....|....*....|...
gi 568937340 531 ISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06640  229 FKEFIDACLNKDPSFRPTAKELL 251
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
298-565 7.73e-16

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: 78.53  E-value: 7.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE-------VAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPhLAIITSLC 370
Cdd:cd05108   13 KVLGSGAFGTVYKGLWIPEgekvkipVAIKELR-EATSPKANKEILDEAYVMASVDNPHVCRLLGICLTST-VQLITQLM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGK-VVITDFGLFSISGVLQAGRRDDK 449
Cdd:cd05108   91 PFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQhVKITDFGLAKLLGAEEKEYHAEG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALG-TIWYELHAREWPFKTQPAEAI--IWQMGTGM-KPNLSQI 525
Cdd:cd05108  171 GKVPIKW---MALESILHRI---------YTHQSDVWSYGvTVWELMTFGSKPYDGIPASEIssILEKGERLpQPPICTI 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568937340 526 gmgkEISDILLFCWAFEQEERPTFTKLMDMLEKLPKRNRR 565
Cdd:cd05108  239 ----DVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQR 274
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
287-558 7.98e-16

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: 78.09  E-value: 7.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWH----GE----VAIRLIDIERDNEDQLKaFKREVMAYRQTRHENVVLFMGAC- 357
Cdd:cd05061    1 WEVSREKITLLRELGQGSFGMVYEGNARdiikGEaetrVAVKTVNESASLRERIE-FLNEASVMKGFTCHHVVRLLGVVs 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 358 MSPPHLAIITSLCKGrTLYSVVRDAKIVLDVNKTR---------QIAQEIVKGMGYLHAKGILHKDLKSKN-VFYDNGKV 427
Cdd:cd05061   80 KGQPTLVVMELMAHG-DLKSYLRSLRPEAENNPGRppptlqemiQMAAEIADGMAYLNAKKFVHRDLAARNcMVAHDFTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 428 VITDFGLFSISGVLQAGRRDDKlriqngwlcHLAPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHA-REWPFKTQP 506
Cdd:cd05061  159 KIGDFGMTRDIYETDYYRKGGK---------GLLP--VRWMAPESLKDGV-FTTSSDMWSFGVVLWEITSlAEQPYQGLS 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 507 AEAII-WQMGTGM--KPNlsqiGMGKEISDILLFCWAFEQEERPTFTKLMDMLEK 558
Cdd:cd05061  227 NEQVLkFVMDGGYldQPD----NCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKD 277
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
295-495 1.02e-15

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: 77.13  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY---HGRWHGEVAIRLID----IERDNEDQLKafkREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14007    3 EIGKPLGKGKFGNVYlarEKKSGFIVALKVISksqlQKSGLEHQLR---REIEIQSHLRHPNILRLYGYFEDKKRIYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGRR 446
Cdd:cd14007   80 EYAPNGELYKELKKQK-RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGsNGELKLADFGW---SVHAPSNRR 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568937340 447 ddklRIQNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYEL 495
Cdd:cd14007  156 ----KTFCGTLDYLPPEMVE---------GKEYDYKVDIWSLGVLCYEL 191
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
290-520 1.07e-15

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: 77.38  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVYHGR--WHGEVA-IRLIDIERDneDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:cd06646    7 PQHDYELIQRVGSGTYGDVYKARnlHTGELAaVKIIKLEPG--DDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWIC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLysvvRDAKIVLDVNKTRQIA---QEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSISGVLQ 442
Cdd:cd06646   85 MEYCGGGSL----QDIYHVTGPLSELQIAyvcRETLQGLAYLHSKGKMHRDIKGANILLtDNGDVKLADFGVAAKITATI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 443 AGRRDDKlriqnGWLCHLAPEIIrqlspdTEEDKLPFSKHSDVFALGTIWYELHAREWP-FKTQPAEAIIWQMGTGMKP 520
Cdd:cd06646  161 AKRKSFI-----GTPYWMAPEVA------AVEKNGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMSKSNFQP 228
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
294-559 1.18e-15

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: 77.67  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHGRWHGE------VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMS------PP 361
Cdd:cd14204    9 LSLGKVLGEGEFGSVMEGELQQPdgtnhkVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEvgsqriPK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCKGRT----LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKN-VFYDNGKVVITDFGLfs 436
Cdd:cd14204   89 PMVILPFMKYGDLhsflLRSRLGSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNcMLRDDMTVCVADFGL-- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 437 iSGVLQAGRRDDKLRIqngwlchlAPEIIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHAREW-PFKTQPAEAIIWQMG 515
Cdd:cd14204  167 -SKKIYSGDYYRQGRI--------AKMPVKWIAVESLADRV-YTVKSDVWAFGVTMWEIATRGMtPYPGVQNHEIYDYLL 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568937340 516 TGMKPNLSQIGMgKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14204  237 HGHRLKQPEDCL-DELYDIMYSCWRSDPTDRPTFTQLRENLEKL 279
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
284-559 1.19e-15

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: 77.65  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 284 LQEWDIPFEQLEIGELIGKGRFGQVYHGRWHGE------VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGAC 357
Cdd:cd05074    1 LKDVLIQEQQFTLGRMLGKGEFGSVREAQLKSEdgsfqkVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 358 MS-------PPHLAIITSLCKGRT----LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NG 425
Cdd:cd05074   81 LRsrakgrlPIPMVILPFMKHGDLhtflLMSRIGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNeNM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 426 KVVITDFGLfsiSGVLQAGrrdDKLRiqNGWLCHLApeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHAR-EWPFKT 504
Cdd:cd05074  161 TVCVADFGL---SKKIYSG---DYYR--QGCASKLP---VKWLALESLADNV-YTTHSDVWAFGVTMWEIMTRgQTPYAG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 505 QPAEAIIWQMGTGMKpnLSQ-IGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05074  229 VENSEIYNYLIKGNR--LKQpPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
298-556 1.78e-15

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: 77.11  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGEVAIR---LIDIERDN--EDQLKAFKREVMAYRQTRHENVVLFMGACM---SPPHLAIitSL 369
Cdd:cd05043   12 DLLQEGTFGRIFHGILRDEKGKEeevLVKTVKDHasEIQVTMLLQESSLLYGLSHQNLLPILHVCIedgEKPMVLY--PY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDVN----KTRQI---AQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGLfsisgvl 441
Cdd:cd05043   90 MNWGNLKLFLQQCRLSEANNpqalSTQQLvhmALQIACGMSYLHRRGVIHKDIAARNCVIDDElQVKITDNAL------- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 qagRRDdklRIQNGWLCHLAPE--IIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHArewpFKTQPAEAI-IWQMGTGM 518
Cdd:cd05043  163 ---SRD---LFPMDYHCLGDNEnrPIKWMSLESLVNKE-YSSASDVWSFGVLLWELMT----LGQTPYVEIdPFEMAAYL 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568937340 519 KP--NLSQ-IGMGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd05043  232 KDgyRLAQpINCPDELFAVMACCWALDPEERPSFQQLVQCL 272
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
290-569 1.92e-15

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: 76.62  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVYHGR--WHGEVA-IRLIDIErDNEDqLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:cd06645    9 PQEDFELIQRIGSGTYGDVYKARnvNTGELAaIKVIKLE-PGED-FAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWIC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlfsISGVLQAGR 445
Cdd:cd06645   87 MEFCGGGSLQDIYH-VTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLtDNGHVKLADFG---VSAQITATI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 RDDKLRIQNGWLchLAPEIIrqlspdTEEDKLPFSKHSDVFALGTIWYELHAREWP-FKTQPAEAIIWQMGTGMKPnlsq 524
Cdd:cd06645  163 AKRKSFIGTPYW--MAPEVA------AVERKGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMTKSNFQP---- 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568937340 525 igmgKEISDILLFCWAFEQEERPTFTKlmdMLEKLPKRNRRLSHP 569
Cdd:cd06645  231 ----PKLKDKMKWSNSFHHFVKMALTK---NPKKRPTAEKLLQHP 268
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
300-562 2.08e-15

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: 76.88  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVY---HGRWHGEVAIRLIDI-----ERDNEDQLKafkrEVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14026    5 LSRGAFGTVSrarHADWRVTVAIKCLKLdspvgDSERNCLLK----EAEILHKARFSYILPILGICNEPEFLGIVTEYMT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVLDVN---KTRqIAQEIVKGMGYLH--AKGILHKDLKSKNVFYDNG-KVVITDFGLFSISGVLQAGR 445
Cdd:cd14026   81 NGSLNELLHEKDIYPDVAwplRLR-ILYEIALGVNYLHnmSPPLLHHDLKTQNILLDGEfHVKIADFGLSKWRQLSISQS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 RDDKLRIQNGWLCHLAPEiirQLSPDteeDKLPFSKHSDVFALGTIWYELHAREWPFK--TQPAEaIIWQMGTGMKPNLS 523
Cdd:cd14026  160 RSSKSAPEGGTIIYMPPE---EYEPS---QKRRASVKHDIYSYAIIMWEVLSRKIPFEevTNPLQ-IMYSVSQGHRPDTG 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568937340 524 QIGMGKEIS------DILLFCWAFEQEERPTFTKLMDMLEKLPKR 562
Cdd:cd14026  233 EDSLPVDIPhratliNLIESGWAQNPDERPSFLKCLIELEPVLRT 277
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
294-554 2.12e-15

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 76.62  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHG---RWHGEVAIRLI-----DIERDNEDQLKAFKREVMAYRQ-TRHENVVLFMGACMSPPHLA 364
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAvdlRTGRKYAIKCLyksgpNSKDGNDFQKLPQLREIDLHRRvSRHPNIITLHDVFETEVAIY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKIVldVNKT---RQIAQEIVKGMGYLHAKGILHKDLKSKNVF--YDNGKVVITDFGLfsisg 439
Cdd:cd13993   82 IVLEYCPNGDLFEAITENRIY--VGKTeliKNVFLQLIDAVKHCHSLGIYHRDIKPENILlsQDEGTVKLCDFGL----- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 440 vlqAGRRDDKLRIQNGWLCHLAPEIIRQlspDTEEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMK 519
Cdd:cd13993  155 ---ATTEKISMDFGVGSEFYMAPECFDE---VGRSLKGYPCAAGDIWSLGIILLNLTFGRNPWKIASESDPIFYDYYLNS 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568937340 520 PNLSQI--GMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd13993  229 PNLFDVilPMSDDFYNLLRQIFTVNPNNRILLPELQL 265
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
300-503 2.36e-15

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: 76.44  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR---WHGEVAI------RLIDI---ERDN---EDQLKAFKREVMAYRQTRHENVV-LFmgACMSPP-- 361
Cdd:cd14008    1 LGRGSFGKVKLALdteTGQLYAIkifnksRLRKRregKNDRgkiKNALDDVRREIAIMKKLDHPNIVrLY--EVIDDPes 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 -HLAIITSLCKGRTLYSVVRDAK-IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlfsIS 438
Cdd:cd14008   79 dKLYLVLEYCEGGPVMELDSGDRvPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTaDGTVKISDFG---VS 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 439 GVLQAGrrDDKLRIQNGWLCHLAPEIIRqlspdteEDKLPFS-KHSDVFALG-TIWYELHAReWPFK 503
Cdd:cd14008  156 EMFEDG--NDTLQKTAGTPAFLAPELCD-------GDSKTYSgKAADIWALGvTLYCLVFGR-LPFN 212
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
299-498 2.54e-15

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: 76.75  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRWHGE-VAIRLIDIERDnedqlKAFKREVMAYrQT---RHENVVLFMGACM----SPPHLAIITSLC 370
Cdd:cd14144    2 SVGKGRYGEVWKGKWRGEkVAVKIFFTTEE-----ASWFRETEIY-QTvlmRHENILGFIAADIkgtgSWTQLYLITDYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAK--------GILHKDLKSKNVFY-DNGKVVITDFGLfSISGVL 441
Cdd:cd14144   76 ENGSLYDFLRGN--TLDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVkKNGTCCIADLGL-AVKFIS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 442 QAGRRDDKLRIQNGWLCHLAPEIirqLSPDTEEDKLPFSKHSDVFALGTIWYELHAR 498
Cdd:cd14144  153 ETNEVDLPPNTRVGTKRYMAPEV---LDESLNRNHFDAYKMADMYSFGLVLWEIARR 206
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
289-559 3.93e-15

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: 75.87  E-value: 3.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 289 IPFEQLEIGELIGKGRFGQVYHGRWH--GE----VAIRLI-----DIERDNedqlkaFKREVMAYRQTRHENVVLFMGAC 357
Cdd:cd05033    1 IDASYVTIEKVIGGGEFGEVCSGSLKlpGKkeidVAIKTLksgysDKQRLD------FLTEASIMGQFDHPNVIRLEGVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 358 MSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFS 436
Cdd:cd05033   75 TKSRPVMIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCkVSDFGLSR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 437 ISGVLQAGRRDDKLRIQNGWLchlAPEII--RQlspdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQ 513
Cdd:cd05033  155 RLEDSEATYTTKGGKIPIRWT---APEAIayRK-----------FTSASDVWSFGIVMWEVMSYgERPYWDMSNQDVIKA 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 514 MGTGMK-------PNLsqigmgkeISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05033  221 VEDGYRlpppmdcPSA--------LYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
343-554 4.24e-15

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


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 75.52  E-value: 4.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 343 RQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY 422
Cdd:cd14043   51 RELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDMKLDWMFKSSLLLDLIKGMRYLHHRGIVHGRLKSRNCVV 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 423 DnGKVV--ITDFGLFSISG---VLQAGRRDDKLRiqngWlchLAPEIIRQlsPDTEEDKlpfSKHSDVFALGTIWYELHA 497
Cdd:cd14043  131 D-GRFVlkITDYGYNEILEaqnLPLPEPAPEELL----W---TAPELLRD--PRLERRG---TFPGDVFSFAIIMQEVIV 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 498 REWPFKT--QPAEAIIWQMGTgmKPNLSQ--IGMGK---EISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd14043  198 RGAPYCMlgLSPEEIIEKVRS--PPPLCRpsVSMDQaplECIQLMKQCWSEAPERRPTFDQIFD 259
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
286-559 4.41e-15

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: 76.54  E-value: 4.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRWHG----------EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMG 355
Cdd:cd05099    6 KWEFPRDRLVLGKPLGEGCFGQVVRAEAYGidksrpdqtvTVAVKMLKDNATDKDLADLISEMELMKLIGKHKNIINLLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 356 ACMSPPHLAIITSLCKGRTLYSVVRDAK-----IVLDVNKTRQ----------IAQEIVKGMGYLHAKGILHKDLKSKNV 420
Cdd:cd05099   86 VCTQEGPLYVIVEYAAKGNLREFLRARRppgpdYTFDITKVPEeqlsfkdlvsCAYQVARGMEYLESRRCIHRDLAARNV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 421 FYDNGKVV-ITDFGLfsISGVLQAgrrDDKLRIQNGWLchlaPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHARE 499
Cdd:cd05099  166 LVTEDNVMkIADFGL--ARGVHDI---DYYKKTSNGRL----P--VKWMAPEALFDRV-YTHQSDVWSFGILMWEIFTLG 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 500 W-PFKTQPAEAIIWQMGTGMK----PNLSQigmgkEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05099  234 GsPYPGIPVEELFKLLREGHRmdkpSNCTH-----ELYMLMRECWHAVPTQRPTFKQLVEALDKV 293
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
300-434 4.60e-15

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: 75.75  E-value: 4.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQ---VYHgRWHGEVAIRLIDIERDNEDQlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd14222    1 LGKGFFGQaikVTH-KATGKVMVMKELIRCDEETQ-KTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLK 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 377 SVVRDAKIVLDVNKTRqIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:cd14222   79 DFLRADDPFPWQQKVS-FAKGIASGMAYLHSMSIIHRDLNSHNCLIKlDKTVVVADFGL 136
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
292-502 4.67e-15

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: 76.24  E-value: 4.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVY--HGRWHGEV-AIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd14168   10 KIFEFKEVLGTGAFSEVVlaEERATGKLfAVKCIP-KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAKIVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFSISGvlqag 444
Cdd:cd14168   89 LVSGGELFDRIVEKGFYTEKDASTLIRQ-VLDAVYYLHRMGIVHRDLKPENLLYfsqdEESKIMISDFGLSKMEG----- 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 445 rRDDKLRIQNGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14168  163 -KGDVMSTACGTPGYVAPEVLAQ---------KPYSKAVDCWSIGVIAYILLCGYPPF 210
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
300-557 4.86e-15

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: 74.95  E-value: 4.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG--EVAIRLIdieRDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYS 377
Cdd:cd14203    3 LGQGCFGEVWMGTWNGttKVAIKTL---KPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEFMSKGSLLDF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 VVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSISgvlqagrRDDKLRIQNGw 456
Cdd:cd14203   80 LKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCkIADFGLARLI-------EDNEYTARQG- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 457 lchlAPEIIRQLSPdteEDKL--PFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGMKPNLSQiGMGKEISD 533
Cdd:cd14203  152 ----AKFPIKWTAP---EAALygRFTIKSDVWSFGILLTELVTKgRVPYPGMNNREVLEQVERGYRMPCPP-GCPESLHE 223
                        250       260
                 ....*....|....*....|....
gi 568937340 534 ILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd14203  224 LMCQCWRKDPEERPTFEYLQSFLE 247
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
292-504 5.13e-15

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: 75.28  E-value: 5.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQL-KAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYRARslhTGLEVAIKMIDKKAMQKAGMvQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQAGRR 446
Cdd:cd14186   81 EMCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTrNMNIKIADFGLAT-----QLKMP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 447 DDKLRIQNGWLCHLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKT 504
Cdd:cd14186  156 HEKHFTMCGTPNYISPEIATRSAHGLE---------SDVWSLGCMFYTLLVGRPPFDT 204
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
293-517 6.13e-15

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 75.01  E-value: 6.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQ---VYHGRWHGEVAIRLIDIERDNEDqLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd08219    1 QYNVLRVVGEGSFGRallVQHVNSDQKYAMKEIRLPKSSSA-VEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDVNKT-RQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSIsgvlqagrrd 447
Cdd:cd08219   80 CDGGDLMQKIKLQRGKLFPEDTiLQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLtQNGKVKLGDFGSARL---------- 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 448 dkLRIQNGWLC-------HLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTG 517
Cdd:cd08219  150 --LTSPGAYACtyvgtpyYVPPEIW---------ENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQG 215
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
298-549 6.85e-15

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: 75.05  E-value: 6.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGR------WhgEVAIRLIDIERDNEDQLkAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14201   12 DLVGHGAFAVVFKGRhrkktdW--EVAIKSINKKNLSKSQI-LLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF--YDNGK--------VVITDFGLfsiSGVL 441
Cdd:cd14201   89 GGDLADYLQ-AKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILlsYASRKkssvsgirIKIADFGF---ARYL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAGRRDDKLriqNGWLCHLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQPAE--AIIWQMGTGMK 519
Cdd:cd14201  165 QSNMMAATL---CGSPMYMAPEVIMSQHYDAK---------ADLWSIGTVIYQCLVGKPPFQANSPQdlRMFYEKNKNLQ 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 568937340 520 PNLSQiGMGKEISDILLFCWAFEQEERPTF 549
Cdd:cd14201  233 PSIPR-ETSPYLADLLLGLLQRNQKDRMDF 261
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
298-554 8.75e-15

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: 74.34  E-value: 8.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRwhGEVAIRLIDIERD-----NEDQLKAFKREVMAYRQT-RHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd13997    6 EQIGSGSFSEVFKVR--SKVDGCLYAVKKSkkpfrGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMELCE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSV----VRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsisgvlqAGRR 446
Cdd:cd13997   84 NGSLQDAleelSPISK--LSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNkGTCKIGDFGL--------ATRL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 DDKLRIQNGWLCHLAPEIIrqlspdteEDKLPFSKHSDVFALGTIWYELhAREWPFktqPAEAIIW-QMGTGMKPNLSQI 525
Cdd:cd13997  154 ETSGDVEEGDSRYLAPELL--------NENYTHLPKADIFSLGVTVYEA-ATGEPL---PRNGQQWqQLRQGKLPLPPGL 221
                        250       260
                 ....*....|....*....|....*....
gi 568937340 526 GMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd13997  222 VLSQELTRLLKVMLDPDPTRRPTADQLLA 250
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
299-565 1.36e-14

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: 74.29  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRW--HGE-----VAIRLIdieRDNEDQlKAFKR---EVMAYRQTRHENVVLFMGACMSPPhLAIITS 368
Cdd:cd05109   14 VLGSGAFGTVYKGIWipDGEnvkipVAIKVL---RENTSP-KANKEildEAYVMAGVGSPYVCRLLGICLTST-VQLVTQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFSISGVLQAGRRD 447
Cdd:cd05109   89 LMPYGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSpNHVKITDFGLARLLDIDETEYHA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 448 DKLRIQNGWLChlAPEIIRQlspdteedklPFSKHSDVFALG-TIWYELHAREWPFKTQPAEAIIWQMGTGMKpnLSQIG 526
Cdd:cd05109  169 DGGKVPIKWMA--LESILHR----------RFTHQSDVWSYGvTVWELMTFGAKPYDGIPAREIPDLLEKGER--LPQPP 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568937340 527 M-GKEISDILLFCWAFEQEERPTFTKLMDMLEKLPKRNRR 565
Cdd:cd05109  235 IcTIDVYMIMVKCWMIDSECRPRFRELVDEFSRMARDPSR 274
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
298-555 1.38e-14

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: 73.80  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHG--RWHG-EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPP--HLAIITSLCKG 372
Cdd:cd13983    7 EVLGRGSFKTVYRAfdTEEGiEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSkkEVIFITELMTS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKG--ILHKDLKSKNVFYD--NGKVVITDFGLFSIsgvlqagRRDD 448
Cdd:cd13983   87 GTLKQYLKRFK-RLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgnTGEVKIGDLGLATL-------LRQS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 KLRIQNGWLCHLAPEIIrqlspdtEEDklpFSKHSDVFALGTIWYELHAREWPFK--TQPAEaiIWQMGT-GMKPN-LSQ 524
Cdd:cd13983  159 FAKSVIGTPEFMAPEMY-------EEH---YDEKVDIYAFGMCLLEMATGEYPYSecTNAAQ--IYKKVTsGIKPEsLSK 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 525 IgMGKEISDILLFCWAfEQEERPTFTKLMDM 555
Cdd:cd13983  227 V-KDPELKDFIEKCLK-PPDERPSARELLEH 255
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
300-559 2.25e-14

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: 73.78  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWH------GE-VAIRliDIERDNEDQLKA-FKREVMAYRQTRHENVVLFMGAC--MSPPHLAIITSL 369
Cdd:cd05080   12 LGEGHFGKVSLYCYDptndgtGEmVAVK--ALKADCGPQHRSgWKQEIDILKTLYHENIVKYKGCCseQGGKSLQLIMEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLdvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGVLQAGRRDD 448
Cdd:cd05080   90 VPLGSLRDYLPKHSIGL--AQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVkIGDFGL---AKAVPEGHEYY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 KLRiQNG-----WlchLAPEIIRqlspdteEDKlpFSKHSDVFALGTIWYELHAREWPFKTQPAEAI------IWQMGTG 517
Cdd:cd05080  165 RVR-EDGdspvfW---YAPECLK-------EYK--FYYASDVWSFGVTLYELLTHCDSSQSPPTKFLemigiaQGQMTVV 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568937340 518 MKPNLSQIGM--------GKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05080  232 RLIELLERGErlpcpdkcPQEVYHLMKNCWETEASFRPTFENLIPILKTV 281
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
300-505 2.51e-14

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: 73.26  E-value: 2.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFG--QVYHGRWHGE-VAIRLIDIERDNEDQLKafkREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd14662    8 IGSGNFGvaRLMRNKETKElVAVKYIERGLKIDENVQ---REIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGELF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG---KVVITDFGlFSISGVLQAgrrddKLRIQ 453
Cdd:cd14662   85 ERICNAG-RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpapRLKICDFG-YSKSSVLHS-----QPKST 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568937340 454 NGWLCHLAPEIIRQLSPDteedklpfSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14662  158 VGTPAYIAPEVLSRKEYD--------GKVADVWSCGVTLYVMLVGAYPFEDP 201
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
295-433 2.55e-14

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: 73.51  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYH------GRWhgeVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd07833    4 EVLGVVGEGAYGVVLKcrnkatGEI---VAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 369 LCkGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFG 433
Cdd:cd07833   81 YV-ERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSeSGVLKLCDFG 145
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
298-502 2.88e-14

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: 72.83  E-value: 2.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHG--RWHG-EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd14082    9 EVLGSGQFGIVYGGkhRKTGrDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGDM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG----KVVITDFGLFSISGvlQAGRRddkl 450
Cdd:cd14082   89 LEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAepfpQVKLCDFGFARIIG--EKSFR---- 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568937340 451 RIQNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14082  163 RSVVGTPAYLAPEVLR---------NKGYNRSLDMWSVGVIIYVSLSGTFPF 205
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
293-553 3.11e-14

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: 72.85  E-value: 3.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPP-HLAIITS 368
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWlvrHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAK-IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGlfsISGVLQAGrr 446
Cdd:cd08223   81 FCEGGDLYTRLKEQKgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIkVGDLG---IARVLESS-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 ddklriqngwlCHLAPEIIRQ---LSPDTEEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLS 523
Cdd:cd08223  156 -----------SDMATTLIGTpyyMSPELFSNK-PYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMP 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 568937340 524 QiGMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd08223  224 K-QYSPELGELIKAMLHQDPEKRPSVKRIL 252
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
292-552 3.19e-14

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: 73.06  E-value: 3.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGEL-IGKGRFGQVYHGRWHGE-----VAIRLIDIERDnedqlKAFKREVMAYRQTRHE----NVVLFMGACMSPp 361
Cdd:cd05115    3 DNLLIDEVeLGSGNFGCVKKGVYKMRkkqidVAIKVLKQGNE-----KAVRDEMMREAQIMHQldnpYIVRMIGVCEAE- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGV 440
Cdd:cd05115   77 ALMLVMEMASGGPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAkISDFGL---SKA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 LQAGRRDDKLRIQNGW-LCHLAPEIIRQLSpdteedklpFSKHSDVFALG-TIWYELHAREWPFKTQPAEAIIWQMGTGM 518
Cdd:cd05115  154 LGADDSYYKARSAGKWpLKWYAPECINFRK---------FSSRSDVWSYGvTMWEAFSYGQKPYKKMKGPEVMSFIEQGK 224
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568937340 519 KPNLSQiGMGKEISDILLFCWAFEQEERPTFTKL 552
Cdd:cd05115  225 RMDCPA-ECPPEMYALMSDCWIYKWEDRPNFLTV 257
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
300-555 3.34e-14

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 72.92  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQ---VYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd08218    8 IGEGSFGKallVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLdvNKTRQIAQEIVK---GMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlfsISGVLQAGRRDDKLRI 452
Cdd:cd08218   88 KRINAQRGVL--FPEDQILDWFVQlclALKHVHDRKILHRDIKSQNIFLtKDGIIKLGDFG---IARVLNSTVELARTCI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 453 qnGWLCHLAPEIIrqlspdteEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSqIGMGKEIS 532
Cdd:cd08218  163 --GTPYYLSPEIC--------ENK-PYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVP-SRYSYDLR 230
                        250       260
                 ....*....|....*....|...
gi 568937340 533 DILLFCWAFEQEERPTFTKLMDM 555
Cdd:cd08218  231 SLVSQLFKRNPRDRPSINSILEK 253
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
295-517 3.98e-14

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


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 72.68  E-value: 3.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG--EVAIRLIDIER-DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14161    6 EFLETLGKGTYGRVKKARDSSgrLVAIKSIRKDRiKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYAS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVLDVnKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISgvlqagRRDDKL 450
Cdd:cd14161   86 RGDLYDYISERQRLSEL-EARHFFRQIVSAVHYCHANGIVHRDLKLENILLDaNGNIKIADFGLSNLY------NQDKFL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 451 RIQNGWLCHLAPEIIrqlspdteeDKLPFS-KHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTG 517
Cdd:cd14161  159 QTYCGSPLYASPEIV---------NGRPYIgPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSG 217
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
297-495 4.35e-14

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: 72.92  E-value: 4.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHGRWHGE-VAI-RLID-IERDNEDQLKAFKREVMAYRQTRHENVVLFMG-ACMSPPHLAIITSLCKG 372
Cdd:cd14158   20 GNKLGEGGFGVVFKGYINDKnVAVkKLAAmVDISTEDLTKQFEQEIQVMAKCQHENLVELLGySCDGPQLCLVYTYMPNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVV-RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSISGvlqAGRRDDKL 450
Cdd:cd14158  100 SLLDRLAcLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPkISDFGLARASE---KFSQTIMT 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340 451 RIQNGWLCHLAPEIIR-QLSPdteedklpfskHSDVFALGTIWYEL 495
Cdd:cd14158  177 ERIVGTTAYMAPEALRgEITP-----------KSDIFSFGVVLLEI 211
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
300-559 4.49e-14

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: 72.59  E-value: 4.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRW--HGEVAIRLIDIERDNEDQlkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYS 377
Cdd:cd05114   12 LGSGLFGVVRLGKWraQYKVAIKAIREGAMSEED---FIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 VVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSIsgVLqagrrDDKLRIQNGw 456
Cdd:cd05114   89 YLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVnDTGVVKVSDFGMTRY--VL-----DDQYTSSSG- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 457 lchlAPEIIRQLSPDTEEDKlPFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTG---MKPNLSQigmgKEIS 532
Cdd:cd05114  161 ----AKFPVKWSPPEVFNYS-KFSSKSDVWSFGVLMWEVFTEgKMPFESKSNYEVVEMVSRGhrlYRPKLAS----KSVY 231
                        250       260
                 ....*....|....*....|....*..
gi 568937340 533 DILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05114  232 EVMYSCWHEKPEGRPTFADLLRTITEI 258
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
298-498 5.45e-14

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: 72.79  E-value: 5.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE-------VAIRLIdierdNEDQLKAFKREVMAYRQ--TRHENVVLFMGACM----SPPHLA 364
Cdd:cd14055    1 KLVGKGRFAEVWKAKLKQNasgqyetVAVKIF-----PYEEYASWKNEKDIFTDasLKHENILQFLTAEErgvgLDRQYW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLysvvRD--AKIVLDVNKTRQIAQEIVKGMGYLHAK---------GILHKDLKSKNVFY-DNGKVVITDF 432
Cdd:cd14055   76 LITAYHENGSL----QDylTRHILSWEDLCKMAGSLARGLAHLHSDrtpcgrpkiPIAHRDLKSSNILVkNDGTCVLADF 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 433 GLfsisgvlqAGRRDDKLRI-------QNGWLCHLAPEIIRqlSPDTEEDKLPFsKHSDVFALGTIWYELHAR 498
Cdd:cd14055  152 GL--------ALRLDPSLSVdelansgQVGTARYMAPEALE--SRVNLEDLESF-KQIDVYSMALVLWEMASR 213
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
294-559 5.48e-14

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: 72.21  E-value: 5.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHGRWH--GE----VAIRLIDIERdNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd05066    6 IKIEKVIGAGEFGEVCSGRLKlpGKreipVAIKTLKAGY-TEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGVLQAG-- 444
Cdd:cd05066   85 EYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCkVSDFGL---SRVLEDDpe 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 ----RRDDKLRIQngWLchlAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGMK 519
Cdd:cd05066  162 aaytTRGGKIPIR--WT---APEAIAYRK---------FTSASDVWSYGIVMWEVMSYgERPYWEMSNQDVIKAIEEGYR 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568937340 520 -PnlSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05066  228 lP--APMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKL 266
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
298-559 5.61e-14

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: 72.31  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHG------RWHGEVAIRLIDIERdNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd05063   11 KVIGAGEFGEVFRGilkmpgRKEVAVAIKTLKPGY-TEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGVLQagrrDD-- 448
Cdd:cd05063   90 NGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECkVSDFGL---SRVLE----DDpe 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 --------KLRIQngWLchlAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGMK 519
Cdd:cd05063  163 gtyttsggKIPIR--WT---APEAIAYRK---------FTSASDVWSFGIVMWEVMSFgERPYWDMSNHEVMKAINDGFR 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568937340 520 -PnlSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05063  229 lP--APMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKL 267
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
299-556 6.45e-14

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: 72.26  E-value: 6.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRWHGE-VAIRLIDI----ERDNEDQLKAFKREVM-----AYRQTR----------HENVVLFMGACM 358
Cdd:cd14000    1 LLGDGGFGSVYRASYKGEpVAVKIFNKhtssNFANVPADTMLRHLRAtdamkNFRLLRqeltvlshlhHPSIVYLLGIGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 359 SPPHLAI-ITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV----FYDNGKVV--ITD 431
Cdd:cd14000   81 HPLMLVLeLAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVlvwtLYPNSAIIikIAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 432 FGLFSIS---GVLQAGrrddklriqnGWLCHLAPEIIRQlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAE 508
Cdd:cd14000  161 YGISRQCcrmGAKGSE----------GTPGFRAPEIARG--------NVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKF 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568937340 509 AIIWQMGTGMKPNLSQ--IGMGKEISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd14000  223 PNEFDIHGGLRPPLKQyeCAPWPEVEVLMKKCWKENPQQRPTAVTVVSIL 272
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
295-535 7.15e-14

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: 71.95  E-value: 7.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLKAF-KREVMAYRQTRHENVVLFMGACMSPP-HLAIITSL 369
Cdd:cd14163    3 QLGKTIGEGTYSKVkeaFSKKHQRKVAIKIIDKSGGPEEFIQRFlPRELQIVERLDHKNIIHVYEMLESADgKIYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLfsiSGVLQAGRRDDK 449
Cdd:cd14163   83 AEDGDVFDCVLHGG-PLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFTLKLTDFGF---AKQLPKGGRELS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 lRIQNGWLCHLAPEIIRQLSPDteedklpfSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMK-PnlSQIGMG 528
Cdd:cd14163  159 -QTFCGSTAYAAPEVLQGVPHD--------SRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGVSlP--GHLGVS 227

                 ....*..
gi 568937340 529 KEISDIL 535
Cdd:cd14163  228 RTCQDLL 234
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
300-554 7.87e-14

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: 71.96  E-value: 7.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHG---RWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSP--PHLAII--TSLCKG 372
Cdd:cd14033    9 IGRGSFKTVYRGldtETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTvrGHKCIIlvTELMTS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKG--ILHKDLKSKNVFYD--NGKVVITDFGLFSIsgvlqagRRDD 448
Cdd:cd14033   89 GTLKTYLKRFR-EMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITgpTGSVKIGDLGLATL-------KRAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 KLRIQNGwlchlAPEIirqLSPDTEEDKlpFSKHSDVFALGTIWYELHAREWPF-KTQPAEAIIWQMGTGMKPNLSQIGM 527
Cdd:cd14033  161 FAKSVIG-----TPEF---MAPEMYEEK--YDEAVDVYAFGMCILEMATSEYPYsECQNAAQIYRKVTSGIKPDSFYKVK 230
                        250       260
                 ....*....|....*....|....*..
gi 568937340 528 GKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd14033  231 VPELKEIIEGCIRTDKDERFTIQDLLE 257
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
288-556 8.66e-14

