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Conserved domains on  [gi|15232374|ref|NP_188719|]
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AGC (cAMP-dependent, cGMP-dependent and protein kinase C) kinase family protein [Arabidopsis thaliana]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
19-365 9.82e-148

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05574:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 316  Bit Score: 421.65  E-value: 9.82e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSA---SSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFE 95
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRL----KGTGKLFAMKVLDKEEMikrNKVKRVLTEREILATLD-----HPFLPTLYASFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSr 175
Cdd:cd05574  72 TSTHLCFVMDYCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLS- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slkkplrphfyqpdpeliidrKKSRSFSRLISptaeknKTGLKKTRSARVNPINRRKTSFSSGERSNSFVGTDEYVSPEV 255
Cdd:cd05574 151 ---------------------KQSSVTPPPVR------KSLRKGSRRSSVKSIEKETFVAEPSARSNSFVGTEEYIAPEV 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN---DLTDLIRRLLVKDPNRRLGCHRGA 332
Cdd:cd05574 204 IKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKELTFPESPPvssEAKDLIRKLLVKDPSKRLGSKRGA 283
                       330       340       350
                ....*....|....*....|....*....|...
gi 15232374 333 AEIKELAFFAGVRWDLLTEVlRPPFIPLRDDGE 365
Cdd:cd05574 284 SEIKRHPFFRGVNWALIRNM-TPPIIPRPDDPI 315
 
Name Accession Description Interval E-value
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-365 9.82e-148

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: 421.65  E-value: 9.82e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSA---SSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFE 95
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRL----KGTGKLFAMKVLDKEEMikrNKVKRVLTEREILATLD-----HPFLPTLYASFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSr 175
Cdd:cd05574  72 TSTHLCFVMDYCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLS- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slkkplrphfyqpdpeliidrKKSRSFSRLISptaeknKTGLKKTRSARVNPINRRKTSFSSGERSNSFVGTDEYVSPEV 255
Cdd:cd05574 151 ---------------------KQSSVTPPPVR------KSLRKGSRRSSVKSIEKETFVAEPSARSNSFVGTEEYIAPEV 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN---DLTDLIRRLLVKDPNRRLGCHRGA 332
Cdd:cd05574 204 IKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKELTFPESPPvssEAKDLIRKLLVKDPSKRLGSKRGA 283
                       330       340       350
                ....*....|....*....|....*....|...
gi 15232374 333 AEIKELAFFAGVRWDLLTEVlRPPFIPLRDDGE 365
Cdd:cd05574 284 SEIKRHPFFRGVNWALIRNM-TPPIIPRPDDPI 315
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
24-341 1.15e-72

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 227.80  E-value: 1.15e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374     24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLR-RARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAW 102
Cdd:smart00220   4 LEKLGEGSFGKVYLARDKKTGKL----VAIKVIKKKKIKKDReRILREIKILKKL-----KHPNIVRLYDVFEDEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    103 AVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkplr 182
Cdd:smart00220  75 VMEYCEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLD---- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    183 phfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIRGDGHD 262
Cdd:smart00220 149 ------------------------------------------------------PGEKLTTFVGTPEYMAPEVLLGKGYG 174
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    263 FAVDWWALGVLTYEMMYGETPFKGKSK-KETFRNVLMKEPEFAGKPNDLT----DLIRRLLVKDPNRRLgchrGAAEIKE 337
Cdd:smart00220 175 KAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPEWDISpeakDLIRKLLVKDPEKRL----TAEEALQ 250

                   ....
gi 15232374    338 LAFF 341
Cdd:smart00220 251 HPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
24-325 1.16e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.03  E-value: 1.16e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASS---LRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYF 100
Cdd:COG0515  12 LRLLGRGGMGVVYLARDL----RLGRPVALKVLRPELAADpeaRERFRREARALARL-----NHPNIVRVYDVGEEDGRP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKp 180
Cdd:COG0515  83 YLVMEYVEGESLADLLRRR--GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGG- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDG 260
Cdd:COG0515 160 -------------------------------------------------------ATLTQTGTVVGTPGYMAPEQARGEP 184
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-----PNDLTDLIRRLLVKDPNRR 325
Cdd:COG0515 185 VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSElrpdlPPALDAIVLRALAKDPEER 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
27-408 1.34e-45

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 159.98  E-value: 1.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   27 LGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASSLRRAR---WEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWA 103
Cdd:PTZ00263  26 LGTGSFGRVRIAK----HKGTGEYYAIKCLKKREILKMKQVQhvaQEKSILMELS-----HPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  104 VPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrp 183
Cdd:PTZ00263  97 LEFVVGGEL--FTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA--------- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  184 hfyqpdpeliidrkksrsfsrlisptaeknktglKKTRsarvnpinrrktsfssgERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:PTZ00263 166 ----------------------------------KKVP-----------------DRTFTLCGTPEYLAPEVIQSKGHGK 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagkPN----DLTDLIRRLLVKDPNRRLGC-HRGAAEIKEL 338
Cdd:PTZ00263 195 AVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKF---PNwfdgRARDLVKGLLQTDHTKRLGTlKGGVADVKNH 271
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374  339 AFFAGVRWDLLTEVLRPPFIPLRDDGELTVGGFDirehfeklrttpsSAPPSPL-RSPPHVCRKNDPFIEF 408
Cdd:PTZ00263 272 PYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-------------KYPDSPVdRLPPLTAAQQAEFAGF 329
Pkinase pfam00069
Protein kinase domain;
24-329 3.14e-39

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 139.69  E-value: 3.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASS--LRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:pfam00069   4 LRKLGSGSFGTVYKAKHR----DTGKIVAIKKIKKEKIKKkkDKNILREIKILKKL-----NHPNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   102 WAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMgiayrdlkpeniliqqsghvtltdfdlsrslkkpl 181
Cdd:pfam00069  75 LVLEYVEGGSLFDLLSEK--GAFSEREAKFIMKQILEGLESGSSL----------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGDGH 261
Cdd:pfam00069 118 ------------------------------------------------------------TTFVGTPWYMAPEVLGGNPY 137
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374   262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN----DLTDLIRRLLVKDPNRRLGCH 329
Cdd:pfam00069 138 GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSnlseEAKDLLKKLLKKDPSKRLTAT 209
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
132-288 1.12e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.52  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  132 YVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfyqpdpeliidrkksrsfsrlisptae 211
Cdd:NF033483 112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARAL---------------------------------- 157
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374  212 knktglkktrsarvnpinrrktSFSSGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKS 288
Cdd:NF033483 158 ----------------------SSTTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
 
Name Accession Description Interval E-value
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-365 9.82e-148

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: 421.65  E-value: 9.82e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSA---SSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFE 95
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRL----KGTGKLFAMKVLDKEEMikrNKVKRVLTEREILATLD-----HPFLPTLYASFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSr 175
Cdd:cd05574  72 TSTHLCFVMDYCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLS- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slkkplrphfyqpdpeliidrKKSRSFSRLISptaeknKTGLKKTRSARVNPINRRKTSFSSGERSNSFVGTDEYVSPEV 255
Cdd:cd05574 151 ---------------------KQSSVTPPPVR------KSLRKGSRRSSVKSIEKETFVAEPSARSNSFVGTEEYIAPEV 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN---DLTDLIRRLLVKDPNRRLGCHRGA 332
Cdd:cd05574 204 IKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKELTFPESPPvssEAKDLIRKLLVKDPSKRLGSKRGA 283
                       330       340       350
                ....*....|....*....|....*....|...
gi 15232374 333 AEIKELAFFAGVRWDLLTEVlRPPFIPLRDDGE 365
Cdd:cd05574 284 SEIKRHPFFRGVNWALIRNM-TPPIIPRPDDPI 315
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
27-341 8.33e-82

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: 251.28  E-value: 8.33e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARW---EIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWA 103
Cdd:cd05123   1 LGKGSFGKVLL----VRKKDTGKLYAMKVLRKKEIIKRKEVEHtlnERNILERVN-----HPFIVKLHYAFQTEEKLYLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrp 183
Cdd:cd05123  72 LDYVPGGELFSHLSKE--GRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLA--------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd05123 141 ------------------------------------------------KELSSDGDRTYTFCGTPEYLAPEVLLGKGYGK 172
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEF-AGKPNDLTDLIRRLLVKDPNRRLGCHrGAAEIKELAFF 341
Cdd:cd05123 173 AVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFpEYVSPEAKSLISGLLQKDPTKRLGSG-GAEEIKAHPFF 250
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
24-341 1.15e-72

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 227.80  E-value: 1.15e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374     24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLR-RARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAW 102
Cdd:smart00220   4 LEKLGEGSFGKVYLARDKKTGKL----VAIKVIKKKKIKKDReRILREIKILKKL-----KHPNIVRLYDVFEDEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    103 AVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkplr 182
Cdd:smart00220  75 VMEYCEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLD---- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    183 phfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIRGDGHD 262
Cdd:smart00220 149 ------------------------------------------------------PGEKLTTFVGTPEYMAPEVLLGKGYG 174
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    263 FAVDWWALGVLTYEMMYGETPFKGKSK-KETFRNVLMKEPEFAGKPNDLT----DLIRRLLVKDPNRRLgchrGAAEIKE 337
Cdd:smart00220 175 KAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPEWDISpeakDLIRKLLVKDPEKRL----TAEEALQ 250

                   ....
gi 15232374    338 LAFF 341
Cdd:smart00220 251 HPFF 254
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
25-385 3.35e-72

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: 229.02  E-value: 3.35e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASslrrARWEIE---VLRRLSVDSNQNPFLPRLLASFESPEYFA 101
Cdd:cd05570   1 KVLGKGSFGKVMLAE----RKKTDELYAIKVLKKEVII----EDDDVEctmTEKRVLALANRHPFLTGLHACFQTEDRLY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkpl 181
Cdd:cd05570  73 FVMEYVNGGDL--MFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMC------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd05570 144 --------------------------------------------------KEGIWGGNTTSTFCGTPDYIAPEILREQDY 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRLGCHR-GAAEIKELA 339
Cdd:cd05570 174 GFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWlSREAVSILKGLLTKDPARRLGCGPkGEADIKAHP 253
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15232374 340 FFAGVRWDLLTEV-LRPPFIPlRDDGELTVGGFDIREHFEKLRTTPS 385
Cdd:cd05570 254 FFRNIDWDKLEKKeVEPPFKP-KVKSPRDTSNFDPEFTSESPRLTPV 299
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
24-408 2.74e-70

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: 225.24  E-value: 2.74e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKS-----SASSLRRArwEIEVLrrlsVDSNqNPFLPRLLASFESPE 98
Cdd:cd05573   6 IKVIGRGAFGEVWLVRDK----DTGQVYAMKILRKSdmlkrEQIAHVRA--ERDIL----ADAD-SPWIVRLHYAFQDED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLK 178
Cdd:cd05573  75 HLYLVMEYMPGGDLMNLLIKY--DVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 KPLRPHFYQPDPELIIDRKKSRSFSRlisptaeknktglkKTRSARVnpinrrktsfssgeRSNSFVGTDEYVSPEVIRG 258
Cdd:cd05573 153 KSGDRESYLNDSVNTLFQDNVLARRR--------------PHKQRRV--------------RAYSAVGTPDYIAPEVLRG 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 259 DGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLvKDPNRRLGchrGAA 333
Cdd:cd05573 205 TGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYSKIMnwkesLVFPDDPDVSPEAIDLIRRLL-CDPEDRLG---SAE 280
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 334 EIKELAFFAGVRWDLLTEvLRPPFIP-LRDDGELTvggfdireHFEKLRTTPSSAPPSPLRSPPHVCRKNDPFIEF 408
Cdd:cd05573 281 EIKAHPFFKGIDWENLRE-SPPPFVPeLSSPTDTS--------NFDDFEDDLLLSEYLSNGSPLLGKGKQLAFVGF 347
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
29-346 1.09e-69

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: 220.94  E-value: 1.09e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  29 KGATGTVFLAhdvvSTSSSSSPFAVKLVPKSSAS---SLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVP 105
Cdd:cd05579   3 RGAYGRVYLA----KKKSTGDLYAIKVIKKRDMIrknQVDSVLAERNILSQA-----QNPFVVKLYYSFQGKKNLYLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLHrqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplrphf 185
Cdd:cd05579  74 YLPGGDLYSLLE--NVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSK---------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yqpdpELIIDRKKSRSFSRLISPTAEKnktglkktrsarvnpinrrktsfssgeRSNSFVGTDEYVSPEVIRGDGHDFAV 265
Cdd:cd05579 142 -----VGLVRRQIKLSIQKKSNGAPEK---------------------------EDRRIVGTPDYLAPEILLGQGHGKTV 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 266 DWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE---PEFAGKPNDLTDLIRRLLVKDPNRRLGcHRGAAEIKELAFFA 342
Cdd:cd05579 190 DWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKiewPEDPEVSDEAKDLISKLLTPDPEKRLG-AKGIEEIKNHPFFK 268

                ....
gi 15232374 343 GVRW 346
Cdd:cd05579 269 GIDW 272
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
25-341 1.87e-68

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: 217.85  E-value: 1.87e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSssssPFAVKLVPKSSASSLRRARW---EIEVLRRLSvdsnqNPFLPRLLASFESPEYFA 101
Cdd:cd05581   7 KPLGEGSYSTVVLAKEKETGK----EYAIKVLDKRHIIKEKKVKYvtiEKEVLSRLA-----HPGIVKLYYTFQDESKLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPL 181
Cdd:cd05581  78 FVLEYAPNGDLLEYIRKY--GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 RPHfyqpdpeliidrkksrsfsrlisptaeknktgLKKTRSARVNPINRRktsfssgeRSNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd05581 156 SPE--------------------------------STKGDADSQIAYNQA--------RAASFVGTAEYVSPELLNEKPA 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEF-AGKPNDLTDLIRRLLVKDPNRRLGCH--RGAAEIKEL 338
Cdd:cd05581 196 GKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFpENFPPDAKDLIQKLLVLDPSKRLGVNenGGYDELKAH 275

                ...
gi 15232374 339 AFF 341
Cdd:cd05581 276 PFF 278
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
26-344 6.35e-68

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: 216.11  E-value: 6.35e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAHDVVSTSSSSSpFAVKLVPKSS----ASSLRRARWEIEVLRRLsvdsNQNPFLPRLLASFESPEYFA 101
Cdd:cd05583   1 VLGTGAYGKVFLVRKVGGHDAGKL-YAMKVLKKATivqkAKTAEHTMTERQVLEAV----RQSPFLVTLHYAFQTDAKLH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNV-LLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkKP 180
Cdd:cd05583  76 LILDYVNGGELFThLYQREH---FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLS----KE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 LRPHfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIRG-- 258
Cdd:cd05583 149 FLPG----------------------------------------------------ENDRAYSFCGTIEYMAPEVVRGgs 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 259 DGHDFAVDWWALGVLTYEMMYGETPF----KGKSKKETFRNVLMKEPEFagkPNDLT----DLIRRLLVKDPNRRLGC-H 329
Cdd:cd05583 177 DGHDKAVDWWSLGVLTYELLTGASPFtvdgERNSQSEISKRILKSHPPI---PKTFSaeakDFILKLLEKDPKKRLGAgP 253
                       330
                ....*....|....*
gi 15232374 330 RGAAEIKELAFFAGV 344
Cdd:cd05583 254 RGAHEIKEHPFFKGL 268
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
19-372 6.97e-66