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: 72.32  E-value: 8.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEQLEIGELIGKGRFGQVYHGRWHG-----------------EVAIRLIDIERdNEDQLKAFKREVMAYRQTRHENV 350
Cdd:cd05097    1 EFPRQQLRLKEKLGEGQFGEVHLCEAEGlaeflgegapefdgqpvLVAVKMLRADV-TKTARNDFLKEIKIMSRLKNPNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 351 VLFMGACMSPPHLAIITSLCKG---------RTLYSVVRDAKIVLDVNKTR--QIAQEIVKGMGYLHAKGILHKDLKSKN 419
Cdd:cd05097   80 IRLLGVCVSDDPLCMITEYMENgdlnqflsqREIESTFTHANNIPSVSIANllYMAVQIASGMKYLASLNFVHRDLATRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 420 VFYDNGKVV-ITDFGLfsiSGVLQAGrrdDKLRIQNgwlchLAPEIIRQLSpdtEEDKL--PFSKHSDVFALGTIWYELH 496
Cdd:cd05097  160 CLVGNHYTIkIADFGM---SRNLYSG---DYYRIQG-----RAVLPIRWMA---WESILlgKFTTASDVWAFGVTLWEMF 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 497 A--REWPFKTQPAEAIIWQMGTGMKPNLSQIGMGK------EISDILLFCWAFEQEERPTFTKLMDML 556
Cdd:cd05097  226 TlcKEQPYSLLSDEQVIENTGEFFRNQGRQIYLSQtplcpsPVFKLMMRCWSRDIKDRPTFNKIHHFL 293
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
291-505 1.03e-13

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: 71.53  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIGELIGKGRFGQVYHGRWHGE---VAIRLI---DIERDN-EDQLkafKREVMAYRQTRHENVVLFMGACMSPPHL 363
Cdd:cd14116    4 LEDFEIGRPLGKGKFGNVYLAREKQSkfiLALKVLfkaQLEKAGvEHQL---RREVEIQSHLRHPNILRLYGYFHDATRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlFSISGvlQ 442
Cdd:cd14116   81 YLILEYAPLGTVYRELQKLS-KFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLgSAGELKIADFG-WSVHA--P 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 443 AGRRDDKLriqnGWLCHLAPEIIRQlspDTEEDKLpfskhsDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14116  157 SSRRTTLC----GTLDYLPPEMIEG---RMHDEKV------DLWSLGVLCYEFLVGKPPFEAN 206
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
291-434 1.12e-13

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: 71.83  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIgelIGKGRFGQVYHGR--WHGE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHlaiit 367
Cdd:cd07840    1 YEKIAQ---IGEGTYGQVYKARnkKTGElVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSKGS----- 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 368 SLCKGRT----------LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGL 434
Cdd:cd07840   73 AKYKGSIymvfeymdhdLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLkLADFGL 150
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
300-498 1.17e-13

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: 71.61  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGE-VAIRLIDIERDnedqlKAFKREVMAYRQT--RHENVVLFMGACM----SPPHLAIITSLCKG 372
Cdd:cd14220    3 IGKGRYGEVWMGKWRGEkVAVKVFFTTEE-----ASWFRETEIYQTVlmRHENILGFIAADIkgtgSWTQLYLITDYHEN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAK--------GILHKDLKSKNVFY-DNGKVVITDFGLfSISGVLQA 443
Cdd:cd14220   78 GSLYDFLKCT--TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIkKNGTCCIADLGL-AVKFNSDT 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 444 GRRDDKLRIQNGWLCHLAPEIIrqlspDTEEDKLPFSKH--SDVFALGTIWYELHAR 498
Cdd:cd14220  155 NEVDVPLNTRVGTKRYMAPEVL-----DESLNKNHFQAYimADIYSFGLIIWEMARR 206
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
287-558 1.38e-13

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: 71.22  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLIDIERDNEDQLKaFKREVMAYRQTRHENVVLFMGAC- 357
Cdd:cd05062    1 WEVAREKITMSRELGQGSFGMVYEGIAKGvvkdepetRVAIKTVNEAASMRERIE-FLNEASVMKEFNCHHVVRLLGVVs 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 358 MSPPHLAIITSLCKGrTLYSVVRDAKIVLDVN---------KTRQIAQEIVKGMGYLHAKGILHKDLKSKN-VFYDNGKV 427
Cdd:cd05062   80 QGQPTLVIMELMTRG-DLKSYLRSLRPEMENNpvqappslkKMIQMAGEIADGMAYLNANKFVHRDLAARNcMVAEDFTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 428 VITDFGLFSISGVLQAGRRDDKlriqngwlcHLAPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHA-REWPFKTQP 506
Cdd:cd05062  159 KIGDFGMTRDIYETDYYRKGGK---------GLLP--VRWMSPESLKDGV-FTTYSDVWSFGVVLWEIATlAEQPYQGMS 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 507 AEAII-WQMGTGM--KPNlsqiGMGKEISDILLFCWAFEQEERPTFTKLMDMLEK 558
Cdd:cd05062  227 NEQVLrFVMEGGLldKPD----NCPDMLFELMRMCWQYNPKMRPSFLEIISSIKE 277
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
291-545 1.40e-13

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: 71.10  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQlkAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14193    3 YYNVNKEEILGGGRFGQVHKCEEKSsglKLAAKIIKARSQKEKE--EVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF---YDNGKVVITDFGLfsisgvlqaG 444
Cdd:cd14193   81 EYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcvsREANQVKIIDFGL---------A 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 RR---DDKLRIQNGWLCHLAPEIIRQlspdteeDKLPFSkhSDVFALGTIWYELHarewpfktqpaeaiiwqmgTGMKPN 521
Cdd:cd14193  152 RRykpREKLRVNFGTPEFLAPEVVNY-------EFVSFP--TDMWSLGVIAYMLL-------------------SGLSPF 203
                        250       260
                 ....*....|....*....|....
gi 568937340 522 LSQiGMGKEISDILLFCWAFEQEE 545
Cdd:cd14193  204 LGE-DDNETLNNILACQWDFEDEE 226
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
292-498 1.43e-13

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: 71.62  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHGE-VAIRLIDIERDnedqlKAFKREVMAYRQT--RHENVVLFMGACM----SPPHLA 364
Cdd:cd14219    5 KQIQMVKQIGKGRYGEVWMGKWRGEkVAVKVFFTTEE-----ASWFRETEIYQTVlmRHENILGFIAADIkgtgSWTQLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAK--------GILHKDLKSKNVFYD-NGKVVITDFGLf 435
Cdd:cd14219   80 LITDYHENGSLYDYLKST--TLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKkNGTCCIADLGL- 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 436 SISGVLQAGRRDDKLRIQNGWLCHLAPEIIrqlspDTEEDKLPFSKH--SDVFALGTIWYELHAR 498
Cdd:cd14219  157 AVKFISDTNEVDIPPNTRVGTKRYMPPEVL-----DESLNRNHFQSYimADMYSFGLILWEVARR 216
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
295-434 1.44e-13

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: 71.45  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAI---RLIDIERDNED-QLKAFkREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd07841    3 EKGKKLGEGTYAVVYKARDKEtgrIVAIkkiKLGERKEAKDGiNFTAL-REIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 368 SLCKGrTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:cd07841   82 EFMET-DLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIAsDGVLKLADFGL 148
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
300-502 1.51e-13

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: 70.72  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYH------GRwhgEVAIRLIDIER--DNEDqlkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14103    1 LGRGKFGTVYRcvekatGK---ELAAKFIKCRKakDRED----VRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKN---VFYDNGKVVITDFGLfsisgvlqaGRR-- 446
Cdd:cd14103   74 GGELFERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENilcVSRTGNQIKIIDFGL---------ARKyd 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 447 -DDKLRIQNGWLCHLAPEIIrqlSPDteedklPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14103  145 pDKKLKVLFGTPEFVAPEVV---NYE------PISYATDMWSVGVICYVLLSGLSPF 192
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
296-502 1.61e-13

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: 70.67  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHGRW-----HGEVAIRLIDIERDNEDQLKAF-KREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14080    4 LGKTIGEGSYSKVKLAEYtksglKEKVACKIIDKKKAPKDFLEKFlPRELEILRKLRHPNIIQVYSIFERGSKVFIFMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIvLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGRRDD 448
Cdd:cd14080   84 AEHGDLLEYIQKRGA-LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDsNNNVKLSDFGF---ARLCPDDDGDV 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 449 KLRIQNGWLCHLAPEIIRQLSPDteedklpfSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14080  160 LSKTFCGSAAYAAPEILQGIPYD--------PKKYDIWSLGVILYIMLCGSMPF 205
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
287-559 1.89e-13

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: 71.20  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG----------EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGA 356
Cdd:cd05098    8 WELPRDRLVLGKPLGEGCFGQVVLAEAIGldkdkpnrvtKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 357 CMSP-PHLAIITSLCKG--RTLYSVVRDAKIVLDVNKTR------------QIAQEIVKGMGYLHAKGILHKDLKSKNVF 421
Cdd:cd05098   88 CTQDgPLYVIVEYASKGnlREYLQARRPPGMEYCYNPSHnpeeqlsskdlvSCAYQVARGMEYLASKKCIHRDLAARNVL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 422 YDNGKVV-ITDFGLFSISGVLQAGRRDDKLRIQNGWlchLAPEIIRqlspdteeDKLpFSKHSDVFALGTIWYELHAREW 500
Cdd:cd05098  168 VTEDNVMkIADFGLARDIHHIDYYKKTTNGRLPVKW---MAPEALF--------DRI-YTHQSDVWSFGVLLWEIFTLGG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 501 -PFKTQPAEAIIWQMGTGMKPNlSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05098  236 sPYPGVPVEELFKLLKEGHRMD-KPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI 294
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
298-553 2.30e-13

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: 70.34  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHG---RWHGEVAIRLIDIERDNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd06647   13 EKIGQGASGTVYTAidvATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQAGRRDDKLRIQ 453
Cdd:cd06647   91 LTDVVTET--CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGmDGSVKLTDFGFCA-----QITPEQSKRSTM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 NGWLCHLAPEII--RQLSPDTeedklpfskhsDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI-GMGKE 530
Cdd:cd06647  164 VGTPYWMAPEVVtrKAYGPKV-----------DIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPeKLSAI 232
                        250       260
                 ....*....|....*....|...
gi 568937340 531 ISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06647  233 FRDFLNRCLEMDVEKRGSAKELL 255
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
298-498 2.58e-13

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: 70.82  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE-VAIRLIdierdNEDQLKAFKREVMAYRQTR--HENVVLFMGA--CMSP--PHLAIIT--- 367
Cdd:cd14053    1 EIKARGRFGAVWKAQYLNRlVAVKIF-----PLQEKQSWLTEREIYSLPGmkHENILQFIGAekHGESleAEYWLITefh 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 ---SLC---KGRTLysvvrdakivlDVNKTRQIAQEIVKGMGYLHA----------KGILHKDLKSKNVFY-DNGKVVIT 430
Cdd:cd14053   76 ergSLCdylKGNVI-----------SWNELCKIAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLLkSDLTACIA 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 431 DFGLfsiSGVLQAGRRDDKLRIQNGWLCHLAPEIIrqlspdteEDKLPFSKHS----DVFALGTIWYELHAR 498
Cdd:cd14053  145 DFGL---ALKFEPGKSCGDTHGQVGTRRYMAPEVL--------EGAINFTRDAflriDMYAMGLVLWELLSR 205
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
287-559 3.03e-13

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: 70.81  E-value: 3.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG----------EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGA 356
Cdd:cd05101   19 WEFPRDKLTLGKPLGEGCFGQVVMAEAVGidkdkpkeavTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 357 CMSPPHLAIITSLCKGRTLYSVVR-----DAKIVLDVNKTRQ----------IAQEIVKGMGYLHAKGILHKDLKSKNVF 421
Cdd:cd05101   99 CTQDGPLYVIVEYASKGNLREYLRarrppGMEYSYDINRVPEeqmtfkdlvsCTYQLARGMEYLASQKCIHRDLAARNVL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 422 YDNGKVV-ITDFGLFSISGVLQAGRRDDKLRIQNGWlchLAPEIIRqlspdteeDKLpFSKHSDVFALGTIWYELHAREW 500
Cdd:cd05101  179 VTENNVMkIADFGLARDINNIDYYKKTTNGRLPVKW---MAPEALF--------DRV-YTHQSDVWSFGVLMWEIFTLGG 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 501 -PFKTQPAEAIIWQMGTGMKPNlSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05101  247 sPYPGIPVEELFKLLKEGHRMD-KPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI 305
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
286-563 3.20e-13

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: 71.16  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLIDiERDNEDQLKAFKREV-MAYRQTRHENVVLFMGA 356
Cdd:cd05102    1 QWEFPRDRLRLGKVLGHGAFGKVVEASAFGidksssceTVAVKMLK-EGATASEHKALMSELkILIHIGNHLNVVNLLGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 357 CMSP--PhLAIITSLCK----------GRTLYSVVRD-----------------------------AKIVLDVNKTRQIA 395
Cdd:cd05102   80 CTKPngP-LMVIVEFCKygnlsnflraKREGFSPYRErsprtrsqvrsmveavradrrsrqgsdrvASFTESTSSTNQPR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 396 QE--------------------IVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsisgvlqagRRD-----DK 449
Cdd:cd05102  159 QEvddlwqspltmedlicysfqVARGMEFLASRKCIHRDLAARNILLSENNVVkICDFGL----------ARDiykdpDY 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIQNGWLchlaPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYE---LHAREWPfKTQPAEAIIWQM--GTGMK-PNLS 523
Cdd:cd05102  229 VRKGSARL----P--LKWMAPESIFDKV-YTTQSDVWSFGVLLWEifsLGASPYP-GVQINEEFCQRLkdGTRMRaPEYA 300
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 568937340 524 QigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKLPKRN 563
Cdd:cd05102  301 T----PEIYRIMLSCWHGDPKERPTFSDLVEILGDLLQEN 336
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
286-559 3.47e-13

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: 70.80  E-value: 3.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHE-NVVLFMGA 356
Cdd:cd14207    1 KWEFARERLKLGKSLGRGAFGKVVQASAFGikksptcrVVAVKMLK-EGATASEYKALMTELKILIHIGHHlNVVNLLGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 357 CM-SPPHLAIITSLCK----------GRTLYSVVRDAKIVLDVNKTRQIAQ----------------------------- 396
Cdd:cd14207   80 CTkSGGPLMVIVEYCKygnlsnylksKRDFFVTNKDTSLQEELIKEKKEAEptggkkkrlesvtssesfassgfqedksl 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 ----------------------------EIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLF-SISGVLQAGRR 446
Cdd:cd14207  160 sdveeeeedsgdfykrpltmedlisysfQVARGMEFLSSRKCIHRDLAARNILLSENNVVkICDFGLArDIYKNPDYVRK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 DDKlRIQNGWLchlAPEIIRqlspdteeDKLpFSKHSDVFALGTIWYE---LHAREWPfKTQPAEAIIWQMGTGMK---P 520
Cdd:cd14207  240 GDA-RLPLKWM---APESIF--------DKI-YSTKSDVWSYGVLLWEifsLGASPYP-GVQIDEDFCSKLKEGIRmraP 305
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 568937340 521 NLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14207  306 EFAT----SEIYQIMLDCWQGDPNERPRFSELVERLGDL 340
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
291-502 4.14e-13

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: 69.82  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIgelIGKGRFGQVYHGR--WHGE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd07829    1 YEKLEK---LGEGTYGVVYKAKdkKTGEiVALKKIRLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKgRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL---FSIsgvlqA 443
Cdd:cd07829   78 EYCD-QDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINrDGVLKLADFGLaraFGI-----P 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 444 GRRDDKlRIQNGWlcHLAPEIIrqlspdteedkLPFSKHS---DVFALGTIWYELhAREWPF 502
Cdd:cd07829  152 LRTYTH-EVVTLW--YRAPEIL-----------LGSKHYStavDIWSVGCIFAEL-ITGKPL 198
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
293-565 4.14e-13

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: 70.48  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRW--HGE-----VAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPhLAI 365
Cdd:cd05110    8 ELKRVKVLGSGAFGTVYKGIWvpEGEtvkipVAIKILN-ETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPT-IQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFSISGVLQAG 444
Cdd:cd05110   86 VTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSpNHVKITDFGLARLLEGDEKE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 RRDDKLRIQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALG-TIWYELHAREWPFKTQPAEAIIWQMGTGMK---P 520
Cdd:cd05110  166 YNADGGKMPIKW---MALECIHYRK---------FTHQSDVWSYGvTIWELMTFGGKPYDGIPTREIPDLLEKGERlpqP 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568937340 521 NLSQIgmgkEISDILLFCWAFEQEERPTFTKLMDMLEKLPKRNRR 565
Cdd:cd05110  234 PICTI----DVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQR 274
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
273-553 4.41e-13

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: 70.04  E-value: 4.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 273 FPRkaSQTSIFLQEWDIPFEQLEIGELIGKGRFGQVY--HGRWHG-EVAIRLIDIERDNEDQLKAFKREVMAYrqTRHEN 349
Cdd:cd06638    1 FPL--SGKTIIFDSFPDPSDTWEIIETIGKGTYGKVFkvLNKKNGsKAAVKILDPIHDIDEEIEAEYNILKAL--SDHPN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 350 VVLFMGA-----CMSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIA---QEIVKGMGYLHAKGILHKDLKSKNVF 421
Cdd:cd06638   77 VVKFYGMyykkdVKNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAyilHEALMGLQHLHVNKTIHRDVKGNNIL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 422 YDN-GKVVITDFGlfsISGVLQAGRRDDKLRIqnGWLCHLAPEII---RQLspDTEEDklpfsKHSDVFALGTIWYELHA 497
Cdd:cd06638  157 LTTeGGVKLVDFG---VSAQLTSTRLRRNTSV--GTPFWMAPEVIaceQQL--DSTYD-----ARCDVWSLGITAIELGD 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 498 REWPF-KTQPAEAiIWQMGTGMKPNLSQIGM-GKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06638  225 GDPPLaDLHPMRA-LFKIPRNPPPTLHQPELwSNEFNDFIRKCLTKDYEKRPTVSDLL 281
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
298-522 6.31e-13

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: 69.27  E-value: 6.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHG----EVAIRLIDIERDNEDQlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd14202    8 DLIGHGAFAVVFKGRHKEkhdlEVAVKCINKKNLAKSQ-TLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY----------DNGKVVITDFGLfsiSGVLQA 443
Cdd:cd14202   87 DLADYLH-TMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysggrksnpNNIRIKIADFGF---ARYLQN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 GRRDDKLriqNGWLCHLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFK-TQPAE-AIIWQMGTGMKPN 521
Cdd:cd14202  163 NMMAATL---CGSPMYMAPEVIMSQHYDAK---------ADLWSIGTIIYQCLTGKAPFQaSSPQDlRLFYEKNKSLSPN 230

                 .
gi 568937340 522 L 522
Cdd:cd14202  231 I 231
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
297-504 6.85e-13

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: 68.80  E-value: 6.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHG---RWHGEVAIRLIDIER-DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14189    6 GRLLGKGGFARCYEMtdlATNKTYAVKVIPHSRvAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsiSGVLQAGrrDDKLR 451
Cdd:cd14189   86 KSLAHIWKARHTLLE-PEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFInENMELKVGDFGL---AARLEPP--EQRKK 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 452 IQNGWLCHLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKT 504
Cdd:cd14189  160 TICGTPNYLAPEVLLRQGHGPE---------SDVWSLGCVMYTLLCGNPPFET 203
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
300-551 7.74e-13

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: 68.55  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRW----HGEVAIRLIDierdNEDQLKA---FKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14120    1 IGHGAFAVVFKGRHrkkpDLPVAIKCIT----KKNLSKSqnlLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG----------KVVITDFGL--FSISGV 440
Cdd:cd14120   77 GDLADYLQ-AKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNsgrkpspndiRLKIADFGFarFLQDGM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 LQAGrrddklriqngwLC----HLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQPAEAI--IWQM 514
Cdd:cd14120  156 MAAT------------LCgspmYMAPEVIMSLQYDAK---------ADLWSIGTIVYQCLTGKAPFQAQTPQELkaFYEK 214
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568937340 515 GTGMKPNLSQiGMGKEISDILLFCWAFEQEERPTFTK 551
Cdd:cd14120  215 NANLRPNIPS-GTSPALKDLLLGLLKRNPKDRIDFED 250
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
280-520 7.76e-13

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: 69.07  E-value: 7.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 280 TSIFLQEwdipFEQLEIgelIGKGRFGQVYHGR--WHGEV-AIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGA 356
Cdd:cd14049    1 TSRYLNE----FEEIAR---LGKGGYGKVYKVRnkLDGQYyAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 357 CMSPPHLA--IITSLCKgRTLYSVVRD-------------AKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF 421
Cdd:cd14049   74 WMEHVQLMlyIQMQLCE-LSLWDWIVErnkrpceeefksaPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 422 YDNG--KVVITDFGLfSISGVLQAGRRDDKLRIQN--------GWLCHLAPEiirQLSPDTEEDKlpfskhSDVFALGTI 491
Cdd:cd14049  153 LHGSdiHVRIGDFGL-ACPDILQDGNDSTTMSRLNglthtsgvGTCLYAAPE---QLEGSHYDFK------SDMYSIGVI 222
                        250       260       270
                 ....*....|....*....|....*....|
gi 568937340 492 WYELHArewPFKTQPAEA-IIWQMGTGMKP 520
Cdd:cd14049  223 LLELFQ---PFGTEMERAeVLTQLRNGQIP 249
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
296-516 9.79e-13

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: 68.53  E-value: 9.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVY------HGRwhgEVAIRLIDIERDNED---QLKAFKREVMAYRQTRHENVVLFMGACMSPPH--LA 364
Cdd:cd06652    6 LGKLLGQGAFGRVYlcydadTGR---ELAVKQVQFDPESPEtskEVNALECEIQLLKNLLHERIVQYYGCLRDPQErtLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFS-ISGVLQ 442
Cdd:cd06652   83 IFMEYMPGGSIKDQLK-SYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSvGNVKLGDFGASKrLQTICL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 443 AGRRDDKLRIQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGT 516
Cdd:cd06652  162 SGTGMKSVTGTPYW---MSPEVISGEG---------YGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIAT 223
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
291-502 1.20e-12

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: 68.40  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIGELIGKGRFGQV---YHGRWHGEVAIRLIDIERDN-------EDQLKAFKREVMAYRQTR-HENVVLFMGACMS 359
Cdd:cd14182    2 YEKYEPKEILGRGVSSVVrrcIHKPTRQEYAVKIIDITGGGsfspeevQELREATLKEIDILRKVSgHPNIIQLKDTYET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 360 PPHLAIITSLCKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlFSIS 438
Cdd:cd14182   82 NTFFFLVFDLMKKGELFDYLTE-KVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLdDDMNIKLTDFG-FSCQ 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 439 gvLQAGrrdDKLRIQNGWLCHLAPEIIrQLSPDTEEDKlpFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14182  160 --LDPG---EKLREVCGTPGYLAPEII-ECSMDDNHPG--YGKEVDMWSTGVIMYTLLAGSPPF 215
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
295-502 1.29e-12

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: 68.18  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRwH---GE-VAIRLIDIERDNEDqLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14078    6 ELHETIGSGGFAKVKLAT-HiltGEkVAIKIMDKKALGDD-LPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTL--YSVVRDAkivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD---NGKVVitDFGLFSISgvlqAGR 445
Cdd:cd14078   84 PGGELfdYIVAKDR---LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDedqNLKLI--DFGLCAKP----KGG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 446 RDDKLRIQNGWLCHLAPEIIrqlspdteEDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14078  155 MDHHLETCCGSPAYAAPELI--------QGKPYIGSEADVWSMGVLLYALLCGFLPF 203
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
297-505 1.33e-12

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: 68.13  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELiGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd14075    8 GEL-GSGNFSQVklgIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVV--------RDAKIVLdvnktrqiAQeIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSISgvlqag 444
Cdd:cd14075   87 ELYTKIstegklseSEAKPLF--------AQ-IVSAVKHMHENNIIHRDLKAENVFYASNNCVkVGDFGFSTHA------ 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 445 RRDDKLRIQNGWLCHLAPEIIRqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14075  152 KRGETLNTFCGSPPYAAPELFK--------DEHYIGIYVDIWALGVLLYFMVTGVMPFRAE 204
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
287-555 1.34e-12

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: 68.55  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQlKAFKREVMAYRQTRH-ENVVLFMGA------ 356
Cdd:cd06616    1 YEFTAEDLKDLGEIGRGAFGTVNkmlHKPSGTIMAVKRIRSTVDEKEQ-KRLLMDLDVVMRSSDcPYIVKFYGAlfregd 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 357 ---CMSpphlAIITSLCKgrtLYsvvrdaKIVLDVNKTR-------QIAQEIVKGMGYLHAK-GILHKDLKSKNVFYD-N 424
Cdd:cd06616   80 cwiCME----LMDISLDK---FY------KYVYEVLDSVipeeilgKIAVATVKALNYLKEElKIIHRDVKPSNILLDrN 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 425 GKVVITDFGlfsISGVLQ---AGRRDDKLRIqngwlcHLAPEIIrqlspDTEEDKLPFSKHSDVFALGTIWYELHAREWP 501
Cdd:cd06616  147 GNIKLCDFG---ISGQLVdsiAKTRDAGCRP------YMAPERI-----DPSASRDGYDVRSDVWSLGITLYEVATGKFP 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 502 F-KTQPAEAIIWQMGTGMKPNLSQiGMGKEISDILL----FCWAFEQEERPTFTKLMDM 555
Cdd:cd06616  213 YpKWNSVFDQLTQVVKGDPPILSN-SEEREFSPSFVnfvnLCLIKDESKRPKYKELLKH 270
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
292-495 1.44e-12

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: 68.62  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRW----HGEVAIRLIDIERDNEDQLKAFKR-----EVMAYRQTRHENVVLFMGACMSPPH 362
Cdd:cd14096    1 ENYRLINKIGEGAFSNVYKAVPlrntGKPVAIKVVRKADLSSDNLKGSSRanilkEVQIMKRLSHPNIVKLLDFQESDEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 LAIITSLCKGRTLYS-VVRDAKIVLDVnkTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN----------------- 424
Cdd:cd14096   81 YYIVLELADGGEIFHqIVRLTYFSEDL--SRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkaddde 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 425 -----------------GKVVITDFGLfsiSGVLqagrRDDKLRIQNGWLCHLAPEIIRQLSpdteedklpFSKHSDVFA 487
Cdd:cd14096  159 tkvdegefipgvggggiGIVKLADFGL---SKQV----WDSNTKTPCGTVGYTAPEVVKDER---------YSKKVDMWA 222

                 ....*...
gi 568937340 488 LGTIWYEL 495
Cdd:cd14096  223 LGCVLYTL 230
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
298-553 1.61e-12

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: 68.60  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd06654   26 EKIGQGASGTVYTAMdvaTGQEVAIRQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQAGRRDDKLRIQ 453
Cdd:cd06654  104 LTDVVTET--CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGmDGSVKLTDFGFCA-----QITPEQSKRSTM 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 NGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI-GMGKEIS 532
Cdd:cd06654  177 VGTPYWMAPEVVTRKA---------YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPeKLSAIFR 247
                        250       260
                 ....*....|....*....|.
gi 568937340 533 DILLFCWAFEQEERPTFTKLM 553
Cdd:cd06654  248 DFLNRCLEMDVEKRGSAKELL 268
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
295-548 1.68e-12

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: 67.68  E-value: 1.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHG---RWHGEVAIRLIDIERDNEDQ-LKAFK--REVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd14133    2 EVLEVLGKGTFGQVVKCydlLTGEEVALKIIKNNKDYLDQsLDEIRllELLNKKDKADKYHIVRLKDVFYFKNHLCIVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCkGRTLYSVVRDAKIV-LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF---YDNGKVVITDFGlfsiSGVLQAG 444
Cdd:cd14133   82 LL-SQNLYEFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILlasYSRCQIKIIDFG----SSCFLTQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 RRDDklRIQNgwLCHLAPEIIrqLSpdteedkLPFSKHSDVFALGTIWYELHAREWPFK-TQPAEAIIWQMGTGMKPNLS 523
Cdd:cd14133  157 RLYS--YIQS--RYYRAPEVI--LG-------LPYDEKIDMWSLGCILAELYTGEPLFPgASEVDQLARIIGTIGIPPAH 223
                        250       260
                 ....*....|....*....|....*....
gi 568937340 524 QIGMGK----EISDILLFCWAFEQEERPT 548
Cdd:cd14133  224 MLDQGKaddeLFVDFLKKLLEIDPKERPT 252
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
295-502 1.71e-12

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 67.82  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGR--WHGE-VAIRLIDIER-DNEDQLKAFKrEVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14074    6 DLEETLGRGHFAVVKLARhvFTGEkVAVKVIDKTKlDDVSKAHLFQ-EVRCMKLVQHPNVVRLYEVIDTQTKLYLILELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV--FYDNGKVVITDFGLfsiSGVLQAGrrdD 448
Cdd:cd14074   85 DGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVvfFEKQGLVKLTDFGF---SNKFQPG---E 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 449 KLRIQNGWLCHLAPEIIRQLSPDteedklpfSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14074  159 KLETSCGSLAYSAPEILLGDEYD--------APAVDIWSLGVILYMLVCGQPPF 204
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
286-563 1.78e-12

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: 68.85  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHE-NVVLFMGA 356
Cdd:cd05103    1 KWEFPRDRLKLGKPLGRGAFGQVIEADAFGidktatcrTVAVKMLK-EGATHSEHRALMSELKILIHIGHHlNVVNLLGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 357 CMSP--PhLAIITSLCKGRTLYSVVR----------------------------DAKIVLDVNKTRQIAQ---------- 396
Cdd:cd05103   80 CTKPggP-LMVIVEFCKFGNLSAYLRskrsefvpyktkgarfrqgkdyvgdisvDLKRRLDSITSSQSSAssgfveeksl 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 ----------------------------EIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsisgvlqagRRD 447
Cdd:cd05103  159 sdveeeeagqedlykdfltledlicysfQVAKGMEFLASRKCIHRDLAARNILLsENNVVKICDFGL----------ARD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 448 -----DKLRIQNGWLchlaPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYE---LHAREWPfKTQPAEAIIWQM--GTG 517
Cdd:cd05103  229 iykdpDYVRKGDARL----P--LKWMAPETIFDRV-YTIQSDVWSFGVLLWEifsLGASPYP-GVKIDEEFCRRLkeGTR 300
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 568937340 518 MK-PNLSQIgmgkEISDILLFCWAFEQEERPTFTKLMDMLEKLPKRN 563
Cdd:cd05103  301 MRaPDYTTP----EMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQAN 343
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
300-505 1.90e-12

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: 67.25  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRwH----GEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTL 375
Cdd:cd14009    1 IGRGSFATVWKGR-HkqtgEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 376 YSVVRDAKIVLDVnKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV----FYDNGKVVITDFGlFSISgvLQAGRRDDKLR 451
Cdd:cd14009   80 SQYIRKRGRLPEA-VARHFMQQLASGLKFLRSKNIIHRDLKPQNLllstSGDDPVLKIADFG-FARS--LQPASMAETLC 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 452 iqnGWLCHLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14009  156 ---GSPLYMAPEILQFQKYDAK---------ADLWSVGAILFEMLVGKPPFRGS 197
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
297-550 1.95e-12

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: 67.68  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELiGKGRFGQVYHGRWHGE-----VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPpHLAIITSLCK 371
Cdd:cd05116    1 GEL-GSGNFGTVKKGYYQMKkvvktVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAE-SWMLVMEMAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVLDVNKTrQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGVLQAGRRDDKL 450
Cdd:cd05116   79 LGPLNKFLQKNRHVTEKNIT-ELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAkISDFGL---SKALRADENYYKA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 451 RIQNGW-LCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGMKPNLSQiGMG 528
Cdd:cd05116  155 QTHGKWpVKWYAPECM---------NYYKFSSKSDVWSFGVLMWEAFSYgQKPYKGMKGNEVTQMIEKGERMECPA-GCP 224
                        250       260
                 ....*....|....*....|..
gi 568937340 529 KEISDILLFCWAFEQEERPTFT 550
Cdd:cd05116  225 PEMYDLMKLCWTYDVDERPGFA 246
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
300-510 2.04e-12

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: 67.51  E-value: 2.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVY--HGRWHGE-VAIRLID----IERDNEDQLKAFKREVMAyrQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd05611    4 ISKGAFGSVYlaKKRSTGDyFAIKVLKksdmIAKNQVTNVKAERAIMMI--QGESPYVAKLYYSFQSKDYLYLVMEYLNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsiSGVLQAGRRDDKLr 451
Cdd:cd05611   82 GDCASLIKTLG-GLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQtGHLKLTDFGL---SRNGLEKRHNKKF- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 452 iqNGWLCHLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPFKTQPAEAI 510
Cdd:cd05611  157 --VGTPDYLAPETILGVGDD---------KMSDWWSLGCVIFEFLFGYPPFHAETPDAV 204
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
300-554 3.00e-12

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: 67.38  E-value: 3.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHG---RWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPH----LAIITSLCKG 372
Cdd:cd14030   33 IGRGSFKTVYKGldtETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMTS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKG--ILHKDLKSKNVFYD--NGKVVITDFGLFSIsgvlqagRRDD 448
Cdd:cd14030  113 GTLKTYLKRFK-VMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgpTGSVKIGDLGLATL-------KRAS 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 KLRIQNGwlchlAPEIirqLSPDTEEDKlpFSKHSDVFALGTIWYELHAREWPF-KTQPAEAIIWQMGTGMKPNLSQIGM 527
Cdd:cd14030  185 FAKSVIG-----TPEF---MAPEMYEEK--YDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRRVTSGVKPASFDKVA 254
                        250       260
                 ....*....|....*....|....*..
gi 568937340 528 GKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd14030  255 IPEVKEIIEGCIRQNKDERYAIKDLLN 281
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
298-553 3.36e-12

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: 67.44  E-value: 3.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd06655   25 EKIGQGASGTVFTAIdvaTGQEVAIKQINLQKQPKKEL--IINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQAGRRDDKLRIQ 453
Cdd:cd06655  103 LTDVVTET--CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGmDGSVKLTDFGFCA-----QITPEQSKRSTM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 NGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI-GMGKEIS 532
Cdd:cd06655  176 VGTPYWMAPEVVTRKA---------YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPeKLSPIFR 246
                        250       260
                 ....*....|....*....|.
gi 568937340 533 DILLFCWAFEQEERPTFTKLM 553
Cdd:cd06655  247 DFLNRCLEMDVEKRGSAKELL 267
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
298-557 3.37e-12

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: 67.69  E-value: 3.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQT-----RHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVllknlKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSiSGVLQagrrDDKLR 451
Cdd:cd05603   81 GELFFHLQRERCFLE-PRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDcQGHVVLTDFGLCK-EGMEP----EETTS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 452 IQNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPaeaiIWQMGTGMKPNLSQIGMGKEI 531
Cdd:cd05603  155 TFCGTPEYLAPEVLR---------KEPYDRTVDWWCLGAVLYEMLYGLPPFYSRD----VSQMYDNILHKPLHLPGGKTV 221
                        250       260
                 ....*....|....*....|....*.
gi 568937340 532 SDILLFCWAFEQEERPTFTKLMDMLE 557
Cdd:cd05603  222 AACDLLQGLLHKDQRRRLGAKADFLE 247
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
298-498 4.07e-12

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: 67.39  E-value: 4.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHG-EVAIRLIDIErdNEDQLKAfKREVMAYRQTRHENVVLFMGACMSPP------HLAIIT--- 367
Cdd:cd14054    1 QLIGQGRYGTVWKGSLDErPVAVKVFPAR--HRQNFQN-EKDIYELPLMEHSNILRFIGADERPTadgrmeYLLVLEyap 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 --SLCKGRTLYSvvrdakivLDVNKTRQIAQEIVKGMGYLHAK---------GILHKDLKSKNVFYDN-GKVVITDFG-- 433
Cdd:cd14054   78 kgSLCSYLRENT--------LDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKAdGSCVICDFGla 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 434 --LFSISGV-LQAGRRDDKLRIQNGWLCHLAPEI------IRQLSpdteedklPFSKHSDVFALGTIWYELHAR 498
Cdd:cd14054  150 mvLRGSSLVrGRPGAAENASISEVGTLRYMAPEVlegavnLRDCE--------SALKQVDVYALGLVLWEIAMR 215
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
297-502 5.23e-12

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: 66.61  E-value: 5.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQ-TRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14106   13 STPLGRGKFAVVrkcIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELcKDCPRVVNLHEVYETRSELILILELAAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF----YDNGKVVITDFGlfsISGVLQAGrrdD 448
Cdd:cd14106   93 GELQTLL-DEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILltseFPLGDIKLCDFG---ISRVIGEG---E 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 449 KLRIQNGWLCHLAPEIirqLSPDteedklPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14106  166 EIREILGTPDYVAPEI---LSYE------PISLATDMWSIGVLTYVLLTGHSPF 210
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
298-559 5.72e-12

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: 66.34  E-value: 5.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE------VAI----RLIDIErdnedQLKAFKREVMAYRQTRHENVVLFMGACMSP---PHLa 364
Cdd:cd05058    1 EVIGKGHFGCVYHGTLIDSdgqkihCAVkslnRITDIE-----EVEQFLKEGIIMKDFSHPNVLSLLGICLPSegsPLV- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGrTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsisgvlqa 443
Cdd:cd05058   75 VLPYMKHG-DLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVkVADFGL--------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 gRRD--DK--LRIQNGWLCHLAPEIIRQLSPDTEEdklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGM 518
Cdd:cd05058  145 -ARDiyDKeyYSVHNHTGAKLPVKWMALESLQTQK----FTTKSDVWSFGVLLWELMTRgAPPYPDVDSFDITVYLLQGR 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 519 K-------PNlsqigmgkEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05058  220 RllqpeycPD--------PLYEVMLSCWHPKPEMRPTFSELVSRISQI 259
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
298-495 6.29e-12

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: 66.58  E-value: 6.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE--------VAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd05091   12 EELGEDRFGKVYKGHLFGTapgeqtqaVAIKTLK-DKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVV---------------RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-YDNGKVVITDFG 433
Cdd:cd05091   91 CSHGDLHEFLvmrsphsdvgstdddKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLvFDKLNVKISDLG 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 434 LFsiSGVLQAgrrdDKLRIQNGwlchlAPEIIRQLSPDTEEDKlPFSKHSDVFALGTIWYEL 495
Cdd:cd05091  171 LF--REVYAA----DYYKLMGN-----SLLPIRWMSPEAIMYG-KFSIDSDIWSYGVVLWEV 220
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
300-561 6.36e-12

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: 66.57  E-value: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG------EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd05094   13 LGEGAFGKVFLAECYNlsptkdKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMKHG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVR----DAKIVLD-----------VNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsi 437
Cdd:cd05094   93 DLNKFLRahgpDAMILVDgqprqakgelgLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVkIGDFGM--- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 438 sgvlqagRRD----DKLRIQNGWLCHlapeiIRQLSPDTEEDKlPFSKHSDVFALGTIWYEL--HAREWPFKTQPAEAI- 510
Cdd:cd05094  170 -------SRDvystDYYRVGGHTMLP-----IRWMPPESIMYR-KFTTESDVWSFGVILWEIftYGKQPWFQLSNTEVIe 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568937340 511 -IWQMGTGMKPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKLPK 561
Cdd:cd05094  237 cITQGRVLERPRVCP----KEVYDIMLGCWQREPQQRLNIKEIYKILHALGK 284
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
297-504 6.46e-12

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: 65.80  E-value: 6.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHG---RWHGEVAIRLIDIER-DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14188    6 GKVLGKGGFAKCYEMtdlTTNKVYAAKIIPHSRvSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSISGVLQAGRRDdklr 451
Cdd:cd14188   86 RSMAHILKARKVLTE-PEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFInENMELKVGDFGLAARLEPLEHRRRT---- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 452 iqngwLC----HLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKT 504
Cdd:cd14188  161 -----ICgtpnYLSPEVLNKQGHGCE---------SDIWALGCVMYTMLLGRPPFET 203
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
296-517 6.55e-12

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: 66.59  E-value: 6.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFG---QVYHGRWHGEVAIRLID-IERDNEDQLKAFKRevmaYRQtrHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14175    5 VKETIGVGSYSvckRCVHKATNMEYAVKVIDkSKRDPSEEIEILLR----YGQ--HPNIITLKDVYDDGKHVYLVTELMR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-----DNGKVVITDFGLFSisgvlqagrr 446
Cdd:cd14175   79 GGELLDKILRQKFFSE-REASSVLHTICKTVEYLHSQGVVHRDLKPSNILYvdesgNPESLRICDFGFAK---------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 ddKLRIQNGWL---CH----LAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPFKTQPA---EAIIWQMGT 516
Cdd:cd14175  148 --QLRAENGLLmtpCYtanfVAPEVLKRQGYD---------EGCDIWSLGILLYTMLAGYTPFANGPSdtpEEILTRIGS 216

                 .
gi 568937340 517 G 517
Cdd:cd14175  217 G 217
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
300-510 8.50e-12

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: 65.62  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVY------HGRWHgevAIRLID----IERDNEDQLKAfKREVMayRQTRHENVV-LFMgACMSPPHLAIITS 368
Cdd:cd05123    1 LGKGSFGKVLlvrkkdTGKLY---AMKVLRkkeiIKRKEVEHTLN-ERNIL--ERVNHPFIVkLHY-AFQTEEKLYLVLD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAKIvLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQAGRRD 447
Cdd:cd05123   74 YVPGGELFSHLSKEGR-FPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDsDGHIKLTDFGLAK-----ELSSDG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 448 DKLRIQNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAI 510
Cdd:cd05123  148 DRTYTFCGTPEYLAPEVLL---------GKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEI 201
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
300-546 9.46e-12

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: 65.76  E-value: 9.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGE--------VAIRLIdiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd05092   13 LGEGAFGKVFLAECHNLlpeqdkmlVAVKAL--KEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVR----DAKIV----------LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGL-- 434
Cdd:cd05092   91 HGDLNRFLRshgpDAKILdggegqapgqLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVkIGDFGMsr 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 435 --FSISGVLQAGRRDDKLRiqngWlchLAPEII--RQlspdteedklpFSKHSDVFALGTIWYEL--HAREWPFKTQPAE 508
Cdd:cd05092  171 diYSTDYYRVGGRTMLPIR----W---MPPESIlyRK-----------FTTESDIWSFGVVLWEIftYGKQPWYQLSNTE 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568937340 509 AI--IWQMGTGMKPNLSQigmgKEISDILLFCWAFEQEER 546
Cdd:cd05092  233 AIecITQGRELERPRTCP----PEVYAIMQGCWQREPQQR 268
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
297-553 9.56e-12

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: 65.87  E-value: 9.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVY------HGRwhgEVAIRLIDIERDNED---QLKAFKREVMAYRQTRHENVVLFMGaCM---SPPHLA 364
Cdd:cd06651   12 GKLLGQGAFGRVYlcydvdTGR---ELAAKQVQFDPESPEtskEVSALECEIQLLKNLQHERIVQYYG-CLrdrAEKTLT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFS-ISGVLQ 442
Cdd:cd06651   88 IFMEYMPGGSVKDQLK-AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSaGNVKLGDFGASKrLQTICM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGrrdDKLRIQNGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTgmKPNL 522
Cdd:cd06651  167 SG---TGIRSVTGTPYWMSPEVISGEG---------YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT--QPTN 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568937340 523 SQI-GMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06651  233 PQLpSHISEHARDFLGCIFVEARHRPSAEELL 264
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
293-561 1.12e-11

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: 65.75  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHGE-------VAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPpHLAI 365
Cdd:cd05111    8 ELRKLKVLGSGVFGTVHKGIWIPEgdsikipVAIKVIQ-DRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGA-SLQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGlfsISGVLQAg 444
Cdd:cd05111   86 VTQLLPLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVqVADFG---VADLLYP- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 rrDDKLRIQNGwlcHLAPeiIRQLSPDTeedkLPFSKH---SDVFALG-TIWYELHAREWPFKT-QPAEAI-IWQMGTGM 518
Cdd:cd05111  162 --DDKKYFYSE---AKTP--IKWMALES----IHFGKYthqSDVWSYGvTVWEMMTFGAEPYAGmRLAEVPdLLEKGERL 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568937340 519 -KPNLSQIgmgkEISDILLFCWAFEQEERPTFTKLMDMLEKLPK 561
Cdd:cd05111  231 aQPQICTI----DVYMVMVKCWMIDENIRPTFKELANEFTRMAR 270
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
295-505 1.14e-11

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: 65.23  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRwH----GEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14072    3 RLLKTIGKGNFAKVKLAR-HvltgREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYS-VVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGrrdD 448
Cdd:cd14072   82 SGGEVFDyLVAHGR--MKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDaDMNIKIADFGF---SNEFTPG---N 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 449 KLRIQNGWLCHLAPEIIRQLSPDTEEdklpfskhSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14072  154 KLDTFCGSPPYAAPELFQGKKYDGPE--------VDVWSLGVILYTLVSGSLPFDGQ 202
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
300-554 1.25e-11

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: 65.51  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHG----RWHgEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMS----PPHLAIITSLCK 371
Cdd:cd14031   18 LGRGAFKTVYKGldteTWV-EVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKG--ILHKDLKSKNVFYD--NGKVVITDFGLFSIsgvlqagrrd 447
Cdd:cd14031   97 SGTLKTYLKRFK-VMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgpTGSVKIGDLGLATL---------- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 448 dkLRIQNGWLCHLAPEIirqLSPDTEEDKlpFSKHSDVFALGTIWYELHAREWPF-KTQPAEAIIWQMGTGMKPNLSQIG 526
Cdd:cd14031  166 --MRTSFAKSVIGTPEF---MAPEMYEEH--YDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRKVTSGIKPASFNKV 238
                        250       260
                 ....*....|....*....|....*...
gi 568937340 527 MGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd14031  239 TDPEVKEIIEGCIRQNKSERLSIKDLLN 266
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
295-434 1.31e-11

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: 65.10  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQ-LKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14073    4 ELLETLGKGTYGKVKLAIERAtgrEVAIKSIKKDKIEDEQdMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYA 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 371 KGRTLYSVVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:cd14073   84 SGGELYDYI-SERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDqNGNAKIADFGL 147
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
316-525 1.33e-11

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: 65.44  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 316 EVAIRLIDIERDNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKivLDVNKTRQIA 395
Cdd:cd06658   49 QVAVKKMDLRKQQRREL--LFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTR--MNEEQIATVC 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 396 QEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSisgvlQAGRRDDKLRIQNGWLCHLAPEIIrqlspdtee 474
Cdd:cd06658  125 LSVLRALSYLHNQGVIHRDIKSDSILLtSDGRIKLSDFGFCA-----QVSKEVPKRKSLVGTPYWMAPEVI--------- 190
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568937340 475 DKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI 525
Cdd:cd06658  191 SRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDS 241
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
298-508 1.36e-11

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: 65.80  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGEVAIRLIDIERDN----EDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEviiaKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsisgvLQAGRRDD-KLR 451
Cdd:cd05595   81 ELFFHLSRERVFTE-DRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKdGHIKITDFGL------CKEGITDGaTMK 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 452 IQNGWLCHLAPEIIrqlspdteEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAE 508
Cdd:cd05595  154 TFCGTPEYLAPEVL--------EDN-DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE 201
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
300-558 1.40e-11

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: 65.62  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG--------EVAIRLIdiERDNEDQLKA-FKREVMAYRQTRHENVVLFMGAC------------M 358
Cdd:cd05050   13 IGQGAFGRVFQARAPGllpyepftMVAVKML--KEEASADMQAdFQREAALMAEFDHPNIVKLLGVCavgkpmcllfeyM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 359 SPPHLAIITSLCKGRTLYSVVRDAKIV-------LDVNKTRQ--IAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVV 428
Cdd:cd05050   91 AYGDLNEFLRHRSPRAQCSLSHSTSSArkcglnpLPLSCTEQlcIAKQVAAGMAYLSERKFVHRDLATRNCLVgENMVVK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 429 ITDFGLFS--ISGVLQAGRRDDKLRIQngWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELhareWPFKTQP 506
Cdd:cd05050  171 IADFGLSRniYSADYYKASENDAIPIR--W---MPPESIFYNR---------YTTESDVWAYGVVLWEI----FSYGMQP 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 507 -----AEAIIWQMGTGMKPNLSQiGMGKEISDILLFCWAFEQEERPTFTKLMDMLEK 558
Cdd:cd05050  233 yygmaHEEVIYYVRDGNVLSCPD-NCPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
294-502 1.44e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 65.99  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHGRWHGEVAIRLIDIerdnedqLKafKREVMAYRQTRHEN-------------VVLFMGACMSP 360
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKC-------LK--KREILKMKQVQHVAqeksilmelshpfIVNMMCSFQDE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 361 PHLAIITSLCKGRTLYSVVRDA-KIVLDVNKTrqIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsis 438
Cdd:PTZ00263  91 NRVYFLLEFVVGGELFTHLRKAgRFPNDVAKF--YHAELVLAFEYLHSKDIIYRDLKPENLLLDNkGHVKVTDFGF---- 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 439 gvlqAGRRDDKLRIQNGWLCHLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPF 502
Cdd:PTZ00263 165 ----AKKVPDRTFTLCGTPEYLAPEVIQSKGHG---------KAVDWWTMGVLLYEFIAGYPPF 215
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
298-553 1.60e-11

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: 65.51  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHG---RWHGEVAIRLIDIERDNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd06656   25 EKIGQGASGTVYTAidiATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQAGRRDDKLRIQ 453
Cdd:cd06656  103 LTDVVTET--CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGmDGSVKLTDFGFCA-----QITPEQSKRSTM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 NGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIG-MGKEIS 532
Cdd:cd06656  176 VGTPYWMAPEVVTRKA---------YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPErLSAVFR 246
                        250       260
                 ....*....|....*....|.
gi 568937340 533 DILLFCWAFEQEERPTFTKLM 553
Cdd:cd06656  247 DFLNRCLEMDVDRRGSAKELL 267
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
296-502 1.61e-11

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: 64.60  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQV---YHGRWHGEVAIRLIDIER-DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14079    6 LGKTLGVGSFGKVklaEHELTGHKVAVKILNRQKiKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYS-VVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGVLQAGrrdDK 449
Cdd:cd14079   86 GGELFDyIVQKGR--LSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVkIADFGL---SNIMRDG---EF 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 450 LRIQNGWLCHLAPEIIrqlspdteEDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14079  158 LKTSCGSPNYAAPEVI--------SGKLYAGPEVDVWSCGVILYALLCGSLPF 202
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
300-559 1.68e-11

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: 65.34  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGE-------VAIRLIDIErDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAI--ITSLC 370
Cdd:cd05079   12 LGEGHFGKVELCRYDPEgdntgeqVAVKSLKPE-SGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIklIMEFL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLF-SISGVLQAGRRDD 448
Cdd:cd05079   91 PSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESeHQVKIGDFGLTkAIETDKEYYTVKD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 449 KLRIQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYEL----HAREWPFKT-----QPAEAiiwQMGTGMK 519
Cdd:cd05079  171 DLDSPVFW---YAPECLIQSK---------FYIASDVWSFGVTLYELltycDSESSPMTLflkmiGPTHG---QMTVTRL 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 520 PNLSQIGM--------GKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05079  236 VRVLEEGKrlprppncPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAI 283
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
296-505 1.71e-11

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: 65.11  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQV---YHGRWHGEVAIRLID------IERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:cd14084   10 MSRTLGSGACGEVklaYDKSTCKKVAIKIINkrkftiGSRREINKPRNIETEIEILKKLSHPCIIKIEDFFDAEDDYYIV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFSISGvlq 442
Cdd:cd14084   90 LELMEGGELFDRVVSNK-RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqeEECLIKITDFGLSKILG--- 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 443 agrRDDKLRIQNGWLCHLAPEIIRQlspdteEDKLPFSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14084  166 ---ETSLMKTLCGTPTYLAPEVLRS------FGTEGYTRAVDCWSLGVILFICLSGYPPFSEE 219
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
286-559 1.97e-11

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: 65.43  E-value: 1.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPFEQLEIGELIGKGRFGQVYHGRWHG----------EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMG 355
Cdd:cd05100    6 KWELSRTRLTLGKPLGEGCFGQVVMAEAIGidkdkpnkpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 356 ACMSPPHLAIITSLCKGRTLYSVVRDAKI---------------VLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV 420
Cdd:cd05100   86 ACTQDGPLYVLVEYASKGNLREYLRARRPpgmdysfdtcklpeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 421 FYDNGKVV-ITDFGLFSISGVLQAGRRDDKLRIQNGWlchLAPEIIRqlspdteeDKLpFSKHSDVFALGTIWYELHAR- 498
Cdd:cd05100  166 LVTEDNVMkIADFGLARDVHNIDYYKKTTNGRLPVKW---MAPEALF--------DRV-YTHQSDVWSFGVLLWEIFTLg 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 499 EWPFKTQPAEAIIWQMGTGMKPNlSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05100  234 GSPYPGIPVEELFKLLKEGHRMD-KPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRV 293
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
300-503 1.99e-11

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: 64.86  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVY--HGRWHGEV-AIRLID---IERDNEDQLKAFKREVMAYRQTRHenVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd05577    1 LGRGGFGEVCacQVKATGKMyACKKLDkkrIKKKKGETMALNEKIILEKVSSPF--IVSLAYAFETKDKLCLVLTLMNGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TL-YSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsisGVLQAGRRDDKLR 451
Cdd:cd05577   79 DLkYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDhGHVRISDLGL----AVEFKGGKKIKGR 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568937340 452 IqnGWLCHLAPEIIRQlspdteedKLPFSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd05577  155 V--GTHGYMAPEVLQK--------EVAYDFSVDWFALGCMLYEMIAGRSPFR 196
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
295-562 2.02e-11

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: 64.43  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYH-GRW--HGEVAIRLIdIERDNedqlKAFKREVMAYRQTR----HENVVLFMGACM--------S 359
Cdd:cd13975    3 KLGRELGRGQYGVVYAcDSWggHFPCALKSV-VPPDD----KHWNDLALEFHYTRslpkHERIVSLHGSVIdysygggsS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 360 PPHLAIITSLckGRTLYSVVRDAkivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlFSIS 438
Cdd:cd13975   78 IAVLLIMERL--HRDLYTGIKAG---LSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDkKNRAKITDLG-FCKP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 439 GVLQAGRrddklriQNGWLCHLAPEIirqlspdteedklpFSKH----SDVFALGTI-WYEL--HAR-EWPFKTQPAEAI 510
Cdd:cd13975  152 EAMMSGS-------IVGTPIHMAPEL--------------FSGKydnsVDVYAFGILfWYLCagHVKlPEAFEQCASKDH 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 511 IWQ-MGTGMKPNLSQIgMGKEISDILLFCWAFEQEERPTFTKLMDMLEKLPKR 562
Cdd:cd13975  211 LWNnVRKGVRPERLPV-FDEECWNLMEACWSGDPSQRPLLGIVQPKLQGIMDR 262
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
295-502 2.18e-11

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: 64.34  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRwH----GEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14071    3 DIERTIGKGNFAVVKLAR-HritkTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYS-VVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGrrdD 448
Cdd:cd14071   82 SNGEIFDyLAQHGR--MSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDaNMNIKIADFGF---SNFFKPG---E 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 449 KLRIQNGWLCHLAPEIIrqlspdteEDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14071  154 LLKTWCGSPPYAAPEVF--------EGKEYEGPQLDIWSLGVVLYVLVCGALPF 199
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
300-553 2.25e-11

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: 65.06  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR---WHGEVAIRLIDIE-RDNEDQLKAFKREVMAYRQTRHENVVLFMGaCMSPPHLA-IITSLCKGrt 374
Cdd:cd06633   29 IGHGSFGAVYFATnshTNEVVAIKKMSYSgKQTNEKWQDIIKEVKFLQQLKHPNTIEYKG-CYLKDHTAwLVMEYCLG-- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 lysvvrDAKIVLDVNKTRQIAQEI-------VKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSISGVLQAGRr 446
Cdd:cd06633  106 ------SASDLLEVHKKPLQEVEIaaithgaLQGLAYLHSHNMIHRDIKAGNILLtEPGQVKLADFGSASIASPANSFV- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 ddklriqnGWLCHLAPEIIRQLSPDTEEDKLpfskhsDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIG 526
Cdd:cd06633  179 --------GTPYWMAPEVILAMDEGQYDGKV------DIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQSNE 244
                        250       260
                 ....*....|....*....|....*..
gi 568937340 527 MGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06633  245 WTDSFRGFVDYCLQKIPQERPSSAELL 271
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
39-84 2.39e-11

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP 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: 410371  Cd Length: 55  Bit Score: 58.96  E-value: 2.39e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568937340  39 IKHRFSTK-YWMSQTCTVCGKGMLFG---LKCKNCKLKCHNKCTKEAP-PC 84
Cdd:cd20821    1 RPHRFVSKtVIKPETCVVCGKRIKFGkkaLKCKDCRVVCHPDCKDKLPlPC 51
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
298-498 2.62e-11

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: 64.68  E-value: 2.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE-VAIRLIDIErdneDQLK-AFKREVMAYRQTRHENVVLFMGACMSPPHLAI----ITSLCK 371
Cdd:cd14141    1 EIKARGRFGCVWKAQLLNEyVAVKIFPIQ----DKLSwQNEYEIYSLPGMKHENILQFIGAEKRGTNLDVdlwlITAFHE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAK----------GILHKDLKSKNVFYDNG-KVVITDFGLfsiSGV 440
Cdd:cd14141   77 KGSLTDYLKAN--VVSWNELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNlTACIADFGL---ALK 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 441 LQAGRRDDKLRIQNGWLCHLAPEIIrqlspdteEDKLPFSKHS----DVFALGTIWYELHAR 498
Cdd:cd14141  152 FEAGKSAGDTHGQVGTRRYMAPEVL--------EGAINFQRDAflriDMYAMGLVLWELASR 205
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
292-505 2.68e-11

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: 64.28  E-value: 2.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYH--GRWHG-EVAIRLIDIER-DNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKEcvERSTGkEFALKIIDKAKcCGKEHL--IENEVSILRRVKHPNIIMLIEEMDTPAELYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVLDVNKTRQIaQEIVKGMGYLHAKGILHKDLKSKNVF---YDNG--KVVITDFGLFSISgvlq 442
Cdd:cd14184   79 ELVKGGDLFDAITSSTKYTERDASAMV-YNLASALKYLHGLCIVHRDIKPENLLvceYPDGtkSLKLGDFGLATVV---- 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 443 agrrDDKLRIQNGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14184  154 ----EGPLYTVCGTPTYVAPEIIAETG---------YGLKVDIWAAGVITYILLCGFPPFRSE 203
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
298-495 2.91e-11

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: 64.98  E-value: 2.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVvlfmgacMSPPHLAIITSLCKGRTLYS 377
Cdd:cd05604    2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNV-------KHPFLVGLHYSFQTTDKLYF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 V---VRDAKIVLDVNKTRQIAQ--------EIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFSiSGVLQAgr 445
Cdd:cd05604   75 VldfVNGGELFFHLQRERSFPEprarfyaaEIASALGYLHSINIVYRDLKPENILLDSqGHIVLTDFGLCK-EGISNS-- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 rdDKLRIQNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYEL 495
Cdd:cd05604  152 --DTTTTFCGTPEYLAPEVIR---------KQPYDNTVDWWCLGSVLYEM 190
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
295-554 3.03e-11

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: 63.87  E-value: 3.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHGE---VAIRLIdIERDNEDQLKAFK-REVMAYRQ-TRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14050    4 TILSKLGEGSFGEVFKVRSREDgklYAVKRS-RSRFRGEKDRKRKlEEVERHEKlGEHPNCVRFIKAWEEKGILYIQTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKG--------------RTLYSVVRDakivldvnktrqiaqeIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGL 434
Cdd:cd14050   83 CDTslqqyceethslpeSEVWNILLD----------------LLKGLKHLHDHGLIHLDIKPANIFLSKDGVCkLGDFGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 435 fsisgVLQAgRRDDKLRIQNGWLCHLAPEIIRQLspdteedklpFSKHSDVFALGTIWYELharewpfKTQ---PAEAII 511
Cdd:cd14050  147 -----VVEL-DKEDIHDAQEGDPRYMAPELLQGS----------FTKAADIFSLGITILEL-------ACNlelPSGGDG 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568937340 512 W-QMGTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd14050  204 WhQLRQGYLPEEFTAGLSPELRSIIKLMMDPDPERRPTAEDLLA 247
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
320-504 3.17e-11

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: 63.87  E-value: 3.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 320 RLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSP-PHLAIITSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEI 398
Cdd:cd13994   29 RRRDDESKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDLhGKWCLVMEYCPGGDLFTLIEKAD-SLSLEEKDCFFKQI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 399 VKGMGYLHAKGILHKDLKSKNV-FYDNGKVVITDFGLFSISGVLQagrrDDKLRIQNGwLC----HLAPEIIRQLSPDte 473
Cdd:cd13994  108 LRGVAYLHSHGIAHRDLKPENIlLDEDGVLKLTDFGTAEVFGMPA----EKESPMSAG-LCgsepYMAPEVFTSGSYD-- 180
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568937340 474 edklPFSKhsDVFALGTIWYELHAREWPFKT 504
Cdd:cd13994  181 ----GRAV--DVWSCGIVLFALFTGRFPWRS 205
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
295-517 3.89e-11

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: 64.27  E-value: 3.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFG---QVYHGRWHGEVAIRLID-IERDNEDQLKAfkreVMAYRQtrHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14177    7 ELKEDIGVGSYSvckRCIHRATNMEFAVKIIDkSKRDPSEEIEI----LMRYGQ--HPNIITLKDVYDDGRYVYLVTELM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY--DNGK---VVITDFGLFSisgvlqagr 445
Cdd:cd14177   81 KGGELLDRILRQKFFSE-REASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmdDSANadsIRICDFGFAK--------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 rddKLRIQNGWL---CH----LAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQP---AEAIIWQMG 515
Cdd:cd14177  151 ---QLRGENGLLltpCYtanfVAPEVLMRQGYDAA---------CDIWSLGVLLYTMLAGYTPFANGPndtPEEILLRIG 218

                 ..
gi 568937340 516 TG 517
Cdd:cd14177  219 SG 220
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
300-493 4.18e-11

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: 63.50  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQV---YHGRWHGEVAIRLIdieRDNEDQLKAFKRE-VMAYRQTRHENVV-LFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd13987    1 LGEGTYGKVllaVHKGSGTKMALKFV---PKPSTKLKDFLREyNISLELSVHPHIIkTYDVAFETEDYYVFAQEYAPYGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-YDNG--KVVITDFGLFSISGVLqagrrddkLR 451
Cdd:cd13987   78 LFSIIPP-QVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLlFDKDcrRVKLCDFGLTRRVGST--------VK 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568937340 452 IQNGWLCHLAPEiirqLSPDTEEDKLPFSKHSDVFALGTIWY 493
Cdd:cd13987  149 RVSGTIPYTAPE----VCEAKKNEGFVVDPSIDVWAFGVLLF 186
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
288-559 4.50e-11

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: 63.74  E-value: 4.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEQLEigELIGKGRFGQVYHGRW------HGEVAIRLIDIERdNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPP 361
Cdd:cd05065    2 DVSCVKIE--EVIGAGEFGEVCRGRLklpgkrEIFVAIKTLKSGY-TEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGV 440
Cdd:cd05065   79 PVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCkVSDFGL---SRF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 LQAGRRDDKlriqngWLCHLAPEI-IRQLSPDTEEDKlPFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGM 518
Cdd:cd05065  156 LEDDTSDPT------YTSSLGGKIpIRWTAPEAIAYR-KFTSASDVWSYGIVMWEVMSYgERPYWDMSNQDVINAIEQDY 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568937340 519 K----PNLSQIgmgkeISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05065  229 RlpppMDCPTA-----LHQLMLDCWQKDRNLRPKFGQIVNTLDKM 268
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
298-502 4.71e-11

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 63.44  E-value: 4.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE---VAIRLIDIE--RDNEDqlkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd14192   10 EVLGGGRFGQVHKCTELSTgltLAAKIIKVKgaKEREE----VKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN---GKVVITDFGLfsisgvLQAGRRDDK 449
Cdd:cd14192   86 GELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNstgNQIKIIDFGL------ARRYKPREK 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 450 LRIQNGWLCHLAPEIIRQlspdteeDKLPFSkhSDVFALGTIWYELHAREWPF 502
Cdd:cd14192  160 LKVNFGTPEFLAPEVVNY-------DFVSFP--TDMWSVGVITYMLLSGLSPF 203
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
300-510 5.04e-11

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: 63.85  E-value: 5.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQV------YHGRwhgEVAIRLIDIERDNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd06659   29 IGEGSTGVVciarekHSGR---QVAVKMMDLRKQQRREL--LFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVrdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQAGRRDDKLRI 452
Cdd:cd06659  104 ALTDIV--SQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTlDGRVKLSDFGFCA-----QISKDVPKRKS 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 453 QNGWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWP-FKTQPAEAI 510
Cdd:cd06659  177 LVGTPYWMAPEVI---------SRCPYGTEVDIWSLGIMVIEMVDGEPPyFSDSPVQAM 226
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
300-553 5.16e-11

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: 63.56  E-value: 5.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHG----RWHgEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPH----LAIITSLCK 371
Cdd:cd14032    9 LGRGSFKTVYKGldteTWV-EVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKG--ILHKDLKSKNVFYD--NGKVVITDFGLFSIsgvlqagRRD 447
Cdd:cd14032   88 SGTLKTYLKRFK-VMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgpTGSVKIGDLGLATL-------KRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 448 DKLRIQNGWLCHLAPEIIRQlspdteedklPFSKHSDVFALGTIWYELHAREWPF-KTQPAEAIIWQMGTGMKPNLSQIG 526
Cdd:cd14032  160 SFAKSVIGTPEFMAPEMYEE----------HYDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRKVTCGIKPASFEKV 229
                        250       260
                 ....*....|....*....|....*..
gi 568937340 527 MGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd14032  230 TDPEIKEIIGECICKNKEERYEIKDLL 256
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
404-555 5.19e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 65.28  E-value: 5.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 404 YLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsiSGVLQAGRRDDKLRIQNGWLCHLAPEIIRqlspdteedKLPFSKH 482
Cdd:PTZ00283 158 HVHSKHMIHRDIKSANILLcSNGLVKLGDFGF---SKMYAATVSDDVGRTFCGTPYYVAPEIWR---------RKPYSKK 225
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 483 SDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTG----MKPNLSqigmgKEISDILLFCWAFEQEERPTFTKLMDM 555
Cdd:PTZ00283 226 ADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGrydpLPPSIS-----PEMQEIVTALLSSDPKRRPSSSKLLNM 297
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
300-502 5.47e-11

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: 63.40  E-value: 5.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFG---QVYHGRWHGEVAIRLIDIErdnEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG---- 372
Cdd:cd14110   11 INRGRFSvvrQCEEKRSGQMLAAKIIPYK---PEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGpell 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 -----RTLYSVVrdakivldvnKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFG---LFSISGVLQA 443
Cdd:cd14110   88 ynlaeRNSYSEA----------EVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLkIVDLGnaqPFNQGKVLMT 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 444 GRRDDklriqngWLCHLAPEIIrqlspdTEEDKLPfskHSDVFALGTIWYELHAREWPF 502
Cdd:cd14110  158 DKKGD-------YVETMAPELL------EGQGAGP---QTDIWAIGVTAFIMLSADYPV 200
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
288-556 5.88e-11

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: 63.80  E-value: 5.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEQLEIGELIGKGRFGQVY--------------------HGRwHGEVAIRLIDIERdNEDQLKAFKREVMAYRQTRH 347
Cdd:cd05096    1 KFPRGHLLFKEKLGEGQFGEVHlcevvnpqdlptlqfpfnvrKGR-PLLVAVKILRPDA-NKNARNDFLKEVKILSRLKD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 348 ENVVLFMGACMSPPHLAIITSLCK----GRTLYSVVRDAK--------------IVLDVNKTRQIAQEIVKGMGYLHAKG 409
Cdd:cd05096   79 PNIIRLLGVCVDEDPLCMITEYMEngdlNQFLSSHHLDDKeengndavppahclPAISYSSLLHVALQIASGMKYLSSLN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 410 ILHKDLKSKNVFY-DNGKVVITDFGLfsiSGVLQAGrrdDKLRIQN---------GWLCHLAPEiirqlspdteedklpF 479
Cdd:cd05096  159 FVHRDLATRNCLVgENLTIKIADFGM---SRNLYAG---DYYRIQGravlpirwmAWECILMGK---------------F 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 480 SKHSDVFALG-TIWYELH-AREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKE------ISDILLFCWAFEQEERPTFTK 551
Cdd:cd05096  218 TTASDVWAFGvTLWEILMlCKEQPYGELTDEQVIENAGEFFRDQGRQVYLFRPppcpqgLYELMLQCWSRDCRERPSFSD 297

                 ....*
gi 568937340 552 LMDML 556
Cdd:cd05096  298 IHAFL 302
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
293-554 6.08e-11