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: 211.67  E-value: 6.97e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRA---RWEIEVLRRLSvdsnqNPFLPRLLASFE 95
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRL----VKHKDSGKYYALKILKKAKIIKLKQVehvLNEKRILSEVR-----HPFIVNLLGSFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLHRqnDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd05580  72 DDRNLYMVMEYVPGGELFSLLRR--SGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SLKkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEV 255
Cdd:cd05580 150 RVK------------------------------------------------------------DRTYTLCGTPEYLAPEI 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRLGC-HRGAA 333
Cdd:cd05580 170 ILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFfDPDAKDLIKRLLVVDLTKRLGNlKNGVE 249
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15232374 334 EIKELAFFAGVRWD-LLTEVLRPPFIP-LRDDGEltVGGFD 372
Cdd:cd05580 250 DIKNHPWFAGIDWDaLLQRKIPAPYVPkVRGPGD--TSNFD 288
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
24-408 8.55e-65

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: 209.95  E-value: 8.55e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSSSSpFAVKLVPKssASSLRRA------RWEIEVLRRLsvdsnQNPFLPRLLASFESP 97
Cdd:cd05584   1 LKVLGKGGYGKVFQVRKTTGSDKGKI-FAMKVLKK--ASIVRNQkdtahtKAERNILEAV-----KHPFIVDLHYAFQTG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrsl 177
Cdd:cd05584  73 GKLYLILEYLSGGELFMHLERE--GIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLC--- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIR 257
Cdd:cd05584 148 ------------------------------------------------------KESIHDGTVTHTFCGTIEYMAPEILT 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLmkepefAGK---PNDLT----DLIRRLLVKDPNRRLG-CH 329
Cdd:cd05584 174 RSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKIL------KGKlnlPPYLTnearDLLKKLLKRNVSSRLGsGP 247
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 330 RGAAEIKELAFFAGVRW-DLLTEVLRPPFIP-LRDDGEltVGGFDIRehFEKLrtTPSSAPPSPLRSPPhvcrKNDPFIE 407
Cdd:cd05584 248 GDAEEIKAHPFFRHINWdDLLAKKVEPPFKPlLQSEED--VSQFDSK--FTKQ--TPVDSPDDSTLSES----ANQVFQG 317

                .
gi 15232374 408 F 408
Cdd:cd05584 318 F 318
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
24-390 6.10e-64

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: 208.23  E-value: 6.10e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSSSSpFAVKLVPKSS----ASSLRRARWEIEVLRRLsvdsNQNPFLPRLLASFESPEY 99
Cdd:cd05614   5 LKVLGTGAYGKVFLVRKVSGHDANKL-YAMKVLRKAAlvqkAKTVEHTRTERNVLEHV----RQSPFLVTLHYAFQTDAK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQNDgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkk 179
Cdd:cd05614  80 LHLILDYVSGGELFTHLYQRDH--FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSK---- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpELIIDRKksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEVIRGD 259
Cdd:cd05614 154 -----------EFLTEEK-----------------------------------------ERTYSFCGTIEYMAPEIIRGK 181
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 -GHDFAVDWWALGVLTYEMMYGETPF----KGKSKKETFRNVLMKEPEFAGKPNDLT-DLIRRLLVKDPNRRLGC-HRGA 332
Cdd:cd05614 182 sGHGKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVArDLLQKLLCKDPKKRLGAgPQGA 261
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 333 AEIKELAFFAGVRW-DLLTEVLRPPFIP-LRDdgELTVGGFdiREHFEKLRT--TPSSAPPS 390
Cdd:cd05614 262 QEIKEHPFFKGLDWeALALRKVNPPFRPsIRS--ELDVGNF--AEEFTNLEPvySPAGTPPS 319
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
24-359 6.01e-61

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: 199.07  E-value: 6.01e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSSSSpFAVKLVPKSS----ASSLRRARWEIEVLRRLsvdsNQNPFLPRLLASFESPEY 99
Cdd:cd05613   5 LKVLGTGAYGKVFLVRKVSGHDAGKL-YAMKVLKKATivqkAKTAEHTRTERQVLEHI----RQSPFLVTLHYAFQTDTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkk 179
Cdd:cd05613  80 LHLILDYINGGEL--FTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSK---- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpELIIDRKksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEVIRG- 258
Cdd:cd05613 154 -----------EFLLDEN-----------------------------------------ERAYSFCGTIEYMAPEIVRGg 181
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 259 -DGHDFAVDWWALGVLTYEMMYGETPF----KGKSKKETFRNVLMKEPEFagkPNDLT----DLIRRLLVKDPNRRLGCH 329
Cdd:cd05613 182 dSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPY---PQEMSalakDIIQRLLMKDPKKRLGCG 258
                       330       340       350
                ....*....|....*....|....*....|..
gi 15232374 330 -RGAAEIKELAFFAGVRWDLLTEVLRP-PFIP 359
Cdd:cd05613 259 pNGADEIKKHPFFQKINWDDLAAKKVPaPFKP 290
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
24-372 1.12e-59

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 198.72  E-value: 1.12e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLA-----HDVVstssssspfAVKLVPKSSASSLRRARweiEVLRRLSVDSNQN-PFLPRLLASFESP 97
Cdd:cd05600  16 LTQVGQGGYGSVFLArkkdtGEIC---------ALKIMKKKVLFKLNEVN---HVLTERDILTTTNsPWLVKLLYAFQDP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSl 177
Cdd:cd05600  84 ENVYLAMEYVPGGDFRTLL--NNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASG- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpelIIDRKKSRSFSrlISPTAEKNKTGLKKTRSARVNPInrrKTSFSSGE-RSNSFVGTDEYVSPEVI 256
Cdd:cd05600 161 ---------------TLSPKKIESMK--IRLEEVKNTAFLELTAKERRNIY---RAMRKEDQnYANSVVGSPDYMAPEVL 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGK------PNDLTDLIRRLLVkDPNRR 325
Cdd:cd05600 221 RGEGYDLTVDYWSLGCILFECLVGFPPFSGSTPNETWANLYhwkktLQRPVYTDPdlefnlSDEAWDLITKLIT-DPQDR 299
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15232374 326 LgchRGAAEIKELAFFAGVRWDLLTEVLRPPFIPLRDDgELTVGGFD 372
Cdd:cd05600 300 L---QSPEQIKNHPFFKNIDWDRLREGSKPPFIPELES-EIDTSYFD 342
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
25-385 1.46e-59

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: 196.45  E-value: 1.46e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSAssLRRARWE---IEvlRRLSVDSNQNPFLPRLLASFESPEYFA 101
Cdd:cd05592   1 KVLGKGSFGKVMLAE----LKGTNQYFAIKALKKDVV--LEDDDVEctmIE--RRVLALASQHPFLTHLFCTFQTESHLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrslkkpl 181
Cdd:cd05592  73 FVMEYLNGGDL--MFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADF---------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktGLKKTRsarvnpINRRKTSfssgersNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd05592 141 ----------------------------------GMCKEN------IYGENKA-------STFCGTPDYIAPEILKGQKY 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagkPNDLT----DLIRRLLVKDPNRRLG---CHRGaaE 334
Cdd:cd05592 174 NQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHY---PRWLTkeaaSCLSLLLERNPEKRLGvpeCPAG--D 248
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 15232374 335 IKELAFFAGVRWDLLTEV-LRPPFIPlRDDGELTVGGFDIREHFEKLRTTPS 385
Cdd:cd05592 249 IRDHPFFKTIDWDKLERReIDPPFKP-KVKSANDVSNFDPDFTMEKPVLTPV 299
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
25-398 5.31e-58

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: 192.53  E-value: 5.31e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSlRRARWEIEVLRRLSVDSNQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKL----YAVKVLQKKAILK-RNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrph 184
Cdd:cd05575  76 DYVNGGEL--FFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLC---------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 185 fyqpdpeliidrkksrsfsrlisptaeknKTGLKktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIRGDGHDFA 264
Cdd:cd05575 144 -----------------------------KEGIE------------------PSDTTSTFCGTPEYLAPEVLRKQPYDRT 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 265 VDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagKPN---DLTDLIRRLLVKDPNRRLGCHRGAAEIKELAFF 341
Cdd:cd05575 177 VDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRL--RTNvspSARDLLEGLLQKDRTKRLGSGNDFLEIKNHSFF 254
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 342 AGVRW-DLLTEVLRPPFIPlrddgELTvGGFDIReHFEKlRTTPSSAPPSPLRSPPHV 398
Cdd:cd05575 255 RPINWdDLEAKKIPPPFNP-----NVS-GPLDLR-NIDP-EFTREPVPASVGKSADSV 304
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
24-347 5.35e-57

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: 187.69  E-value: 5.35e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARwEIEVLRRLSVDSNQNPFLPRLLASFESPEYFAWA 103
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRSTGDY----FAIKVLKKSDMIAKNQVT-NVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplrp 183
Cdd:cd05611  76 MEYLNGGDCASLI--KTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSR-------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlisptaeknkTGLKKTRSARvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd05611 146 -------------------------------NGLEKRHNKK-------------------FVGTPDYLAPETILGVGDDK 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMK-----EPEFAGKPNDLTDLIRRLLVKDPNRRLGCHrGAAEIKEL 338
Cdd:cd05611 176 MSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRrinwpEEVKEFCSPEAVDLINRLLCMDPAKRLGAN-GYQEIKSH 254

                ....*....
gi 15232374 339 AFFAGVRWD 347
Cdd:cd05611 255 PFFKSINWD 263
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
27-348 1.27e-55

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: 184.35  E-value: 1.27e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARW---EIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWA 103
Cdd:cd05572   1 LGVGGFGRVEL----VQLKSKGRTFALKCVKKRHIVQTRQQEHifsEKEILEECN-----SPFIVKLYRTFKDKKYLYML 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkplrp 183
Cdd:cd05572  72 MEYCLGGELWTILRDR--GLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLG----- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd05572 145 -----------------------------------------------------SGRKTWTFCGTPEYVAPEIILNKGYDF 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKK--ETFRNVL-----MKEPEFAGKpnDLTDLIRRLLVKDPNRRLGCHR-GAAEI 335
Cdd:cd05572 172 SVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILkgidkIEFPKYIDK--NAKNLIKQLLRRNPEERLGYLKgGIRDI 249
                       330
                ....*....|...
gi 15232374 336 KELAFFAGVRWDL 348
Cdd:cd05572 250 KKHKWFEGFDWEG 262
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
19-406 1.30e-55

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 187.75  E-value: 1.30e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSS---ASSLRRARWEIEVLrrlsVDSNqNPFLPRLLASFE 95
Cdd:cd05629   1 EDFHTVKVIGKGAFGEVRL----VQKKDTGKIYAMKTLLKSEmfkKDQLAHVKAERDVL----AESD-SPWVVSLYYSFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLHRQNdgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd05629  72 DAQYLYLIMEFLPGGDLMTMLIKYD--TFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLST 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SLKKPLRPHFYQpdpeliidrkksrsfsRLISPTAekNKTGLKKTRSARVNPI---------------NRRKTSFSSger 240
Cdd:cd05629 150 GFHKQHDSAYYQ----------------KLLQGKS--NKNRIDNRNSVAVDSInltmsskdqiatwkkNRRLMAYST--- 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 241 snsfVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEpEFAGKPNDLT------DLI 314
Cdd:cd05629 209 ----VGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIGWPPFCSENSHETYRKIINWR-ETLYFPDDIHlsveaeDLI 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 315 RRLLVkDPNRRLGCHrGAAEIKELAFFAGVRWDLLTEVlRPPFIP-LRddgELTVGGFDIREHFEKLRTTPSSAPPSPlR 393
Cdd:cd05629 284 RRLIT-NAENRLGRG-GAHEIKSHPFFRGVDWDTIRQI-RAPFIPqLK---SITDTSYFPTDELEQVPEAPALKQAAP-A 356
                       410
                ....*....|...
gi 15232374 394 SPPHVCRKNDPFI 406
Cdd:cd05629 357 QQEESVELDLAFI 369
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
24-394 2.56e-55

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: 185.58  E-value: 2.56e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASslrrARWEIEVL---RRL--SVDSNQNPFLPRLLASFESPE 98
Cdd:cd05589   4 IAVLGRGHFGKVLLAEY----KPTGELFAIKALKKGDII----ARDEVESLmceKRIfeTVNSARHPFLVNLFACFQTPE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLnvLLHRQNDgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslk 178
Cdd:cd05589  76 HVCFVMEYAAGGDL--MMHIHED-VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC---- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRG 258
Cdd:cd05589 149 -----------------------------------------------------KEGMGFGDRTSTFCGTPEFLAPEVLTD 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 259 DGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE---PEFAGkpNDLTDLIRRLLVKDPNRRLGC-HRGAAE 334
Cdd:cd05589 176 TSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEvryPRFLS--TEAISIMRRLLRKNPERRLGAsERDAED 253
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 335 IKELAFFAGVRWD-LLTEVLRPPFIPLRDDGElTVGGFDirEHF--EKLRTTPsSAPPSPLRS 394
Cdd:cd05589 254 VKKQPFFRNIDWEaLLARKIKPPFVPTIKSPE-DVSNFD--EEFtsEKPVLTP-PKEPRPLTE 312
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
25-391 2.57e-55

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: 185.30  E-value: 2.57e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSSSSpFAVKLVPKSSASSLRRARWEIEvlRRLSVDSNqNPFLPRLLASFESPEYFAWAV 104
Cdd:cd05582   1 KVLGQGSFGKVFLVRKITGPDAGTL-YAMKVLKKATLKVRDRVRTKME--RDILADVN-HPFIVKLHYAFQTEGKLYLIL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLNVLLHRqnDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrph 184
Cdd:cd05582  77 DFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLS---------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 185 fyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRGDGHDFA 264
Cdd:cd05582 145 -----------------------------------------------KESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQS 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 265 VDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEpefAGKPNDLT----DLIRRLLVKDPNRRLGC-HRGAAEIKELA 339
Cdd:cd05582 178 ADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAK---LGMPQFLSpeaqSLLRALFKRNPANRLGAgPDGVEEIKRHP 254
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 340 FFAGVRWD-LLTEVLRPPFIPlrddgelTVGGFDIREHF--EKLRTTPSSAPPSP 391
Cdd:cd05582 255 FFATIDWNkLYRKEIKPPFKP-------AVSRPDDTFYFdpEFTSRTPKDSPGVP 302
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
25-397 1.13e-54

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: 183.71  E-value: 1.13e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSS-------ASSLRRARweieVLRRLSvdsnqNPFLPRLLASFESP 97
Cdd:cd05571   1 KVLGKGTFGKVIL----CREKATGELYAIKILKKEViiakdevAHTLTENR----VLQNTR-----HPFLTSLKYSFQTN 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrsl 177
Cdd:cd05571  68 DRLCFVMEYVNGGEL--FFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLC--- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIR 257
Cdd:cd05571 143 ------------------------------------------------------KEEISYGATTKTFCGTPEYLAPEVLE 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagkPNDLT----DLIRRLLVKDPNRRLG-CHRGA 332
Cdd:cd05571 169 DNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRF---PSTLSpeakSLLAGLLKKDPKKRLGgGPRDA 245
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374 333 AEIKELAFFAGVRW-DLLTEVLRPPFIPLRDDgELTVGGFDirEHF--EKLRTTP---SSAPPSPLRSPPH 397
Cdd:cd05571 246 KEIMEHPFFASINWdDLYQKKIPPPFKPQVTS-ETDTRYFD--EEFtaESVELTPpdrGDLLGLEEEERPH 313
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
24-329 1.40e-54

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: 181.13  E-value: 1.40e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSS------ASSLRRarwEIEVLRRLSvdsnqNPFLPRLLASFESP 97
Cdd:cd14007   5 GKPLGKGKFGNVYLARE----KKSGFIVALKVISKSQlqksglEHQLRR---EIEIQSHLR-----HPNILRLYGYFEDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRsl 177
Cdd:cd14007  73 KRIYLILEYAPNGELYKELKKQ--KRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSV-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarVNPINRRKTsfssgersnsFVGTDEYVSPEVIR 257
Cdd:cd14007 149 -----------------------------------------------HAPSNRRKT----------FCGTLDYLPPEMVE 171
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRLGCH 329
Cdd:cd14007 172 GKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSvSPEAKDLISKLLQKDPSKRLSLE 244
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
25-408 1.58e-54

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: 183.25  E-value: 1.58e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAhdvvSTSSSSSPFAVKLVPKSSASSlRRARWEIEVLRRLSVDSNQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd05603   1 KVIGKGSFGKVLLA----KRKCDGKFYAVKVLQKKTILK-KKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslKKPLRPH 184
Cdd:cd05603  76 DYVNGGEL--FFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLC---KEGMEPE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 185 fyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEVIRGDGHDFA 264
Cdd:cd05603 151 ------------------------------------------------------ETTSTFCGTPEYLAPEVLRKEPYDRT 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 265 VDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAG-KPNDLTDLIRRLLVKDPNRRLGCHRGAAEIKELAFFAG 343
Cdd:cd05603 177 VDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGgKTVAACDLLQGLLHKDQRRRLGAKADFLEIKNHVFFSP 256
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 344 VRW-DLLTEVLRPPFIPlrddgelTVGGFDIREHFEKlRTTPSSAPPSPLRSP---PHVCRKNDPFIEF 408
Cdd:cd05603 257 INWdDLYHKRITPPYNP-------NVAGPADLRHFDP-EFTQEAVPHSVGRTPdltASSSSSSSAFLGF 317
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-372 1.47e-53

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: 179.94  E-value: 1.47e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARW---EIEVLRRLSvdsnqNPFLPRLLASFE 95
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHY----YALKVMAIPEVIRLKQEQHvhnEKRVLKEVS-----HPFIIRLFWTEH 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd05612  72 DQRFLYMLMEYVPGGELFSYL--RNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SLKkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEV 255
Cdd:cd05612 150 KLR------------------------------------------------------------DRTWTLCGTPEYLAPEV 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAgKPNDLT--DLIRRLLVKDPNRRLGCHR-GA 332
Cdd:cd05612 170 IQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFP-RHLDLYakDLIKKLLVVDRTRRLGNMKnGA 248
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15232374 333 AEIKELAFFAGVRWDL-LTEVLRPPFIP-LRDDGEltVGGFD 372
Cdd:cd05612 249 DDVKNHRWFKSVDWDDvPQRKLKPPIVPkVSHDGD--TSNFD 288
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
24-341 5.60e-52

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: 174.37  E-value: 5.60e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFlahdVVSTSSSSSPFAVKLVPKS---SASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYF 100
Cdd:cd05578   5 LRVIGKGSFGKVC----IVQKKDTKKMFAMKYMNKQkciEKDSVRNVLNELEILQEL-----EHPFLVNLWYSFQDEEDM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNvlLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKp 180
Cdd:cd05578  76 YMVVDLLLGGDLR--YHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTD- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGDG 260
Cdd:cd05578 153 ---------------------------------------------------------GTLATSTSGTKPYMAPEVFMRAG 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKK---ETFRNVLMKEPEF-AGKPNDLTDLIRRLLVKDPNRRLGCHRgaaEIK 336
Cdd:cd05578 176 YSFAVDWWSLGVTAYEMLRGKRPYEIHSRTsieEIRAKFETASVLYpAGWSEEAIDLINKLLERDPQKRLGDLS---DLK 252

                ....*
gi 15232374 337 ELAFF 341
Cdd:cd05578 253 NHPYF 257
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
17-346 1.31e-51

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: 174.52  E-value: 1.31e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  17 DLDSIKalkILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSAssLRRARWEIEVLRRLSVDSNQNPFLPRLLASFES 96
Cdd:cd05609   1 DFETIK---LISNGAYGAVYL----VRHRETRQRFAMKKINKQNL--ILRNQIQQVFVERDILTFAENPFVVSMYCSFET 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PEYFAWAVPYCSGGDLNVLLHrqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrs 176
Cdd:cd05609  72 KRHLCMVMEYVEGGDCATLLK--NIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLS-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 lkkplrphfyqpdpeliidrkksrsfsrlisptaeknKTGL-KKTRSARVNPINRRKTSFSSGERsnsfVGTDEYVSPEV 255
Cdd:cd05609 148 -------------------------------------KIGLmSLTTNLYEGHIEKDTREFLDKQV----CGTPEYIAPEV 186
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK----PNDLTDLIRRLLVKDPNRRLGChRG 331
Cdd:cd05609 187 ILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGddalPDDAQDLITRLLQQNPLERLGT-GG 265
                       330
                ....*....|....*
gi 15232374 332 AAEIKELAFFAGVRW 346
Cdd:cd05609 266 AEEVKQHPFFQDLDW 280
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
24-408 2.84e-51

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 175.20  E-value: 2.84e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVKlvpkssasSLRRArweiEVLRRlsvdsNQ---------------NPFLP 88
Cdd:cd05598   6 IKTIGVGAFGEVSLVRKKDTNAL----YAMK--------TLRKK----DVLKR-----NQvahvkaerdilaeadNEWVV 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  89 RLLASFESPEYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTL 168
Cdd:cd05598  65 KLYYSFQDKENLYFVMDYIPGGDLMSLLIKK--GIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 169 TDFDLSrslkkplrphfyqpdpeliidrkksrsfsrlisptaeknkTGLkktrsarvnpinrRKTSFSSGERSNSFVGTD 248
Cdd:cd05598 143 TDFGLC----------------------------------------TGF-------------RWTHDSKYYLAHSLVGTP 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 249 EYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVkDPN 323
Cdd:cd05598 170 NYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwrttLKIPHEANLSPEAKDLILRLCC-DAE 248
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 324 RRLGCHrGAAEIKELAFFAGVRWDLLTEVlRPPFIP-LRDDGEltVGGFDIREHfEKLRTTPS----SAPPSPLRSPPHv 398
Cdd:cd05598 249 DRLGRN-GADEIKAHPFFAGIDWEKLRKQ-KAPYIPtIRHPTD--TSNFDPVDP-EKLRSSDEepttPNDPDNGKHPEH- 322
                       410
                ....*....|
gi 15232374 399 crkndPFIEF 408
Cdd:cd05598 323 -----AFYEF 327
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
25-326 3.18e-51

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: 172.66  E-value: 3.18e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRA--RWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAW 102
Cdd:cd05117   6 KVLGRGSFGVVRLAVH----KKTGEEYAVKIIDKKKLKSEDEEmlRREIEILKRLD-----HPNIVKLYEVFEDDKNLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDL-NVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ---QSGHVTLTDFDLSRslk 178
Cdd:cd05117  77 VMELCTGGELfDRIVKK---GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGLAK--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kplrphFYQPDPELiidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRG 258
Cdd:cd05117 151 ------IFEEGEKL-------------------------------------------------KTVCGTPYYVAPEVLKG 175
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 259 DGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKP-NDLT----DLIRRLLVKDPNRRL 326
Cdd:cd05117 176 KGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEwKNVSeeakDLIKRLLVVDPKKRL 248
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
19-408 7.11e-51

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


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 173.57  E-value: 7.11e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSAssLRR-----ARWEIEVLrrlsVDSNqNPFLPRLLAS 93
Cdd:cd05599   1 EDFEPLKVIGRGAFGEVRL----VRKKDTGHVYAMKKLRKSEM--LEKeqvahVRAERDIL----AEAD-NPWVVKLYYS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 FESPEYFAWAVPYCSGGDLNVLLHRQNdgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDL 173
Cdd:cd05599  70 FQDEENLYLIMEFLPGGDMMTLLMKKD--TLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SrslkkplrphfyqpdpeliidrkksrsfsrlisptaeknkTGLKKTRSArvnpinrrktsFSSgersnsfVGTDEYVSP 253
Cdd:cd05599 148 C----------------------------------------TGLKKSHLA-----------YST-------VGTPDYIAP 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVkDPNRRLGC 328
Cdd:cd05599 170 EVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwretLVFPPEVPISPEAKDLIERLLC-DAEHRLGA 248
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 329 HrGAAEIKELAFFAGVRWDLLTEvLRPPFIPlrddgelTVGGFDIREHFEKLRTTPSSAPPSPLRSPPH--VCRKNDPFI 406
Cdd:cd05599 249 N-GVEEIKSHPFFKGVDWDHIRE-RPAPILP-------EVKSILDTSNFDEFEEVDLQIPSSPEAGKDSkeLKSKDWVFI 319

                ..
gi 15232374 407 EF 408
Cdd:cd05599 320 GY 321
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
24-374 7.50e-51

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: 174.30  E-value: 7.50e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKssASSLRRARWEIEVLRRLSVDSNQNPFLPRLLASFESPEYFAWA 103
Cdd:cd05610   9 VKPISRGAFGKVYLGR----KKNNSKLYAVKVVKK--ADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR-SLKKPLR 182
Cdd:cd05610  83 MEYLIGGDVKSLLHIY--GYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvTLNRELN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 PHFYQPDPELIIDRKK-SRSFSRLISPTAEknkTGLKKTRSARVNPINRRKTSFSSGERsnsFVGTDEYVSPEVIRGDGH 261
Cdd:cd05610 161 MMDILTTPSMAKPKNDySRTPGQVLSLISS---LGFNTPTPYRTPKSVRRGAARVEGER---ILGTPDYLAPELLLGKPH 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPNDLTD----LIRRLLVKDPNRRlgchRGAAEIKE 337
Cdd:cd05610 235 GPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGEEELSVnaqnAIEILLTMDPTKR----AGLKELKQ 310
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15232374 338 LAFFAGVRWDLLTEVlRPPFIPLRDDgELTVGGFDIR 374
Cdd:cd05610 311 HPLFHGVDWENLQNQ-TMPFIPQPDD-ETDTSYFEAR 345
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
24-406 9.16e-51

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: 173.61  E-value: 9.16e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASSlRRARWEIEVLRRLSVDSNQNPFLPRLLASFESPEYFAWA 103
Cdd:cd05604   1 LKVIGKGSFGKVLLAK----RKRDGKYYAVKVLQKKVILN-RKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrp 183
Cdd:cd05604  76 LDFVNGGEL--FFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLC--------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd05604 145 ------------------------------------------------KEGISNSDTTTTFCGTPEYLAPEVIRKQPYDN 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKepEFAGKPNDLT---DLIRRLLVKDPNRRLGCHRGAAEIKELAF 340
Cdd:cd05604 177 TVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHK--PLVLRPGISLtawSILEELLEKDRQLRLGAKEDFLEIKNHPF 254
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 341 FAGVRW-DLLTEVLRPPFIPlrddgelTVGGFDIREHFEKLRTTPSsappsplrSPPHVCRKNDPFI 406
Cdd:cd05604 255 FESINWtDLVQKKIPPPFNP-------NVNGPDDISNFDAEFTEEM--------VPYSVCVSSDYSI 306
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
26-359 1.54e-50

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: 172.76  E-value: 1.54e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKS---SASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAW 102
Cdd:cd05585   1 VIGKGSFGKVMQ----VRKKDTSRIYALKTIRKAhivSRSEVTHTLAERTVLAQVD-----CPFIVPLKFSFQSPEKLYL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplr 182
Cdd:cd05585  72 VLAFINGGEL--FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLC-------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRGDGHD 262
Cdd:cd05585 142 -------------------------------------------------KLNMKDDDKTNTFCGTPEYLAPELLLGHGYT 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 263 FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFA-GKPNDLTDLIRRLLVKDPNRRLGCHrGAAEIKELAFF 341
Cdd:cd05585 173 KAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPdGFDRDAKDLLIGLLNRDPTKRLGYN-GAQEIKNHPFF 251
                       330
                ....*....|....*....
gi 15232374 342 AGVRWD-LLTEVLRPPFIP 359
Cdd:cd05585 252 DQIDWKrLLMKKIQPPFKP 270
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
82-408 2.15e-48

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 167.49  E-value: 2.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  82 NQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQnDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ 161
Cdd:cd05601  58 ANSPWITKLQYAFQDSENLYLVMEYHPGGDLLSLLSRY-DDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILID 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 162 QSGHVTLTDFDlsrslkkplrphfyqpdpeliidrkksrSFSRLisptaeknktglkktrsarvnpiNRRKTSFssgerS 241
Cdd:cd05601 137 RTGHIKLADFG----------------------------SAAKL-----------------------SSDKTVT-----S 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 242 NSFVGTDEYVSPEVIRGDGHDFA------VDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDL 310
Cdd:cd05601 161 KMPVGTPDYIAPEVLTSMNGGSKgtygveCDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMnfkkfLKFPEDPKVSESA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 311 TDLIRRLLVkDPNRRLGcHRGaaeIKELAFFAGVRWDLLTEVLrPPFIP-LRDDGEltVGGFDireHFEKLRTTPSSapp 389
Cdd:cd05601 241 VDLIKGLLT-DAKERLG-YEG---LCCHPFFSGIDWNNLRQTV-PPFVPtLTSDDD--TSNFD---EFEPKKTRPSY--- 306
                       330
                ....*....|....*....
gi 15232374 390 SPLRSPPHVCRKNDPFIEF 408
Cdd:cd05601 307 ENFNKSKGFSGKDLPFVGF 325
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
24-326 3.00e-48

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: 164.61  E-value: 3.00e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKS--SASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd14003   5 GKTLGEGSFGKVKLARHKLTGEK----VAIKIIDKSklKEEIEEKIKREIEIMKLL-----NHPNIIKLYEVIETENKIY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLnvlLHR-QNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkp 180
Cdd:cd14003  76 LVMEYASGGEL---FDYiVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSN----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktSFSSGERSNSFVGTDEYVSPEVIRGDG 260
Cdd:cd14003 148 -----------------------------------------------------EFRGGSLLKTFCGTPAYAAPEVLLGRK 174
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 261 HD-FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14003 175 YDgPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHlSPDARDLIRRMLVVDPSKRI 242
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
27-372 1.80e-47

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: 165.05  E-value: 1.80e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLahdvVSTSSSSSPFAVKLVPKS---SASSLRRARWEIEVLRRLSVDSNqnPFLPRLLASFESPEYFAWA 103
Cdd:cd05586   1 IGKGTFGQVYQ----VRKKDTRRIYAMKVLSKKvivAKKEVAHTIGERNILVRTALDES--PFIVGLKFSFQTPTDLYLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplrp 183
Cdd:cd05586  75 TDYMSGGEL--FWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSK-------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlisPTAEKNKTglkktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVIRGD-GHD 262
Cdd:cd05586 145 ------------------------ADLTDNKT-------------------------TNTFCGTTEYLAPEVLLDEkGYT 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 263 FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagkPNDLTDL-----IRRLLVKDPNRRLGCHRGAAEIKE 337
Cdd:cd05586 176 KMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRF---PKDVLSDegrsfVKGLLNRNPKHRLGAHDDAVELKE 252
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 15232374 338 LAFFAGVRWDLLTE-VLRPPFIPLRDDgELTVGGFD 372
Cdd:cd05586 253 HPFFADIDWDLLSKkKITPPFKPIVDS-DTDVSNFD 287
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
25-359 3.21e-47