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: 63.39  E-value: 6.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHG--EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHE-NVVLFMGACMSPPHLAIITSL 369
Cdd:cd14131    2 PYEILKQLGKGGSSKVYKVLNPKkkIYALKRVDLEGADEQTLQSYKNEIELLKKLKGSdRIIQLYDYEVTDEDDYLYMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVV----RDAKIvlDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGlfsISGVLQagr 445
Cdd:cd14131   82 ECGEIDLATIlkkkRPKPI--DPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGRLKLIDFG---IAKAIQ--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 rDDKLRI----QNGWLCHLAPEIIRQLSPDTEEDK-LPFSKHSDVFALGTIWYELHAREWPFK------------TQPAE 508
Cdd:cd14131  154 -NDTTSIvrdsQVGTLNYMSPEAIKDTSASGEGKPkSKIGRPSDVWSLGCILYQMVYGKTPFQhitnpiaklqaiIDPNH 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340 509 AIIWqmgtgmkPNLSqigmGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd14131  233 EIEF-------PDIP----NPDLIDVMKRCLQRDPKKRPSIPELLN 267
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
288-558 6.14e-11

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: 63.47  E-value: 6.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEQLEIGELIGKGRFGQVYHGRWHGE-------------------VAIRLIDIERdNEDQLKAFKREVMAYRQTRHE 348
Cdd:cd05095    1 EFPRKLLTFKEKLGEGQFGEVHLCEAEGMekfmdkdfalevsenqpvlVAVKMLRADA-NKNARNDFLKEIKIMSRLKDP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 349 NVVLFMGACMSPPHLAIITSLCKGRTLY-----------SVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKS 417
Cdd:cd05095   80 NIIRLLAVCITDDPLCMITEYMENGDLNqflsrqqpegqLALPSNALTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 418 KNVFY-DNGKVVITDFGLfsiSGVLQAGrrdDKLRIQNgwlchLAPEIIRQLSpdtEEDKL--PFSKHSDVFALG-TIWY 493
Cdd:cd05095  160 RNCLVgKNYTIKIADFGM---SRNLYSG---DYYRIQG-----RAVLPIRWMS---WESILlgKFTTASDVWAFGvTLWE 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 494 ELH-AREWPFKTQPAEAIIWQMG-----TGMKPNLSQIGMGKE-ISDILLFCWAFEQEERPTFTKLMDMLEK 558
Cdd:cd05095  226 TLTfCREQPYSQLSDEQVIENTGeffrdQGRQTYLPQPALCPDsVYKLMLSCWRRDTKDRPSFQEIHTLLQE 297
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
295-502 6.59e-11

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: 63.04  E-value: 6.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRwHGE----VAIRLIDIERDNEDQLKAF-KREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14081    4 RLGKTLGKGQTGLVKLAK-HCVtgqkVAIKIVNKEKLSKESVLMKvEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGvlqagrRDD 448
Cdd:cd14081   83 VSGGELFDYLVK-KGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDeKNNIKIADFGMASLQP------EGS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 449 KLRIQNGWLCHLAPEIIRQLSPDteedklpfSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14081  156 LLETSCGSPHYACPEVIKGEKYD--------GRKADIWSCGVILYALLVGALPF 201
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
295-503 7.02e-11

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: 63.06  E-value: 7.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGR--WHGE-VAIRLIDI-ERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd08224    3 EIEKKIGKGQFSVVYRARclLDGRlVALKKVQIfEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLELA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKivldvnKTRQIAQE---------IVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL---FSi 437
Cdd:cd08224   83 DAGDLSRLIKHFK------KQKRLIPErtiwkyfvqLCSALEHMHSKRIMHRDIKPANVFITaNGVVKLGDLGLgrfFS- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 438 SGVLQAGRRddklriqNGWLCHLAPEIIRqlspdteEDKLPFSkhSDVFALGTIWYELHAREWPFK 503
Cdd:cd08224  156 SKTTAAHSL-------VGTPYYMSPERIR-------EQGYDFK--SDIWSLGCLLYEMAALQSPFY 205
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
292-502 7.04e-11

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: 63.12  E-value: 7.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHGEVAIRLID--IERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkfLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFSISGVLqagr 445
Cdd:cd14088   81 ATGREVFDWILDQGYYSE-RDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYynrlKNSKIVISDFHLAKLENGL---- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 446 rddkLRIQNGWLCHLAPEII-RQlspdteedklPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14088  156 ----IKEPCGTPEYLAPEVVgRQ----------RYGRPVDCWAIGVIMYILLSGNPPF 199
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
296-502 7.10e-11

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: 62.95  E-value: 7.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHG---RWHGEVAIRLIDIERDNEDQLKAF-KREVMAYRQTRHENVVlfmgacmsppHLAIITSLCK 371
Cdd:cd14164    4 LGTTIGEGSFSKVKLAtsqKYCCKVAIKIVDRRRASPDFVQKFlPRELSILRRVNHPNIV----------QMFECIEVAN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRtLYSVVRDAKIVL----------DVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY--DNGKVVITDFGlFSisg 439
Cdd:cd14164   74 GR-LYIVMEAAATDLlqkiqevhhiPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLsaDDRKIKIADFG-FA--- 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 440 vLQAGRRDDKLRIQNGWLCHLAPEIIRQLSPDteedklpfSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14164  149 -RFVEDYPELSTTFCGSRAYTPPEVILGTPYD--------PKKYDVWSLGVVLYVMVTGTMPF 202
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
290-554 8.22e-11

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: 63.09  E-value: 8.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQLKAfkrEVMAYRQ-TRHENVVLFMGACMSPPH--- 362
Cdd:cd06639   20 PSDTWDIIETIGKGTYGKVYkvtNKKDGSLAAVKILDPISDVDEEIEA---EYNILRSlPNHPNVVKFYGMFYKADQyvg 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 --LAIITSLCKGRTLYSVVRDAKIV---LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlfs 436
Cdd:cd06639   97 gqLWLVLELCNGGSVTELVKGLLKCgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTtEGGVKLVDFG--- 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 437 ISGVLQAGRRDDKLRIqnGWLCHLAPEIIrqlSPDTEEDKlPFSKHSDVFALGTIWYELHAREWP-FKTQPAEAiIWQMG 515
Cdd:cd06639  174 VSAQLTSARLRRNTSV--GTPFWMAPEVI---ACEQQYDY-SYDARCDVWSLGITAIELADGDPPlFDMHPVKA-LFKIP 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568937340 516 TGMKPNLSQIGMG-KEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd06639  247 RNPPPTLLNPEKWcRGFSHFISQCLIKDFEKRPSVTHLLE 286
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
299-495 1.02e-10

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: 62.28  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRWHGE-VAIRLIDierdNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPhlAIITSLCKGRTLYS 377
Cdd:cd14068    1 LLGDGGFGSVYRAVYRGEdVAVKIFN----KHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSLDA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 VVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV----FYDNGKVV--ITDFGLFSISGVLqagrrddKLR 451
Cdd:cd14068   75 LLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVllftLYPNCAIIakIADYGIAQYCCRM-------GIK 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568937340 452 IQNGWLCHLAPEIIRqlspdteeDKLPFSKHSDVFALGTIWYEL 495
Cdd:cd14068  148 TSEGTPGFRAPEVAR--------GNVIYNQQADVYSFGLLLYDI 183
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
289-558 1.02e-10

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: 62.87  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 289 IPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSP 360
Cdd:cd05049    2 IKRDTIVLKRELGEGAFGKVFLGECYNlepeqdkmLVAVKTLK-DASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 361 PHLAIITSLCKGRTLYSVVR----DAKIVL--DVNKTR-------QIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKV 427
Cdd:cd05049   81 DPLLMVFEYMEHGDLNKFLRshgpDAAFLAseDSAPGEltlsqllHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 428 V-ITDFGLfsisgvlqagRRD----DKLRIQNGwlcHLAPeiIRQLSPDTEEDKlPFSKHSDVFALGTIWYEL--HAREW 500
Cdd:cd05049  161 VkIGDFGM----------SRDiystDYYRVGGH---TMLP--IRWMPPESILYR-KFTTESDVWSFGVVLWEIftYGKQP 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 501 PFKTQPAEAI--IWQMGTGMKPNlsqiGMGKEISDILLFCWAFEQEERPTFTKLMDMLEK 558
Cdd:cd05049  225 WFQLSNTEVIecITQGRLLQRPR----TCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
300-548 1.07e-10

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: 62.70  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG-----EVAIRLIDIERDNEDQLKaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd05087    5 IGHGWFGKVFLGEVNSglsstQVVVKELKASASVQDQMQ-FLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAK----IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKN-VFYDNGKVVITDFGLFSISGVLQAGRRDDK 449
Cdd:cd05087   84 LKGYLRSCRaaesMAPDPLTLQRMACEVACGLLHLHRNNFVHSDLALRNcLLTADLTVKIGDYGLSHCKYKEDYFVTADQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIQNGWlchLAPEIIRQLSPD-TEEDKlpfSKHSDVFALG-TIW--YELHAREWPFKTQP---AEAIIWQMGTGMKPNL 522
Cdd:cd05087  164 LWVPLRW---IAPELVDEVHGNlLVVDQ---TKQSNVWSLGvTIWelFELGNQPYRHYSDRqvlTYTVREQQLKLPKPQL 237
                        250       260
                 ....*....|....*....|....*.
gi 568937340 523 sQIGMGKEISDILLFCWaFEQEERPT 548
Cdd:cd05087  238 -KLSLAERWYEVMQFCW-LQPEQRPT 261
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
295-502 1.07e-10

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: 62.50  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQL----KAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14105    8 DIGEELGSGQFAVVKKCREKStglEYAAKFIKKRRSKASRRgvsrEDIEREVSILRQVLHPNIITLHDVFENKTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-----DNGKVVITDFGLfsisgvlq 442
Cdd:cd14105   88 ELVAGGELFDFLAE-KESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldknvPIPRIKLIDFGL-------- 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 443 AGRRDDKLRIQN--GWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14105  159 AHKIEDGNEFKNifGTPEFVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPF 211
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
295-505 1.09e-10

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: 62.46  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY--HGRWHGE-VAIRLIDIERDNEDQLKAFKREVMAYRQT-------------RHENVVLFMGACM 358
Cdd:cd14077    4 EFVKTIGAGSMGKVKlaKHIRTGEkCAIKIIPRASNAGLKKEREKRLEKEISRDirtireaalssllNHPHICRLRDFLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 359 SPPHLAIITSLCKGRTLYS-VVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFS 436
Cdd:cd14077   84 TPNHYYMLFEYVDGGQLLDyIISHGK--LKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISkSGNIKIIDFGLSN 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 437 ISgvlqagRRDDKLRIQNGWLCHLAPEIIrQLSPDTeedklpfSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14077  162 LY------DPRRLLRTFCGSLYFAAPELL-QAQPYT-------GPEVDVWSFGVVLYVLVCGKVPFDDE 216
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
297-504 1.29e-10

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: 62.26  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYH-------GRWHGEVAIRLIDIERDNEDQLKAfkrEVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14187   12 GRFLGKGGFAKCYEitdadtkEVFAGKIVPKSLLLKPHQKEKMSM---EIAIHRSLAHQHVVGFHGFFEDNDFVYVVLEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsISGVLQAGRRDD 448
Cdd:cd14187   89 CRRRSLLELHKRRKALTE-PEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLnDDMEVKIGDFGL--ATKVEYDGERKK 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 449 KLriqNGWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPFKT 504
Cdd:cd14187  166 TL---CGTPNYIAPEVL---------SKKGHSFEVDIWSIGCIMYTLLVGKPPFET 209
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
294-549 1.30e-10

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: 62.11  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHGRWHGEVAIRLIDIE-------RDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLaII 366
Cdd:cd05037    1 ITFHEHLGQGTFTNIYDGILREVGDGRVQEVEvllkvldSDHRDISESFFETASLMSQISHKHLVKLYGVCVADENI-MV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVitdFGLFSISGVLQ 442
Cdd:cd05037   80 QEYVRYGPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLaregLDGYPP---FIKLSDPGVPI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGRRDDKLRIQNGWlchLAPEIIRQLS--PDTEEDKLPFskhsdvfalGTIWYELHAR-EWPFKT-QPAEAIIWQMGTGM 518
Cdd:cd05037  157 TVLSREERVDRIPW---IAPECLRNLQanLTIAADKWSF---------GTTLWEICSGgEEPLSAlSSQEKLQFYEDQHQ 224
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 519 KPNLSQIGMGKEISDillfCWAFEQEERPTF 549
Cdd:cd05037  225 LPAPDCAELAELIMQ----CWTYEPTKRPSF 251
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
298-510 1.33e-10

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: 63.18  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGEVAIRLIDIERDN----EDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd05593   21 KLLGKGTFGKVILVREKASGKYYAMKILKKEviiaKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSiSGVLQAGrrddKLRI 452
Cdd:cd05593  101 ELFFHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDkDGHIKITDFGLCK-EGITDAA----TMKT 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 453 QNGWLCHLAPEIIrqlspdteEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAEAI 510
Cdd:cd05593  175 FCGTPEYLAPEVL--------EDN-DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 223
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
300-502 1.35e-10

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: 62.24  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYhgrwhgevairLIDIERDNED-QLKAF-KREVMAYRQTRH---ENVVlfMGACMSP------------PH 362
Cdd:cd05572    1 LGVGGFGRVE-----------LVQLKSKGRTfALKCVkKRHIVQTRQQEHifsEKEI--LEECNSPfivklyrtfkdkKY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 LAIITSLCKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVL 441
Cdd:cd05572   68 LYMLMEYCLGGELWTILRD-RGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDsNGYVKLVDFGF---AKKL 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 442 QAGRRDdklriqngW-LC----HLAPEIIRQLSPDteedklpFSkhSDVFALGTIWYELHAREWPF 502
Cdd:cd05572  144 GSGRKT--------WtFCgtpeYVAPEIILNKGYD-------FS--VDYWSLGILLYELLTGRPPF 192
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
295-434 1.54e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 63.66  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHG---RWHGEVAIRLI--DIERDNEDQLKaFKREVMAYRQTRHENVV-------------LFMga 356
Cdd:NF033483  10 EIGERIGRGGMAEVYLAkdtRLDRDVAVKVLrpDLARDPEFVAR-FRREAQSAASLSHPNIVsvydvgedggipyIVM-- 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 357 cmspphlaiitSLCKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:NF033483  87 -----------EYVDGRTLKDYIRE-HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITkDGRVKVTDFGI 153
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
287-559 1.59e-10

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: 63.12  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLID-IERDNEDQLKAFKREVMAYRQTrHENVVLFMGAC 357
Cdd:cd05105   32 WEFPRDGLVLGRILGSGAFGKVVEGTAYGlsrsqpvmKVAVKMLKpTARSSEKQALMSELKIMTHLGP-HLNIVNLLGAC 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 358 MSPPHLAIITSLC--------------------------------------------------KG--------------- 372
Cdd:cd05105  111 TKSGPIYIITEYCfygdlvnylhknrdnflsrhpekpkkdldifginpadestrsyvilsfenKGdymdmkqadttqyvp 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 --------------RTLYS----------------VVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY 422
Cdd:cd05105  191 mleikeaskysdiqRSNYDrpasykgsndsevknlLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLL 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 423 DNGKVV-ITDFGLfsisgvlqagRRD---DKLRIQNGwlCHLAPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHAR 498
Cdd:cd05105  271 AQGKIVkICDFGL----------ARDimhDSNYVSKG--STFLP--VKWMAPESIFDNL-YTTLSDVWSYGILLWEIFSL 335
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 499 -EWPFKTQPAEAIIW---QMGTGM-KPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05105  336 gGTPYPGMIVDSTFYnkiKSGYRMaKPDHAT----QEVYDIMVKCWNSEPEKRPSFLHLSDIVESL 397
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
298-498 1.81e-10

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: 61.97  E-value: 1.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE-VAIRLIDIErdnEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA----IITSLCKG 372
Cdd:cd14140    1 EIKARGRFGCVWKAQLMNEyVAVKIFPIQ---DKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEmelwLITAFHDK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLH-----AKG------ILHKDLKSKNVFYDNG-KVVITDFGLfsiSGV 440
Cdd:cd14140   78 GSLTDYLKGN--IVSWNELCHIAETMARGLSYLHedvprCKGeghkpaIAHRDFKSKNVLLKNDlTAVLADFGL---AVR 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 441 LQAGRRDDKLRIQNGWLCHLAPEIIrqlspdteEDKLPFSKHS----DVFALGTIWYELHAR 498
Cdd:cd14140  153 FEPGKPPGDTHGQVGTRRYMAPEVL--------EGAINFQRDSflriDMYAMGLVLWELVSR 206
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
295-517 1.83e-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: 62.34  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFG---QVYHGRWHGEVAIRLID-IERDNEDQLKAFKRevmaYRQtrHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14178    6 EIKEDIGIGSYSvckRCVHKATSTEYAVKIIDkSKRDPSEEIEILLR----YGQ--HPNIITLKDVYDDGKFVYLVMELM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVV--------RDAKIVLDVnktrqiaqeIVKGMGYLHAKGILHKDLKSKNVFY-----DNGKVVITDFGLFSi 437
Cdd:cd14178   80 RGGELLDRIlrqkcfseREASAVLCT---------ITKTVEYLHSQGVVHRDLKPSNILYmdesgNPESIRICDFGFAK- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 438 sgvlqagrrddKLRIQNGWL---CH----LAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQP---A 507
Cdd:cd14178  150 -----------QLRAENGLLmtpCYtanfVAPEVLKRQGYDAA---------CDIWSLGILLYTMLAGFTPFANGPddtP 209
                        250
                 ....*....|
gi 568937340 508 EAIIWQMGTG 517
Cdd:cd14178  210 EEILARIGSG 219
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
295-517 1.87e-10

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: 62.73  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFG---QVYHGRWHGEVAIRLIDIE-RDNEDQLKAFKRevmaYRQtrHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14176   22 EVKEDIGVGSYSvckRCIHKATNMEFAVKIIDKSkRDPTEEIEILLR----YGQ--HPNIITLKDVYDDGKYVYVVTELM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY--DNGK---VVITDFGLFSisgvlqagr 445
Cdd:cd14176   96 KGGELLDKILRQKFFSE-REASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdESGNpesIRICDFGFAK--------- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 rddKLRIQNGWL---CH----LAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQP---AEAIIWQMG 515
Cdd:cd14176  166 ---QLRAENGLLmtpCYtanfVAPEVLERQGYDAA---------CDIWSLGVLLYTMLTGYTPFANGPddtPEEILARIG 233

                 ..
gi 568937340 516 TG 517
Cdd:cd14176  234 SG 235
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
298-502 1.98e-10

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: 61.47  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQLKAFKREVMayRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd14190   10 EVLGGGKFGKVHtctEKRTGLKLAAKVINKQNSKDKEMVLLEIQVM--NQLNHRNLIQLYEAIETPNEIVLFMEYVEGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG---KVVITDFGLfsisgvlqaGRR---DD 448
Cdd:cd14190   88 LFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRtghQVKIIDFGL---------ARRynpRE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 449 KLRIQNGWLCHLAPEIIRQlspdteeDKLPFSkhSDVFALGTIWYELHAREWPF 502
Cdd:cd14190  159 KLKVNFGTPEFLSPEVVNY-------DQVSFP--TDMWSMGVITYMLLSGLSPF 203
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
295-502 2.04e-10

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: 61.79  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPH--LAIITSL 369
Cdd:cd08217    3 EVLETIGKGSFGTVRkvrRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANttLYIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIV---LDVNKTRQIAQEIVKGMGYLHAKG-----ILHKDLKSKNVFYDNGKVV-ITDFGLfsiSGV 440
Cdd:cd08217   83 CEGGDLAQLIKKCKKEnqyIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVkLGDFGL---ARV 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 441 LQAGRRDDKLRIqnGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd08217  160 LSHDSSFAKTYV--GTPYYMSPELLN---------EQSYDEKSDIWSLGCLIYELCALHPPF 210
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
300-433 2.06e-10

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: 62.12  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWH---GEVAIRL---IDIERDNEDQlkafKREVMAYRQTRHENVV-LF-MGACMSPPHLAIITSLCK 371
Cdd:cd13988    1 LGQGATANVFRGRHKktgDLYAVKVfnnLSFMRPLDVQ----MREFEVLKKLNHKNIVkLFaIEEELTTRHKVLVMELCP 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 372 GRTLYSVVRDAKIV--LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKN---VFYDNGKVV--ITDFG 433
Cdd:cd13988   77 CGSLYTVLEEPSNAygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNimrVIGEDGQSVykLTDFG 145
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
311-559 2.41e-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: 61.44  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 311 GRWHGEVAIrLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDA-----KIV 385
Cdd:cd14044   27 GKYDKKVVI-LKDLKNNEGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKisypdGTF 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 386 LDVNKTRQIAQEIVKGMGYLHAKGI-LHKDLKSKNVFYDNGKVV-ITDFGLFSIsgvlQAGRRDDklriqngWLchlAPE 463
Cdd:cd14044  106 MDWEFKISVMYDIAKGMSYLHSSKTeVHGRLKSTNCVVDSRMVVkITDFGCNSI----LPPSKDL-------WT---APE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 464 IIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQP----AEAIIW-QMGTGMKP-----NLSQIGMgKEISD 533
Cdd:cd14044  172 HLRQAG---------TSQKGDVYSYGIIAQEIILRKETFYTAAcsdrKEKIYRvQNPKGMKPfrpdlNLESAGE-REREV 241
                        250       260
                 ....*....|....*....|....*...
gi 568937340 534 ILLF--CWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14044  242 YGLVknCWEEDPEKRPDFKKIENTLAKI 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
295-502 2.51e-10

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: 61.56  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQL----KAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14195    8 EMGEELGSGQFAIVRKCREKGtgkEYAAKFIKKRRLSSSRRgvsrEEIEREVNILREIQHPNIITLHDIFENKTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-----DNGKVVITDFGlfsISGVLQ 442
Cdd:cd14195   88 ELVSGGELFDFLAE-KESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldknvPNPRIKLIDFG---IAHKIE 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGrrdDKLRIQNGWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14195  164 AG---NEFKNIFGTPEFVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPF 211
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
295-529 2.93e-10

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: 61.50  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY---HGRWHGEVAIRLIDIE-RDNEDQLkafkrEVMaYRQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14091    3 EIKEEIGKGSYSVCKrciHKATGKEYAVKIIDKSkRDPSEEI-----EIL-LRYGQHPNIITLRDVYDDGNSVYLVTELL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVV--------RDAKIVLDVnktrqiaqeIVKGMGYLHAKGILHKDLKSKNVFY--DNGK---VVITDFGlFSi 437
Cdd:cd14091   77 RGGELLDRIlrqkffseREASAVMKT---------LTKTVEYLHSQGVVHRDLKPSNILYadESGDpesLRICDFG-FA- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 438 sgvlqagrrdDKLRIQNGWL---CH----LAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPFKTQP---A 507
Cdd:cd14091  146 ----------KQLRAENGLLmtpCYtanfVAPEVLKKQGYD---------AACDIWSLGVLLYTMLAGYTPFASGPndtP 206
                        250       260
                 ....*....|....*....|..
gi 568937340 508 EAIiwqmgtgmkpnLSQIGMGK 529
Cdd:cd14091  207 EVI-----------LARIGSGK 217
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
298-434 3.86e-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: 60.91  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWH--GE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKgRT 374
Cdd:cd07839    6 EKIGEGTYGTVFKAKNRetHEiVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCD-QD 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 375 LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL 434
Cdd:cd07839   85 LKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLInKNGELKLADFGL 145
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
298-523 4.03e-10

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: 61.57  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQT-----RHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd05602   13 KVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVllknvKHPFLVGLHFSFQTTDKLYFVLDYING 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFsisgvlqagRRDDKLR 451
Cdd:cd05602   93 GELFYHLQRERCFLE-PRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSqGHIVLTDFGLC---------KENIEPN 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 452 IQNGWLC----HLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAI---IWQMGTGMKPNLS 523
Cdd:cd05602  163 GTTSTFCgtpeYLAPEVLH---------KQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMydnILNKPLQLKPNIT 232
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
317-525 4.06e-10

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: 61.19  E-value: 4.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 317 VAIRLIDIERDNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKivLDVNKTRQIAQ 396
Cdd:cd06657   48 VAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTR--MNEEQIAAVCL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 EIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQAGRRDDKLRIQNGWLCHLAPEIIrqlspdteeD 475
Cdd:cd06657  124 AVLKALSVLHAQGVIHRDIKSDSILLThDGRVKLSDFGFCA-----QVSKEVPRRKSLVGTPYWMAPELI---------S 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568937340 476 KLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQI 525
Cdd:cd06657  190 RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNL 239
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
300-510 4.06e-10

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: 60.53  E-value: 4.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd06648   15 IGEGSTGIVciaTDKSTGRQVAVKKMDLRKQQRREL--LFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLDvnktrQIA---QEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSisgvlQAGRRDDKLRI 452
Cdd:cd06648   93 DIVTHTRMNEE-----QIAtvcRAVLKALSFLHSQGVIHRDIKSDSILLtSDGRVKLSDFGFCA-----QVSKEVPRRKS 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 453 QNGWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWP-FKTQPAEAI 510
Cdd:cd06648  163 LVGTPYWMAPEVI---------SRLPYGTEVDIWSLGIMVIEMVDGEPPyFNEPPLQAM 212
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
293-433 4.15e-10

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: 60.98  E-value: 4.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWH--GE-VAIRLIDierdnedQLKAFK-REVMAYRQTRHENVVLFMGACmspphlaiITS 368
Cdd:cd14137    5 SYTIEKVIGSGSFGVVYQAKLLetGEvVAIKKVL-------QDKRYKnRELQIMRRLKHPNIVKLKYFF--------YSS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGR-------------TLYSVVRD---AKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD--NGKVVIT 430
Cdd:cd14137   70 GEKKDevylnlvmeympeTLYRVIRHyskNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpeTGVLKLC 149

                 ...
gi 568937340 431 DFG 433
Cdd:cd14137  150 DFG 152
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
300-561 4.60e-10

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: 60.82  E-value: 4.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG------EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd05093   13 LGEGAFGKVFLAECYNlcpeqdKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVR----DAKIVLDVNKTRQ--------IAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsisgv 440
Cdd:cd05093   93 DLNKFLRahgpDAVLMAEGNRPAEltqsqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLVgENLLVKIGDFGM------ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 lqagRRD----DKLRIQNGWLCHlapeiIRQLSPDTEEDKlPFSKHSDVFALGTIWYEL--HAREWPFKTQPAEAI--IW 512
Cdd:cd05093  167 ----SRDvystDYYRVGGHTMLP-----IRWMPPESIMYR-KFTTESDVWSLGVVLWEIftYGKQPWYQLSNNEVIecIT 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568937340 513 QMGTGMKPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKLPK 561
Cdd:cd05093  237 QGRVLQRPRTCP----KEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAK 281
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
296-502 4.71e-10

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: 60.56  E-value: 4.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLKAF-KREVMAYRQTRHENVV----LFMgacMSPPHLAIIT 367
Cdd:cd14165    5 LGINLGEGSYAKVksaYSERLKCNVAIKIIDKKKAPDDFVEKFlPRELEILARLNHKSIIktyeIFE---TSDGKVYIVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGlFSisgvlQAGRR 446
Cdd:cd14165   82 ELGVQGDLLEFIK-LRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDfNIKLTDFG-FS-----KRCLR 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 447 DDKLRIQ-----NGWLCHLAPEIIRQLSPDteedklpfSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14165  155 DENGRIVlsktfCGSAAYAAPEVLQGIPYD--------PRIYDIWSLGVILYIMVCGSMPY 207
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
293-495 4.98e-10

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


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 60.81  E-value: 4.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRwH---GE-VAIRLIDIERDNEDQLKAFKREVMAYRQTR-HENVVLFMGACMSPPHLAIIT 367
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAK-DretGEtVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLcKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLfsisGVLQAGRR 446
Cdd:cd07832   80 EY-MLSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIsSTGVLKIADFGL----ARLFSEED 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568937340 447 DDKLRIQNGWLCHLAPEII---RQLSPDTeedklpfskhsDVFALGTIWYEL 495
Cdd:cd07832  155 PRLYSHQVATRWYRAPELLygsRKYDEGV-----------DLWAVGCIFAEL 195
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
299-503 5.10e-10

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: 60.69  E-value: 5.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQV--YHGRWHGEV-AIRLID---IERDNEDQLKAFKREVMayRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd05607    9 VLGKGGFGEVcaVQVKNTGQMyACKKLDkkrLKKKSGEKMALLEKEIL--EKVNSPFIVSLAYAFETKTHLCLVMSLMNG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTL-YSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGRRDDKL 450
Cdd:cd05607   87 GDLkYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDdNGNCRLSDLGL---AVEVKEGKPITQR 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 451 RIQNGWlchLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd05607  164 AGTNGY---MAPEILKE---------ESYSYPVDWFAMGCSIYEMVAGRTPFR 204
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
298-434 6.62e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 60.51  E-value: 6.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII-------- 366
Cdd:cd07861    6 EKIGEGTYGVVYKGRnkkTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVfeflsmdl 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 367 ----TSLCKGRTLysvvrDAKIVldvnktRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGL 434
Cdd:cd07861   86 kkylDSLPKGKYM-----DAELV------KSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNkGVIKLADFGL 147
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
292-502 6.75e-10

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 60.03  E-value: 6.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQLKAFK----REVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd14194    5 DYYDTGEELGSGQFAVVKKCREKStglQYAAKFIKKRRTKSSRRGVSRedieREVSILKEIQHPNVITLHEVYENKTDVI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFYDNG-----KVVITDFGLfsisg 439
Cdd:cd14194   85 LILELVAGGELFDFLAEKESLTEEEATEFLKQ-ILNGVYYLHSLQIAHFDLKPENIMLLDRnvpkpRIKIIDFGL----- 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 440 vlqAGRRDDKLRIQN--GWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14194  159 ---AHKIDFGNEFKNifGTPEFVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPF 211
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
300-548 8.92e-10

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: 59.91  E-value: 8.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQV-----YHGRWHGEVAIRLIDIERDNEDQLKaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd05042    3 IGNGWFGKVllgeiYSGTSVAQVVVKELKASANPKEQDT-FLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVL----DVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGLFSISGVLQAGRRDDK 449
Cdd:cd05042   82 LKAYLRSEREHErgdsDTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDlTVKIGDYGLAHSRYKEDYIETDDK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LRIQNGWlchLAPEIIRQLspdteEDKLPF---SKHSDVFALG-TIW--YELHAREWPFKT--QPAEAIIWQMGTGM-KP 520
Cdd:cd05042  162 LWFPLRW---TAPELVTEF-----HDRLLVvdqTKYSNIWSLGvTLWelFENGAQPYSNLSdlDVLAQVVREQDTKLpKP 233
                        250       260
                 ....*....|....*....|....*...
gi 568937340 521 NLsQIGMGKEISDILLFCWaFEQEERPT 548
Cdd:cd05042  234 QL-ELPYSDRWYEVLQFCW-LSPEQRPA 259
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
300-502 9.53e-10

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: 59.32  E-value: 9.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLKAFKR--------EVMAY-RQTRHENVV---------LFMGACM 358
Cdd:cd14004    8 MGEGAYGQVnlaIYKSKGKEVVIKFIFKERILVDTWVRDRKlgtvpleiHILDTlNKRSHPNIVklldffeddEFYYLVM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 359 sPPHlaiitslCKGRTLYSVVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlfsI 437
Cdd:cd14004   88 -EKH-------GSGMDLFDFI-ERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDgNGTIKLIDFG---S 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 438 SGVLQAGRRDdklrIQNGWLCHLAPEIIRqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14004  156 AAYIKSGPFD----TFVGTIDYAAPEVLR--------GNPYGGKEQDIWALGVLLYTLVFKENPF 208
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
288-558 1.01e-09

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: 59.71  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEQLEIGELIGKGRFGQVYHGRWHGE--------VAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACM- 358
Cdd:cd05036    2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMpgdpsplqVAVKTLP-ELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFq 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 359 SPPHLaIITSLCKGRTLYSVVRDAK------IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN---GKVV- 428
Cdd:cd05036   81 RLPRF-ILLELMAGGDLKSFLRENRprpeqpSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCkgpGRVAk 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 429 ITDFGLfsisgvlqaGR---RDDKLRiQNGwlCHLAPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELHAREW-PFKT 504
Cdd:cd05036  160 IGDFGM---------ARdiyRADYYR-KGG--KAMLP--VKWMPPEAFLDGI-FTSKTDVWSFGVLLWEIFSLGYmPYPG 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 505 QPAEAIIwQMGTG---MKPNLSQIGmgkEISDILLFCWAFEQEERPTFTKLMDMLEK 558
Cdd:cd05036  225 KSNQEVM-EFVTSggrMDPPKNCPG---PVYRIMTQCWQHIPEDRPNFSTILERLNY 277
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
293-559 1.03e-09

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: 59.83  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHG---EVAI-RLIDIErdnEDQLKAFKREVMAYRQTR-HENVVLFMGACMSPPHLA--- 364
Cdd:cd14036    1 KLRIKRVIAEGGFAFVYEAQDVGtgkEYALkRLLSNE---EEKNKAIIQEINFMKKLSgHPNIVQFCSAASIGKEESdqg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 -----IITSLCKGRtLYSVVR--DAKIVLDVNKTRQIAQEIVKGMGYLHAKG--ILHKDLKSKNVFYDNGKVV-ITDFGL 434
Cdd:cd14036   78 qaeylLLTELCKGQ-LVDFVKkvEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIkLCDFGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 435 ---------FSISGVLQAGRRDDKLRiqNGWLCHLAPEIIRQLSpdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14036  157 atteahypdYSWSAQKRSLVEDEITR--NTTPMYRTPEMIDLYS------NYPIGEKQDIWALGCILYLLCFRKHPFEDG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 506 PAEAIIwQMGTGMKPNLSQIGMgkeISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14036  229 AKLRII-NAKYTIPPNDTQYTV---FHDLIRSTLKVNPEERLSITEIVEQLQEL 278
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
300-553 1.04e-09

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: 59.39  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVY---HGRWHGEVAIRLIDIE-RDNEDQLKAFKREVMAYRQTRHENVVLFMGaCMSPPHLA-IITSLCKGrt 374
Cdd:cd06607    9 IGHGSFGAVYyarNKRTSEVVAIKKMSYSgKQSTEKWQDIIKEVKFLRQLRHPNTIEYKG-CYLREHTAwLVMEYCLG-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 lysvvrDAKIVLDVNKTRQIAQEI-------VKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlfSISGVLQAgrr 446
Cdd:cd06607   86 ------SASDIVEVHKKPLQEVEIaaichgaLQGLAYLHSHNRIHRDVKAGNILLtEPGTVKLADFG--SASLVCPA--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 ddklriqNG------WlchLAPEIIRQLspdteeDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKP 520
Cdd:cd06607  155 -------NSfvgtpyW---MAPEVILAM------DEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSP 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568937340 521 NLSQIGMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06607  219 TLSSGEWSDDFRNFVDSCLQKIPQDRPSAEDLL 251
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
273-438 1.05e-09

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 58.88  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 273 FPRKASQTSIFLQEWD------IPFEQLEIG--ELIGKGRFGQVYHGRWHGE-VA--IRLIDIERDNedqlkaFKREVMA 341
Cdd:COG2112   13 YPRSESELEERLEELKslgitsIYSGGTLIGglRLLGKGYRGVVFLGKLGGKkVAlkIRRTDSPRPS------LKKEAEI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 342 YRQTRHENV---VLFMGAcmspphLAIITSLCKGRTLysvvRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLK-- 416
Cdd:COG2112   87 LKKANGAGVgpkLYDYGR------DFLVMEYIEGEPL----KDWLENLDKEELRKVIRELLEAAYLLDRIGIDHGELSrp 156
                        170       180
                 ....*....|....*....|..
gi 568937340 417 SKNVFYDNGKVVITDFGLFSIS 438
Cdd:COG2112  157 GKHVIVDKGRPYIIDFESASIS 178
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
295-502 1.11e-09

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: 59.58  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQL----KAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14196    8 DIGEELGSGQFAIVKKCREKStglEYAAKFIKKRQSRASRRgvsrEEIEREVSILRQVLHPNIITLHDVYENRTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVI-----TDFGLfsisgvlq 442
Cdd:cd14196   88 ELVSGGELFDFLAQKESLSEEEATSFIKQ-ILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIphiklIDFGL-------- 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 443 AGRRDDKLRIQN--GWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14196  159 AHEIEDGVEFKNifGTPEFVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPF 211
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
295-434 1.20e-09

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: 59.60  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHGE---VAIRLIDIERDNEDQLKAFKREVMAYRQTR---HENVVLFMGACMSPP-----HL 363
Cdd:cd07838    2 EEVAEIGEGAYGTVYKARDLQDgrfVALKKVRVPLSEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHGPRtdrelKL 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 364 AIITSLCKG--RTLYSvvRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGL 434
Cdd:cd07838   82 TLVFEHVDQdlATYLD--KCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSdGQVKLADFGL 153
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
296-511 1.22e-09

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: 59.49  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHGrwhgevairlidIERDNEDQLKA------------FKREVMAYRQTRHENVVLFMGACMSPPHL 363
Cdd:cd14104    4 IAEELGRGQFGIVHRC------------VETSSKKTYMAkfvkvkgadqvlVKKEISILNIARHRNILRLHESFESHEEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRDAKIVLD----VNKTRQIAQeivkGMGYLHAKGILHKDLKSKNVFYDNGK---VVITDFGLfs 436
Cdd:cd14104   72 VMIFEFISGVDIFERITTARFELNereiVSYVRQVCE----ALEFLHSKNIGHFDIRPENIIYCTRRgsyIKIIEFGQ-- 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 437 iSGVLQAGrrdDKLRIQNGWLCHLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPFKTQPAEAII 511
Cdd:cd14104  146 -SRQLKPG---DKFRLQYTSAEFYAPEVHQHESVSTA---------TDMWSLGCLVYVLLSGINPFEAETNQQTI 207
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
294-559 1.36e-09

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: 59.17  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHG------RWHGEVAIRLIdieRD--NEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAI 365
Cdd:cd05064    7 IKIERILGTGRFGELCRGclklpsKRELPVAIHTL---RAgcSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsisgvLQAG 444
Cdd:cd05064   84 VTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCkISGFRR------LQED 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 RRDDKLRIQNGWLCHL--APEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQMGTGMK-- 519
Cdd:cd05064  158 KSEAIYTTMSGKSPVLwaAPEAIQYHH---------FSSASDVWSFGIVMWEVMSYgERPYWDMSGQDVIKAVEDGFRlp 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568937340 520 -----PNLsqigmgkeISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05064  229 aprncPNL--------LHQLMLDCWQKERGERPRFSQIHSILSKM 265
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
298-573 1.38e-09

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: 59.21  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQ-VYHGRWHG-EVAIRLIdierdnedqLKAF----KREVMAYRQT-RHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd13982    7 KVLGYGSEGTiVFRGTFDGrPVAVKRL---------LPEFfdfaDREVQLLRESdEHPNVIRYFCTEKDRQFLYIALELC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGrTLYSVV-RDAKIVLDVNKTRQ---IAQEIVKGMGYLHAKGILHKDLKSKNVFYD------NGKVVITDFGL------ 434
Cdd:cd13982   78 AA-SLQDLVeSPRESKLFLRPGLEpvrLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnahgNVRAMISDFGLckkldv 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 435 -----FSISGVlqAGrrddklriQNGWlchLAPEIIRQlspdteEDKLPFSKHSDVFALG-TIWYELHAREWPF-KTQPA 507
Cdd:cd13982  157 grssfSRRSGV--AG--------TSGW---IAPEMLSG------STKRRQTRAVDIFSLGcVFYYVLSGGSHPFgDKLER 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 508 EAIIWQMGTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLmdmleklpkrnrrLSHPgHFW 573
Cdd:cd13982  218 EANILKGKYSLDKLLSLGEHGPEAQDLIERMIDFDPEKRPSAEEV-------------LNHP-FFW 269
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
298-559 1.58e-09

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: 58.90  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE-----VAIRLIDiERDNEDQLKAFKREV-MAYRQTRHENVVLFMGACMS----------PP 361
Cdd:cd05047    1 DVIGEGNFGQVLKARIKKDglrmdAAIKRMK-EYASKDDHRDFAGELeVLCKLGHHPNIINLLGACEHrgylylaieyAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCKGRTL-----YSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLf 435
Cdd:cd05047   80 HGNLLDFLRKSRVLetdpaFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVgENYVAKIADFGL- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 436 siSGVLQAGRRDDKLRIQNGWLChlapeiIRQLSPDTeedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQM 514
Cdd:cd05047  159 --SRGQEVYVKKTMGRLPVRWMA------IESLNYSV------YTTNSDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKL 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568937340 515 GTGMKPNlSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05047  225 PQGYRLE-KPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 268
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
287-495 2.17e-09

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


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 59.23  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPfEQLEIGELIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHL 363
Cdd:cd07851   11 WEVP-DRYQNLSPVGSGAYGQVcsaFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 A------IITSLCkGRTLYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-FYDNGKVVITDFGLfs 436
Cdd:cd07851   90 EdfqdvyLVTHLM-GADLNNIVKCQK--LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLaVNEDCELKILDFGL-- 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 437 isgvlqAGRRDDKLR--IQNGWlcHLAPEIIRqlspdteeDKLPFSKHSDVFALGTIWYEL 495
Cdd:cd07851  165 ------ARHTDDEMTgyVATRW--YRAPEIML--------NWMHYNQTVDIWSVGCIMAEL 209
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
300-438 2.18e-09

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: 58.92  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR--WHGE-VAIRLIDIERDNEdqlkAFK----REVMAYRQTRHENVVLFMGACMSPphlAIITSLCKG 372
Cdd:cd07865   20 IGQGTFGEVFKARhrKTGQiVALKKVLMENEKE----GFPitalREIKILQLLKHENVVNLIEICRTK---ATPYNRYKG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 rTLYSV-----------VRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL---FSI 437
Cdd:cd07865   93 -SIYLVfefcehdlaglLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITkDGVLKLADFGLaraFSL 171

                 .
gi 568937340 438 S 438
Cdd:cd07865  172 A 172
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
292-433 2.23e-09

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: 58.59  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRwHGE----VAIRLIdIERDNEDQLKAFK-REVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCR-HKEtgqiVAIKKF-LESEDDKMVKKIAmREIKMLKQLRHENLVNLIEVFRRKKRWYLV 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 367 TSLCKgRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFG 433
Cdd:cd07846   79 FEFVD-HTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVkLCDFG 145
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
292-517 2.46e-09

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: 58.47  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHG---EVAIRLIDIE--RDNEDQLKafkREVMAYRQTRHENVVLFMGACMSPPHLAII 366
Cdd:cd14183    6 ERYKVGRTIGDGNFAVVKECVERStgrEYALKIINKSkcRGKEHMIQ---NEVSILRRVKHPNIVLLIEEMDMPTELYLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRDAKIVLDVNKTRQIaQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVV-ITDFGLFSISgvl 441
Cdd:cd14183   83 MELVKGGDLFDAITSTNKYTERDASGML-YNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLkLGDFGLATVV--- 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 442 qagrrDDKLRIQNGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFK--TQPAEAIIWQMGTG 517
Cdd:cd14183  159 -----DGPLYTVCGTPTYVAPEIIAETG---------YGLKVDIWAAGVITYILLCGFPPFRgsGDDQEVLFDQILMG 222
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
292-548 2.61e-09

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: 58.51  E-value: 2.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYH-------GRWhgeVAIRLIDIERDNEDQLKAFKREVMAYRQTR---HENVVLFMGACMspp 361
Cdd:cd07862    1 QQYECVAEIGEGAYGKVFKardlkngGRF---VALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCT--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 hlaiiTSLCKGRTLYSVV-----RDAKIVLD--------VNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKV 427
Cdd:cd07862   75 -----VSRTDRETKLTLVfehvdQDLTTYLDkvpepgvpTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVtSSGQI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 428 VITDFGLFSISGVLQAgrrddkLRIQNGWLCHLAPEIIRQLSPDTEED--------------KLPFSKHSDVFALGTIWY 493
Cdd:cd07862  150 KLADFGLARIYSFQMA------LTSVVVTLWYRAPEVLLQSSYATPVDlwsvgcifaemfrrKPLFRGSSDVDQLGKILD 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 494 EL---HAREWP---------FKTQPAEAIiwqmgTGMKPNLSQIGmgkeiSDILLFCWAFEQEERPT 548
Cdd:cd07862  224 VIglpGEEDWPrdvalprqaFHSKSAQPI-----EKFVTDIDELG-----KDLLLKCLTFNPAKRIS 280
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
298-494 2.68e-09

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: 58.59  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGR---WHGEV-AIRLIdieRDNEDQLKAFKR---EVMAYRQTR---HENVVLFMGACMSPPHLAIIT 367
Cdd:cd14052    6 ELIGSGEFSQVYKVServPTGKVyAVKKL---KPNYAGAKDRLRrleEVSILRELTldgHDNIVQLIDSWEYHGHLYIQT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKI--VLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFS----ISGV 440
Cdd:cd14052   83 ELCENGSLDVFLSELGLlgRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITfEGTLKIGDFGMATvwplIRGI 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 441 LQAGRRDdklriqngwlcHLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYE 494
Cdd:cd14052  163 EREGDRE-----------YIAPEILSEHMYD---------KPADIFSLGLILLE 196
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
300-505 2.96e-09

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


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 58.66  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHgEVAIRL---IDIERDNEDQLKAFKREVMAYRQ----------------------TRHENVVLFM 354
Cdd:cd14018    1 IGKGCNAAVYEAALF-PLAIKMmwnISAGSSSEAILRSMGNELVPAPNvallgeygevtrlglqngrkllAPHPNIIRVQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 355 GA-CMSPPHL---------AIITSL-----CKGRTLYSVVRDAKIVL----DVN--KTRQ----IAQeIVKGMGYLHAKG 409
Cdd:cd14018   80 RAfTDSVPLLpgaiedypdVLPARLnpsglGHNRTLFLVMKNYPCTLrqylWVNtpSYRLarvmILQ-LLEGVDHLVRHG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 410 ILHKDLKSKNVF--YDNG---KVVITDFG--LFSISGVLQAGRRDDKL-RIQNGwlCHLAPEIIRQL-SPDTeedKLPFS 480
Cdd:cd14018  159 IAHRDLKSDNILleLDFDgcpWLVIADFGccLADDSIGLQLPFSSWYVdRGGNA--CLMAPEVSTAVpGPGV---VINYS 233
                        250       260
                 ....*....|....*....|....*
gi 568937340 481 KhSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14018  234 K-ADAWAVGAIAYEIFGLSNPFYGL 257
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
287-559 3.23e-09

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: 59.25  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLID-IERDNEDQLKAFKREVMAYRQTrHENVVLFMGAC 357
Cdd:cd05107   32 WEMPRDNLVLGRTLGSGAFGRVVEATAHGlshsqstmKVAVKMLKsTARSSEKQALMSELKIMSHLGP-HLNIVNLLGAC 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 358 MSPPHLAIITSLC----------------------KGRTLYSVVRDAKIV------------------LDVNKTRQI--- 394
Cdd:cd05107  111 TKGGPIYIITEYCrygdlvdylhrnkhtflqyyldKNRDDGSLISGGSTPlsqrkshvslgsesdggyMDMSKDESAdyv 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 395 -----------------------------AQE-------------------------IVKGMGYLHAKGILHKDLKSKNV 420
Cdd:cd05107  191 pmqdmkgtvkyadiessnyespydqylpsAPErtrrdtlinespalsymdlvgfsyqVANGMEFLASKNCVHRDLAARNV 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 421 FYDNGKVV-ITDFGLfsisgvlqagRRD---DKLRIQNGwlCHLAPeiIRQLSPDTEEDKLpFSKHSDVFALGTIWYELH 496
Cdd:cd05107  271 LICEGKLVkICDFGL----------ARDimrDSNYISKG--STFLP--LKWMAPESIFNNL-YTTLSDVWSFGILLWEIF 335
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 497 A------REWPFKTQPAEAIiwQMGTGM-KPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05107  336 TlggtpyPELPMNEQFYNAI--KRGYRMaKPAHAS----DEIYEIMQKCWEEKFEIRPDFSQLVHLVGDL 399
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
291-434 3.66e-09

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: 58.15  E-value: 3.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIgelIGKGRFGQVYHGR--WHGE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVV---------------L 352
Cdd:cd07845    9 FEKLNR---IGEGTYGIVYRARdtTSGEiVALKKVRMDNERDGIPISSLREITLLLNLRHPNIVelkevvvgkhldsifL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 353 FMGACmspphlaiitslckGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITD 431
Cdd:cd07845   86 VMEYC--------------EQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLtDKGCLKIAD 151

                 ...
gi 568937340 432 FGL 434
Cdd:cd07845  152 FGL 154
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
300-568 3.88e-09

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: 58.11  E-value: 3.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR---WHGEVAIRLIDIE-RDNEDQLKAFKREVMAYRQTRHENVVLFMGaCMSPPHLA-IITSLCKGrt 374
Cdd:cd06634   23 IGHGSFGAVYFARdvrNNEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQKLRHPNTIEYRG-CYLREHTAwLVMEYCLG-- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 lysvvrDAKIVLDVNKTRQIAQEI-------VKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSISGVLQAGRr 446
Cdd:cd06634  100 ------SASDLLEVHKKPLQEVEIaaithgaLQGLAYLHSHNMIHRDVKAGNILLtEPGLVKLGDFGSASIMAPANSFV- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 ddklriqnGWLCHLAPEIIRQLspdteeDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKP------ 520
Cdd:cd06634  173 --------GTPYWMAPEVILAM------DEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPalqsgh 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 521 -----------NLSQIGMGKEISDILLfCWAFEQEERPTfTKLMDMLEKLPKRNRRLSH 568
Cdd:cd06634  239 wseyfrnfvdsCLQKIPQDRPTSDVLL-KHRFLLRERPP-TVIMDLIQRTKDAVRELDN 295
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
395-502 4.05e-09

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: 58.17  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 395 AQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLF--SISGvlqagrrDDKLRIQNGWLCHLAPEIIRQlspd 471
Cdd:cd05587  103 AAEIAVGLFFLHSKGIIYRDLKLDNVMLDaEGHIKIADFGMCkeGIFG-------GKTTRTFCGTPDYIAPEIIAY---- 171
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568937340 472 teedkLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05587  172 -----QPYGKSVDWWAYGVLLYEMLAGQPPF 197
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
293-495 4.06e-09

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: 57.68  E-value: 4.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHGEVAIR-LIDIERDNEDQLKAFKREVMAYRQ-TRHENVVLFMG---ACMSPP--HLAI 365
Cdd:cd14037    4 HVTIEKYLAEGGFAHVYLVKTSNGGNRAaLKRVYVNDEHDLNVCKREIEIMKRlSGHKNIVGYIDssaNRSGNGvyEVLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGrtlysvvrdaKIVLDVNKTR-----------QIAQEIVKGMGYLHA--KGILHKDLKSKNVFY-DNGKVVITD 431
Cdd:cd14037   84 LMEYCKG----------GGVIDLMNQRlqtglteseilKIFCDVCEAVAAMHYlkPPLIHRDLKVENVLIsDSGNYKLCD 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 432 FGlfSISGVLQAGRRDDKLR-----IQ-NGWLCHLAPEIIRQLSpdteedKLPFSKHSDVFALGTIWYEL 495
Cdd:cd14037  154 FG--SATTKILPPQTKQGVTyveedIKkYTTLQYRAPEMIDLYR------GKPITEKSDIWALGCLLYKL 215
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
295-493 4.54e-09

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: 57.60  E-value: 4.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFG---QVYHGRWHGEVAIRLIDIERDNEdqlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14108    5 DIHKEIGRGAFSylrRVKEKSSDLSFAAKFIPVRAKKK---TSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKIVldVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGK---VVITDFglfsisGVLQAGRRDD 448
Cdd:cd14108   82 EELLERITKRPTVC--ESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdqVRICDF------GNAQELTPNE 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568937340 449 KLRIQNGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWY 493
Cdd:cd14108  154 PQYCKYGTPEFVAPEIVNQ---------SPVSKVTDIWPVGVIAY 189
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
300-562 4.80e-09

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: 58.14  E-value: 4.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHG---RWHGEVAIRLIDIE-RDNEDQLKAFKREVMAYRQTRHENVVLFMGaCMSPPHLA-IITSLCKGRT 374
Cdd:cd06635   33 IGHGSFGAVYFArdvRTSEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQRIKHPNSIEYKG-CYLREHTAwLVMEYCLGSA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 lYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSISGVLQAGRrddklriq 453
Cdd:cd06635  112 -SDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLtEPGQVKLADFGSASIASPANSFV-------- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 454 nGWLCHLAPEIIRQLspdteeDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEISD 533
Cdd:cd06635  183 -GTPYWMAPEVILAM------DEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRN 255
                        250       260
                 ....*....|....*....|....*....
gi 568937340 534 ILLFCWAFEQEERPTFTKLMDMLEKLPKR 562
Cdd:cd06635  256 FVDSCLQKIPQDRPTSEELLKHMFVLRER 284
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
364-438 4.91e-09

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 55.35  E-value: 4.91e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 364 AIITSLCKGRTLYSVVRDAKivldvnKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSIS 438
Cdd:COG3642   32 DLVMEYIEGETLADLLEEGE------LPPELLRELGRLLARLHRAGIVHGDLTTSNILVDDGGVYLIDFGLARYS 100
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
297-553 5.10e-09

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: 57.44  E-value: 5.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHGRWHGE---VAIRLIDIERDN----EDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd06630    5 GPLLGTGAFSSCYQARDVKTgtlMAVKQVSFCRNSsseqEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVV-ITDFGlfsisgvlQAGRRD 447
Cdd:cd06630   85 MAGGSVASLLSKYGAFSENVIINYTLQ-ILRGLAYLHDNQIIHRDLKGANLLVDStGQRLrIADFG--------AAARLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 448 DKL----RIQN---GWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPF---KTQPAEAIIWQMGTG 517
Cdd:cd06630  156 SKGtgagEFQGqllGTIAFMAPEVLR---------GEQYGRSCDVWSVGCVIIEMATAKPPWnaeKISNHLALIFKIASA 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568937340 518 MKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd06630  227 TTPPPIPEHLSPGLRDVTLRCLELQPEDRPPARELL 262
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
324-577 6.11e-09

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: 57.43  E-value: 6.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 324 IERDNEDQL-KAFKREVMAYRQTRHENVVLFMGACM--SPPHLAIITSLCKGRTLYSVVRdaKIVLDVNKTRQ-----IA 395
Cdd:cd06621   34 ITTDPNPDVqKQILRELEINKSCASPYIVKYYGAFLdeQDSSIGIAMEYCEGGSLDSIYK--KVKKKGGRIGEkvlgkIA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 396 QEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlfsISGvlQAGRRDDKLRIqnGWLCHLAPEIIRqlspdtee 474
Cdd:cd06621  112 ESVLKGLSYLHSRKIIHRDIKPSNILLTrKGQVKLCDFG---VSG--ELVNSLAGTFT--GTSYYMAPERIQ-------- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 475 dKLPFSKHSDVFALGTIWYELHAREWPF---KTQPAEAI-IWQMGTGMK-PNLSQ-----IGMGKEISDILLFCWAFEQE 544
Cdd:cd06621  177 -GGPYSITSDVWSLGLTLLEVAQNRFPFppeGEPPLGPIeLLSYIVNMPnPELKDepengIKWSESFKDFIEKCLEKDGT 255
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568937340 545 ERPTFTKLmdmleklpkrnrrLSHPghFWKSAE 577
Cdd:cd06621  256 RRPGPWQM-------------LAHP--WIKAQE 273
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
377-558 6.15e-09

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: 57.99  E-value: 6.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLF----SISGVLQAGrrddKLR 451
Cdd:cd05104  202 EILEEDELALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITkICDFGLArdirNDSNYVVKG----NAR 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 452 IQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQM---GTGM-KPNLSQig 526
Cdd:cd05104  278 LPVKW---MAPESIFECV---------YTFESDVWSYGILLWEIFSLgSSPYPGMPVDSKFYKMikeGYRMdSPEFAP-- 343
                        170       180       190
                 ....*....|....*....|....*....|..
gi 568937340 527 mgKEISDILLFCWAFEQEERPTFTKLMDMLEK 558
Cdd:cd05104  344 --SEMYDIMRSCWDADPLKRPTFKQIVQLIEQ 373
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
291-434 6.69e-09

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 57.11  E-value: 6.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEigeLIGKGRFGQVYHG--RWHGE-VAIRLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd07836    2 FKQLE---KLGEGTYATVYKGrnRTTGEiVALKEIHLDAEEGTPSTAI-REISLMKELKHENIVRLHDVIHTENKLMLVF 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 368 SLCKGR-TLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:cd07836   78 EYMDKDlKKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINkRGELKLADFGL 146
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
300-495 7.19e-09

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: 57.71  E-value: 7.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGE---VAIRLID---IERDNEDQlkafkrEVMAYRQTRHENVvlfmgacMSPPHLAIITSLCKGR 373
Cdd:cd05575    3 IGKGSFGKVLLARHKAEgklYAVKVLQkkaILKRNEVK------HIMAERNVLLKNV-------KHPFLVGLHYSFQTKD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYsvvrdakIVLD-VN-----------------KTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:cd05575   70 KLY-------FVLDyVNggelffhlqrerhfpepRARFYAAEIASALGYLHSLNIIYRDLKPENILLDsQGHVVLTDFGL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 435 FSiSGVlqagRRDDKLRIQNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYEL 495
Cdd:cd05575  143 CK-EGI----EPSDTTSTFCGTPEYLAPEVLR---------KQPYDRTVDWWCLGAVLYEM 189
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
391-503 8.09e-09

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: 56.88  E-value: 8.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 391 TRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGlfsISGVLQAGRRDDKLriqNGWLCHLAPEII-RQL 468
Cdd:cd05578  102 VKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEqGHVHITDFN---IATKLTDGTLATST---SGTKPYMAPEVFmRAG 175
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568937340 469 spdteedklpFSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd05578  176 ----------YSFAVDWWSLGVTAYEMLRGKRPYE 200
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
292-504 8.87e-09

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: 56.80  E-value: 8.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRW---HGEVAIRLI---DIERDN-EDQLKafkREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd14117    6 DDFDIGRPLGKGKFGNVYLAREkqsKFIVALKVLfksQIEKEGvEHQLR---REIEIQSHLRHPNILRLYNYFHDRKRIY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGVLqa 443
Cdd:cd14117   83 LILEYAPRGELYKELQKHG-RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGyKGELKIADFGWSVHAPSL-- 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 444 gRRddklRIQNGWLCHLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPFKT 504
Cdd:cd14117  160 -RR----RTMCGTLDYLPPEMIEGRTHD---------EKVDLWCIGVLCYELLVGMPPFES 206
pknD PRK13184
serine/threonine-protein kinase PknD;
292-503 9.19e-09

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 58.63  E-value: 9.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGrwHGEVAIRLIDIER------DNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAI 365
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLA--YDPVCSRRVALKKiredlsENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVR----------DAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGL 434
Cdd:PRK13184  80 TMPYIEGYTLKSLLKsvwqkeslskELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLfGEVVILDWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 435 fsisGVLQAGRRDDKLRI---QNGWLCH--------------LAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHA 497
Cdd:PRK13184 160 ----AIFKKLEEEDLLDIdvdERNICYSsmtipgkivgtpdyMAPERLL---------GVPASESTDIYALGVILYQMLT 226

                 ....*.
gi 568937340 498 REWPFK 503
Cdd:PRK13184 227 LSFPYR 232
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
299-547 9.61e-09

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 56.56  E-value: 9.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHG---RWHGEVAIRLIDIERDNEDQLKA-----FKREVMAYRQTRHENVV-LFMGACMSPPHLAIITSL 369
Cdd:cd13990    7 LLGKGGFSEVYKAfdlVEQRYVACKIHQLNKDWSEEKKQnyikhALREYEIHKSLDHPRIVkLYDVFEIDTDSFCTVLEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDVnKTRQIAQEIVKGMGYL--HAKGILHKDLKSKNVFYDNGKVV----ITDFGLFSISGvlQA 443
Cdd:cd13990   87 CDGNDLDFYLKQHKSIPER-EARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSgeikITDFGLSKIMD--DE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 GRRDDKLRIQN---GWLCHLAPEIIrqlspDTEEDKLPFSKHSDVFALGTIWYE-LHAREwPFKTQPAEAIIWQMGTGM- 518
Cdd:cd13990  164 SYNSDGMELTSqgaGTYWYLPPECF-----VVGKTPPKISSKVDVWSVGVIFYQmLYGRK-PFGHNQSQEAILEENTILk 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568937340 519 --------KPNLSQigmgkEISDILLFCWAFEQEERP 547
Cdd:cd13990  238 atevefpsKPVVSS-----EAKDFIRRCLTYRKEDRP 269
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
298-502 9.73e-09

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: 57.26  E-value: 9.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVY------HGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQtrhENVVLFMGAC--MSPPHLAIITSL 369
Cdd:cd05620    1 KVLGKGSFGKVLlaelkgKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAW---ENPFLTHLYCtfQTKEHLFFVMEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLF--SISGvlqagrr 446
Cdd:cd05620   78 LNGGDLMFHIQD-KGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDrDGHIKIADFGMCkeNVFG------- 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 447 DDKLRIQNGWLCHLAPEIIRQLspdteedKLPFSkhSDVFALGTIWYELHAREWPF 502
Cdd:cd05620  150 DNRASTFCGTPDYIAPEILQGL-------KYTFS--VDWWSFGVLLYEMLIGQSPF 196
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
292-502 9.93e-09

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: 56.66  E-value: 9.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRrcvQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAKIVLDVNKTRQIaQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGL-FSISGVLQA 443
Cdd:cd14086   81 LVTGGELFEDIVAREFYSEADASHCI-QQILESVNHCHQNGIVHRDLKPENLLLasksKGAAVKLADFGLaIEVQGDQQA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 444 grrddklriqngWL------CHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14086  160 ------------WFgfagtpGYLSPEVLR---------KDPYGKPVDIWACGVILYILLVGYPPF 203
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
300-499 1.08e-08

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: 56.89  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR--WHGE-VAIRLIDIErDNEDQLK-AFKREVMAYR---QTRHENVVLFMGACMspphlaiiTSLCKG 372
Cdd:cd07863    8 IGVGAYGTVYKARdpHSGHfVALKSVRVQ-TNEDGLPlSTVREVALLKrleAFDHPNIVRLMDVCA--------TSRTDR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVV-----RDAKIVLD--------VNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFSIS 438
Cdd:cd07863   79 ETKVTLVfehvdQDLRTYLDkvpppglpAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSgGQVKLADFGLARIY 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 439 GVLQAgrrddkLRIQNGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHARE 499
Cdd:cd07863  159 SCQMA------LTPVVVTLWYRAPEVLLQST---------YATPVDMWSVGCIFAEMFRRK 204
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
295-502 1.13e-08

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: 56.17  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYH------GR-WHGEVAIRLIDIERDNedqlkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14191    5 DIEERLGSGKFGQVFRlvekktKKvWAGKFFKAYSAKEKEN------IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN---GKVVITDFGLfsisgvlqaG 444
Cdd:cd14191   79 EMVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktgTKIKLIDFGL---------A 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 445 RRDDK---LRIQNGWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14191  150 RRLENagsLKVLFGTPEFVAPEVI---------NYEPIGYATDMWSIGVICYILVSGLSPF 201
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
386-510 1.26e-08

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 56.40  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 386 LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGK--VVITDFGLFSISGVLQagrrddklrIQNGWLCHLAPE 463
Cdd:PHA03390 106 LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKdrIYLCDYGLCKIIGTPS---------CYDGTLDYFSPE 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568937340 464 IIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAI 510
Cdd:PHA03390 177 KIK---------GHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEEL 214
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
298-440 1.28e-08

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 56.53  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGR--WHGE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVlfmgacmspPHLAIITSlckGRT 374
Cdd:cd07835    5 EKIGEGTYGVVYKARdkLTGEiVALKKIRLETEDEGVPSTAIREISLLKELNHPNIV---------RLLDVVHS---ENK 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 375 LYSVVR----DAKIVLDVNKTRQIAQEIVK--------GMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGV 440
Cdd:cd07835   73 LYLVFEfldlDLKKYMDSSPLTGLDPPLIKsylyqllqGIAFCHSHRVLHRDLKPQNLLIDtEGALKLADFGLARAFGV 151
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
300-434 1.38e-08

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 56.17  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHG---RWHGEVAIRLIDIErdnedQLKAFKREVMAyrQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd13995   12 IPRGAFGKVYLAqdtKTKKRMACKLIPVE-----QFKPSDVEIQA--CFRHENIAELYGALLWEETVHLFMEAGEGGSVL 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 377 SVV------RDAKIVLdvnktrqIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGL 434
Cdd:cd13995   85 EKLescgpmREFEIIW-------VTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLVDFGL 141
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
292-502 1.49e-08

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: 56.43  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVY---HGRWHGEVAIRLID----IERDNEDQLKAFKRevmAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRlvkHKDSGKYYALKILKkakiIKLKQVEHVLNEKR---ILSEVRHPFIVNLLGSFQDDRNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsisgvlqA 443
Cdd:cd05580   78 MVMEYVPGGELFSLLRRSG-RFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDsDGHIKITDFGF--------A 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 444 GRRDDklriqNGW-LC----HLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05580  149 KRVKD-----RTYtLCgtpeYLAPEIIL---------SKGHGKAVDWWALGILIYEMLAGYPPF 198
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
285-559 1.51e-08

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: 56.78  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 285 QEWDIPFEQLEIGELIGKGRFGQVYHGRWHG--------EVAIRLIDiERDNEDQLKAFKREVMAYRQT-RHENVVLFMG 355
Cdd:cd05106   31 EKWEFPRDNLQFGKTLGAGAFGKVVEATAFGlgkednvlRVAVKMLK-ASAHTDEREALMSELKILSHLgQHKNIVNLLG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 356 ACMSPPHLAIITSLC-----------KGRTLYSVV------------------------RDAKIV--------------- 385
Cdd:cd05106  110 ACTHGGPVLVITEYCcygdllnflrkKAETFLNFVmalpeisetssdyknitlekkyirSDSGFSsqgsdtyvemrpvss 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 386 -------------------LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGL----FSISGVL 441
Cdd:cd05106  190 sssqssdskdeedtedswpLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAkICDFGLardiMNDSNYV 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAGrrddKLRIQNGWlchLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAR-EWPFKTQPAEAIIWQM---GTG 517
Cdd:cd05106  270 VKG----NARLPVKW---MAPESIFDCV---------YTVQSDVWSYGILLWEIFSLgKSPYPGILVNSKFYKMvkrGYQ 333
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 568937340 518 M-KPNLSQigmgKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05106  334 MsRPDFAP----PEIYSIMKMCWNLEPTERPTFSQISQLIQRQ 372
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
293-548 1.51e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 57.82  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  293 QLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPH--LAIIT 367
Cdd:PTZ00266   14 EYEVIKKIGNGRFGEVFlvkHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKANqkLYILM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  368 SLC----------KGRTLYSVVRDAKIVldvnktrQIAQEIVKGMGYLH-------AKGILHKDLKSKNVFYD------- 423
Cdd:PTZ00266   94 EFCdagdlsrniqKCYKMFGKIEEHAIV-------DITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLStgirhig 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340  424 ---------NGKVV--ITDFGLFSISGVlqagrrDDKLRIQNGWLCHLAPEIIRQlSPDTEEDKlpfskhSDVFALGTIW 492
Cdd:PTZ00266  167 kitaqannlNGRPIakIGDFGLSKNIGI------ESMAHSCVGTPYYWSPELLLH-ETKSYDDK------SDMWALGCII 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340  493 YELHAREWPF-KTQPAEAIIWQMGTGmkPNLSQIGMGKEISDILLFCWAFEQEERPT 548
Cdd:PTZ00266  234 YELCSGKTPFhKANNFSQLISELKRG--PDLPIKGKSKELNILIKNLLNLSAKERPS 288
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
299-434 1.62e-08

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: 56.38  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQV---YHGRWHGEVAI-RLIDIERDNEDQLKAFkREVMAYRQTRHENVV----LFMgacmsPP------HLA 364
Cdd:cd07834    7 PIGSGAYGVVcsaYDKRTGRKVAIkKISNVFDDLIDAKRIL-REIKILRHLKHENIIglldILR-----PPspeefnDVY 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 365 IITSLcKGRTLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL 434
Cdd:cd07834   81 IVTEL-METDLHKVIK-SPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVnSNCDLKICDFGL 149
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
317-507 1.69e-08

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: 56.15  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 317 VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKgrtlYSVVRD----------AKIVL 386
Cdd:cd08216   28 VAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMA----YGSCRDllkthfpeglPELAI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 387 dvnktRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITdfGLFSISGVLQAGRRDDKLR------IQNgwLCH 459
Cdd:cd08216  104 -----AFILRDVLNALEYIHSKGYIHRSVKASHILISgDGKVVLS--GLRYAYSMVKHGKRQRVVHdfpkssEKN--LPW 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568937340 460 LAPEIIRQ-LSPDTEEdklpfskhSDVFALGTIWYELHAREWPFKTQPA 507
Cdd:cd08216  175 LSPEVLQQnLLGYNEK--------SDIYSVGITACELANGVVPFSDMPA 215
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
287-495 1.82e-08

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: 56.60  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPfEQLEIGELIGKGRFGQV---YHGRWHGEVAIRliDIERDNEDQLKAFK--REVMAYRQTRHENVVLFMGAcMSPP 361
Cdd:cd07878   11 WEVP-ERYQNLTPVGSGAYGSVcsaYDTRLRQKVAVK--KLSRPFQSLIHARRtyRELRLLKHMKHENVIGLLDV-FTPA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 -------HLAIITSLcKGRTLYSVVRDAKIVLDvnKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-FYDNGKVVITDFG 433
Cdd:cd07878   87 tsienfnEVYLVTNL-MGADLNNIVKCQKLSDE--HVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVaVNEDCELRILDFG 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 434 LfsisgvlqAGRRDDKLR--IQNGWlcHLAPEIIRQLspdteedkLPFSKHSDVFALGTIWYEL 495
Cdd:cd07878  164 L--------ARQADDEMTgyVATRW--YRAPEIMLNW--------MHYNQTVDIWSVGCIMAEL 209
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
300-433 2.04e-08