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: 164.02  E-value: 3.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKS---SASSLRRARWEIEVLRrlsvdSNQNPFLPRLLASFESPEYFA 101
Cdd:cd05595   1 KLLGKGTFGKVIL----VREKATGRYYAMKILRKEviiAKDEVAHTVTESRVLQ-----NTRHPFLTALKYAFQTHDRLC 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkpl 181
Cdd:cd05595  72 FVMEYANGGEL--FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLC------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd05595 143 --------------------------------------------------KEGITDGATMKTFCGTPEYLAPEVLEDNDY 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagkPNDLT----DLIRRLLVKDPNRRLGCH-RGAAEIK 336
Cdd:cd05595 173 GRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRF---PRTLSpeakSLLAGLLKKDPKQRLGGGpSDAKEVM 249
                       330       340
                ....*....|....*....|....
gi 15232374 337 ELAFFAGVRW-DLLTEVLRPPFIP 359
Cdd:cd05595 250 EHRFFLSINWqDVVQKKLLPPFKP 273
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
19-408 3.92e-47

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 164.06  E-value: 3.92e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVflahDVVSTSSSSSPFAVKLVPKssASSLRRA-----RWEIEVLrrlsVDSNQnPFLPRLLAS 93
Cdd:cd05597   1 DDFEILKVIGRGAFGEV----AVVKLKSTEKVYAMKILNK--WEMLKRAetacfREERDVL----VNGDR-RWITKLHYA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 FESPEYFAWAVPYCSGGDLNVLLHRQNDGVfSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDl 173
Cdd:cd05597  70 FQDENYLYLVMDYYCGGDLLTLLSKFEDRL-PEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 srslkkplrphfyqpdpeliidrkksrsfsrlisptaeknkTGLKKTRSARVnpinrrktsfssgeRSNSFVGTDEYVSP 253
Cdd:cd05597 148 -----------------------------------------SCLKLREDGTV--------------QSSVAVGTPDYISP 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVIR--GDGHDF---AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFA------GKPNDLTDLIRRLLVkDP 322
Cdd:cd05597 173 EILQamEDGKGRygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHFSfpddedDVSEEAKDLIRRLIC-SR 251
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 323 NRRLGcHRGAAEIKELAFFAGVRWDLLTEVlRPPFIPlRDDGELTVGGFDIREhfEKLRTTPSSAPPS-PLRSPPHVcrk 401
Cdd:cd05597 252 ERRLG-QNGIDDFKKHPFFEGIDWDNIRDS-TPPYIP-EVTSPTDTSNFDVDD--DDLRHTDSLPPPSnAAFSGLHL--- 323

                ....*..
gi 15232374 402 ndPFIEF 408
Cdd:cd05597 324 --PFVGF 328
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
25-359 2.75e-46

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: 161.65  E-value: 2.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASSLRRARWEIeVLRRLSVDSNQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd05620   1 KVLGKGSFGKVLLAE----LKGKGEYFAVKALKKDVVLIDDDVECTM-VEKRVLALAWENPFLTHLYCTFQTKEHLFFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrph 184
Cdd:cd05620  76 EFLNGGDL--MFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMC---------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 185 fyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRGDGHDFA 264
Cdd:cd05620 144 -----------------------------------------------KENVFGDNRASTFCGTPDYIAPEILQGLKYTFS 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 265 VDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagkPNDLT----DLIRRLLVKDPNRRLGChrgAAEIKELAF 340
Cdd:cd05620 177 VDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHY---PRWITkeskDILEKLFERDPTRRLGV---VGNIRGHPF 250
                       330       340
                ....*....|....*....|
gi 15232374 341 FAGVRWDLLTE-VLRPPFIP 359
Cdd:cd05620 251 FKTINWTALEKrELDPPFKP 270
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
85-359 4.02e-46

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: 160.00  E-value: 4.02e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  85 PFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG 164
Cdd:cd05577  53 PFIVSLAYAFETKDKLCLVLTLMNGGDLKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHG 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 165 HVTLTDFDLSRSLKKPLRPHFYqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnsf 244
Cdd:cd05577 133 HVRISDLGLAVEFKGGKKIKGR---------------------------------------------------------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 245 VGTDEYVSPEVIRGD-GHDFAVDWWALGVLTYEMMYGETPFK----GKSKKETFRNVLMKEPEFAGK-PNDLTDLIRRLL 318
Cdd:cd05577 155 VGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRqrkeKVDKEELKRRTLEMAVEYPDSfSPEARSLCEGLL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15232374 319 VKDPNRRLGCH-RGAAEIKELAFFAGVRWDLL-TEVLRPPFIP 359
Cdd:cd05577 235 QKDPERRLGCRgGSADEVKEHPFFRSLNWQRLeAGMLEPPFVP 277
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
16-359 9.38e-46

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: 160.47  E-value: 9.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSVdSNQNPFLPRLLASFE 95
Cdd:cd05619   2 LTIEDFVLHKMLGKGSFGKVFLAE----LKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSL-AWEHPFLTHLFCTFQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd05619  77 TKENLFFVMEYLNGGDL--MFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slkkplrphfyqpdpeliidrkksrsfsrlisptaeKNKTGLKKTrsarvnpinrrktsfssgersNSFVGTDEYVSPEV 255
Cdd:cd05619 155 ------------------------------------ENMLGDAKT---------------------STFCGTPDYIAPEI 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAG-KPNDLTDLIRRLLVKDPNRRLGChRGaaE 334
Cdd:cd05619 178 LLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRwLEKEAKDILVKLFVREPERRLGV-RG--D 254
                       330       340
                ....*....|....*....|....*.
gi 15232374 335 IKELAFFAGVRWDLLTE-VLRPPFIP 359
Cdd:cd05619 255 IRQHPFFREINWEALEErEIEPPFKP 280
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
24-325 1.16e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.03  E-value: 1.16e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASS---LRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYF 100
Cdd:COG0515  12 LRLLGRGGMGVVYLARDL----RLGRPVALKVLRPELAADpeaRERFRREARALARL-----NHPNIVRVYDVGEEDGRP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKp 180
Cdd:COG0515  83 YLVMEYVEGESLADLLRRR--GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGG- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDG 260
Cdd:COG0515 160 -------------------------------------------------------ATLTQTGTVVGTPGYMAPEQARGEP 184
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-----PNDLTDLIRRLLVKDPNRR 325
Cdd:COG0515 185 VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSElrpdlPPALDAIVLRALAKDPEER 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
27-408 1.34e-45

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 159.98  E-value: 1.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   27 LGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASSLRRAR---WEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWA 103
Cdd:PTZ00263  26 LGTGSFGRVRIAK----HKGTGEYYAIKCLKKREILKMKQVQhvaQEKSILMELS-----HPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  104 VPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrp 183
Cdd:PTZ00263  97 LEFVVGGEL--FTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA--------- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  184 hfyqpdpeliidrkksrsfsrlisptaeknktglKKTRsarvnpinrrktsfssgERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:PTZ00263 166 ----------------------------------KKVP-----------------DRTFTLCGTPEYLAPEVIQSKGHGK 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagkPN----DLTDLIRRLLVKDPNRRLGC-HRGAAEIKEL 338
Cdd:PTZ00263 195 AVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKF---PNwfdgRARDLVKGLLQTDHTKRLGTlKGGVADVKNH 271
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374  339 AFFAGVRWDLLTEVLRPPFIPLRDDGELTVGGFDirehfeklrttpsSAPPSPL-RSPPHVCRKNDPFIEF 408
Cdd:PTZ00263 272 PYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-------------KYPDSPVdRLPPLTAAQQAEFAGF 329
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
24-391 1.94e-45

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: 159.80  E-value: 1.94e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRARwEIEVLRRLSVDSNQNPFLPRLLASFESPEYFAWA 103
Cdd:cd05602  12 LKVIGKGSFGKVLLARH----KSDEKFYAVKVLQKKAILKKKEEK-HIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSlkkplrp 183
Cdd:cd05602  87 LDYINGGEL--FYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKE------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlispTAEKNKTglkktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd05602 158 -------------------------NIEPNGT-------------------------TSTFCGTPEYLAPEVLHKQPYDR 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagKP---NDLTDLIRRLLVKDPNRRLGCHRGAAEIKELAF 340
Cdd:cd05602 188 TVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQL--KPnitNSARHLLEGLLQKDRTKRLGAKDDFTEIKNHIF 265
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 341 FAGVRW-DLLTEVLRPPFIPlrddgelTVGGFDIREHFEKLRT---TPSSAPPSP 391
Cdd:cd05602 266 FSPINWdDLINKKITPPFNP-------NVSGPNDLRHFDPEFTdepVPNSIGQSP 313
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
24-385 1.53e-44

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: 157.17  E-value: 1.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSAssLRRARWE-IEVLRRLSVDSNQNPFLPRLLASFESPEYFAW 102
Cdd:cd05587   1 LMVLGKGSFGKVMLAE----RKGTDELYAIKILKKDVI--IQDDDVEcTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplr 182
Cdd:cd05587  75 VMEYVNGGDL--MYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCK------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phfyqpdpeliidrkksrsfsrlisptaeKNKTGLKKTRSarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHD 262
Cdd:cd05587 146 -----------------------------EGIFGGKTTRT---------------------FCGTPDYIAPEIIAYQPYG 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 263 FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagkPNDLT----DLIRRLLVKDPNRRLGC-HRGAAEIKE 337
Cdd:cd05587 176 KSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSY---PKSLSkeavSICKGLLTKHPAKRLGCgPTGERDIKE 252
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15232374 338 LAFFAGVRWD-LLTEVLRPPFIPlRDDGELTVGGFDIREHFEKLRTTPS 385
Cdd:cd05587 253 HPFFRRIDWEkLERREIQPPFKP-KIKSPRDAENFDKEFTKEPPVLTPT 300
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
70-359 1.78e-44

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: 155.98  E-value: 1.78e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRlsVDSnqnPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIA 149
Cdd:cd05605  50 EKQILEK--VNS---RFVVSLAYAYETKDALCLVLTIMNGGDLKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIV 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 150 YRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfyqPDPELIIDRkksrsfsrlisptaeknktglkktrsarvnpin 229
Cdd:cd05605 125 YRDLKPENILLDDHGHVRISDLGLAVEI----------PEGETIRGR--------------------------------- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 230 rrktsfssgersnsfVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKK----ETFRNVLMKEPEFAG 305
Cdd:cd05605 162 ---------------VGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKvkreEVDRRVKEDQEEYSE 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 306 K-PNDLTDLIRRLLVKDPNRRLGCHR-GAAEIKELAFFAGVRWDLLTE-VLRPPFIP 359
Cdd:cd05605 227 KfSEEAKSICSQLLQKDPKTRLGCRGeGAEDVKSHPFFKSINFKRLEAgLLEPPFVP 283
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
25-359 3.71e-44

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: 156.11  E-value: 3.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAH----DVVstssssspFAVKLVPKSSAssLRRARWEIEVL-RRLSVDSNQNPFLPRLLASFESPEY 99
Cdd:cd05591   1 KVLGKGSFGKVMLAErkgtDEV--------YAIKVLKKDVI--LQDDDVDCTMTeKRILALAAKHPFLTALHSCFQTKDR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQNDgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkk 179
Cdd:cd05591  71 LFFVMEYVNGGDLMFQIQRARK--FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC----- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRGD 259
Cdd:cd05591 144 ----------------------------------------------------KEGILNGKTTTTFCGTPDYIAPEILQEL 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE---PEFAGKpnDLTDLIRRLLVKDPNRRLGC---HRGAA 333
Cdd:cd05591 172 EYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDvlyPVWLSK--EAVSILKAFMTKNPAKRLGCvasQGGED 249
                       330       340
                ....*....|....*....|....*..
gi 15232374 334 EIKELAFFAGVRWDLLTEV-LRPPFIP 359
Cdd:cd05591 250 AIRQHPFFREIDWEALEQRkVKPPFKP 276
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
27-337 4.12e-44

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: 152.42  E-value: 4.12e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASSLR-RARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVP 105
Cdd:cd00180   1 LGKGSFGKVYKARDK----ETGKKVAVKVIPKEKLKKLLeELLREIEILKKLN-----HPNIVKLYDVFETENFLYLVME 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphf 185
Cdd:cd00180  72 YCEGGSLKDLL-KENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDL-------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrkTSFSSGERSNSFVGTDEYVSPEVIRGDGHDFAV 265
Cdd:cd00180 143 -----------------------------------------------DSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKV 175
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 266 DWWALGVLTYEMmygetpfkgkskketfrnvlmkepefagkpNDLTDLIRRLLVKDPNRRLgchrGAAEIKE 337
Cdd:cd00180 176 DIWSLGVILYEL------------------------------EELKDLIRRMLQYDPKKRP----SAKELLE 213
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
18-359 8.28e-44

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: 156.01  E-value: 8.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  18 LDSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKS---SASSLRRARWEIEVLRrlsvdSNQNPFLPRLLASF 94
Cdd:cd05593  14 MNDFDYLKLLGKGTFGKVIL----VREKASGKYYAMKILKKEviiAKDEVAHTLTESRVLK-----NTRHPFLTSLKYSF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd05593  85 QTKDRLCFVMEYVNGGEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 rslkkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPE 254
Cdd:cd05593 163 ---------------------------------------------------------KEGITDAATMKTFCGTPEYLAPE 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 255 VIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRLGCH-RGA 332
Cdd:cd05593 186 VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTlSADAKSLLSGLLIKDPNKRLGGGpDDA 265
                       330       340
                ....*....|....*....|....*...
gi 15232374 333 AEIKELAFFAGVRW-DLLTEVLRPPFIP 359
Cdd:cd05593 266 KEIMRHSFFTGVNWqDVYDKKLVPPFKP 293
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
24-325 3.97e-43

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: 151.59  E-value: 3.97e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSAS---SLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYF 100
Cdd:cd14014   5 VRLLGRGGMGEVYRARD----TLLGRPVAIKVLRPELAEdeeFRERFLREARALARLS-----HPNIVRVYDVGEDDGRP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkp 180
Cdd:cd14014  76 YIVMEYVEGGSLADLLRER--GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktSFSSGERSNSFVGTDEYVSPEVIRGDG 260
Cdd:cd14014 151 -----------------------------------------------------GDSGLTQTGSVLGTPAYMAPEQARGGP 177
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFA-----GKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14014 178 VDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPsplnpDVPPALDAIILRALAKDPEER 247
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
25-372 7.20e-43

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: 152.75  E-value: 7.20e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSVdSNQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd05590   1 RVLGKGSFGKVMLAR----LKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSL-ARNHPFLTQLYCCFQTPDRLFFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrph 184
Cdd:cd05590  76 EFVNGGDL--MFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMC---------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 185 fyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIRGDGHDFA 264
Cdd:cd05590 144 -----------------------------------------------KEGIFNGKTTSTFCGTPDYIAPEILQEMLYGPS 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 265 VDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAG-KPNDLTDLIRRLLVKDPNRRLGC--HRGAAEIKELAFF 341
Cdd:cd05590 177 VDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTwLSQDAVDILKAFMTKNPTMRLGSltLGGEEAILRHPFF 256
                       330       340       350
                ....*....|....*....|....*....|..
gi 15232374 342 AGVRWDLLTE-VLRPPFIPlRDDGELTVGGFD 372
Cdd:cd05590 257 KELDWEKLNRrQIEPPFRP-RIKSREDVSNFD 287
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
16-384 1.22e-42

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: 152.87  E-value: 1.22e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARWeIEVLRRLSVDSNQNPFLPRLLASFE 95
Cdd:cd05617  12 LGLQDFDLIRVIGRGSYAKVLL----VRLKKNDQIYAMKVVKKELVHDDEDIDW-VQTEKHVFEQASSNPFLVGLHSCFQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSr 175
Cdd:cd05617  87 TTSRLFLVIEYVNGGDL--MFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMC- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slKKPLRPhfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEV 255
Cdd:cd05617 164 --KEGLGP------------------------------------------------------GDTTSTFCGTPNYIAPEI 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFK------GKSKKETFRNVLMKEPefAGKPNDLT----DLIRRLLVKDPNRR 325
Cdd:cd05617 188 LRGEEYGFSVDWWALGVLMFEMMAGRSPFDiitdnpDMNTEDYLFQVILEKP--IRIPRFLSvkasHVLKGFLNKDPKER 265
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 326 LGC--HRGAAEIKELAFFAGVRWDLLTE-VLRPPFIP-LRDDGELTvgGFDIREHFEKLRTTP 384
Cdd:cd05617 266 LGCqpQTGFSDIKSHTFFRSIDWDLLEKkQVTPPFKPqITDDYGLE--NFDTQFTSEPVQLTP 326
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
19-359 1.74e-42

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: 150.63  E-value: 1.74e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARW---EIEVLRrlSVDSnqnPFLPRLLASFE 95
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVML----VRHKETGNYYAMKILDKQKVVKLKQVEHtlnEKRILQ--AINF---PFLVKLEYSFK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd14209  72 DNSNLYMVMEYVPGGEMFSHLRRI--GRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SLKkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEV 255
Cdd:cd14209 150 RVK------------------------------------------------------------GRTWTLCGTPEYLAPEI 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEF-AGKPNDLTDLIRRLLVKDPNRRLGCHR-GAA 333
Cdd:cd14209 170 ILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFpSHFSSDLKDLLRNLLQVDLTKRFGNLKnGVN 249
                       330       340
                ....*....|....*....|....*..
gi 15232374 334 EIKELAFFAGVRW-DLLTEVLRPPFIP 359
Cdd:cd14209 250 DIKNHKWFATTDWiAIYQRKVEAPFIP 276
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
85-359 1.85e-42

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: 150.28  E-value: 1.85e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  85 PFLPRLLASFESPEYFAWAVPYCSGGDLNvlLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG 164
Cdd:cd05606  58 PFIVCMTYAFQTPDKLCFILDLMNGGDLH--YHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHG 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 165 HVTLTDFDLSRSLKKPlRPHfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnSF 244
Cdd:cd05606 136 HVRISDLGLACDFSKK-KPH----------------------------------------------------------AS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 245 VGTDEYVSPEVI-RGDGHDFAVDWWALGVLTYEMMYGETPF---KGKSKKETFRNVLMKEPEFAGK-PNDLTDLIRRLLV 319
Cdd:cd05606 157 VGTHGYMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPFrqhKTKDKHEIDRMTLTMNVELPDSfSPELKSLLEGLLQ 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15232374 320 KDPNRRLGCH-RGAAEIKELAFFAGVRWDLLTEV-LRPPFIP 359
Cdd:cd05606 237 RDVSKRLGCLgRGATEVKEHPFFKGVDWQQVYLQkYPPPLIP 278
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
18-389 1.05e-41

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 150.59  E-value: 1.05e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  18 LDSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARwEIEVLRRLSVDSNqNPFLPRLLASFESP 97
Cdd:cd05627   1 LDDFESLKVIGRGAFGEVRL----VQKKDTGHIYAMKILRKADMLEKEQVA-HIRAERDILVEAD-GAWVVKMFYSFQDK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQNdgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd05627  75 RNLYLIMEFLPGGDMMTLLMKKD--TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 KKPLRPHFYqpdpeliidrkksRSFSRliSPTAEKNKTGLKKTRSARVNPINRRKTSFSSgersnsfVGTDEYVSPEVIR 257
Cdd:cd05627 153 KKAHRTEFY-------------RNLTH--NPPSDFSFQNMNSKRKAETWKKNRRQLAYST-------VGTPDYIAPEVFM 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKP-----NDLTDLIRRLLVkDPNRRLGcHRGA 332
Cdd:cd05627 211 QTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMNWKETLVFPPevpisEKAKDLILRFCT-DAENRIG-SNGV 288
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 333 AEIKELAFFAGVRWDLLTEvlRPPFIPLRDDGELTVGGFDIREHFEKLRTTPSSAPP 389
Cdd:cd05627 289 EEIKSHPFFEGVDWEHIRE--RPAAIPIEIKSIDDTSNFDDFPESDILQPAPNTTEP 343
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
24-389 2.37e-41

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: 148.61  E-value: 2.37e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASSLRRARWEIeVLRRLSVDSNQNPFLPRLLASFESPEYFAWA 103
Cdd:cd05616   5 LMVLGKGSFGKVMLAE----RKGTDELYAVKILKKDVVIQDDDVECTM-VEKRVLALSGKPPFLTQLHSCFQTMDRLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplrp 183
Cdd:cd05616  80 MEYVNGGDL--MYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK-------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpELIIDrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd05616 150 -------ENIWD------------------------------------------GVTTKTFCGTPDYIAPEIIAYQPYGK 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL---MKEPEFAGKpnDLTDLIRRLLVKDPNRRLGCH-RGAAEIKELA 339
Cdd:cd05616 181 SVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMehnVAYPKSMSK--EAVAICKGLMTKHPGKRLGCGpEGERDIKEHA 258
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232374 340 FFAGVRWDLLT-EVLRPPFIPLRDDGEltvggfdiREHFEKL--RTTPSSAPP 389
Cdd:cd05616 259 FFRYIDWEKLErKEIQPPYKPKACGRN--------AENFDRFftRHPPVLTPP 303
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
18-359 5.73e-41

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: 148.64  E-value: 5.73e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  18 LDSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKS---SASSLRRARWEIEVLRrlsvdSNQNPFLPRLLASF 94
Cdd:cd05594  24 MNDFEYLKLLGKGTFGKVIL----VKEKATGRYYAMKILKKEvivAKDEVAHTLTENRVLQ-----NSRHPFLTALKYSF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHT-MGIAYRDLKPENILIQQSGHVTLTDFDL 173
Cdd:cd05594  95 QTHDRLCFVMEYANGGEL--FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SrslkkplrphfyqpdpeliidrkksrsfsrlisptaeknKTGLKktrsarvnpinrrktsfsSGERSNSFVGTDEYVSP 253
Cdd:cd05594 173 C---------------------------------------KEGIK------------------DGATMKTFCGTPEYLAP 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFagkPNDLT----DLIRRLLVKDPNRRL-GC 328
Cdd:cd05594 196 EVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRF---PRTLSpeakSLLSGLLKKDPKQRLgGG 272
                       330       340       350
                ....*....|....*....|....*....|..
gi 15232374 329 HRGAAEIKELAFFAGVRW-DLLTEVLRPPFIP 359
Cdd:cd05594 273 PDDAKEIMQHKFFAGIVWqDVYEKKLVPPFKP 304
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
20-359 6.05e-41

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: 146.71  E-value: 6.05e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  20 SIKALKILGKGATGTVFLAH-DVVSTSSSSSPFAVKLVPKSSASSLrrARWEIEVLRRLSvdsnqNPFLPRLLASFESPE 98
Cdd:cd05630   1 TFRQYRVLGKGGFGEVCACQvRATGKMYACKKLEKKRIKKRKGEAM--ALNEKQILEKVN-----SRFVVSLAYAYETKD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslk 178
Cdd:cd05630  74 ALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kplrphFYQPDPELIIDRkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRG 258
Cdd:cd05630 150 ------VHVPEGQTIKGR------------------------------------------------VGTVGYMAPEVVKN 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 259 DGHDFAVDWWALGVLTYEMMYGETPFKGKSKK----ETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRLGCH-RGA 332
Cdd:cd05630 176 ERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKikreEVERLVKEVPEEYSEKfSPQARSLCSMLLCKDPAERLGCRgGGA 255
                       330       340
                ....*....|....*....|....*...
gi 15232374 333 AEIKELAFFAGVRWDLLTE-VLRPPFIP 359
Cdd:cd05630 256 REVKEHPLFKKLNFKRLGAgMLEPPFKP 283
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
16-384 1.40e-40

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: 147.87  E-value: 1.40e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARWeIEVLRRLSVDSNQNPFLPRLLASFE 95
Cdd:cd05618  17 LGLQDFDLLRVIGRGSYAKVLL----VRLKKTERIYAMKVVKKELVNDDEDIDW-VQTEKHVFEQASNHPFLVGLHSCFQ 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSr 175
Cdd:cd05618  92 TESRLFFVIEYVNGGDL--MFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMC- 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slKKPLRPhfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEV 255
Cdd:cd05618 169 --KEGLRP------------------------------------------------------GDTTSTFCGTPNYIAPEI 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFK--GKSKKET-------FRNVLMKEPEFagkPNDLT----DLIRRLLVKDP 322
Cdd:cd05618 193 LRGEDYGFSVDWWALGVLMFEMMAGRSPFDivGSSDNPDqntedylFQVILEKQIRI---PRSLSvkaaSVLKSFLNKDP 269
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 323 NRRLGCH--RGAAEIKELAFFAGVRWDLLTE-VLRPPFIPlRDDGELTVGGFDIREHFEKLRTTP 384
Cdd:cd05618 270 KERLGCHpqTGFADIQGHPFFRNVDWDLMEQkQVVPPFKP-NISGEFGLDNFDSQFTNEPVQLTP 333
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
25-384 3.67e-40

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: 145.64  E-value: 3.67e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARWeIEVLRRLSVDSNQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd05588   1 RVIGRGSYAKVLM----VELKKTKRIYAMKVIKKELVNDDEDIDW-VQTEKHVFETASNHPFLVGLHSCFQTESRLFFVI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslKKPLRPh 184
Cdd:cd05588  76 EFVNGGDL--MFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMC---KEGLRP- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 185 fyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGDGHDFA 264
Cdd:cd05588 150 -----------------------------------------------------GDTTSTFCGTPNYIAPEILRGEDYGFS 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 265 VDWWALGVLTYEMMYGETPFK--GKSKKET-------FRNVLMKEPEFagkPNDLT----DLIRRLLVKDPNRRLGCHR- 330
Cdd:cd05588 177 VDWWALGVLMFEMLAGRSPFDivGSSDNPDqntedylFQVILEKPIRI---PRSLSvkaaSVLKGFLNKNPAERLGCHPq 253
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 331 -GAAEIKELAFFAGVRWDLL-TEVLRPPFIPlRDDGELTVGGFDIREHFEKLRTTP 384
Cdd:cd05588 254 tGFADIQSHPFFRTIDWEQLeQKQVTPPYKP-RIESERDLENFDPQFTNEPVQLTP 308
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
24-359 4.65e-40

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 146.73  E-value: 4.65e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASsLRRARWEIEVLRRLSVDSNqNPFLPRLLASFESPEYFAWA 103
Cdd:cd05625   6 IKTLGIGAFGEVCLARKV----DTKALYATKTLRKKDVL-LRNQVAHVKAERDILAEAD-NEWVVRLYYSFQDKDNLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLRP 183
Cdd:cd05625  80 MDYIPGGDMMSLLIRM--GVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 HFYQPDPELiidRKKSRSFSrlisptaekNKTGLKKTRSA--RVNPINRRKTSFSSGERSNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd05625 158 KYYQSGDHL---RQDSMDFS---------NEWGDPENCRCgdRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGY 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRlLVKDPNRRLGcHRGAAEIK 336
Cdd:cd05625 226 TQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVInwqtsLHIPPQAKLSPEASDLIIK-LCRGPEDRLG-KNGADEIK 303
                       330       340
                ....*....|....*....|...
gi 15232374 337 ELAFFAGVRWDLLTEVLRPPFIP 359
Cdd:cd05625 304 AHPFFKTIDFSSDLRQQSAPYIP 326
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
19-359 6.51e-40

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: 144.73  E-value: 6.51e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAH-DVVSTSSSSSPFAVKLVPKSSASSLrrARWEIEVLRRLSvdsnqNPFLPRLLASFESP 97
Cdd:cd05632   2 NTFRQYRVLGKGGFGEVCACQvRATGKMYACKRLEKKRIKKRKGESM--ALNEKQILEKVN-----SQFVVNLAYAYETK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd05632  75 DALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqPDPELIIDRkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIR 257
Cdd:cd05632 155 ----------PEGESIRGR------------------------------------------------VGTVGYMAPEVLN 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKK----ETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRLGCHR-G 331
Cdd:cd05632 177 NQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKvkreEVDRRVLETEEVYSAKfSEEAKSICKMLLTKDPKQRLGCQEeG 256
                       330       340
                ....*....|....*....|....*....
gi 15232374 332 AAEIKELAFFAGVRWDLLTE-VLRPPFIP 359
Cdd:cd05632 257 AGEVKRHPFFRNMNFKRLEAgMLDPPFVP 285
Pkinase pfam00069
Protein kinase domain;
24-329 3.14e-39

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 139.69  E-value: 3.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASS--LRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:pfam00069   4 LRKLGSGSFGTVYKAKHR----DTGKIVAIKKIKKEKIKKkkDKNILREIKILKKL-----NHPNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   102 WAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMgiayrdlkpeniliqqsghvtltdfdlsrslkkpl 181
Cdd:pfam00069  75 LVLEYVEGGSLFDLLSEK--GAFSEREAKFIMKQILEGLESGSSL----------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGDGH 261
Cdd:pfam00069 118 ------------------------------------------------------------TTFVGTPWYMAPEVLGGNPY 137
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374   262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN----DLTDLIRRLLVKDPNRRLGCH 329
Cdd:pfam00069 138 GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSnlseEAKDLLKKLLKKDPSKRLTAT 209
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
17-392 3.31e-39

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: 143.60  E-value: 3.31e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  17 DLDSIKA-----LKILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASSLRRARWEIeVLRRLSVDSNQNPFLPRLL 91
Cdd:cd05615   3 NLDRVRLtdfnfLMVLGKGSFGKVMLAE----RKGSDELYAIKILKKDVVIQDDDVECTM-VEKRVLALQDKPPFLTQLH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  92 ASFESPEYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:cd05615  78 SCFQTVDRLYFVMEYVNGGDL--MYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 172 DLSRslkkplrphfyqpdpELIIDrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYV 251
Cdd:cd05615 156 GMCK---------------EHMVE------------------------------------------GVTTRTFCGTPDYI 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 252 SPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRLGC-H 329
Cdd:cd05615 179 APEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSlSKEAVSICKGLMTKHPAKRLGCgP 258
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 330 RGAAEIKELAFFAGVRWD-LLTEVLRPPFIPlrddgelTVGGFDIrEHFEKL--RTTPSSAPPSPL 392
Cdd:cd05615 259 EGERDIREHAFFRRIDWDkLENREIQPPFKP-------KVCGKGA-ENFDKFftRGQPVLTPPDQL 316
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
22-325 3.50e-39