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: 53.21  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVY---HGRWHGEVAIRLIDIeRDNEDQLKAFKREVMAYRQTRHE-NVVLFMGACMSPPHLAIITSLCKGRTL 375
Cdd:cd13968    1 MGEGASAKVFwaeGECTTIGVAVKIGDD-VNNEEGEDLESEMDILRRLKGLElNIPKVLVTEDVDGPNILLMELVKGGTL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 376 YSVVRdaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFG 433
Cdd:cd13968   80 IAYTQ--EEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLsEDGNVKLIDFG 136
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
295-494 2.48e-08

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: 55.49  E-value: 2.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY---HGRWHGEVAIRLID----IERDNEDQlkAF-KREVMayrqTRHEN--VVLFMGACMSPPHLA 364
Cdd:cd05609    3 ETIKLISNGAYGAVYlvrHRETRQRFAMKKINkqnlILRNQIQQ--VFvERDIL----TFAENpfVVSMYCSFETKRHLC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGL-----FSIS 438
Cdd:cd05609   77 MVMEYVEGGDCATLLKNIG-PLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSmGHIKLTDFGLskiglMSLT 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 439 GVLQAGRRDDKLRI-QNGWLC----HLAPEII-RQlspdteedklPFSKHSDVFALGTIWYE 494
Cdd:cd05609  156 TNLYEGHIEKDTREfLDKQVCgtpeYIAPEVIlRQ----------GYGKPVDWWAMGIILYE 207
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
292-502 2.55e-08

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


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 55.52  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERD-NEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHlvrDRISEHYYALKVMAIPEViRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVldVNKT-RQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlqagr 445
Cdd:cd05612   81 EYVPGGELFSYLRNSGRF--SNSTgLFYASEIVCALEYLHSKEIVYRDLKPENILLDkEGHIKLTDFGFAK--------- 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 446 rddKLRIQNGWLC----HLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05612  150 ---KLRDRTWTLCgtpeYLAPEVIQSKGHN---------KAVDWWALGILIYEMLVGYPPF 198
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
292-434 2.67e-08

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 55.58  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWH--GE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMgacmspphlAIITS 368
Cdd:cd07864    7 DKFDIIGIIGEGTYGQVYKAKDKdtGElVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLK---------EIVTD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 -------LCKGRTLYSVVR----------DAKIV-LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVI 429
Cdd:cd07864   78 kqdaldfKKDKGAFYLVFEymdhdlmgllESGLVhFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNkGQIKL 157

                 ....*
gi 568937340 430 TDFGL 434
Cdd:cd07864  158 ADFGL 162
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
395-505 2.71e-08

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: 55.78  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 395 AQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFSisgvlqagrrddklriQNGW-------LC----HLAP 462
Cdd:cd05616  107 AAEIAIGLFFLQSKGIIYRDLKLDNVMLDSeGHIKIADFGMCK----------------ENIWdgvttktFCgtpdYIAP 170
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568937340 463 EIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd05616  171 EIIAY---------QPYGKSVDWWAFGVLLYEMLAGQAPFEGE 204
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
397-504 2.77e-08

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: 55.09  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 EIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsiSGVLQAGrRDDKLRIQNGWLCHLAPEIIRqlSPDTEED 475
Cdd:cd05583  107 EIVLALEHLHKLGIIYRDIKLENILLDsEGHVVLTDFGL---SKEFLPG-ENDRAYSFCGTIEYMAPEVVR--GGSDGHD 180
                         90       100
                 ....*....|....*....|....*....
gi 568937340 476 KLpfskhSDVFALGTIWYELHAREWPFKT 504
Cdd:cd05583  181 KA-----VDWWSLGVLTYELLTGASPFTV 204
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
395-505 2.77e-08

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: 55.27  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 395 AQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsiSGVLQAGRrdDKLRIQNGWLCHLAPEIIRqlspDTE 473
Cdd:cd05608  111 TAQIISGLEHLHQRRIIYRDLKPENVLLDDdGNVRISDLGL---AVELKDGQ--TKTKGYAGTPGFMAPELLL----GEE 181
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568937340 474 EDklpFSkhSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd05608  182 YD---YS--VDYFTLGVTLYEMIAARGPFRAR 208
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
270-518 2.89e-08

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 56.17  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 270 ARSFPRKASQTSIFLqEWDIPFEQL-----------EIGELIGKGRFGQVyhgrwhgeVAIRLIDIER-------DNEDQ 331
Cdd:cd05624   40 SHSPLRRDKYVSEFL-EWAKPFTQLvkemqlhrddfEIIKVIGRGAFGEV--------AVVKMKNTERiyamkilNKWEM 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 332 LKafKREVMAYRQTRHenvVLFMGAC----------MSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKG 401
Cdd:cd05624  111 LK--RAETACFREERN---VLVNGDCqwittlhyafQDENYLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLA 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 402 MGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlfSISGVLQAGRRDDKLRIqnGWLCHLAPEIIRQLspdteEDKL-PF 479
Cdd:cd05624  186 IHSIHQLHYVHRDIKPDNVLLDmNGHIRLADFG--SCLKMNDDGTVQSSVAV--GTPDYISPEILQAM-----EDGMgKY 256
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568937340 480 SKHSDVFALGTIWYELHAREWPFKtqpAEAIIWQMGTGM 518
Cdd:cd05624  257 GPECDWWSLGVCMYEMLYGETPFY---AESLVETYGKIM 292
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
288-559 3.35e-08

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: 55.39  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEqleigELIGKGRFGQVYHGRWHGE-----VAIRLI-DIERDNEDQLKAFKREVMAyRQTRHENVVLFMGACMSPP 361
Cdd:cd05089    3 DIKFE-----DVIGEGNFGQVIKAMIKKDglkmnAAIKMLkEFASENDHRDFAGELEVLC-KLGHHPNIINLLGACENRG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCKGRTLYSVVRDAKIV---------------LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNG 425
Cdd:cd05089   77 YLYIAIEYAPYGNLLDFLRKSRVLetdpafakehgtastLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVgENL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 426 KVVITDFGLfsiSGVLQAGRRDDKLRIQNGWLChlapeiIRQLSPDTeedklpFSKHSDVFALGTIWYELHAR-EWPFKT 504
Cdd:cd05089  157 VSKIADFGL---SRGEEVYVKKTMGRLPVRWMA------IESLNYSV------YTTKSDVWSFGVLLWEIVSLgGTPYCG 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 505 QPAEAIIWQMGTGMKPNLSQiGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05089  222 MTCAELYEKLPQGYRMEKPR-NCDDEVYELMRQCWRDRPYERPPFSQISVQLSRM 275
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
41-84 3.45e-08

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: 49.82  E-value: 3.45e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568937340  41 HRFSTKYWMSQT-CTVCGKGMLF----GLKCKNCKLKCHNKCTKEAP-PC 84
Cdd:cd00029    1 HRFVPTTFSSPTfCDVCGKLIWGlfkqGLKCSDCGLVCHKKCLDKAPsPC 50
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
295-434 3.86e-08

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: 55.26  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHG--RWHGE-VAIRLI-DIERDNEDQLKAFkREVMAYRQTR-HENVVlfmgacmspPHLAIITSL 369
Cdd:cd07852   10 EILKKLGKGAYGIVWKAidKKTGEvVALKKIfDAFRNATDAQRTF-REIMFLQELNdHPNII---------KLLNVIRAE 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 370 CkGRTLY-----------SVVRdAKIVLDVNKtRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGL 434
Cdd:cd07852   80 N-DKDIYlvfeymetdlhAVIR-ANILEDIHK-QYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDcRVKLADFGL 153
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
397-502 3.93e-08

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: 55.01  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 EIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfSISGVLQAGRRDDKLriqNGWLCHLAPEIIRqlSPDTEED 475
Cdd:cd05613  113 EIVLALEHLHKLGIIYRDIKLENILLDsSGHVVLTDFGL-SKEFLLDENERAYSF---CGTIEYMAPEIVR--GGDSGHD 186
                         90       100
                 ....*....|....*....|....*..
gi 568937340 476 KLpfskhSDVFALGTIWYELHAREWPF 502
Cdd:cd05613  187 KA-----VDWWSLGVLMYELLTGASPF 208
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
301-524 4.10e-08

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: 54.44  E-value: 4.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 301 GKGRFGQVY--HGRWHGEVAIRLIdIERDNEDQLKAFKrEVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT-LYS 377
Cdd:cd14111   12 ARGRFGVIRrcRENATGKNFPAKI-VPYQAEEKQGVLQ-EYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKElLHS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 VVRDAKIVLD--VNKTRQIAQeivkGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFG---LFSISGVLQAGRRddklr 451
Cdd:cd14111   90 LIDRFRYSEDdvVGYLVQILQ----GLEYLHGRRVLHLDIKPDNIMVTNLNAIkIVDFGsaqSFNPLSLRQLGRR----- 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 452 iqNGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKT---QPAEAIIWQM---GTGMKPNLSQ 524
Cdd:cd14111  161 --TGTLEYMAPEMVK---------GEPVGPPADIWSIGVLTYIMLSGRSPFEDqdpQETEAKILVAkfdAFKLYPNVSQ 228
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
283-505 4.10e-08

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 55.26  E-value: 4.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 283 FLQEWDIPFEQLEIGEligkGRFG---QVYHGRWHGEVAIRLIDIERDNEDQlkafkREVMAYRQTR-HENVVLFMGACM 358
Cdd:cd14180    1 FFQCYELDLEEPALGE----GSFSvcrKCRHRQSGQEYAVKIISRRMEANTQ-----REVAALRLCQsHPNIVALHEVLH 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 359 SPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTrQIAQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGL 434
Cdd:cd14180   72 DQYHTYLVMELLRGGELLDRIKKKARFSESEAS-QLMRSLVSAVSFMHEAGVVHRDLKPENILYadesDGAVLKVIDFGF 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 435 fsisgvlqagrrdDKLRIQNG--------WLCHLAPEIIRQLSPDteedklpfsKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14180  151 -------------ARLRPQGSrplqtpcfTLQYAAPELFSNQGYD---------ESCDLWSLGVILYTMLSGQVPFQSK 207
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
397-502 4.53e-08

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: 55.10  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 EIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFsisgvlqagrrddKLRIQNGWLCH--------LAPEIIRQ 467
Cdd:cd05584  108 EITLALGHLHSLGIIYRDLKPENILLDaQGHVKLTDFGLC-------------KESIHDGTVTHtfcgtieyMAPEILTR 174
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568937340 468 LSPDteedklpfsKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05584  175 SGHG---------KAVDWWSLGALMYDMLTGAPPF 200
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
300-547 4.54e-08

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: 54.59  E-value: 4.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQV-YHGRWHGE-VAIRLIDIER-------DNEDQLK------------AFKREVMAYRQTRHENVVLFMGACM 358
Cdd:cd14067    1 LGQGGSGTViYRARYQGQpVAVKRFHIKKckkrtdgSADTMLKhlraadamknfsEFRQEASMLHSLQHPCIVYLIGISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 359 SPP----HLAIITSLckGRTLYSVVRDAKIV-LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY------DNGKV 427
Cdd:cd14067   81 HPLcfalELAPLGSL--NTVLEENHKGSSFMpLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvqEHINI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 428 VITDFGLFSIS---GVLQAgrrddklriqNGWLCHLAPEIirqlspdteEDKLPFSKHSDVFALGTIWYELHAREWPFKT 504
Cdd:cd14067  159 KLSDYGISRQSfheGALGV----------EGTPGYQAPEI---------RPRIVYDEKVDMFSYGMVLYELLSGQRPSLG 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 505 QPAEAIIWQMGTGMKPNLsqiGMGKEI-----SDILLFCWAFEQEERP 547
Cdd:cd14067  220 HHQLQIAKKLSKGIRPVL---GQPEEVqffrlQALMMECWDTKPEKRP 264
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
312-555 6.52e-08

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


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 53.90  E-value: 6.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 312 RWHGEVAIRLIDIERDNED--------QLKAFKREVMAYRQTRHENVVLFMGACMSPP------HLAIITSLCKGRTLYS 377
Cdd:cd14012   14 EVVLDNSKKPGKFLTSQEYfktsngkkQIQLLEKELESLKKLRHPNLVSYLAFSIERRgrsdgwKVYLLTEYAPGGSLSE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 378 VVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN----GKVVITDFGLfsisGVLQA---GRRDDKL 450
Cdd:cd14012   94 LL-DSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRdagtGIVKLTDYSL----GKTLLdmcSRGSLDE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 451 RIQNGWlchLAPEIIRQlspdteedKLPFSKHSDVFALGTIWYELharewPFKtqpaeAIIWQMGTGMKPNLSQIGMGKE 530
Cdd:cd14012  169 FKQTYW---LPPELAQG--------SKSPTRKTDVWDLGLLFLQM-----LFG-----LDVLEKYTSPNPVLVSLDLSAS 227
                        250       260
                 ....*....|....*....|....*
gi 568937340 531 ISDILLFCWAFEQEERPTFTKLMDM 555
Cdd:cd14012  228 LQDFLSKCLSLDPKKRPTALELLPH 252
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
300-495 6.70e-08

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: 54.24  E-value: 6.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKgRTLY 376
Cdd:cd07873   10 LGEGTYATVYKGRsklTDNLVALKEIRLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLD-KDLK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSISGVLQAGRRDDKLRIqng 455
Cdd:cd07873   88 QYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLInERGELKLADFGLARAKSIPTKTYSNEVVTL--- 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568937340 456 WlcHLAPEIirqLSPDTEedklpFSKHSDVFALGTIWYEL 495
Cdd:cd07873  165 W--YRPPDI---LLGSTD-----YSTQIDMWGVGCIFYEM 194
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
284-559 6.98e-08

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: 54.23  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 284 LQEWDIPFEqleigELIGKGRFGQVYHGR-----WHGEVAI-RLIDIERDNEDQLKAFKREVMAyRQTRHENVVLFMGAC 357
Cdd:cd05088    4 LEWNDIKFQ-----DVIGEGNFGQVLKARikkdgLRMDAAIkRMKEYASKDDHRDFAGELEVLC-KLGHHPNIINLLGAC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 358 MS----------PPHLAIITSLCKGRTL-----YSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY 422
Cdd:cd05088   78 EHrgylylaieyAPHGNLLDFLRKSRVLetdpaFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 423 -DNGKVVITDFGLfsiSGVLQAGRRDDKLRIQNGWLChlapeiIRQLSPDTeedklpFSKHSDVFALGTIWYELHARE-W 500
Cdd:cd05088  158 gENYVAKIADFGL---SRGQEVYVKKTMGRLPVRWMA------IESLNYSV------YTTNSDVWSYGVLLWEIVSLGgT 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 501 PFKTQPAEAIIWQMGTGMKPNlSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd05088  223 PYCGMTCAELYEKLPQGYRLE-KPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 280
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
395-511 7.53e-08

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: 54.53  E-value: 7.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 395 AQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFsisgvlqagrrddKLRIQNGWLCH--------LAPEII 465
Cdd:cd05570  102 AAEICLALQFLHERGIIYRDLKLDNVLLDAeGHIKIADFGMC-------------KEGIWGGNTTStfcgtpdyIAPEIL 168
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340 466 RQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAII 511
Cdd:cd05570  169 RE---------QDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELF 205
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
295-434 9.56e-08

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: 53.48  E-value: 9.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHG---EVAIRLIDIER--DNEDQLKAfkrEVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14095    3 DIGRVIGDGNFAVVKECRDKAtdkEYALKIIDKAKckGKEHMIEN---EVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDVNKTRQIaQEIVKGMGYLHAKGILHKDLKSKNVF-YDNGKVVIT----DFGL 434
Cdd:cd14095   80 VKGGDLFDAITSSTKFTERDASRMV-TDLAQALKYLHSLSIVHRDIKPENLLvVEHEDGSKSlklaDFGL 148
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
287-495 1.03e-07

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: 54.28  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPfEQLEIGELIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGAcMSPPH- 362
Cdd:cd07877   13 WEVP-ERYQNLSPVGSGAYGSVcaaFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDV-FTPARs 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 ------LAIITSLcKGRTLYSVVRDAKIVLDvnKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-FYDNGKVVITDFGLf 435
Cdd:cd07877   91 leefndVYLVTHL-MGADLNNIVKCQKLTDD--HVQFLIYQILRGLKYIHSADIIHRDLKPSNLaVNEDCELKILDFGL- 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 436 sisgvlqAGRRDDKLR--IQNGWlcHLAPEIIRQLspdteedkLPFSKHSDVFALGTIWYEL 495
Cdd:cd07877  167 -------ARHTDDEMTgyVATRW--YRAPEIMLNW--------MHYNQTVDIWSVGCIMAEL 211
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
295-502 1.04e-07

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: 53.68  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd14085    6 EIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDK-KIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFSISgvlqagrrDDKL 450
Cdd:cd14085   85 LFDRIVEKGYYSERDAADAVKQ-ILEAVAYLHENGIVHRDLKPENLLYatpaPDAPLKIADFGLSKIV--------DQQV 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568937340 451 RIQN--GWLCHLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYELHAREWPF 502
Cdd:cd14085  156 TMKTvcGTPGYCAPEILRGCAYGPE---------VDMWSVGVITYILLCGFEPF 200
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
300-514 1.05e-07

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: 53.61  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQLKA-FKREVMAYRQTRHENVVlfmGACMSPPHLAIIT-------- 367
Cdd:cd13989    1 LGSGGFGYVTLWKHQDtgeYVAIKKCRQELSPSDKNRErWCLEVQIMKKLNHPNVV---SARDVPPELEKLSpndlplla 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 -SLCKGRTLYSVVRDAKIV--LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD--NGKVV--ITDFGLfsisgv 440
Cdd:cd13989   78 mEYCSGGDLRKVLNQPENCcgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQqgGGRVIykLIDLGY------ 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 441 lqAGRRDDKLRIQN--GWLCHLAPEIIrqlspdtEEDKLPFSkhSDVFALGTIWYELHAREWPF--KTQPAEaiiWQM 514
Cdd:cd13989  152 --AKELDQGSLCTSfvGTLQYLAPELF-------ESKKYTCT--VDYWSFGTLAFECITGYRPFlpNWQPVQ---WHG 215
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
296-434 1.18e-07

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: 53.23  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHGR---WHGEVAIRlIDIERDNEDQLKafkREVMAYRQ--------------TRHENVVLFM---G 355
Cdd:cd14016    4 LVKKIGSGSFGEVYLGIdlkTGEEVAIK-IEKKDSKHPQLE---YEAKVYKLlqggpgiprlywfgQEGDYNVMVMdllG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 356 acmspPHLAIITSLCKGR-TLysvvrdaKIVLdvnktrQIAQEIVKGMGYLHAKGILHKDLKSKN----VFYDNGKVVIT 430
Cdd:cd14016   80 -----PSLEDLFNKCGRKfSL-------KTVL------MLADQMISRLEYLHSKGYIHRDIKPENflmgLGKNSNKVYLI 141

                 ....
gi 568937340 431 DFGL 434
Cdd:cd14016  142 DFGL 145
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
338-433 1.19e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 54.11  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 338 EVMAYRQTRHENVV-----LFMGA--CMSPPHLAiitslckgRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGI 410
Cdd:PHA03209 107 EAMLLQNVNHPSVIrmkdtLVSGAitCMVLPHYS--------SDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRI 178
                         90       100
                 ....*....|....*....|....
gi 568937340 411 LHKDLKSKNVFYDN-GKVVITDFG 433
Cdd:PHA03209 179 IHRDVKTENIFINDvDQVCIGDLG 202
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
300-434 1.21e-07

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: 53.47  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFmgacmsppHLAIITSLCKGRTLY 376
Cdd:cd07871   13 LGEGTYATVFKGRsklTENLVALKEIRLEHEEGAPCTAI-REVSLLKNLKHANIVTL--------HDIIHTERCLTLVFE 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 377 SVVRDAKIVLD-------VNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL 434
Cdd:cd07871   84 YLDSDLKQYLDncgnlmsMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLInEKGELKLADFGL 149
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
298-497 1.34e-07

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: 53.46  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKgRT 374
Cdd:cd07872   12 EKLGEGTYATVFKGRsklTENLVALKEIRLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD-KD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSISGVLQAGRRDDKLRIq 453
Cdd:cd07872   90 LKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLInERGELKLADFGLARAKSVPTKTYSNEVVTL- 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568937340 454 ngWLchlapeiirqLSPDTEEDKLPFSKHSDVFALGTIWYELHA 497
Cdd:cd07872  169 --WY----------RPPDVLLGSSEYSTQIDMWGVGCIFFEMAS 200
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
295-493 1.36e-07

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: 52.97  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFG---QVYHGRWHGEVAIRLIDIErdNEDQLKAFK-REVMAyrQTRHENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd14107    5 EVKEEIGRGTFGfvkRVTHKGNGECCAAKFIPLR--SSTRARAFQeRDILA--RLSHRRLTCLLDQFETRKTLILILELC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLY------SVVRDAKIVLDVnktrqiaQEIVKGMGYLHAKGILHKDLKSKN---VFYDNGKVVITDFGLfsisgvl 441
Cdd:cd14107   81 SSEELLdrlflkGVVTEAEVKLYI-------QQVLEGIGYLHGMNILHLDIKPDNilmVSPTREDIKICDFGF------- 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 442 qaGRRDDKLRIQ---NGWLCHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWY 493
Cdd:cd14107  147 --AQEITPSEHQfskYGSPEFVAPEIVHQ---------EPVSAATDIWALGVIAY 190
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
291-510 1.49e-07

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: 53.88  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEigeLIGKGRFGQVY------HGRWHgevAIRLIDIERD-NEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHL 363
Cdd:cd05594   27 FEYLK---LLGKGTFGKVIlvkekaTGRYY---AMKILKKEVIvAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLY-SVVRDAkiVLDVNKTRQIAQEIVKGMGYLHA-KGILHKDLKSKNVFYD-NGKVVITDFGLfsisgv 440
Cdd:cd05594  101 CFVMEYANGGELFfHLSRER--VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDkDGHIKITDFGL------ 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 441 LQAGRRDD-KLRIQNGWLCHLAPEIIrqlspdteEDKlPFSKHSDVFALGTIWYELHAREWPFKTQPAEAI 510
Cdd:cd05594  173 CKEGIKDGaTMKTFCGTPEYLAPEVL--------EDN-DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 234
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
300-502 1.58e-07

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: 53.00  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQV--YHGRWHGE-VAIRLIDIERDNEDQLKaFKREVMAYRQTRHENVVlfmGACMSP----------PHLAIi 366
Cdd:cd14039    1 LGTGGFGNVclYQNQETGEkIAIKSCRLELSVKNKDR-WCHEIQIMKKLNHPNVV---KACDVPeemnflvndvPLLAM- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 tSLCKGRTLYSVVRDAKIVLDVNKTR--QIAQEIVKGMGYLHAKGILHKDLKSKNvfydngkVVITDFGLFSISGVLQAG 444
Cdd:cd14039   76 -EYCSGGDLRKLLNKPENCCGLKESQvlSLLSDIGSGIQYLHENKIIHRDLKPEN-------IVLQEINGKIVHKIIDLG 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 445 RRDDklrIQNGWLCHLAPEIIRQLSPDTEEDKlPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14039  148 YAKD---LDQGSLCTSFVGTLQYLAPELFENK-SYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
291-502 1.63e-07

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: 53.49  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIGELIGKGRFGQVYHGRWHGE---VAIRLIDIE--RDNEDqLKAFKREVMAYRQTRHENVVLFMGACMSPPH--L 363
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNdqiYAMKVVKKElvHDDED-IDWVQTEKHVFEQASSNPFLVGLHSCFQTTSrlF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQ 442
Cdd:cd05617   93 LVIEYVNGGDLMFHMQRQRK--LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDaDGHIKLTDYGMCK-----E 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 443 AGRRDDKLRIQNGWLCHLAPEIIRQlspdteeDKLPFSkhSDVFALGTIWYELHAREWPF 502
Cdd:cd05617  166 GLGPGDTTSTFCGTPNYIAPEILRG-------EEYGFS--VDWWALGVLMFEMMAGRSPF 216
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
295-434 1.64e-07

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: 52.92  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWH--GE-VAIRlidierdnedQLKA-FK--------REVMAYRQ-TRHENVVLFMGACMSPP 361
Cdd:cd07830    2 KVIKQLGDGTFGSVYLARNKetGElVAIK----------KMKKkFYsweecmnlREVKSLRKlNEHPNIVKLKEVFREND 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 362 HLAIITSLCKGrTLYSVVRDAK-IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGL 434
Cdd:cd07830   72 ELYFVFEYMEG-NLYQLMKDRKgKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVkIADFGL 145
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
300-434 1.92e-07

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: 53.06  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRW-----HGEVAIRLIDIERDNEDQLKAFK-REVMAYRQTRHENVVLFMGACMSPphlaiitslcKGR 373
Cdd:cd07842    8 IGRGTYGRVYKAKRkngkdGKEYAIKKFKGDKEQYTGISQSAcREIALLRELKHENVVSLVEVFLEH----------ADK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVV--------------RDAK-IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-----YDNGKVVITDFG 433
Cdd:cd07842   78 SVYLLFdyaehdlwqiikfhRQAKrVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILvmgegPERGVVKIGDLG 157

                 .
gi 568937340 434 L 434
Cdd:cd07842  158 L 158
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
337-511 2.13e-07

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: 53.07  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 337 REVMAYRQTR-HENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDL 415
Cdd:cd14092   47 REVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGGELLERIRKKK-RFTESEASRIMRQLVSAVSFMHSKGVVHRDL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 416 KSKNVFY----DNGKVVITDFGlFSisgvlqagrrddKLRIQNGWL---C----HLAPEIIRQLSPDTEEDklpfsKHSD 484
Cdd:cd14092  126 KPENLLFtdedDDAEIKIVDFG-FA------------RLKPENQPLktpCftlpYAAPEVLKQALSTQGYD-----ESCD 187
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568937340 485 VFALGTIWYELHAREWPFKT----QPAEAII 511
Cdd:cd14092  188 LWSLGVILYTMLSGQVPFQSpsrnESAAEIM 218
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
300-502 2.41e-07

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: 52.69  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWH--GEV-AIRLID----IERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd05589    7 LGRGHFGKVLLAEYKptGELfAIKALKkgdiIARDEVESLMCEKRIFETVNSARHPFLVNLFACFQTPEHVCFVMEYAAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTLYSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSiSGVLQAGRrddklr 451
Cdd:cd05589   87 GDLMMHIHED--VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDtEGYVKIADFGLCK-EGMGFGDR------ 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 452 iqNGWLC----HLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05589  158 --TSTFCgtpeFLAPEVLTDTS---------YTRAVDWWGLGVLIYEMLVGESPF 201
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
294-502 2.57e-07

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: 52.34  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHGRWH---GEVAIRLIDI-ERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd08228    4 FQIEKKIGRGQFSEVYRATCLldrKPVALKKVQIfEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDVNKTRQIAQEIVK---GMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL--FSISGVLQA 443
Cdd:cd08228   84 ADAGDLSQMIKYFKKQKRLIPERTVWKYFVQlcsAVEHMHSRRVMHRDIKPANVFITaTGVVKLGDLGLgrFFSSKTTAA 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 444 grrddklRIQNGWLCHLAPEIIrqlspdtEEDKLPFSkhSDVFALGTIWYELHAREWPF 502
Cdd:cd08228  164 -------HSLVGTPYYMSPERI-------HENGYNFK--SDIWSLGCLLYEMAALQSPF 206
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
288-502 2.61e-07

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: 52.44  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEQLEIGELIGKGRFG---QVYHGRWHGEVAIRLIDIERDNEDQlKAFKREVMAYRQTRHENVVLFMGACMS-PPHL 363
Cdd:cd06620    1 DLKNQDLETLKDLGAGNGGsvsKVLHIPTGTIMAKKVIHIDAKSSVR-KQILRELQILHECHSPYIVSFYGAFLNeNNNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKGRTLYSVVRDAK-IVLDVNKtrQIAQEIVKGMGYLHAK-GILHKDLKSKNVFYDN-GKVVITDFGlfsISGV 440
Cdd:cd06620   80 IICMEYMDCGSLDKILKKKGpFPEEVLG--KIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSkGQIKLCDFG---VSGE 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 441 LQAGRRDDKLriqnGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd06620  155 LINSIADTFV----GTSTYMSPERIQGGK---------YSVKSDVWSLGLSIIELALGEFPF 203
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
299-546 2.66e-07

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 52.75  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRWHGE---VAIRLIDIERDNEDQLKAFK-----REVMAYRQTRHENVV-LFMGACMSPPHLAIITSL 369
Cdd:cd14041   13 LLGRGGFSEVYKAFDLTEqryVAVKIHQLNKNWRDEKKENYhkhacREYRIHKELDHPRIVkLYDYFSLDTDSFCTVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLHA--KGILHKDLKSKNVFYDNG----KVVITDFGLFSISGVLQA 443
Cdd:cd14041   93 CEGNDLDFYLKQHKLMSE-KEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGtacgEIKITDFGLSKIMDDDSY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 GRRDD-KLRIQN-GWLCHLAPE--IIRQLSPDteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMK 519
Cdd:cd14041  172 NSVDGmELTSQGaGTYWYLPPEcfVVGKEPPK-------ISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILK 244
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 520 PNLSQI----GMGKEISDILLFCWAFEQEER 546
Cdd:cd14041  245 ATEVQFppkpVVTPEAKAFIRRCLAYRKEDR 275
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
300-440 2.78e-07

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: 52.27  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVY---HGRWHGEVAIRLI-----DIERDNEdqlkafKREVMAYRQ-TRHENVVLFMGACMSPPH--LAIITS 368
Cdd:cd07831    7 IGEGTFSEVLkaqSRKTGKYYAIKCMkkhfkSLEQVNN------LREIQALRRlSPHPNILRLIEVLFDRKTgrLALVFE 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 369 LCKGrTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGlfSISGV 440
Cdd:cd07831   81 LMDM-NLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDILKLADFG--SCRGI 149
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
337-508 2.78e-07

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: 52.28  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 337 REVMAYRQTRHENVVLFMGACMSPP--HLAIITSLCKGRTLYSVVRDAKIVLDvnKTRQIAQEIVKGMGYLHAKGILHKD 414
Cdd:cd14199   74 QEIAILKKLDHPNVVKLVEVLDDPSedHLYMVFELVKQGPVMEVPTLKPLSED--QARFYFQDLIKGIEYLHYQKIIHRD 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 415 LKSKNVFY-DNGKVVITDFGlfsISGVLQAGrrDDKLRIQNGWLCHLAPEIIrqlspdTEEDKLPFSKHSDVFALGTIWY 493
Cdd:cd14199  152 VKPSNLLVgEDGHIKIADFG---VSNEFEGS--DALLTNTVGTPAFMAPETL------SETRKIFSGKALDVWAMGVTLY 220
                        170       180
                 ....*....|....*....|....*..
gi 568937340 494 ELHAREWPF------------KTQPAE 508
Cdd:cd14199  221 CFVFGQCPFmderilslhskiKTQPLE 247
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
296-434 2.84e-07

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 52.84  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHG---RWHGEVAIRLIDIERDNEDQLKAFK------------REVMAYRQTRHENVVLFMGACMSP 360
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAydtLTGKIVAIKKVKIIEISNDVTKDRQlvgmcgihfttlRELKIMNEIKHENIMGLVDVYVEG 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 361 PHLAIITSLCKGrTLYSVVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGL 434
Cdd:PTZ00024  93 DFINLVMDIMAS-DLKKVV-DRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSkGICKIADFGL 165
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
386-546 2.90e-07

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: 52.62  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 386 LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLF--SISGvlqagrrDDKLRIQNGWLCHLAP 462
Cdd:cd05619  103 FDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKdGHIKIADFGMCkeNMLG-------DAKTSTFCGTPDYIAP 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 463 EIIRQLSPDTEEDKLPFskhsdvfalGTIWYELHAREWPFKTQPAEAIIW--QMGTGMKPNLsqigMGKEISDILLFCWA 540
Cdd:cd05619  176 EILLGQKYNTSVDWWSF---------GVLLYEMLIGQSPFHGQDEEELFQsiRMDNPFYPRW----LEKEAKDILVKLFV 242

                 ....*.
gi 568937340 541 FEQEER 546
Cdd:cd05619  243 REPERR 248
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
300-552 3.03e-07

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: 52.26  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWH-----GEVAIRLIDIERDNEDQLKaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd14206    5 IGNGWFGKVILGEIFsdytpAQVVVKELRVSAGPLEQRK-FISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAK---------IVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSISGVLQAG 444
Cdd:cd14206   84 LKRYLRAQRkadgmtpdlPTRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVrIGDYGLSHNNYKEDYY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 RRDDKLRIQNGWlchLAPEIIRQLSPD---TEEdklpfSKHSDVFALGTIWYELhareWPFKTQP----------AEAII 511
Cdd:cd14206  164 LTPDRLWIPLRW---VAPELLDELHGNlivVDQ-----SKESNVWSLGVTIWEL----FEFGAQPyrhlsdeevlTFVVR 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568937340 512 WQMGTGMKPNLsQIGMGKEISDILLFCWaFEQEERPTFTKL 552
Cdd:cd14206  232 EQQMKLAKPRL-KLPYADYWYEIMQSCW-LPPSQRPSVEEL 270
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
295-434 3.10e-07

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: 51.87  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGR---WHGEVAIRLidiERDNEDQlKAFKREVMAYRQT---RHenVVLFMGACMSPPHLAIITS 368
Cdd:cd14017    3 KVVKKIGGGGFGEIYKVRdvvDGEEVAMKV---ESKSQPK-QVLKMEVAVLKKLqgkPH--FCRLIGCGRTERYNYIVMT 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 369 LCkGRTLYSVVRDA-KIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-----FYDNGKVVITDFGL 434
Cdd:cd14017   77 LL-GPNLAELRRSQpRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFaigrgPSDERTVYILDFGL 147
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
298-440 3.17e-07

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: 52.12  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGR--WHGE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFmgacmspphLAIITSlckGRT 374
Cdd:cd07860    6 EKIGEGTYGVVYKARnkLTGEvVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKL---------LDVIHT---ENK 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 375 LYSVV----RDAKIVLDVNKTRQIAQEIVK--------GMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGV 440
Cdd:cd07860   74 LYLVFeflhQDLKKFMDASALTGIPLPLIKsylfqllqGLAFCHSHRVLHRDLKPQNLLINtEGAIKLADFGLARAFGV 152
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
291-434 4.17e-07

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: 51.93  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIGELIGKGRFGQVYHGRwHGE----VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFmgacmspPHLAII 366
Cdd:cd07866    7 LRDYEILGKLGEGTFGEVYKAR-QIKtgrvVALKKILMHNEKDGFPITALREIKILKKLKHPNVVPL-------IDMAVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSV--------------VRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITD 431
Cdd:cd07866   79 RPDKSKRKRGSVymvtpymdhdlsglLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNqGILKIAD 158

                 ...
gi 568937340 432 FGL 434
Cdd:cd07866  159 FGL 161
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
397-502 4.36e-07

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: 52.23  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 EIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFsisgvlQAGRRDDKLRIQN--GWLCHLAPEIIRqlspdte 473
Cdd:cd05614  113 EIILALEHLHKLGIVYRDIKLENILLDSeGHVVLTDFGLS------KEFLTEEKERTYSfcGTIEYMAPEIIR------- 179
                         90       100
                 ....*....|....*....|....*....
gi 568937340 474 eDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05614  180 -GKSGHGKAVDWWSLGILMFELLTGASPF 207
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
298-434 4.40e-07

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 51.97  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRwhgevairlidiERDNED--QLKAFKREVMAYR----QTRHENVVL------FMGAC----MSPP 361
Cdd:cd05571    1 KVLGKGTFGKVILCR------------EKATGElyAIKILKKEVIIAKdevaHTLTENRVLqntrhpFLTSLkysfQTND 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937340 362 HLAIITSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:cd05571   69 RLCFVMEYVNGGELFFHLSRER-VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDkDGHIKITDFGL 141
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
291-502 4.62e-07

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: 51.43  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIGELIGKGRFGQVYH--GRWHGEV-AIRLIDIERDNEDQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd14114    1 YDHYDILEELGTGAFGVVHRctERATGNNfAAKFIMTPHESDKET--VRKEIQIMNQLHHPKLINLHDAFEDDNEMVLIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGK---VVITDFGLfsisgvlqAG 444
Cdd:cd14114   79 EFLSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRsneVKLIDFGL--------AT 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 RRDDK--LRIQNGWLCHLAPEIIrqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14114  151 HLDPKesVKVTTGTAEFAAPEIV---------EREPVGFYTDMWAVGVLSYVLLSGLSPF 201
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
300-434 4.69e-07

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: 51.99  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLfMGACMSPPH------LAIITSLC 370
Cdd:cd07858   13 IGRGAYGIVCSAKnseTNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIA-IKDIMPPPHreafndVYIVYELM 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 371 KgRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:cd07858   92 D-TDLHQIIRSSQ-TLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNaNCDLKICDFGL 154
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
265-437 4.97e-07

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 52.13  E-value: 4.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 265 LSLLSARSFPRKASQTSIFLQEWDIPFEQLEIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDnEDQLKAFKREVMA 341
Cdd:PLN00034  47 LPPPSSSSSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPtgrLYALKVIYGNHE-DTVRRQICREIEI 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 342 YRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLysvvrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF 421
Cdd:PLN00034 126 LRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSL-----EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLL 200
                        170
                 ....*....|....*..
gi 568937340 422 YDNGK-VVITDFGLFSI 437
Cdd:PLN00034 201 INSAKnVKIADFGVSRI 217
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
278-502 5.01e-07

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: 51.96  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 278 SQTSIFLQEWDIPfeqleigELIGKGRFGQVYHGRWHGE---VAIRLIDIERDNEDQ-LKAFKREVMAYRQTRHENVVLF 353
Cdd:cd05618   13 ASSSLGLQDFDLL-------RVIGRGSYAKVLLVRLKKTeriYAMKVVKKELVNDDEdIDWVQTEKHVFEQASNHPFLVG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 354 MGACMSPPH--LAIITSLCKGRTLYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVIT 430
Cdd:cd05618   86 LHSCFQTESrlFFVIEYVNGGDLMFHMQRQRK--LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSeGHIKLT 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 431 DFGLFSisgvlQAGRRDDKLRIQNGWLCHLAPEIIRQlspdteEDklpFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05618  164 DYGMCK-----EGLRPGDTTSTFCGTPNYIAPEILRG------ED---YGFSVDWWALGVLMFEMMAGRSPF 221
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
332-495 5.52e-07

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: 51.70  E-value: 5.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 332 LKAFKREVMAYRQTRHENVV-----LFMGACMSPPHLAIITSLckgRTLYSVVR----DAKIVLDVNK-----TRQIAQE 397
Cdd:cd07854   46 VKHALREIKIIRRLDHDNIVkvyevLGPSGSDLTEDVGSLTEL---NSVYIVQEymetDLANVLEQGPlseehARLFMYQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 398 IVKGMGYLHAKGILHKDLKSKNVFYDNGKVV--ITDFGL-------FSISGVLQAGrrddklrIQNGWlcHLAPEIIrqL 468
Cdd:cd07854  123 LLRGLKYIHSANVLHRDLKPANVFINTEDLVlkIGDFGLarivdphYSHKGYLSEG-------LVTKW--YRSPRLL--L 191
                        170       180
                 ....*....|....*....|....*..
gi 568937340 469 SPDTeedklpFSKHSDVFALGTIWYEL 495
Cdd:cd07854  192 SPNN------YTKAIDMWAAGCIFAEM 212
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
300-559 5.61e-07

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: 51.36  E-value: 5.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG-EVAIRLI--DIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd14159    1 IGEGGFGCVYQAVMRNtEYAVKRLkeDSELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVR--DAKIVLDVNKTRQIAQEIVKGMGYLH--AKGILHKDLKSKNVFYD---NGKvvITDFGL--FSISGVlQAGRRD 447
Cdd:cd14159   81 DRLHcqVSCPCLSWSQRLHVLLGTARAIQYLHsdSPSLIHGDVKSSNILLDaalNPK--LGDFGLarFSRRPK-QPGMSS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 448 DKLRIQN--GWLCHLAPEIIR--QLSPDTeedklpfskhsDVFALGTIWYELHAREWPFKTQPAEAIIWQ---------- 513
Cdd:cd14159  158 TLARTQTvrGTLAYLPEEYVKtgTLSVEI-----------DVYSFGVVLLELLTGRRAMEVDSCSPTKYLkdlvkeeeea 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 514 ------MGTGMKPNLSQIGM------------------GKEISDILLFCWAFEQEERPTFTKLMDMLEKL 559
Cdd:cd14159  227 qhtpttMTHSAEAQAAQLATsicqkhldpqagpcppelGIEISQLACRCLHRRAKKRPPMTEVFQELERL 296
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
300-495 5.64e-07

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: 51.28  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGE---VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd08221    8 LGRGAFGEAVLYRKTEDnslVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SvvrdaKIVLDVNKTRQIAQ------EIVKGMGYLHAKGILHKDLKSKNVFYDngKVVITDFGLFSISGVLqagrrDDKL 450
Cdd:cd08221   88 D-----KIAQQKNQLFPEEVvlwylyQIVSAVSHIHKAGILHRDIKTLNIFLT--KADLVKLGDFGISKVL-----DSES 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340 451 RIQN---GWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYEL 495
Cdd:cd08221  156 SMAEsivGTPYYMSPELVQ---------GVKYNFKSDIWAVGCVLYEL 194
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
287-508 6.53e-07

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: 51.13  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQL--EIGELiGKGRFGQVYHGRWHGE---VAIRLIDIERDNEDQLKafkREVMAYRQTRHENVVLFMGACMSPP 361
Cdd:cd14113    1 WKDNFDSFysEVAEL-GRGRFSVVKKCDQRGTkraVATKFVNKKLMKRDQVT---HELGVLQSLQHPQLVGLLDTFETPT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLC-KGRTLYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG----KVVITDFGlfs 436
Cdd:cd14113   77 SYILVLEMAdQGRLLDYVVRWGN--LTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSlskpTIKLADFG--- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 437 isgvlqagrrdDKLRIQNGWLCH--------LAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAE 508
Cdd:cd14113  152 -----------DAVQLNTTYYIHqllgspefAAPEIIL---------GNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVE 211
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
393-553 6.74e-07

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: 51.22  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 393 QIAQEIVKGMGYLHAK-GILHKDLKSKNVFYD-NGKVVITDFGlfsISGVLQAGRRDDKlriQNGWLCHLAPEiirQLSP 470
Cdd:cd06618  118 KMTVSIVKALHYLKEKhGVIHRDVKPSNILLDeSGNVKLCDFG---ISGRLVDSKAKTR---SAGCAAYMAPE---RIDP 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 471 DTEEDklpFSKHSDVFALGTIWYELHAREWPFKTQPAEaiiWQMGTGM------KPNLSQiGMGKEISDILLFCWAFEQE 544
Cdd:cd06618  189 PDNPK---YDIRADVWSLGISLVELATGQFPYRNCKTE---FEVLTKIlneeppSLPPNE-GFSPDFCSFVDLCLTKDHR 261

                 ....*....
gi 568937340 545 ERPTFTKLM 553
Cdd:cd06618  262 YRPKYRELL 270
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
395-502 8.32e-07

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: 50.87  E-value: 8.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 395 AQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsisgvlqAGRRDDKLriqngW-LC----HLAPEIIrqL 468
Cdd:cd14209  107 AAQIVLAFEYLHSLDLIYRDLKPENLLIDqQGYIKVTDFGF--------AKRVKGRT-----WtLCgtpeYLAPEII--L 171
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568937340 469 SPdteedklPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14209  172 SK-------GYNKAVDWWALGVLIYEMAAGYPPF 198
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
363-554 8.44e-07

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 50.76  E-value: 8.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 LAIITSLCKGRTLYSVVRDAKivlDVNKTRQIAQEIVKGMG----YLHAKGILHKDLKSKNVFY----DNGKVVITDFGl 434
Cdd:cd14172   76 LLIIMECMEGGELFSRIQERG---DQAFTEREASEIMRDIGtaiqYLHSMNIAHRDVKPENLLYtskeKDAVLKLTDFG- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 435 FSISGVLQagrrdDKLRIQNGWLCHLAPEIirqLSPDTeedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIiwqm 514
Cdd:cd14172  152 FAKETTVQ-----NALQTPCYTPYYVAPEV---LGPEK------YDKSCDMWSLGVIMYILLCGFPPFYSNTGQAI---- 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568937340 515 GTGMK----------PNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd14172  214 SPGMKrrirmgqygfPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMN 263
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
300-437 9.39e-07

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: 51.03  E-value: 9.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd07856   18 VGMGAFGLVCSARdqlTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTELLGTDLH 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 377 SVVRDAKIvldvnkTRQIAQ----EIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFSI 437
Cdd:cd07856   98 RLLTSRPL------EKQFIQyflyQILRGLKYVHSAGVIHRDLKPSNILVnENCDLKICDFGLARI 157
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
397-553 9.93e-07

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 51.56  E-value: 9.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 EIVKGMGYLHAKGILHKDLKSKNVF-YDNGKVVITDFGL---FSISGVLQAGRRddklriqngwLC----HLAPEIIrql 468
Cdd:PTZ00267 177 QIVLALDEVHSRKMMHRDLKSANIFlMPTGIIKLGDFGFskqYSDSVSLDVASS----------FCgtpyYLAPELW--- 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 469 spdteeDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMK---PNLSQIGMgKEISDILLfcwAFEQEE 545
Cdd:PTZ00267 244 ------ERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYdpfPCPVSSGM-KALLDPLL---SKNPAL 313

                 ....*...
gi 568937340 546 RPTFTKLM 553
Cdd:PTZ00267 314 RPTTQQLL 321
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
338-433 1.03e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 51.62  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 338 EVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKgRTLYSVVRDAKIVLD----VNKTRQIAQEIVKGMGYLHAKGILHK 413
Cdd:PHA03210 213 EILALGRLNHENILKIEEILRSEANTYMITQKYD-FDLYSFMYDEAFDWKdrplLKQTRAIMKQLLCAVEYIHDKKLIHR 291
                         90       100
                 ....*....|....*....|.
gi 568937340 414 DLKSKNVFYD-NGKVVITDFG 433
Cdd:PHA03210 292 DIKLENIFLNcDGKIVLGDFG 312
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
395-502 1.16e-06

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: 50.77  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 395 AQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFS---ISGVlqagrrddKLRIQNGWLCHLAPEIIRQlsp 470
Cdd:cd05615  117 AAEISVGLFFLHKKGIIYRDLKLDNVMLDsEGHIKIADFGMCKehmVEGV--------TTRTFCGTPDYIAPEIIAY--- 185
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568937340 471 dteedkLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05615  186 ------QPYGRSVDWWAYGVLLYEMLAGQPPF 211
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
292-565 1.29e-06

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 50.62  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNED---QLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAI 365
Cdd:cd14094    3 DVYELCEVIGKGPFSVVRrciHRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTL-YSVVR--DAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY---DN-GKVVITDFGL---F 435
Cdd:cd14094   83 VFEFMDGADLcFEIVKraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENsAPVKLGGFGVaiqL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 436 SISGVLQAGRRddklriqnGWLCHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPF---KTQPAEAII- 511
Cdd:cd14094  163 GESGLVAGGRV--------GTPHFMAPEVVK---------REPYGKPVDVWGCGVILFILLSGCLPFygtKERLFEGIIk 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 512 --WQMGTGMKPNLSQIGM-----------GKEIS--DILLFCWAFEQEERPTFTKLMDMLEKLPKRNRR 565
Cdd:cd14094  226 gkYKMNPRQWSHISESAKdlvrrmlmldpAERITvyEALNHPWIKERDRYAYRIHLPETVEQLRKFNAR 294
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
292-434 1.30e-06

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 50.20  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGR---WHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPphlaiits 368
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARdrvTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSE-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 lckgRTLYSVVR----DAKIVLD----VNKTRQIAQ----EIVKGMGYLHAKGILHKDLKSKNVFYD--NGKVVITDFGL 434
Cdd:PLN00009  74 ----KRLYLVFEyldlDLKKHMDsspdFAKNPRLIKtylyQILRGIAYCHSHRVLHRDLKPQNLLIDrrTNALKLADFGL 149
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
298-494 1.31e-06

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: 49.98  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVY---HGRWHGE-VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGR 373
Cdd:cd14121    1 EKLGSGTYATVYkayRKSGAREvVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 374 TLYSVVRdAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV---FYDNGKVVITDFGlFSisgvlQAGRRDDKL 450
Cdd:cd14121   81 DLSRFIR-SRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLllsSRYNPVLKLADFG-FA-----QHLKPNDEA 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568937340 451 RIQNGWLCHLAPEIIRQLSPDTEedklpfskhSDVFALGTIWYE 494
Cdd:cd14121  154 HSLRGSPLYMAPEMILKKKYDAR---------VDLWSVGVILYE 188
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
316-515 1.31e-06

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: 50.41  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 316 EVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVvlfmgacmspphLAIITSLCKGRTLYSV---VRDAKIVLDVNKTR 392
Cdd:cd14173   29 EYAVKIIE-KRPGHSRSRVFREVEMLYQCQGHRNV------------LELIEFFEEEDKFYLVfekMRGGSILSHIHRRR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 393 Q--------IAQEIVKGMGYLHAKGILHKDLKSKNVFYDN----GKVVITDFGLFsiSGVLQAGR----RDDKLRIQNGW 456
Cdd:cd14173   96 HfneleasvVVQDIASALDFLHNKGIAHRDLKPENILCEHpnqvSPVKICDFDLG--SGIKLNSDcspiSTPELLTPCGS 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 457 LCHLAPEIIRQLSpdteEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMG 515
Cdd:cd14173  174 AEYMAPEVVEAFN----EEASIYDKRCDLWSLGVILYIMLSGYPPFVGRCGSDCGWDRG 228
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
317-522 1.37e-06

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 50.71  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 317 VAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLckgrTLYSVVRDAKIVLDVNKTRQIA- 395
Cdd:cd08227   28 VTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF----MAYGSAKDLICTHFMDGMSELAi 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 396 ----QEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITdfGLFSISGVLQAGRRddkLRIQNGWLCHLApEIIRQLSP 470
Cdd:cd08227  104 ayilQGVLKALDYIHHMGYVHRSVKASHILISvDGKVYLS--GLRSNLSMINHGQR---LRVVHDFPKYSV-KVLPWLSP 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 471 DTEEDKLP-FSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNL 522
Cdd:cd08227  178 EVLQQNLQgYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCL 230
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
299-505 1.49e-06

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: 50.02  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVY--HGRWHGevaiRLIDIERDNEDQLKAFKREVMAYRQTR------HENVVLFMGACMSPPHLAIITSLC 370
Cdd:cd05630    7 VLGKGGFGEVCacQVRATG----KMYACKKLEKKRIKKRKGEAMALNEKQilekvnSRFVVSLAYAYETKDALCLVLTLM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTL-YSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsisGVLQAGRRDD 448
Cdd:cd05630   83 NGGDLkFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDhGHIRISDLGL----AVHVPEGQTI 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 449 KLRIqnGWLCHLAPEIIRQlspdteeDKLPFSkhSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd05630  159 KGRV--GTVGYMAPEVVKN-------ERYTFS--PDWWALGCLLYEMIAGQSPFQQR 204
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
298-553 1.54e-06

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. 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 Wee1a 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: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 50.02  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHgrwhgevAIRLID-----IERDNE------DQLKAFkREVMAYRQT-RHENVVLFMGACMSPPHLAI 365
Cdd:cd14138   11 EKIGSGEFGSVFK-------CVKRLDgciyaIKRSKKplagsvDEQNAL-REVYAHAVLgQHSHVVRYYSAWAEDDHMLI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQ---EIVKGMGYLHAKGILHKDLKSKNVF------------------YDN 424
Cdd:cd14138   83 QNEYCNGGSLADAISENYRIMSYFTEPELKDlllQVARGLKYIHSMSLVHMDIKPSNIFisrtsipnaaseegdedeWAS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 425 GKVV--ITDFGLFSISGVLQAGRRDDKLriqngwlchLAPEIIrqlspdtEEDKLPFSKhSDVFALG-TIWYELHARewP 501
Cdd:cd14138  163 NKVIfkIGDLGHVTRVSSPQVEEGDSRF---------LANEVL-------QENYTHLPK-ADIFALAlTVVCAAGAE--P 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 502 FktqPAEAIIW-QMGTGMKPNLSQIgMGKEISDILLFCWAFEQEERPTFTKLM 553
Cdd:cd14138  224 L---PTNGDQWhEIRQGKLPRIPQV-LSQEFLDLLKVMIHPDPERRPSAVALV 272
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
41-83 1.84e-06

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: 45.15  E-value: 1.84e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568937340    41 HRFSTKYW-MSQTCTVCGK----GMLFGLKCKNCKLKCHNKCTKEAPP 83
Cdd:smart00109   1 HKHVFRTFtKPTFCCVCRKsiwgSFKQGLRCSECKVKCHKKCADKVPK 48
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
386-562 1.98e-06

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: 49.67  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 386 LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlfsISGVLQAGrrDDKLRIQNGWLCHLAPEi 464
Cdd:cd14118  112 LSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLgDDGHVKIADFG---VSNEFEGD--DALLSSTAGTPAFMAPE- 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 465 irQLSPDTEEdklpFS-KHSDVFALGTIWYELHAREWPFKtqpAEAIiwqmgtgmkpnlsqIGMGKEI-SDILLFCwafe 542
Cdd:cd14118  186 --ALSESRKK----FSgKALDIWAMGVTLYCFVFGRCPFE---DDHI--------------LGLHEKIkTDPVVFP---- 238
                        170       180
                 ....*....|....*....|....*
gi 568937340 543 qeERPTFT-KLMD----MLEKLPKR 562
Cdd:cd14118  239 --DDPVVSeQLKDlilrMLDKNPSE 261
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
296-562 2.39e-06

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: 49.64  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHGRW---HGEVAIRLIDI-----ERDNEDQLKafkrEVMAYRQTRHENVVLFMGACMSPPHLAIIT 367
Cdd:cd08229   28 IEKKIGRGQFSEVYRATClldGVPVALKKVQIfdlmdAKARADCIK----EIDLLKQLNHPNVIKYYASFIEDNELNIVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 368 SLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVK---GMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL--FSISGVL 441
Cdd:cd08229  104 ELADAGDLSRMIKHFKKQKRLIPEKTVWKYFVQlcsALEHMHSRRVMHRDIKPANVFITaTGVVKLGDLGLgrFFSSKTT 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 442 QAgrrddklRIQNGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAE--AIIWQMGTGMK 519
Cdd:cd08229  184 AA-------HSLVGTPYYMSPERIHENG---------YNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCDY 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568937340 520 PNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKLPKR 562
Cdd:cd08229  248 PPLPSDHYSEELRQLVNMCINPDPEKRPDITYVYDVAKRMHAR 290
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
299-564 2.40e-06

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 49.67  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVY-----HGRWHGEVAIRLIDIERDNEDQLKAFK---REVMAYRQTRHENVV-LFMGACMSPPHLAIITSL 369
Cdd:cd14040   13 LLGRGGFSEVYkafdlYEQRYAAVKIHQLNKSWRDEKKENYHKhacREYRIHKELDHPRIVkLYDYFSLDTDTFCTVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAKIVLDvNKTRQIAQEIVKGMGYLH--AKGILHKDLKSKNVFYDNG----KVVITDFGLFSISGVLQA 443
Cdd:cd14040   93 CEGNDLDFYLKQHKLMSE-KEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacgEIKITDFGLSKIMDDDSY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 444 GRRDDKLRIQN-GWLCHLAPE--IIRQLSPDteedklpFSKHSDVFALGTIWYE-LHAREwPFKTQPAEAIIWQMGTGMK 519
Cdd:cd14040  172 GVDGMDLTSQGaGTYWYLPPEcfVVGKEPPK-------ISNKVDVWSVGVIFFQcLYGRK-PFGHNQSQQDILQENTILK 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568937340 520 PNLSQIGMGKEISD----ILLFCWAFEQEERPTFTKLMDMLEKLPKRNR 564
Cdd:cd14040  244 ATEVQFPVKPVVSNeakaFIRRCLAYRKEDRFDVHQLASDPYLLPHMRR 292
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
395-504 2.57e-06

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: 49.28  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 395 AQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsiSGVLQAGrrdDKLRIQNGWLCHLAPEIIRQlspdte 473
Cdd:cd05605  108 AAEITCGLEHLHSERIVYRDLKPENILLDDhGHVRISDLGL---AVEIPEG---ETIRGRVGTVGYMAPEVVKN------ 175
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568937340 474 eDKLPFSkhSDVFALGTIWYELHAREWPFKT 504
Cdd:cd05605  176 -ERYTFS--PDWWGLGCLIYEMIEGQAPFRA 203
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
294-503 2.69e-06

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: 49.66  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 294 LEIGELIGKGRFGQVYHGRWH--GEV-AIRLIDIERDNEDQ---LKAFKREVMAYRQTRHENVVLFMG-ACMSPPHLAII 366
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRKAdtGKMyAMKCLDKKRIKMKQgetLALNERIMLSLVSTGDCPFIVCMSyAFHTPDKLSFI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRDAKIVLDVNkTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL---FSisgvlq 442
Cdd:cd14223   82 LDLMNGGDLHYHLSQHGVFSEAE-MRFYAAEIILGLEHMHSRFVVYRDLKPANILLDeFGHVRISDLGLacdFS------ 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 443 agrrDDKLRIQNGWLCHLAPEIIRQlspdteedKLPFSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd14223  155 ----KKKPHASVGTHGYMAPEVLQK--------GVAYDSSADWFSLGCMLFKLLRGHSPFR 203
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
391-502 2.70e-06

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: 49.15  E-value: 2.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 391 TRQIAQeIVKGMGYLHAKGILHKDLKSKNVF----YDNGKVVITDFGLFSISGvlQAGrrddKLRIQNGWLCHLAPEIir 466
Cdd:cd14198  113 IRLIRQ-ILEGVYYLHQNNIVHLDLKPQNILlssiYPLGDIKIVDFGMSRKIG--HAC----ELREIMGTPEYLAPEI-- 183
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568937340 467 qLSPDteedklPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14198  184 -LNYD------PITTATDMWNIGVIAYMLLTHESPF 212
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
295-433 2.77e-06

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: 49.47  E-value: 2.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVY----HGRwHGEVAIRLIdieRDNEDQLKAFKREVMAYRQTRH------ENVVLFMGACMSPPHLA 364
Cdd:cd14210   16 EVLSVLGKGSFGQVVkcldHKT-GQLVAIKII---RNKKRFHQQALVEVKILKHLNDndpddkHNIVRYKDSFIFRGHLC 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 365 IITSLCkGRTLYSVVRDAKIV-LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-FYDNGKVVIT--DFG 433
Cdd:cd14210   92 IVFELL-SINLYELLKSNNFQgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENIlLKQPSKSSIKviDFG 163
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
293-434 2.80e-06

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 49.78  E-value: 2.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLfMGACMSPPhlaiitSL 369
Cdd:cd07859    1 RYKIQEVIGKGSYGVVcsaIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVE-IKHIMLPP------SR 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 370 CKGRTLYSVVR----DAKIVLDVNK--TRQIAQ----EIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:cd07859   74 REFKDIYVVFElmesDLHQVIKANDdlTPEHHQfflyQLLRALKYIHTANVFHRDLKPKNILANaDCKLKICDFGL 149
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
286-518 2.92e-06

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 50.01  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 286 EWDIPF-----------EQLEIGELIGKGRFgqvyhgrwhGEVAIrlidIERDNEDQLKAF----KREVMAYRQT---RH 347
Cdd:cd05623   55 EWAKPFtskvkqmrlhkEDFEILKVIGRGAF---------GEVAV----VKLKNADKVFAMkilnKWEMLKRAETacfRE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 348 ENVVLFMGAC--MSPPHLA--------IITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKS 417
Cdd:cd05623  122 ERDVLVNGDSqwITTLHYAfqddnnlyLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKP 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 418 KNVFYD-NGKVVITDFGlfSISGVLQAGRRDDKLRIqnGWLCHLAPEIIRQLspdtEEDKLPFSKHSDVFALGTIWYELH 496
Cdd:cd05623  202 DNILMDmNGHIRLADFG--SCLKLMEDGTVQSSVAV--GTPDYISPEILQAM----EDGKGKYGPECDWWSLGVCMYEML 273
                        250       260
                 ....*....|....*....|..
gi 568937340 497 AREWPFKtqpAEAIIWQMGTGM 518
Cdd:cd05623  274 YGETPFY---AESLVETYGKIM 292
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
298-434 2.93e-06

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: 49.31  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRW--HGE-VAIRLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFMGACMSPPHLAII-----TSL 369
Cdd:cd07869   11 EKLGEGSYATVYKGKSkvNGKlVALKVIRLQEEEGTPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTLVfeyvhTDL 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 370 CKgrtlysVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL 434
Cdd:cd07869   90 CQ------YMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLIsDTGELKLADFGL 149
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
298-515 3.00e-06

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: 49.26  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVY------HGRwhgEVAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd14174    8 ELLGEGAYAKVQgcvslqNGK---EYAVKIIE-KNAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN----GKVVITDFGLFSISGVLQAGR-- 445
Cdd:cd14174   84 GGSILAHIQKRK-HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESpdkvSPVKICDFDLGSGVKLNSACTpi 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 RDDKLRIQNGWLCHLAPEIIRQLspdTEEDKLpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMG 515
Cdd:cd14174  163 TTPELTTPCGSAEYMAPEVVEVF---TDEATF-YDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCGWDRG 228
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
295-505 3.20e-06

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: 48.79  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQV---YHGRWHGEVAIRLIDIE--RDNEDQLKAfkrEVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14185    3 EIGRTIGDGNFAVVkecRHWNENQEYAMKIIDKSklKGKEDMIES---EILIIKSLSHPNIVKLFEVYETEKEIYLILEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVRDAkIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVV-ITDFGL--------FS 436
Cdd:cd14185   80 VRGGDLFDAIIES-VKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLkLADFGLakyvtgpiFT 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 437 ISGVLQagrrddklriqngwlcHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd14185  159 VCGTPT----------------YVAPEILSEKG---------YGLEVDMWAAGVILYILLCGFPPFRSP 202
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
298-503 3.53e-06

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: 49.03  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHG--EV-AIRLID---IERDNEDQLKAFKREVMAYrQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGtdEVyAIKVLKkdvILQDDDVDCTMTEKRILAL-AAKHPFLTALHSCFQTKDRLFFVMEYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 372 GRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsisgvLQAGRRDDKL 450
Cdd:cd05591   80 GGDLMFQIQRAR-KFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDaEGHCKLADFGM------CKEGILNGKT 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 451 RIQngwLC----HLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd05591  153 TTT---FCgtpdYIAPEILQE---------LEYGPSVDWWALGVLMYEMMAGQPPFE 197
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
397-526 3.88e-06

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 48.94  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 EIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL---FSISGVLQAGRRDDklRIQNGWlcHLAPEIIRQLSpdt 472
Cdd:cd07857  113 QILCGLKYIHSANVLHRDLKPGNLLVNaDCELKICDFGLargFSENPGENAGFMTE--YVATRW--YRAPEIMLSFQ--- 185
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 473 eedklPFSKHSDVFALGTIWYELHAREWPFK----TQPAEAIIWQMGTGMKPNLSQIG 526
Cdd:cd07857  186 -----SYTKAIDVWSVGCILAELLGRKPVFKgkdyVDQLNQILQVLGTPDEETLSRIG 238
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
41-82 4.12e-06

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; 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. 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. Members of this family contain two copies of C1 domain. 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: 410387  Cd Length: 50  Bit Score: 43.96  E-value: 4.12e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340  41 HRFSTKYWMSQT-CTVCGKgMLFG-----LKCKNCKLKCHNKCTKEAP 82
Cdd:cd20837    1 HRFKVYNYMSPTfCDHCGS-LLWGlfrqgLKCEECGMNVHHKCQKKVA 47
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
296-560 4.32e-06

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: 48.83  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 296 IGELIGKGRFGQVYHGRwhGEVAIRLIDIER----DNEDQLKAfKREVMAYRQTRHENVVLFMGACMSP----PHLA-II 366
Cdd:cd13986    4 IQRLLGEGGFSFVYLVE--DLSTGRLYALKKilchSKEDVKEA-MREIENYRLFNHPNILRLLDSQIVKeaggKKEVyLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRDakivLDVNKTR-------QIAQEIVKGMGYLHA---KGILHKDLKSKNV-FYDNGKVVITDFGLF 435
Cdd:cd13986   81 LPYYKRGSLQDEIER----RLVKGTFfpedrilHIFLGICRGLKAMHEpelVPYAHRDIKPGNVlLSEDDEPILMDLGSM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 436 SISGVLQAGRRdDKLRIQ-----NGWLCHLAPEIIRQLSPDTEEDKlpfskhSDVFALGTIWYELHAREWPFKtqpaeaI 510
Cdd:cd13986  157 NPARIEIEGRR-EALALQdwaaeHCTMPYRAPELFDVKSHCTIDEK------TDIWSLGCTLYALMYGESPFE------R 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937340 511 IWQMGTGM-------------KPNLSQigmgkEISDILLFCWAFEQEERPTFTKLMDMLEKLP 560
Cdd:cd13986  224 IFQKGDSLalavlsgnysfpdNSRYSE-----ELHQLVKSMLVVNPAERPSIDDLLSRVHDLI 281
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
298-434 4.43e-06

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: 48.77  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWHGE---VAIRLID---IERDNEDQLKAFKREVMAyrQTRHENVVLFMGACMSPPHLAIITSLCK 371
Cdd:cd05574    7 KLLGKGDVGRVYLVRLKGTgklFAMKVLDkeeMIKRNKVKRVLTEREILA--TLDHPFLPTLYASFQTSTHLCFVMDYCP 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 372 GRTLYSVV-RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF-YDNGKVVITDFGL 434
Cdd:cd05574   85 GGELFRLLqKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILlHESGHIMLTDFDL 149
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
300-434 5.23e-06

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: 48.37  E-value: 5.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGR--WHGE-VAIRLIDIERDNEdqlkAFK----REVMAYRQTRHENVV----LFMGACMspphlaiits 368
Cdd:cd07843   13 IEEGTYGVVYRARdkKTGEiVALKKLKMEKEKE----GFPitslREINILLKLQHPNIVtvkeVVVGSNL---------- 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 369 lckgRTLYSVVR----DAKIVLDVNKTR-------QIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGL 434
Cdd:cd07843   79 ----DKIYMVMEyvehDLKSLMETMKQPflqsevkCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNrGILKICDFGL 152
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
41-84 5.64e-06

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: 43.58  E-value: 5.64e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568937340   41 HRFSTK-YWMSQTCTVCGKGMLF----GLKCKNCKLKCHNKCTKEAPPC 84
Cdd:pfam00130   1 HHFVHRnFKQPTFCDHCGEFLWGlgkqGLKCSWCKLNVHKRCHEKVPPE 49
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
292-438 5.65e-06

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: 48.72  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTrhenvvlfMGACMSPPHLAIITSLCK 371
Cdd:cd05610    4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDA--------LALSKSPFIVHLYYSLQS 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 372 GRTLYSVVR-----DAKIVL------DVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFSIS 438
Cdd:cd05610   76 ANNVYLVMEyliggDVKSLLhiygyfDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNeGHIKLTDFGLSKVT 154
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
299-570 5.76e-06

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: 48.34  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYH------GRWHGEVAIRLIDIERDNEDQLKAFKREVMAyrQTRHENVVLFMGACMSPPHLAIITSLCKG 372
Cdd:cd05585    1 VIGKGSFGKVMQvrkkdtSRIYALKTIRKAHIVSRSEVTHTLAERTVLA--QVDCPFIVPLKFSFQSPEKLYLVLAFING 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 373 RTL-YSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISgvlqaGRRDDKL 450
Cdd:cd05585   79 GELfHHLQREGR--FDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDyTGHIALCDFGLCKLN-----MKDDDKT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 451 RIQNGWLCHLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYElharewpfktqpaeaiiwqMGTGMKP----NLSQig 526
Cdd:cd05585  152 NTFCGTPEYLAPELLLGHG---------YTKAVDWWTLGVLLYE-------------------MLTGLPPfydeNTNE-- 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568937340 527 MGKEI-SDILLFCWAFEQEERptftklmDMLEKLPKRN--RRLSHPG 570
Cdd:cd05585  202 MYRKIlQEPLRFPDGFDRDAK-------DLLIGLLNRDptKRLGYNG 241
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
288-506 5.93e-06

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: 48.08  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 288 DIPFEQLEIGELIGKGRFGQVYHGRW------HGE-VAIRLIDiERDNEDQLKAFKREVMAYRQTRHENVVLFMGAC-MS 359
Cdd:cd05090    1 ELPLSAVRFMEELGECAFGKIYKGHLylpgmdHAQlVAIKTLK-DYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVtQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 360 PPHLAIITSLCKG--------RTLYSVVR-------DAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-D 423
Cdd:cd05090   80 QPVCMLFEFMNQGdlheflimRSPHSDVGcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVgE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 424 NGKVVITDFGLFsisgvlQAGRRDDKLRIQNGwlcHLAPeiIRQLSPDTEEDKlPFSKHSDVFALGTIWYELhareWPFK 503
Cdd:cd05090  160 QLHVKISDLGLS------REIYSSDYYRVQNK---SLLP--IRWMPPEAIMYG-KFSSDSDIWSFGVVLWEI----FSFG 223