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: 141.06  E-value: 3.50e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVvstsSSSSPFAVKLVP--KSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEY 99
Cdd:cd08215   3 EKIRVIGKGSFGSAYLVRRK----SDGKLYVLKEIDlsNMSEKEREEALNEVKLLSKL-----KHPNIVKYYESFEENGK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQNDGV--FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd08215  74 LCIVMEYADGGDLAQKIKKQKKKGqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrkksrsfsrliSPTAEKNKTglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIR 257
Cdd:cd08215 154 -----------------------------ESTTDLAKT----------------------------VVGTPYYLSPELCE 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEfagkP------NDLTDLIRRLLVKDPNRR 325
Cdd:cd08215 177 NKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYP----PipsqysSELRDLVNSMLQKDPEKR 246
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
83-359 3.86e-39

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 141.67  E-value: 3.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  83 QNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQ 162
Cdd:cd05631  58 NSRFVVSLAYAYETKDALCLVLTIMNGGDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDD 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 163 SGHVTLTDFDLSRSLkkplrphfyqpdPEliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSN 242
Cdd:cd05631 138 RGHIRISDLGLAVQI------------PE----------------------------------------------GETVR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 243 SFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKK----ETFRNVLMKEPEFAGK-PNDLTDLIRRL 317
Cdd:cd05631 160 GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERvkreEVDRRVKEDQEEYSEKfSEDAKSICRML 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15232374 318 LVKDPNRRLGCH-RGAAEIKELAFFAGVRWDLL-TEVLRPPFIP 359
Cdd:cd05631 240 LTKNPKERLGCRgNGAAGVKQHPIFKNINFKRLeANMLEPPFCP 283
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
19-360 6.09e-39

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 143.64  E-value: 6.09e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKssASSLRRAR-WEIEVLRRLSVDSNqNPFLPRLLASFESP 97
Cdd:cd05628   1 EDFESLKVIGRGAFGEVRL----VQKKDTGHVYAMKILRK--ADMLEKEQvGHIRAERDILVEAD-SLWVVKMFYSFQDK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQNdgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd05628  74 LNLYLIMEFLPGGDMMTLLMKKD--TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 KKPLRPHFYqpdpeliidRKKSRSfsrLISPTAEKNktgLKKTRSARVNPINRRKTSFSSgersnsfVGTDEYVSPEVIR 257
Cdd:cd05628 152 KKAHRTEFY---------RNLNHS---LPSDFTFQN---MNSKRKAETWKRNRRQLAFST-------VGTPDYIAPEVFM 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKP-----NDLTDLIRRLLVkDPNRRLGChRGA 332
Cdd:cd05628 210 QTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLIFPPevpisEKAKDLILRFCC-EWEHRIGA-PGV 287
                       330       340
                ....*....|....*....|....*...
gi 15232374 333 AEIKELAFFAGVRWDLLTEvlRPPFIPL 360
Cdd:cd05628 288 EEIKTNPFFEGVDWEHIRE--RPAAIPI 313
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
24-325 7.38e-38

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: 137.33  E-value: 7.38e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSssssPFAVKLVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYfAWA 103
Cdd:cd05122   5 LEKIGKGGFGVVYKARHKKTGQ----IVAIKKINLESKEKKESILNEIAILKKC-----KHPNIVKYYGSYLKKDE-LWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 V-PYCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplr 182
Cdd:cd05122  75 VmEFCSGGSLKDLL-KNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLS-------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrkTSFSSGERSNSFVGTDEYVSPEVIRGDGHD 262
Cdd:cd05122 146 --------------------------------------------------AQLSDGKTRNTFVGTPYWMAPEVIQGKPYG 175
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 263 FAVDWWALGVLTYEMMYGETPF-KGKSKKETFRNVLMKEPEFAGKPN---DLTDLIRRLLVKDPNRR 325
Cdd:cd05122 176 FKADIWSLGITAIEMAEGKPPYsELPPMKALFLIATNGPPGLRNPKKwskEFKDFLKKCLQKDPEKR 242
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
24-408 1.52e-37

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 139.05  E-value: 1.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSAssLRRAR----WEievLRRLSVDSNqNPFLPRLLASFESPEY 99
Cdd:cd05596  31 IKVIGRGAFGEVQL----VRHKSTKKVYAMKLLSKFEM--IKRSDsaffWE---ERDIMAHAN-SEWIVQLHYAFQDDKY 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDlsrslkk 179
Cdd:cd05596 101 LYMVMDYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFG------- 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptaeknkTGLKKTRSARVnpinrrktsfssgeRSNSFVGTDEYVSPEVIRGD 259
Cdd:cd05596 171 -----------------------------------TCMKMDKDGLV--------------RSDTAVGTPDYISPEVLKSQ 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 GHD----FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVkDPNRRLGcHR 330
Cdd:cd05596 202 GGDgvygRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMnhknsLQFPDDVEISKDAKSLICAFLT-DREVRLG-RN 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 331 GAAEIKELAFFAGVRWDLLTevLR---PPFIPlrddgELTvGGFDIR--EHFEKLRTTPSSAPPSPLRSPPHVcrkndPF 405
Cdd:cd05596 280 GIEEIKAHPFFKNDQWTWDN--IRetvPPVVP-----ELS-SDIDTSnfDDIEEDETPEETFPVPKAFVGNHL-----PF 346

                ...
gi 15232374 406 IEF 408
Cdd:cd05596 347 VGF 349
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
25-325 2.51e-37

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: 136.11  E-value: 2.51e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSssspFAVK--LVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAW 102
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGEL----MAVKevELSGDSEEELEALEREIRILSSL-----KHPNIVRYLGTERTENTLNI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlr 182
Cdd:cd06606  77 FLEYVPGGSLASLL--KKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEI-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDGHD 262
Cdd:cd06606 153 -----------------------------------------------------ATGEGTKSLRGTPYWMAPEVIRGEGYG 179
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 263 FAVDWWALGVLTYEMMYGETPFKGKSKKETfrnVLMK------EPEFagkPNDLT----DLIRRLLVKDPNRR 325
Cdd:cd06606 180 RAADIWSLGCTVIEMATGKPPWSELGNPVA---ALFKigssgePPPI---PEHLSeeakDFLRKCLQRDPKKR 246
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
16-390 4.42e-37

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: 139.37  E-value: 4.42e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVflahDVVSTSSSSSPFAVKLVPKSSAssLRRArwEIEVLR--RLSVDSNQNPFLPRLLAS 93
Cdd:cd05624  69 LHRDDFEIIKVIGRGAFGEV----AVVKMKNTERIYAMKILNKWEM--LKRA--ETACFReeRNVLVNGDCQWITTLHYA 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 FESPEYFAWAVPYCSGGDLNVLLHRQNDGVfSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDl 173
Cdd:cd05624 141 FQDENYLYLVMDYYVGGDLLTLLSKFEDKL-PEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFG- 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 srslkkplrphfyqpdpeliidrkksrsfsrlisptaeknkTGLKKTRSARVnpinrrktsfssgeRSNSFVGTDEYVSP 253
Cdd:cd05624 219 -----------------------------------------SCLKMNDDGTV--------------QSSVAVGTPDYISP 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVIRG--DG---HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAgKPNDLT-------DLIRRLLVKD 321
Cdd:cd05624 244 EILQAmeDGmgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQ-FPSHVTdvseeakDLIQRLICSR 322
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 322 pNRRLGCHrGAAEIKELAFFAGVRWDLLTEvLRPPFIPLRDDGELTvGGFDIREhfEKLRtTPSSAPPS 390
Cdd:cd05624 323 -ERRLGQN-GIEDFKKHAFFEGLNWENIRN-LEAPYIPDVSSPSDT-SNFDVDD--DVLR-NPEILPPS 384
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
24-359 8.32e-37

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 137.84  E-value: 8.32e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASSlRRARWEIEVLRRLSVDSNqNPFLPRLLASFESPEYFAWA 103
Cdd:cd05626   6 IKTLGIGAFGEVCLACKV----DTHALYAMKTLRKKDVLN-RNQVAHVKAERDILAEAD-NEWVVKLYYSFQDKDNLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLRP 183
Cdd:cd05626  80 MDYIPGGDMMSLLIRM--EVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWTHNS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 HFYQPDPELIIDRKKSRSFSRLISptaeKNKTGlkktrsARVNPINRRKTSFSSGERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd05626 158 KYYQKGSHIRQDSMEPSDLWDDVS----NCRCG------DRLKTLEQRATKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQ 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKKET------FRNVLMKEPEFAGKPnDLTDLIRRLLVKdPNRRLGcHRGAAEIKE 337
Cdd:cd05626 228 LCDWWSVGVILFEMLVGQPPFLAPTPTETqlkvinWENTLHIPPQVKLSP-EAVDLITKLCCS-AEERLG-RNGADDIKA 304
                       330       340
                ....*....|....*....|....
gi 15232374 338 LAFFAGVrwDLLTEVLR--PPFIP 359
Cdd:cd05626 305 HPFFSEV--DFSSDIRTqpAPYVP 326
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
25-341 9.38e-37

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: 134.60  E-value: 9.38e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSAS---SLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd14099   7 KFLGKGGFAKCYEVTDM----STGKVYAGKVVPKSSLTkpkQREKLKSEIKIHRSL-----KHPNIVKFHDCFEDEENVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPl 181
Cdd:cd14099  78 ILLELCSNGSLMELLKRR--KALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYD- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGD-G 260
Cdd:cd14099 155 --------------------------------------------------------GERKKTLCGTPNYIAPEVLEKKkG 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE---PEFAGKPNDLTDLIRRLLVKDPNRRLgchrGAAEIKE 337
Cdd:cd14099 179 HSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEysfPSHLSISDEAKDLIRSMLQPDPTKRP----SLDEILS 254

                ....
gi 15232374 338 LAFF 341
Cdd:cd14099 255 HPFF 258
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
51-326 3.76e-36

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: 132.78  E-value: 3.76e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSsASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDL-NVLLHRqndGVFSSSVI 129
Cdd:cd14006  21 FAAKFIPKR-DKKKEAVLREISILNQL-----QHPRIIQLHEAYESPTELVLILELCSGGELlDRLAER---GSLSEEEV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 130 RFYVAEIVCALEHLHTMGIAYRDLKPENILIQ--QSGHVTLTDFDLSRSLKKplrphfyqpdpeliidrkksrsfsrlis 207
Cdd:cd14006  92 RTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLNP---------------------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 208 ptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGK 287
Cdd:cd14006 144 ------------------------------GEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGE 193
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15232374 288 SKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14006 194 DDQETLANISacrvdFSEEYFSSVSQEAKDFIRKLLVKEPRKRP 237
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
27-337 9.97e-36

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: 131.91  E-value: 9.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASSLRRARW--------------EIEVLRRLsvdsnQNPFLPRLLA 92
Cdd:cd14008   1 LGRGSFGKVKLALDT----ETGQLYAIKIFNKSRLRKRREGKNdrgkiknalddvrrEIAIMKKL-----DHPNIVRLYE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  93 SFESPE----YFAwaVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTL 168
Cdd:cd14008  72 VIDDPEsdklYLV--LEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 169 TDFDLSRSLkkplrphfyqpdpeliidrkksrsfsrlisptaEKNKTGLKKTrsarvnpinrrktsfssgersnsfVGTD 248
Cdd:cd14008 150 SDFGVSEMF---------------------------------EDGNDTLQKT------------------------AGTP 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 249 EYVSPEVIRGDG---HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN---DLTDLIRRLLVKDP 322
Cdd:cd14008 173 AFLAPELCDGDSktySGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPPElspELKDLLRRMLEKDP 252
                       330
                ....*....|....*
gi 15232374 323 NRRLgchrGAAEIKE 337
Cdd:cd14008 253 EKRI----TLKEIKE 263
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
89-327 3.36e-35

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: 130.88  E-value: 3.36e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  89 RLLASFESP---EYFAW---------AVPYCSGGDLNVLLhRQnDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPE 156
Cdd:cd14010  46 RLTHELKHPnvlKFYEWyetsnhlwlVVEYCTGGDLETLL-RQ-DGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPS 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 157 NILIQQSGHVTLTDFDLSR----SLKKPLRPhfyqpdpeliidrkksrsfsrlisPTAEKNKTGLKKTRSARvnpinrrk 232
Cdd:cd14010 124 NILLDGNGTLKLSDFGLARregeILKELFGQ------------------------FSDEGNVNKVSKKQAKR-------- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 233 tsfssgersnsfvGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEP-----EFAGKP 307
Cdd:cd14010 172 -------------GTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPpppppKVSSKP 238
                       250       260
                ....*....|....*....|.
gi 15232374 308 N-DLTDLIRRLLVKDPNRRLG 327
Cdd:cd14010 239 SpDFKSLLKGLLEKDPAKRLS 259
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
79-373 1.52e-34

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: 130.55  E-value: 1.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  79 VDSNQNPFLPRLLASFESPEYFAWAVPYCSGGDLNvlLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENI 158
Cdd:cd14223  57 VSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLH--YHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANI 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 159 LIQQSGHVTLTDFDLSRSLKKPlRPHfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssg 238
Cdd:cd14223 135 LLDEFGHVRISDLGLACDFSKK-KPH------------------------------------------------------ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 239 ersnSFVGTDEYVSPEVI-RGDGHDFAVDWWALGVLTYEMMYGETPF---KGKSKKETFRNVLMKEPEFAGK-PNDLTDL 313
Cdd:cd14223 160 ----ASVGTHGYMAPEVLqKGVAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTMAVELPDSfSPELRSL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 314 IRRLLVKDPNRRLGC-HRGAAEIKELAFFAGVRWDLL-TEVLRPPFIPLRddGELTVG-GFDI 373
Cdd:cd14223 236 LEGLLQRDVNRRLGCmGRGAQEVKEEPFFRGLDWQMVfLQKYPPPLIPPR--GEVNAAdAFDI 296
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
79-373 2.51e-34

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: 130.57  E-value: 2.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  79 VDSNQNPFLPRLLASFESPEYFAWAVPYCSGGDLNvlLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENI 158
Cdd:cd05633  62 VSTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLH--YHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANI 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 159 LIQQSGHVTLTDFDLSRSLKKPlRPHfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssg 238
Cdd:cd05633 140 LLDEHGHVRISDLGLACDFSKK-KPH------------------------------------------------------ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 239 ersnSFVGTDEYVSPEVI-RGDGHDFAVDWWALGVLTYEMMYGETPF---KGKSKKETFRNVLMKEPEFAGK-PNDLTDL 313
Cdd:cd05633 165 ----ASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDSfSPELKSL 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 314 IRRLLVKDPNRRLGCHRGAA-EIKELAFFAGVRWD-LLTEVLRPPFIPLRddGELTVG-GFDI 373
Cdd:cd05633 241 LEGLLQRDVSKRLGCHGRGAqEVKEHSFFKGIDWQqVYLQKYPPPLIPPR--GEVNAAdAFDI 301
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
24-359 3.47e-32

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: 123.09  E-value: 3.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFlahdVVSTSSSSSPFAVKLVPKS---SASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYF 100
Cdd:cd05607   7 FRVLGKGGFGEVC----AVQVKNTGQMYACKKLDKKrlkKKSGEKMALLEKEILEKVN-----SPFIVSLAYAFETKTHL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNV-LLHRQNDGVFSSSVIrFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKK 179
Cdd:cd05607  78 CLVMSLMNGGDLKYhIYNVGERGIEMERVI-FYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 PlrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvNPINRRktsfssgersnsfVGTDEYVSPEVIRGD 259
Cdd:cd05607 157 G---------------------------------------------KPITQR-------------AGTNGYMAPEILKEE 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPFKGK----SKKETFRNVLMKEPEFAgKPN---DLTDLIRRLLVKDPNRRLGCHRGA 332
Cdd:cd05607 179 SYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLEDEVKFE-HQNfteEAKDICRLFLAKKPENRLGSRTND 257
                       330       340
                ....*....|....*....|....*...
gi 15232374 333 AEIKELAFFAGVRWDLL-TEVLRPPFIP 359
Cdd:cd05607 258 DDPRKHEFFKSINFPRLeAGLIDPPFVP 285
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
27-329 4.97e-32

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: 121.56  E-value: 4.97e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd14103   1 LGRGKFGTVYR----CVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQL-----RHPRLLQLYDAFETPREMVLVMEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDLnvlLHR--QNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENIL-IQQSGH-VTLTDFDLSRslkkplr 182
Cdd:cd14103  72 VAGGEL---FERvvDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLAR------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phFYQPDPELiidrkksrsfsrlisptaeknktglkktrsaRVNpinrrktsfssgersnsfVGTDEYVSPEVIRGDGHD 262
Cdd:cd14103 142 --KYDPDKKL-------------------------------KVL------------------FGTPEFVAPEVVNYEPIS 170
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 263 FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLM-----KEPEFAGKPNDLTDLIRRLLVKDPNRRLGCH 329
Cdd:cd14103 171 YATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRakwdfDDEAFDDISDEAKDFISKLLVKDPRKRMSAA 242
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
16-408 2.78e-31

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: 123.20  E-value: 2.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVflahDVVSTSSSSSPFAVKLVPKSSAssLRRA-----RWEIEVLrrLSVDSNqnpFLPRL 90
Cdd:cd05623  69 LHKEDFEILKVIGRGAFGEV----AVVKLKNADKVFAMKILNKWEM--LKRAetacfREERDVL--VNGDSQ---WITTL 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  91 LASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVfSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTD 170
Cdd:cd05623 138 HYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRL-PEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLAD 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 171 FDlsrslkkplrphfyqpdpeliidrkksrsfsrlisptaeknkTGLKKTRSARVnpinrrktsfssgeRSNSFVGTDEY 250
Cdd:cd05623 217 FG------------------------------------------SCLKLMEDGTV--------------QSSVAVGTPDY 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 251 VSPEVIRG--DG---HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEF------AGKPNDLTDLIRRLLV 319
Cdd:cd05623 241 ISPEILQAmeDGkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFqfptqvTDVSENAKDLIRRLIC 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 320 KDpNRRLGcHRGAAEIKELAFFAGVRWDLLTEVlRPPFIPlRDDGELTVGGFDIREhfEKLRTTPSSAPPSPLRSPPHvc 399
Cdd:cd05623 321 SR-EHRLG-QNGIEDFKNHPFFVGIDWDNIRNC-EAPYIP-EVSSPTDTSNFDVDD--DCLKNCETMPPPTHTAFSGH-- 392

                ....*....
gi 15232374 400 rkNDPFIEF 408
Cdd:cd05623 393 --HLPFVGF 399
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
19-359 2.42e-30

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: 118.06  E-value: 2.42e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHdvvsTSSSSSPFAVKLVPKSSASslRRARWEIEVLRRLSVDSNQNPFLPRLLASFESPE 98
Cdd:cd05608   1 DWFLDFRVLGKGGFGEVSACQ----MRATGKLYACKKLNKKRLK--KRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLNVLLHR--QNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd05608  75 DLCLVMTIMNGGDLRYHIYNvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LKkplrphfyqpdpeliidrkksrsfsrlisptAEKNKTglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVI 256
Cdd:cd05608 155 LK-------------------------------DGQTKT--------------------------KGYAGTPGFMAPELL 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGK----SKKETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRLGCHRG 331
Cdd:cd05608 178 LGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSEKfSPASKSICEALLAKDPEKRLGFRDG 257
                       330       340       350
                ....*....|....*....|....*....|
gi 15232374 332 A-AEIKELAFFAGVRW-DLLTEVLRPPFIP 359
Cdd:cd05608 258 NcDGLRTHPFFRDINWrKLEAGILPPPFVP 287
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
24-325 8.55e-30

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: 115.74  E-value: 8.55e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSSSspFAVKLVPKSSASS------LRRarwEIEVLRRLsvdsnQNPFLPRLLASFESP 97
Cdd:cd14080   5 GKTIGEGSYSKVKLAEYTKSGLKEK--VACKIIDKKKAPKdflekfLPR---ELEILRKL-----RHPNIIQVYSIFERG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrsl 177
Cdd:cd14080  75 SKVFIFMEYAEHGDL--LEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDF------ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrkksrSFSRLISPTaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIR 257
Cdd:cd14080 147 -----------------------GFARLCPDD--------------------------DGDVLSKTFCGSAAYAAPEILQ 177
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 258 GDGHD-FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPNDLT----DLIRRLLVKDPNRR 325
Cdd:cd14080 178 GIPYDpKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSVKKLSpeckDLIDQLLEPDPTKR 250
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
27-325 4.65e-29

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: 113.40  E-value: 4.65e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLA----HDVvstssssspfAVKL--VPKSSASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYF 100
Cdd:cd13999   1 IGSGSFGEVYKGkwrgTDV----------AIKKlkVEDDNDELLKEFRREVSILSKLR-----HPNIVQFIGACLSPPPL 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVLLHRQNdGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkp 180
Cdd:cd13999  66 CIVTEYMPGGSLYDLLHKKK-IPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSR----- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaEKNKTGLKKTrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIRGDG 260
Cdd:cd13999 140 ------------------------------IKNSTTEKMT----------------------GVVGTPRWMAPEVLRGEP 167
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPE---FAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd13999 168 YTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRppiPPDCPPELSKLIKRCWNEDPEKR 235
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
51-326 5.91e-29

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: 113.99  E-value: 5.91e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPK--SSASSLRRARWEIEVLRrLSVDsnqNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLhrQNDGVFSSSV 128
Cdd:cd14106  36 YAAKFLRKrrRGQDCRNEILHEIAVLE-LCKD---CPRVVNLHEVYETRSELILILELAAGGELQTLL--DEEECLTEAD 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQS---GHVTLTDFDLSRSLKKplrphfyqpdpeliidrkksrsfsrl 205
Cdd:cd14106 110 VRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFGISRVIGE-------------------------- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 206 isptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFK 285
Cdd:cd14106 164 --------------------------------GEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFG 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15232374 286 GKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14106 212 GDDKQETFLNISqcnldFPEELFKDVSPLAIDFIKRLLVKDPEKRL 257
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
24-325 1.94e-28

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: 112.18  E-value: 1.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRA----RWEIEVLRRLsvdsnQNPFLPRLLASFESPEY 99
Cdd:cd14098   5 IDRLGSGTFAEVKKAVEVETGKM----RAIKQIVKRKVAGNDKNlqlfQREINILKSL-----EHPGIVRLIDWYEDDQH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG--HVTLTDFdlsrsl 177
Cdd:cd14098  76 IYLVMEYVEGGDLMDFI--MAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDF------ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrkksrsfsrlisptaeknktGLKKTrsarvnpinrrktsFSSGERSNSFVGTDEYVSPEVIR 257
Cdd:cd14098 148 --------------------------------------GLAKV--------------IHTGTFLVTFCGTMAYLAPEILM 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 258 G------DGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRnvLMKEPEFAGKP-NDLT------DLIRRLLVKDPNR 324
Cdd:cd14098 176 SkeqnlqGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEK--RIRKGRYTQPPlVDFNiseeaiDFILRLLDVDPEK 253

                .
gi 15232374 325 R 325
Cdd:cd14098 254 R 254
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
19-363 4.34e-28

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: 114.33  E-value: 4.34e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSAssLRRAR----WEievlRRLSVDSNQNPFLPRLLASF 94
Cdd:cd05622  73 EDYEVVKVIGRGAFGEVQL----VRHKSTRKVYAMKLLSKFEM--IKRSDsaffWE----ERDIMAFANSPWVVQLFYAF 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEYFAWAVPYCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDls 174
Cdd:cd05622 143 QDDRYLYMVMEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-- 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 rslkkplrphfyqpdpeliidrkksrsfsrlisptaeknkTGLKKTRSARVnpinrrktsfssgeRSNSFVGTDEYVSPE 254
Cdd:cd05622 218 ----------------------------------------TCMKMNKEGMV--------------RCDTAVGTPDYISPE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 255 VIRGDGHD----FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVkDPNRR 325
Cdd:cd05622 244 VLKSQGGDgyygRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhknsLTFPDDNDISKEAKNLICAFLT-DREVR 322
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15232374 326 LGcHRGAAEIKELAFFAGVRWDLltEVLRPPFIPLRDD 363
Cdd:cd05622 323 LG-RNGVEEIKRHLFFKNDQWAW--ETLRDTVAPVVPD 357
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
20-325 6.09e-28

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: 110.90  E-value: 6.09e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  20 SIKALKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSL-------RRARWEIEVLRRLSvdsnQNPFLPRLLA 92
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLRTGRK----YAIKCLYKSGPNSKdgndfqkLPQLREIDLHRRVS----RHPNIITLHD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  93 SFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI-QQSGHVTLTDF 171
Cdd:cd13993  73 VFETEVAIYIVLEYCPNGDLFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLsQDEGTVKLCDF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 172 DLSrslkkplrphfyqpdpeliIDRKKSRSFSrlisptaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYV 251
Cdd:cd13993 153 GLA-------------------TTEKISMDFG-----------------------------------------VGSEFYM 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 252 SPEVIRGDGHDF------AVDWWALGVLTYEMMYGETPFKGKSKKE-TFRNVLMKEPEFAGK----PNDLTDLIRRLLVK 320
Cdd:cd13993 173 APECFDEVGRSLkgypcaAGDIWSLGIILLNLTFGRNPWKIASESDpIFYDYYLNSPNLFDVilpmSDDFYNLLRQIFTV 252

                ....*
gi 15232374 321 DPNRR 325
Cdd:cd13993 253 NPNNR 257
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
27-327 6.16e-28

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: 110.39  E-value: 6.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSssssPFAVKLVPKS--SASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGE----VVAIKEISRKklNKKLQENLESEIAILKSI-----KHPNIVRLYDVQKTEDFIYLVL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHvtltdfdlsrslkkplrph 184
Cdd:cd14009  72 EYCAGGDLSQYIRKR--GRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGD------------------- 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 185 fyqpDPEL-IIDrkksRSFSRLISPtaeknkTGLKKTrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd14009 131 ----DPVLkIAD----FGFARSLQP------ASMAET-----------------------LCGSPLYMAPEILQFQKYDA 173
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNV--LMKEPEFAGKPN---DLTDLIRRLLVKDPNRRLG 327
Cdd:cd14009 174 KADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIerSDAVIPFPIAAQlspDCKDLLRRLLRRDPAERIS 242
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
24-325 6.10e-27

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: 107.86  E-value: 6.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASS---LRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYF 100
Cdd:cd14073   6 LETLGKGTYGKVKLAIE----RATGREVAIKSIKKDKIEDeqdMVRIRREIEIMSSL-----NHPHIIRIYEVFENKDKI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkp 180
Cdd:cd14073  77 VIVMEYASGGELYDYI--SERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLS------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaekNKtglkktrsarvnpinrrktsFSSGERSNSFVGTDEYVSPEVIRGDG 260
Cdd:cd14073 149 --------------------------------NL--------------------YSKDKLLQTFCGSPLYASPEIVNGTP 176
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 261 -HDFAVDWWALGVLTYEMMYGETPFKG---KSKKETFRNVLMKEPEfagKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14073 177 yQGPEVDCWSLGVLLYTLVYGTMPFDGsdfKRLVKQISSGDYREPT---QPSDASGLIRWMLTVNPKRR 242
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
52-328 1.23e-26

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: 106.95  E-value: 1.23e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLVPKS--SASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGgDLNVLLhrQNDGVFSSSVI 129
Cdd:cd14002  30 ALKFIPKRgkSEKELRNLRQEIEILRKLN-----HPNIIEMLDSFETKKEFVVVTEYAQG-ELFQIL--EDDGTLPEEEV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 130 RFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfyqpdpeliidrkksrSFSRLISpt 209
Cdd:cd14002 102 RSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAM-----------------------SCNTLVL-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 210 aeknkTGLKktrsarvnpinrrktsfssgersnsfvGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSk 289
Cdd:cd14002 157 -----TSIK---------------------------GTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNS- 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15232374 290 keTFRNVLM--KEPEFAGKP--NDLTDLIRRLLVKDPNRRLGC 328
Cdd:cd14002 204 --IYQLVQMivKDPVKWPSNmsPEFKSFLQGLLNKDPSKRLSW 244
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
24-359 1.76e-26

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 108.53  E-value: 1.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   24 LKILGKGATGTVFLAHdvvSTSSSSSPFAVKLVPKSSAssLRRARWEIEVLRRLSVDSNQNPFLPRLLASFESPEYFAWA 103
Cdd:PTZ00426  35 IRTLGTGSFGRVILAT---YKNEDFPPVAIKRFEKSKI--IKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  104 VPYCSGGDLNVLLHRQNDgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplrp 183
Cdd:PTZ00426 110 LEFVIGGEFFTFLRRNKR--FPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAK-------- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  184 hfyqpdpelIIDrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:PTZ00426 180 ---------VVD-------------------------------------------TRTYTLCGTPEYIAPEILLNVGHGK 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL---MKEPEFAGkpNDLTDLIRRLLVKDPNRRLG-CHRGAAEIKELA 339
Cdd:PTZ00426 208 AADWWTLGIFIYEILVGCPPFYANEPLLIYQKILegiIYFPKFLD--NNCKHLMKKLLSHDLTKRYGnLKKGAQNVKEHP 285
                        330       340
                 ....*....|....*....|.
gi 15232374  340 FFAGVRW-DLLTEVLRPPFIP 359
Cdd:PTZ00426 286 WFGNIDWvSLLHKNVEVPYKP 306
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
22-329 2.53e-26

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: 106.16  E-value: 2.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSSsspfAVKLVpKSSASSLRRARWEIEVLRRLSvDSNQNPFLPRLLASFESPE--Y 99
Cdd:cd05118   2 EVLRKIGEGAFGTVWLARDKVTGEKV----AIKKI-KNDFRHPKAALREIKLLKHLN-DVEGHPNIVKLLDVFEHRGgnH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCsGGDLNVLLHRQNDGvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI-QQSGHVTLTDFDLSRSLK 178
Cdd:cd05118  76 LCLVFELM-GMNLYELIKDYPRG-LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILInLELGQLKLADFGLARSFT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kplrPHFYqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRG 258
Cdd:cd05118 154 ----SPPY-------------------------------------------------------TPYVATRWYRAPEVLLG 174
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 259 DGH-DFAVDWWALGVLTYEMMYGETPFKGKSKKETfrnvLMKEPEFAGkPNDLTDLIRRLLVKDPNRRLGCH 329
Cdd:cd05118 175 AKPyGSSIDIWSLGCILAELLTGRPLFPGDSEVDQ----LAKIVRLLG-TPEALDLLSKMLKYDPAKRITAS 241
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
25-341 3.73e-26