                 ...
gi 568937340 504 TQP 506
Cdd:cd05090  224 LQP 226
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
387-512 6.69e-06

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 48.15  E-value: 6.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 387 DVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSISGVlqagrRDDKLRIQNGWLCHLAPEII 465
Cdd:cd05592   94 DEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDrEGHIKIADFGMCKENIY-----GENKASTFCGTPDYIAPEIL 168
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568937340 466 RQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIW 512
Cdd:cd05592  169 KGQK---------YNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFW 206
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
337-502 6.87e-06

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: 48.02  E-value: 6.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 337 REVMAYRQTRHENVVLFMGACMSPP--HLAIITSLCKGRTLYSVVRDAKIVLDvnKTRQIAQEIVKGMGYLHAKGILHKD 414
Cdd:cd14200   72 QEIAILKKLDHVNIVKLIEVLDDPAedNLYMVFDLLRKGPVMEVPSDKPFSED--QARLYFRDIVLGIEYLHYQKIVHRD 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 415 LKSKNVFY-DNGKVVITDFGLFSisgvlQAGRRDDKLRIQNGWLCHLAPEIIrqlsPDTEEDklpFS-KHSDVFALGTIW 492
Cdd:cd14200  150 IKPSNLLLgDDGHVKIADFGVSN-----QFEGNDALLSSTAGTPAFMAPETL----SDSGQS---FSgKALDVWAMGVTL 217
                        170
                 ....*....|
gi 568937340 493 YELHAREWPF 502
Cdd:cd14200  218 YCFVYGKCPF 227
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
297-515 7.22e-06

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: 48.18  E-value: 7.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQV------YHGRwhgEVAIRLIDiERDNEDQLKAFkREVMAYRQTR-HENVVLFMGACMSPPHLAIITSL 369
Cdd:cd14090    7 GELLGEGAYASVqtcinlYTGK---EYAVKIIE-KHPGHSRSRVF-REVETLHQCQgHPNILQLIEYFEDDERFYLVFEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKGRTLYSVVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVV---ITDFGLfsISGVLQAGR 445
Cdd:cd14090   82 MRGGPLLSHI-EKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCEsMDKVSpvkICDFDL--GSGIKLSST 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 446 RDD-----KLRIQNGWLCHLAPEIIRQLSpdteEDKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMG 515
Cdd:cd14090  159 SMTpvttpELLTPVGSAEYMAPEVVDAFV----GEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEDCGWDRG 229
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
287-434 7.38e-06

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: 47.92  E-value: 7.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPF---EQLEIGELIGKGRFGQV---YHGRWHGEVAIRLIDIERdnedqLKAFKREVMAYRQTR-HENVVLFMGACMS 359
Cdd:cd14132   10 LNVEWgsqDDYEIIRKIGRGKYSEVfegINIGNNEKVVIKVLKPVK-----KKKIKREIKILQNLRgGPNIVKLLDVVKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 360 P--PHLAIITSLCKG---RTLYSVVRDAKIvldvnktRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD--NGKVVITDF 432
Cdd:cd14132   85 PqsKTPSLIFEYVNNtdfKTLYPTLTDYDI-------RYYMYELLKALDYCHSKGIMHRDVKPHNIMIDheKRKLRLIDW 157

                 ..
gi 568937340 433 GL 434
Cdd:cd14132  158 GL 159
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
300-475 8.19e-06

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of 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. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK 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: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 47.89  E-value: 8.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDqlkafkrEVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 376
Cdd:cd13991   14 IGRGSFGEVHRMEDKQtgfQCAVKKVRLEVFRAE-------ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 377 SVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY--DNGKVVITDFGLfsiSGVLQAGRRDDKLRIQN 454
Cdd:cd13991   87 QLIKEQG-CLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLssDGSDAFLCDFGH---AECLDPDGLGKSLFTGD 162
                        170       180
                 ....*....|....*....|....
gi 568937340 455 ---GWLCHLAPEIIRQLSPDTEED 475
Cdd:cd13991  163 yipGTETHMAPEVVLGKPCDAKVD 186
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
299-535 9.04e-06

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 47.82  E-value: 9.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 299 LIGKGRFGQVYHGRW--HGEV-AIRLIDIERDNEDQ--LKAFKREVMAYRQTRHEN---VVLFMGACMSPPHLAIITSLC 370
Cdd:cd05606    1 IIGRGGFGEVYGCRKadTGKMyAMKCLDKKRIKMKQgeTLALNERIMLSLVSTGGDcpfIVCMTYAFQTPDKLCFILDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTL-YSVVRDAkiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL---FSisgvlqagr 445
Cdd:cd05606   81 NGGDLhYHLSQHG--VFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDeHGHVRISDLGLacdFS--------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 446 rDDKLRIQNGWLCHLAPEIIRQlspdteedKLPFSKHSDVFALGTIWYELHAREWPFKTQPAEAI--IWQMGTGMKPNLS 523
Cdd:cd05606  150 -KKKPHASVGTHGYMAPEVLQK--------GVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKheIDRMTLTMNVELP 220
                        250
                 ....*....|..
gi 568937340 524 QiGMGKEISDIL 535
Cdd:cd05606  221 D-SFSPELKSLL 231
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
394-502 1.03e-05

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK 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: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 47.40  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 394 IAQEIVKGMGYLHAKGILHKDLKSKNVFYD--NGKVVITDFGLFSisgvlQAGRRDDKLRIQNGwlchlAPEIIrqlSPD 471
Cdd:cd13974  137 IFYDVVRVVEALHKKNIVHRDLKLGNMVLNkrTRKITITNFCLGK-----HLVSEDDLLKDQRG-----SPAYI---SPD 203
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568937340 472 TEEDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd13974  204 VLSGKPYLGKPSDMWALGVVLFTMLYGQFPF 234
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
293-554 1.04e-05

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; 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 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 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: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 47.27  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHGE---VAIRLIDIERDNE-DQLKAFKR---EVMAYRQ--TRHENVVLFMGACMSPPHL 363
Cdd:cd14100    1 QYQVGPLLGSGGFGSVYSGIRVADgapVAIKHVEKDRVSEwGELPNGTRvpmEIVLLKKvgSGFRGVIRLLDWFERPDSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSLCKG-RTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD--NGKVVITDFGlfsiSGV 440
Cdd:cd14100   81 VLVLERPEPvQDLFDFITE-RGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlnTGELKLIDFG----SGA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 441 LqagRRDDKLRIQNGWLCHLAPEIIRqlspdteedklpFSKH----SDVFALGTIWYELHAREWPFKtQPAEAIIWQMgt 516
Cdd:cd14100  156 L---LKDTVYTDFDGTRVYSPPEWIR------------FHRYhgrsAAVWSLGILLYDMVCGDIPFE-HDEEIIRGQV-- 217
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568937340 517 gmkpnLSQIGMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd14100  218 -----FFRQRVSSECQHLIKWCLALRPSDRPSFEDIQN 250
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
298-505 1.19e-05

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: 47.59  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRW---HGEVAIRLIdiERD---NEDQLKAFKREVMAYRQTRHENVVLFMGACM-SPPHLAIITSLC 370
Cdd:cd05590    1 RVLGKGSFGKVMLARLkesGRLYAVKVL--KKDvilQDDDVECTMTEKRILSLARNHPFLTQLYCCFqTPDRLFFVMEFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsisgvLQAGRRDDK 449
Cdd:cd05590   79 NGGDLMFHIQKSR-RFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHeGHCKLADFGM------CKEGIFNGK 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 450 LriqNGWLC----HLAPEIIRQLSpdteedklpFSKHSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd05590  152 T---TSTFCgtpdYIAPEILQEML---------YGPSVDWWAMGVLLYEMLCGHAPFEAE 199
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
291-499 1.19e-05

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; 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. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and 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. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 47.70  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 291 FEQLEIGELIGKGRFGQVyhgrwhgevaIRLIDIERDNEDQLKAFKREVMAYRQTRHE----------------NVVLFM 354
Cdd:cd14226   12 MDRYEIDSLIGKGSFGQV----------VKAYDHVEQEWVAIKIIKNKKAFLNQAQIEvrllelmnkhdtenkyYIVRLK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 355 GACMSPPHLAIITSLCKgRTLYSVVRDAKIV-LDVNKTRQIAQEIVKGMGYLHAK--GILHKDLKSKNVFYDNGK---VV 428
Cdd:cd14226   82 RHFMFRNHLCLVFELLS-YNLYDLLRNTNFRgVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLCNPKrsaIK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 429 ITDFGlfsisGVLQAGRRDDKLrIQNGWlcHLAPEIIRQlspdteedkLPFSKHSDVFALGTIWYELHARE 499
Cdd:cd14226  161 IIDFG-----SSCQLGQRIYQY-IQSRF--YRSPEVLLG---------LPYDLAIDMWSLGCILVEMHTGE 214
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
392-502 1.20e-05

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: 47.42  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 392 RQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLfsisgvLQAGRRD-DKLRIQNGWLCHLAPEIIRQls 469
Cdd:cd05588   99 RFYSAEISLALNFLHEKGIIYRDLKLDNVLLDsEGHIKLTDYGM------CKEGLRPgDTTSTFCGTPNYIAPEILRG-- 170
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568937340 470 pdteEDklpFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05588  171 ----ED---YGFSVDWWALGVLMFEMLAGRSPF 196
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
37-82 1.28e-05

protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. 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: 410364  Cd Length: 56  Bit Score: 42.62  E-value: 1.28e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568937340  37 NSIKHRFSTKYWMSQT-CTVCGKGMLFG---LKCKNCKLKCHNKCTKEAP 82
Cdd:cd20814    1 HNIPHRFTTGLNMRATkCAVCLDGVPFGrqaSKCSECGIVCHPKCSSSLP 50
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
397-503 1.30e-05

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: 46.87  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 EIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGlfsISGVLQAGRRDDKLRIQNGWLCHLAPEIIRQLspdteED 475
Cdd:cd14119  105 QLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLkISDFG---VAEALDLFAEDDTCTTSQGSPAFQPPEIANGQ-----DS 176
                         90       100
                 ....*....|....*....|....*...
gi 568937340 476 KLPFSkhSDVFALGTIWYELHAREWPFK 503
Cdd:cd14119  177 FSGFK--VDIWSAGVTLYNMTTGKYPFE 202
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
295-501 1.31e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 47.44  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 295 EIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHE-----NVVLFMGACMSPPHLAIITSL 369
Cdd:cd14211    2 EVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLVFEM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKgRTLYSVVRDAKIV-LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-----KVVITDFGlfSISGVLQA 443
Cdd:cd14211   82 LE-QNLYDFLKQNKFSpLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPvrqpyRVKVIDFG--SASHVSKA 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 444 grrddklrIQNGWL---CHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHArEWP 501
Cdd:cd14211  159 --------VCSTYLqsrYYRAPEIIL---------GLPFCEAIDMWSLGCVIAELFL-GWP 201
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
287-503 1.36e-05

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: 47.64  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 287 WDIPFEQLEIgELIGKGRFGQVYH---GRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHL 363
Cdd:cd07880   11 WEVPDRYRDL-KQVGSGAYGTVCSaldRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 364 AIITSL-----CKGRTLYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV-FYDNGKVVITDFGLfsi 437
Cdd:cd07880   90 DRFHDFylvmpFMGTDLGKLMKHEK--LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLaVNEDCELKILDFGL--- 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 438 sgvlqAGRRDDKLR--IQNGWlcHLAPEIIRQLspdteedkLPFSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd07880  165 -----ARQTDSEMTgyVVTRW--YRAPEVILNW--------MHYTQTVDIWSVGCIMAEMLTGKPLFK 217
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
300-502 1.48e-05

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: 47.18  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYH------GRWHGEVAIRLIDIERDNEDQLKAFKREVMAyRQTRHEN--VVLFMGACMSPPHLAIITS-LC 370
Cdd:cd05586    1 IGKGTFGQVYQvrkkdtRRIYAMKVLSKKVIVAKKEVAHTIGERNILV-RTALDESpfIVGLKFSFQTPTDLYLVTDyMS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 371 KGRTLYSVVRDAKIVLDvnKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFsisgvlQAGRRDDK 449
Cdd:cd05586   80 GGELFWHLQKEGRFSED--RAKFYIAELVLALEHLHKNDIVYRDLKPENILLDaNGHIALCDFGLS------KADLTDNK 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 450 LriqNGWLC----HLAPEIIRqlspdteeDKLPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05586  152 T---TNTFCgtteYLAPEVLL--------DEKGYTKMVDFWSLGVLVFEMCCGWSPF 197
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
395-505 1.67e-05

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: 46.89  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 395 AQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLfsiSGVLQAGrrdDKLRIQNGWLCHLAPEIIRQlspdte 473
Cdd:cd05632  110 AAEILCGLEDLHRENTVYRDLKPENILLDDyGHIRISDLGL---AVKIPEG---ESIRGRVGTVGYMAPEVLNN------ 177
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568937340 474 eDKLPFSkhSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd05632  178 -QRYTLS--PDYWGLGCLIYEMIEGQSPFRGR 206
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
292-495 1.73e-05

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: 47.28  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYhgrwhgevairlidIERDNED-QLKAFKR----EVMAYRQTRH---ENvvLFMGACMSP--- 360
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVW--------------LVRDKDTgQVYAMKIlrksDMLKREQIAHvraER--DILADADSPwiv 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 361 ---------PHLAIITSLCKGRTLYSVVRDaKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVIT 430
Cdd:cd05573   65 rlhyafqdeDHLYLVMEYMPGGDLMNLLIK-YDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDaDGHIKLA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 431 DFGL------FSISGVLQAGRRDDKLRIQNGW----------LCH--------LAPEIIRQLSPDTEedklpfskhSDVF 486
Cdd:cd05573  144 DFGLctkmnkSGDRESYLNDSVNTLFQDNVLArrrphkqrrvRAYsavgtpdyIAPEVLRGTGYGPE---------CDWW 214

                 ....*....
gi 568937340 487 ALGTIWYEL 495
Cdd:cd05573  215 SLGVILYEM 223
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
289-503 1.74e-05

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: 46.98  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 289 IPFEQLEIGELIGKGRFGQVYHGRWH--GEV-AIRLIDIERDNEDQ---LKAFKREVMAYRQTRHENVVLFMG-ACMSPP 361
Cdd:cd05633    2 LTMNDFSVHRIIGRGGFGEVYGCRKAdtGKMyAMKCLDKKRIKMKQgetLALNERIMLSLVSTGDCPFIVCMTyAFHTPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCKGRTLYSVVRDAKiVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL---FSi 437
Cdd:cd05633   82 KLCFILDLMNGGDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDeHGHVRISDLGLacdFS- 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 438 sgvlqagrrDDKLRIQNGWLCHLAPEIIRQLSpdteedklPFSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd05633  160 ---------KKKPHASVGTHGYMAPEVLQKGT--------AYDSSADWFSLGCMLFKLLRGHSPFR 208
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
39-83 1.86e-05

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: 42.28  E-value: 1.86e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340  39 IKHRFSTKYWMSQT-CTVCGKGMLFGLKCKNCKLKCHNKCTKEAPP 83
Cdd:cd20811    1 ISHNFVRKTFFTLAfCDVCRKLLFQGFRCQTCGFKFHQRCSDQVPA 46
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
300-548 2.00e-05

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: 46.40  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRWHGEVAI-RLIDIERDNEDQLKA---FKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTL 375
Cdd:cd05086    5 IGNGWFGKVLLGEIYTGTSVaRVVVKELKASANPKEqddFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 376 --------YSVVRDAKIVLdvnkTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGLFSISGVLQAGRR 446
Cdd:cd05086   85 ktylanqqEKLRGDSQIML----LQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDlTVKVGDYGIGFSRYKEDYIET 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 447 DDKLRIQNGWlchLAPEIIRQLspdteEDKL---PFSKHSDVFALG-TIW--YELHAREWP--FKTQPAEAIIWQMGTGM 518
Cdd:cd05086  161 DDKKYAPLRW---TAPELVTSF-----QDGLlaaEQTKYSNIWSLGvTLWelFENAAQPYSdlSDREVLNHVIKERQVKL 232
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568937340 519 -KPNLSQiGMGKEISDILLFCWaFEQEERPT 548
Cdd:cd05086  233 fKPHLEQ-PYSDRWYEVLQFCW-LSPEKRPT 261
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
375-502 2.23e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 47.15  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVrDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGlfsisGVLQAGRRDDKLRIQ 453
Cdd:PHA03207 172 LFTYV-DRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEpENAVLGDFG-----AACKLDAHPDTPQCY 245
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568937340 454 nGWLCHL---APEIirqLSPDteedklPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:PHA03207 246 -GWSGTLetnSPEL---LALD------PYCAKTDIWSAGLVLFEMSVKNVTL 287
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
292-421 2.75e-05

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: 46.07  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIgELIGKGRFGQVYH--GRWHGEV-AIR--LIDIERDNEDQLKAfkREVMAYRQT-RHENVVLFMGACMSPPHLAI 365
Cdd:cd14139    1 EFLEL-EKIGVGEFGSVYKciKRLDGCVyAIKrsMRPFAGSSNEQLAL--HEVYAHAVLgHHPHVVRYYSAWAEDDHMII 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 366 ITSLCKGRTLYSVV---RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVF 421
Cdd:cd14139   78 QNEYCNGGSLQDAIsenTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIF 136
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
298-434 2.94e-05

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: 46.11  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHG--RWHGE-VAIRLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFMGACMSPPHLAII-----TSL 369
Cdd:cd07870    6 EKLGEGSYATVYKGisRINGQlVALKVISMKTEEGVPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTFVfeymhTDL 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 370 CKgrtlYSVVRDAKivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGL 434
Cdd:cd07870   85 AQ----YMIQHPGG--LHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYlGELKLADFGL 144
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
53-84 3.34e-05

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. 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: 410367  Cd Length: 51  Bit Score: 41.54  E-value: 3.34e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568937340  53 CTVCgKGML-----FGLKCKNCKLKCHNKCTKEAPPC 84
Cdd:cd20817   14 CDVC-KELLvglskQGLRCKNCKMNVHHKCQEGVPDC 49
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
363-554 3.87e-05

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 45.80  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 363 LAIITSLCKGRTLYSVVRDAKivlDVNKTRQIAQEIVKGMG----YLHAKGILHKDLKSKNVFYD----NGKVVITDFGL 434
Cdd:cd14170   74 LLIVMECLDGGELFSRIQDRG---DQAFTEREASEIMKSIGeaiqYLHSINIAHRDVKPENLLYTskrpNAILKLTDFGF 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 435 fsisgvLQAGRRDDKLRIQNGWLCHLAPEIirqLSPDTeedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAII--- 511
Cdd:cd14170  151 ------AKETTSHNSLTTPCYTPYYVAPEV---LGPEK------YDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgm 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340 512 ---WQMGTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMD 554
Cdd:cd14170  216 ktrIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMN 261
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
290-502 4.96e-05

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 45.31  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQ---LEIGELIGKGRFGQVYHGrwhgevairlidIERDNEDQLKA-FKREVMAYRQTR----HENVVLFMGACM--- 358
Cdd:cd14197    4 PFQErysLSPGRELGRGKFAVVRKC------------VEKDSGKEFAAkFMRKRRKGQDCRmeiiHEIAVLELAQANpwv 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 359 --------SPPHLAIITSLCKGRTLYS-VVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN----G 425
Cdd:cd14197   72 inlhevyeTASEMILVLEYAAGGEIFNqCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSesplG 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937340 426 KVVITDFGLFSISgvlqagRRDDKLRIQNGWLCHLAPEIirqLSPDteedklPFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd14197  152 DIKIVDFGLSRIL------KNSEELREIMGTPEYVAPEI---LSYE------PISTATDMWSIGVLAYVMLTGISPF 213
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
298-434 5.46e-05

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: 45.45  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 298 ELIGKGRFGQVYHGRWH---GEVAIRLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFmgacmsppHLAIITSlckgRT 374
Cdd:cd07844    6 DKLGEGSYATVYKGRSKltgQLVALKEIRLEHEEGAPFTAI-REASLLKDLKHANIVTL--------HDIIHTK----KT 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937340 375 LYSV----VRDAKIVLD-------VNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL 434
Cdd:cd07844   73 LTLVfeylDTDLKQYMDdcggglsMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLIsERGELKLADFGL 144
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
391-433 5.57e-05

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 45.26  E-value: 5.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568937340 391 TRQIAQEIVKGMGYLHAK-GILHKDLKSKNV--FYDNGKVVITDFG 433
Cdd:cd14136  121 VKKIARQVLQGLDYLHTKcGIIHTDIKPENVllCISKIEVKIADLG 166
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
329-554 8.37e-05

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 44.59  E-value: 8.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 329 EDQLKAfKREV-MAYRQTRHENVV----LFMGACMSPPHLAIITSLCKGRTLYSVVRDAKivlDVNKTRQIAQEIVKGMG 403
Cdd:cd14089   35 RDNPKA-RREVeLHWRASGCPHIVriidVYENTYQGRKCLLVVMECMEGGELFSRIQERA---DSAFTEREAAEIMRQIG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 404 ----YLHAKGILHKDLKSKNVFY----DNGKVVITDFGLfsisgvlqAGRRDDKLRIQNGwlC----HLAPEIirqLSPD 471
Cdd:cd14089  111 savaHLHSMNIAHRDLKPENLLYsskgPNAILKLTDFGF--------AKETTTKKSLQTP--CytpyYVAPEV---LGPE 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 472 TeedklpFSKHSDVFALGTIWYELHAREWPFKTQPAEAIiwqmGTGMK------------PNLSQI-GMGKEISDILLfc 538
Cdd:cd14089  178 K------YDKSCDMWSLGVIMYILLCGYPPFYSNHGLAI----SPGMKkrirngqyefpnPEWSNVsEEAKDLIRGLL-- 245
                        250
                 ....*....|....*.
gi 568937340 539 wAFEQEERPTFTKLMD 554
Cdd:cd14089  246 -KTDPSERLTIEEVMN 260
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
41-84 8.38e-05

protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. 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: 410368  Cd Length: 56  Bit Score: 40.36  E-value: 8.38e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568937340  41 HRFSTKYWMSQT-CTVCG---KGMLFGLKCKNCKLKCHNKC-TKEAPPC 84
Cdd:cd20818    4 HKFATVQFNIPTyCEVCNsfiWLMEKGLVCQVCKFTCHKKCySKITAPC 52
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
290-503 8.73e-05

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: 44.44  E-value: 8.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 290 PFEQLEIGELIGKGRFGQVYHG-----RWHGEVAIRLIDIERDNEDQLkafkREVMAYRQTRHENVVLFMGACMSPPHLA 364
Cdd:cd14112    1 PTGRFSFGSEIFRGRFSVIVKAvdsttETDAHCAVKIFEVSDEASEAV----REFESLRTLQHENVQRLIAAFKPSNFAY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 365 IITslckgRTLYSVVRDAKIVLDVNKTRQIA---QEIVKGMGYLHAKGILHKDLKSKNVFYDNGK---VVITDFGlfSIS 438
Cdd:cd14112   77 LVM-----EKLQEDVFTRFSSNDYYSEEQVAttvRQILDALHYLHFKGIAHLDVQPDNIMFQSVRswqVKLVDFG--RAQ 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 439 GVLQAGRRDDklriqNGWLCHLAPEIIrqlspdteEDKLPFSKHSDVFALGTIWYELHAREWPFK 503
Cdd:cd14112  150 KVSKLGKVPV-----DGDTDWASPEFH--------NPETPITVQSDIWGLGVLTFCLLSGFHPFT 201
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
41-84 9.12e-05

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; 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. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) 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. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. 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: 410343  Cd Length: 50  Bit Score: 40.34  E-value: 9.12e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568937340  41 HRFSTKYWMSQT-CTVCGKgMLFGL-----KCKNCKLKCHNKCTKEAPPC 84
Cdd:cd20793    1 HKFKVHTYYSPTfCDHCGS-LLYGLvrqglKCKDCGMNVHHRCKENVPHL 49
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
293-433 1.02e-04

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; 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 three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 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: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 44.07  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVYHGRWHG---EVAIRLIdiERDNEDQLKAFKREVMAYRQtrhenVVLFMGACMSPPHLAIITSL 369
Cdd:cd14101    1 QYTMGNLLGKGGFGTVYAGHRISdglQVAIKQI--SRNRVQQWSKLPGVNPVPNE-----VALLQSVGGGPGHRGVIRLL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 ------------------CKGRTLYSVVRDAkivLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD--NGKVVI 429
Cdd:cd14101   74 dwfeipegfllvlerpqhCQDLFDYITERGA---LDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlrTGDIKL 150

                 ....
gi 568937340 430 TDFG 433
Cdd:cd14101  151 IDFG 154
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
300-526 1.24e-04

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: 44.73  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVY------HGRwhgEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVvlfMGA--CMSPPHLA------I 365
Cdd:cd07853    8 IGYGAFGVVWsvtdprDGK---RVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNV---LSAldILQPPHIDpfeeiyV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLDVNKTrqIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFSISgvlqag 444
Cdd:cd07853   82 VTELMQSDLHKIIVSPQPLSSDHVKV--FLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLkICDFGLARVE------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 445 RRDDKlriqngwlCHLAPEIIRQL--SPDTeedkLPFSKHS----DVFALGTIWYELHAREWPFKTQ-PAEA---IIWQM 514
Cdd:cd07853  154 EPDES--------KHMTQEVVTQYyrAPEI----LMGSRHYtsavDIWSVGCIFAELLGRRILFQAQsPIQQldlITDLL 221
                        250
                 ....*....|..
gi 568937340 515 GTgmkPNLSQIG 526
Cdd:cd07853  222 GT---PSLEAMR 230
PRK14879 PRK14879
Kae1-associated kinase Bud32;
297-443 1.27e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 43.36  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 297 GELIGKGRFGQVYHGRWHGEVAIRLIDIE---RDNE--DQLKAF--KREVMAYRQTRHENV----VLFMgacmSPPHLAI 365
Cdd:PRK14879   1 MKLIKRGAEAEIYLGDFLGIKAVIKWRIPkryRHPEldERIRRErtRREARIMSRARKAGVnvpaVYFV----DPENFII 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 366 ITSLCKGRTLYSVVRDAKIVLdvnktRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGL--FSISGVLQA 443
Cdd:PRK14879  77 VMEYIEGEPLKDLINSNGMEE-----LELSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDFGLaeFSKDLEDRA 151
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
41-83 1.28e-04

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: 39.95  E-value: 1.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568937340  41 HRFSTKYWMSQT-CTVCGKGM--LF--GLKCKNCKLKCHNKCTKEAPP 83
Cdd:cd20809    1 HKFIVRTFSTPTkCNHCTSLMvgLVrqGLVCEVCGYACHVSCADKAPQ 48
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
377-433 1.53e-04

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 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: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 43.97  E-value: 1.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568937340 377 SVVRDAKIVldvnktRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD--NGKVVITDFG 433
Cdd:cd14013  114 GPKRENVII------KSIMRQILVALRKLHSTGIVHRDVKPQNIIVSegDGQFKIIDLG 166
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
292-434 1.56e-04

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: 44.28  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVYHGRWHG---EVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAiits 368
Cdd:cd07855    5 DRYEPIETIGSGAYGVVCSAIDTKsgqKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYA---- 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 369 lcKGRTLYsVVRDA------KIV-----LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGL 434
Cdd:cd07855   81 --DFKDVY-VVLDLmesdlhHIIhsdqpLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNeNCELKIGDFGM 155
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
292-502 1.75e-04

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: 43.71  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS 368
Cdd:cd06619    1 QDIQYQEILGHGNGGTVYkayHLLTRRILAVKVIPLDITVELQ-KQIMSELEILYKCDSPYIIGFYGAFFVENRISICTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 369 LCKGRTLYSVVRDAKIVLDvnktrQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFSisgvlQAGRRD 447
Cdd:cd06619   80 FMDGGSLDVYRKIPEHVLG-----RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTrGQVKLCDFGVST-----QLVNSI 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568937340 448 DKLRIqnGWLCHLAPEIIrqlspDTEEdklpFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd06619  150 AKTYV--GTNAYMAPERI-----SGEQ----YGIHSDVWSLGISFMELALGRFPY 193
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
300-504 1.86e-04

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: 43.51  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 300 IGKGRFGQVYHGRwHGE----VAI-RLIDIERDNEDQLKAFkREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 374
Cdd:cd07847    9 IGEGSYGVVFKCR-NREtgqiVAIkKFVESEDDPVIKKIAL-REIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDHTV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 375 LYSVVRDAKIVlDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSIsgvLQAGRRDDKLRIQ 453
Cdd:cd07847   87 LNELEKNPRGV-PEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITkQGQIKLCDFGFARI---LTGPGDDYTDYVA 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568937340 454 NGWlcHLAPEIirqLSPDTEedklpFSKHSDVFALGTIWYELHARE--WPFKT 504
Cdd:cd07847  163 TRW--YRAPEL---LVGDTQ-----YGPPVDVWAIGCVFAELLTGQplWPGKS 205
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
293-519 2.15e-04

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 43.45  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 293 QLEIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSL 369
Cdd:cd07848    2 KFEVLGVVGEGAYGVVLkcrHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 370 CKgRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLfsISGVLQAGRRDD 448
Cdd:cd07848   82 VE-KNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLkLCDFGF--ARNLSEGSNANY 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937340 449 KLRIQNGWlcHLAPEIIRqlspdteedKLPFSKHSDVFALGTIWYELHAREWPFktqPAEAIIWQMGTGMK 519
Cdd:cd07848  159 TEYVATRW--YRSPELLL---------GAPYGKAVDMWSVGCILGELSDGQPLF---PGESEIDQLFTIQK 215
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
388-558 2.56e-04

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: 43.16  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 388 VNKTRQIAQEIVKGMGYLH-AKGILHKDLKSKNVfydngkVVITDFGLFSISGVLQAGRRDDKLRI-QNGWLCHLAPEII 465
Cdd:cd14001  109 AATILKVALSIARALEYLHnEKKILHGDIKSGNV------LIKGDFESVKLCDFGVSLPLTENLEVdSDPKAQYVGTEPW 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 466 RqlSPDTEEDKLPFSKHSDVFALGTIWYELHAREWP---------------FKTQPAEAIIWQMGTGMKPNLSQIGMGKE 530
Cdd:cd14001  183 K--AKEALEEGGVITDKADIFAYGLVLWEMMTLSVPhlnlldiedddedesFDEDEEDEEAYYGTLGTRPALNLGELDDS 260
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568937340 531 ISDIL-LFCWAFEQ--EERPTFTKLMDMLEK 558
Cdd:cd14001  261 YQKVIeLFYACTQEdpKDRPSAAHIVEALEA 291
C1_CeDKF1-like_rpt1 cd20797
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
38-82 2.70e-04

first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the first 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: 410347  Cd Length: 56  Bit Score: 38.99  E-value: 2.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568937340  38 SIKHRFSTKYWMSQT-CTVCGKgMLFGL-----KCKNCKLKCHNKCTkEAP 82
Cdd:cd20797    1 TRPHVVEVEQYMTPTfCDYCGE-MLTGLmkqgvKCKNCRCNFHKRCA-NAP 49
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
397-434 2.96e-04

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 42.20  E-value: 2.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568937340  397 EIVKGMGY----LHAKGILHKDLKSKNVFYDNGKVVITDFGL 434
Cdd:TIGR03724  94 ELAREIGRlvgkLHKAGIVHGDLTTSNIIVRDDKVYLIDFGL 135
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
292-502 3.60e-04

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 43.07  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGELIGKGRFGQVY---HGRWHGEVAIRLID----IERDNEdqlkAF---KREVMAYRQTRHenVVLFMGACMSPP 361
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQlvrHKSTRKVYAMKLLSkfemIKRSDS----AFfweERDIMAFANSPW--VVQLFYAFQDDR 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 362 HLAIITSLCKGRTLYSVVRDakivLDVNK--TRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFglfsis 438
Cdd:cd05622  147 YLYMVMEYMPGGDLVNLMSN----YDVPEkwARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDkSGHLKLADF------ 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937340 439 GVLQAGRRDDKLRIQN--GWLCHLAPEIIRQLSPDTEedklpFSKHSDVFALGTIWYELHAREWPF 502
Cdd:cd05622  217 GTCMKMNKEGMVRCDTavGTPDYISPEVLKSQGGDGY-----YGRECDWWSVGVFLYEMLVGDTPF 277
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
41-77 4.16e-04

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first 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: 410372  Cd Length: 52  Bit Score: 38.42  E-value: 4.16e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 568937340  41 HRFSTK-YWMSQTCTVCGKGMLF-GLKCKNCKLKCHNKC 77
Cdd:cd20822    3 HKFVQKqFYQIMRCAVCGEFLVNaGYQCEDCKYTCHKKC 41
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
41-77 4.26e-04

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 5 (RASSF5) and similar proteins; RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. It is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. It contains a C1 domain, which is descibed in this model. 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: 410436  Cd Length: 50  Bit Score: 38.52  E-value: 4.26e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568937340  41 HRFSTKYWMSQTCTVCGKGML-FGLKCKNCKLKCHNKC 77
Cdd:cd20886    4 HRFEPGALGPGWCDLCGRYILsQALRCTNCKYTCHSEC 41
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
292-495 4.28e-04

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: 42.39  E-value: 4.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 292 EQLEIGElIGKGRFGQVYH--GRWHGEV-AI-RLIDIERDNEDQLKAFkREVMAYRQT-RHENVVLFMGACMSPPHLAII 366
Cdd:cd14051    1 EFHEVEK-IGSGEFGSVYKciNRLDGCVyAIkKSKKPVAGSVDEQNAL-NEVYAHAVLgKHPHVVRYYSAWAEDDHMIIQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 367 TSLCKGRTLYSVVRD---AKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISGVLQA 443
Cdd:cd14051   79 NEYCNGGSLADAISEnekAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSSEEEEEDFEGEED 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937340 444 GRRDDKLRIQNGWLCH----------------LAPEIIRQlspdtEEDKLPfskHSDVFALGTIWYEL 495
Cdd:cd14051  159 NPESNEVTYKIGDLGHvtsisnpqveegdcrfLANEILQE-----NYSHLP---KADIFALALTVYEA 218
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
397-505 4.88e-04

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: 42.39  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937340 397 EIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFSisgvlQAGRRDDKLRIQNGWLCHLAPEIIRQLSPDTEed 475
Cdd:cd05582  105 ELALALDHLHSLGIIYRDLKPENILLDeDGHIKLTDFGLSK-----ESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQS-- 177
                         90       100       110
                 ....*....|....*....|....*....|
gi 568937340 476 klpfskhSDVFALGTIWYELHAREWPFKTQ 505
Cdd:cd05582  178 -------ADWWSFGVLMFEMLTGSLPFQGK 200
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
41-84 5.98e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. 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: 410376  Cd Length: 52  Bit Score: 38.14  E-value: 5.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568937340  41 HRFSTK-YWMSQTCTVCGKGML-FGLKCKNCKLKCHNKC-TKEAPPC 84
Cdd:cd20826    3 HSFKEKsFRKPRTCDVCKQIIWnEGSSCRVCKYACHRKCePKVTAAC 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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