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: 105.80  E-value: 3.73e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLA-HDVVSTSSssspfAVKLVPKSSA---SSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYF 100
Cdd:cd14081   7 KTLGKGQTGLVKLAkHCVTGQKV-----AIKIVNKEKLskeSVLMKVEREIAIMKLI-----EHPNVLKLYDVYENKKYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDL-NVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkk 179
Cdd:cd14081  77 YLVLEYVSGGELfDYLVKK---GRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfYQPDpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGD 259
Cdd:cd14081 150 ------LQPE------------------------------------------------GSLLETSCGSPHYACPEVIKGE 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 GHD-FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE---PEFAgkPNDLTDLIRRLLVKDPNRRLGCHrgaaEI 335
Cdd:cd14081 176 KYDgRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVfhiPHFI--SPDAQDLLRRMLEVNPEKRITIE----EI 249

                ....*.
gi 15232374 336 KELAFF 341
Cdd:cd14081 250 KKHPWF 255
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
24-363 5.56e-26

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 108.16  E-value: 5.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSAssLRRAR----WEievlRRLSVDSNQNPFLPRLLASFESPEY 99
Cdd:cd05621  57 VKVIGRGAFGEVQL----VRHKASQKVYAMKLLSKFEM--IKRSDsaffWE----ERDIMAFANSPWVVQLFCAFQDDKY 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkk 179
Cdd:cd05621 127 LYMVMEYMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKM-- 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptaekNKTGLKKTRSArvnpinrrktsfssgersnsfVGTDEYVSPEVIRGD 259
Cdd:cd05621 202 ---------------------------------DETGMVHCDTA---------------------VGTPDYISPEVLKSQ 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 GHD----FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVkDPNRRLGcHR 330
Cdd:cd05621 228 GGDgyygRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhknsLNFPDDVEISKHAKNLICAFLT-DREVRLG-RN 305
                       330       340       350
                ....*....|....*....|....*....|....*
gi 15232374 331 GAAEIKELAFFAGVRW--DLLTEVLRPPFIPLRDD 363
Cdd:cd05621 306 GVEEIKQHPFFRNDQWnwDNIRETAAPVVPELSSD 340
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
25-328 1.13e-25

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: 104.76  E-value: 1.13e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSA----SSLRRarwEIEVLRRLSvdsnqNPFLPRLLASFESPEYF 100
Cdd:cd14083   9 EVLGTGAFSEVVLAED----KATGKLVAIKCIDKKALkgkeDSLEN---EIAVLRKIK-----HPNIVQLLDIYESKSHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDL-NVLLHRqndGVFS----SSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILiqqsghvtltdfdlsr 175
Cdd:cd14083  77 YLVMELVTGGELfDRIVEK---GSYTekdaSHLIR----QVLEAVDYLHSLGIVHRDLKPENLL---------------- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slkkplrphFYQPDPELIIdrkksrsfsrLISptaeknKTGLKKTRsarvnpinrrktsfSSGERSNSfVGTDEYVSPEV 255
Cdd:cd14083 134 ---------YYSPDEDSKI----------MIS------DFGLSKME--------------DSGVMSTA-CGTPGYVAPEV 173
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFaGKP--NDLT----DLIRRLLVKDPNRRLGC 328
Cdd:cd14083 174 LAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEF-DSPywDDISdsakDFIRHLMEKDPNKRYTC 251
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
24-329 1.69e-25

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 104.21  E-value: 1.69e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRA-RWEIEVLRRlsvdsNQNPFLPRLLASFESPEYFAW 102
Cdd:cd06623   6 VKVLGQGSSGVVYKVRH----KPTGKIYALKKIHVDGDEEFRKQlLRELKTLRS-----CESPYVVKCYGAFYKEGEISI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLNVLLHRqnDGVFSSSVIRFYVAEIVCALEHLHTM-GIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkpl 181
Cdd:cd06623  77 VLEYMDGGSLADLLKK--VGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLE--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd06623 152 ------------------------------------------------------NTLDQCNTFVGTVTYMSPERIQGESY 177
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKgKSKKETF----RNVLMKEPEFA---GKPNDLTDLIRRLLVKDPNRRLGCH 329
Cdd:cd06623 178 SYAADIWSLGLTLLECALGKFPFL-PPGQPSFfelmQAICDGPPPSLpaeEFSPEFRDFISACLQKDPKKRPSAA 251
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
26-326 1.96e-25

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: 104.36  E-value: 1.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSS-------ASSLRRA-RWEIEVLRRLSvdsnQNPFLPRLLASFESP 97
Cdd:cd14093  10 ILGRGVSSTVRRCIE----KETGQEFAVKIIDITGeksseneAEELREAtRREIEILRQVS----GHPNIIELHDVFESP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLhrqNDGV-FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd14093  82 TFIFLVFELCRKGELFDYL---TEVVtLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LKKplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVI 256
Cdd:cd14093 159 LDE----------------------------------------------------------GEKLRELCGTPGYLAPEVL 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 257 R------GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14093 181 KcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMegkyeFGSPEWDDISDTAKDLISKLLVVDPKKR 260

                .
gi 15232374 326 L 326
Cdd:cd14093 261 L 261
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
27-325 2.71e-25

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: 104.44  E-value: 2.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAhdvVSTSSSSSPFAVKLVPKSSASSLRRARW-------EIEVLRRLSvdsnqNPFLPRLLASFESPEY 99
Cdd:cd14096   9 IGEGAFSNVYKA---VPLRNTGKPVAIKVVRKADLSSDNLKGSsranilkEVQIMKRLS-----HPNIVKLLDFQESDEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQNdgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQsghvtltdFDLSRSLKK 179
Cdd:cd14096  81 YYIVLELADGGEIFHQIVRLT--YFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEP--------IPFIPSIVK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 PLRphfyQPDPELIIDRKKsrsfsrlISPTAEKNKTGLKKTRSARVNPINRRKTSFSSgersnsfVGTDEYVSPEVIRGD 259
Cdd:cd14096 151 LRK----ADDDETKVDEGE-------FIPGVGGGGIGIVKLADFGLSKQVWDSNTKTP-------CGTVGYTAPEVVKDE 212
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAgKP------NDLTDLIRRLLVKDPNRR 325
Cdd:cd14096 213 RYSKKVDMWALGCVLYTLLCGFPPFYDESIETLTEKISRGDYTFL-SPwwdeisKSAKDLISHLLTVDPAKR 283
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
27-341 2.71e-25

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: 103.54  E-value: 2.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSSSspFAVKLVPKSSASSLR-----RARWEIEVLRRLS-------VDSNQNpflprllasf 94
Cdd:cd13994   1 IGKGATSVVRIVTKKNPRSGVL--YAVKEYRRRDDESKRkdyvkRLTSEYIISSKLHhpnivkvLDLCQD---------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEYfaWAV-PYCSGGDLNVLLHRqnDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDL 173
Cdd:cd13994  69 LHGKW--CLVmEYCPGGDLFTLIEK--ADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGT 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SRSLKkplrphfYQPDPEliidrkkSRSFSRLisptaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSP 253
Cdd:cd13994 145 AEVFG-------MPAEKE-------SPMSAGL---------------------------------------CGSEPYMAP 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVIRGDGHD-FAVDWWALGVLTYEMMYGETPFKGKSK---------KETFRNVLMKEPEFAGKPNDLTDLIRRLLVKDPN 323
Cdd:cd13994 172 EVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWRSAKKsdsaykayeKSGDFTNGPYEPIENLLPSECRRLIYRMLHPDPE 251
                       330
                ....*....|....*...
gi 15232374 324 RRLgchrGAAEIKELAFF 341
Cdd:cd13994 252 KRI----TIDEALNDPWV 265
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
22-326 8.82e-25

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 102.10  E-value: 8.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSssssPFAVKLVPKSSASSLR---RARWEIEVLRRLsvdsnQNPFLPRLLASFESPE 98
Cdd:cd14663   3 ELGRTLGEGTFAKVKFARNTKTGE----SVAIKIIDKEQVAREGmveQIKREIAIMKLL-----RHPNIVELHEVMATKT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrSLK 178
Cdd:cd14663  74 KIFFVMELVTGGELFSKI--AKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLS-ALS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 KPLRPhfyqpdpeliidrkksrsfsrlisptaeknkTGLKKTRsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRG 258
Cdd:cd14663 151 EQFRQ-------------------------------DGLLHTT-----------------------CGTPNYVAPEVLAR 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 259 DGHD-FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14663 177 RGYDgAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWfSPGAKSLIKRILDPNPSTRI 246
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
25-326 9.45e-25

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: 102.47  E-value: 9.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSssspFAVKLVPKS--------SASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFES 96
Cdd:cd14084  12 RTLGSGACGEVKLAYDKSTCKK----VAIKIINKRkftigsrrEINKPRNIETEIEILKKLS-----HPCIIKIEDFFDA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PEYFAWAVPYCSGGDLnvlLHRQNDGV-FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTL---TDFD 172
Cdd:cd14084  83 EDDYYIVLELMEGGEL---FDRVVSNKrLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLikiTDFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 173 LSRSLkkplrphfyqpdpeliidrkksrsfsrlisptaekNKTGLKKTRsarvnpinrrktsfssgersnsfVGTDEYVS 252
Cdd:cd14084 160 LSKIL-----------------------------------GETSLMKTL-----------------------CGTPTYLA 181
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 253 PEVIRGDG---HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMK------EPEFAGKPNDLTDLIRRLLVKDPN 323
Cdd:cd14084 182 PEVLRSFGtegYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEQILSgkytfiPKAWKNVSEEAKDLVKKMLVVDPS 261

                ...
gi 15232374 324 RRL 326
Cdd:cd14084 262 RRP 264
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
22-325 1.24e-24

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: 101.99  E-value: 1.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSssspFAVKLVP-KSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLlasfespeYF 100
Cdd:cd13996   9 EEIELLGSGGFGSVYKVRNKVDGVT----YAIKKIRlTEKSSASEKVLREVKALAKL-----NHPNIVRY--------YT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWA--------VPYCSGGDLNVLLHRQN-DGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQS-GHVTLTD 170
Cdd:cd13996  72 AWVeepplyiqMELCEGGTLRDWIDRRNsSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 171 FDLSRSLKkplrphfyqpdpeliidrkksrsfsrlisptaeknktglKKTRSARVNPINrrkTSFSSGERSnSFVGTDEY 250
Cdd:cd13996 152 FGLATSIG---------------------------------------NQKRELNNLNNN---NNGNTSNNS-VGIGTPLY 188
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 251 VSPEVIRGDGHDFAVDWWALGVLTYEMMYgetPFKGKSKKETFRNVLMK---EPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd13996 189 ASPEQLDGENYNEKADIYSLGIILFEMLH---PFKTAMERSTILTDLRNgilPESFKAKHPKEADLIQSLLSKNPEER 263
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
20-325 1.32e-24

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 102.03  E-value: 1.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  20 SIKALKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARWEIEVLRRLSvdsnQNPFLPRLLAS---FES 96
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNTGRR----YALKRMYFNDEEQLRVAIKEIEIMKRLC----GHPNIVQYYDSailSSE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PEYFAW-AVPYCSGGDLNVLLHRQNDGvFSSSVIRFYVAEIVCALEHLHTMG--IAYRDLKPENILIQQSGHVTLTDFDl 173
Cdd:cd13985  73 GRKEVLlLMEYCPGSLVDILEKSPPSP-LSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SRSlkkplrPHFYQPdpeliiDRKKSRsfsrlisPTAEKNktglkktrsarvnpINRRKTSfssgersnsfvgtdEYVSP 253
Cdd:cd13985 151 SAT------TEHYPL------ERAEEV-------NIIEEE--------------IQKNTTP--------------MYRAP 183
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 254 EVI---RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFrNVLMKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd13985 184 EMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIV-AGKYSIPEQPRYSPELHDLIRHMLTPDPAER 257
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
18-326 1.55e-24

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: 101.57  E-value: 1.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  18 LDSIKALKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSassLRRARWEIEVLRRLSVDSN-QNPFLPRLLASFES 96
Cdd:cd14116   4 LEDFEIGRPLGKGKFGNVYLARE----KQSKFILALKVLFKAQ---LEKAGVEHQLRREVEIQSHlRHPNILRLYGYFHD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PEYFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd14116  77 ATRVYLILEYAPLGTVYREL--QKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 lkkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvNPINRRKTsfssgersnsFVGTDEYVSPEVI 256
Cdd:cd14116 155 -------------------------------------------------APSSRRTT----------LCGTLDYLPPEMI 175
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFR---NVLMKEPEFAGkpNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14116 176 EGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKrisRVEFTFPDFVT--EGARDLISRLLKHNPSQRP 246
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
24-325 3.86e-24

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: 100.36  E-value: 3.86e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVpKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWA 103
Cdd:cd06614   5 LEKIGEGASGEVYKATDRATGKE----VAIKKM-RLRKQNKELIINEILIMKEC-----KHPNIVDYYDSYLVGDELWVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrp 183
Cdd:cd06614  75 MEYMDGGSLTDII-TQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQL------ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlispTAEKNKtglkktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd06614 148 -------------------------TKEKSK--------------------------RNSVVGTPYWMAPEVIKRKDYGP 176
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 264 AVDWWALGVLTYEMMYGETP-FKGKSKKETFRNVLMKEPEFAGKPN---DLTDLIRRLLVKDPNRR 325
Cdd:cd06614 177 KVDIWSLGIMCIEMAEGEPPyLEEPPLRALFLITTKGIPPLKNPEKwspEFKDFLNKCLVKDPEKR 242
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
18-329 3.90e-24

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: 100.35  E-value: 3.90e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  18 LDSIKALKILGKGATGTVflaHDVVSTSSSSSpFAVKLVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESP 97
Cdd:cd14114   1 YDHYDILEELGTGAFGVV---HRCTERATGNN-FAAKFIMTPHESDKETVRKEIQIMNQL-----HHPKLINLHDAFEDD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRfYVAEIVCALEHLHTMGIAYRDLKPENILIQ--QSGHVTLTDFDLSR 175
Cdd:cd14114  72 NEMVLILEFLSGGELFERIAAEHYKMSEAEVIN-YMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLAT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SLkkplrphfyqpDPELIIdrkksrsfsrlisptaeknktglKKTrsarvnpinrrktsfssgersnsfVGTDEYVSPEV 255
Cdd:cd14114 151 HL-----------DPKESV-----------------------KVT------------------------TGTAEFAAPEI 172
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRLGCH 329
Cdd:cd14114 173 VEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKscdwnFDDSAFSGISEEAKDFIRKLLLADPNKRMTIH 251
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
22-328 8.36e-24

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: 99.39  E-value: 8.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARWEIEVlrRLSVdSNQNPFLPRLLASFESPEYFA 101
Cdd:cd08530   3 KVLKKLGKGSYGSVYK----VKRLSDNQVYALKEVNLGSLSQKEREDSVNEI--RLLA-SVNHPNIIRYKEAFLDGNRLC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQNDG--VFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKK 179
Cdd:cd08530  76 IVMEYAPFGDLSKLISKRKKKrrLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptaeknktGLKKTRsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRGD 259
Cdd:cd08530 156 ------------------------------------NLAKTQ-----------------------IGTPLYAAPEVWKGR 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE--PEFAGKPNDLTDLIRRLLVKDPNRRLGC 328
Cdd:cd08530 177 PYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKfpPIPPVYSQDLQQIIRSLLQVNPKKRPSC 247
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
27-326 8.88e-24

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: 99.28  E-value: 8.88e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAH------DVVstssssspfAVKLVPKSS--ASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPE 98
Cdd:cd14121   3 LGSGTYATVYKAYrksgarEVV---------AVKCVSKSSlnKASTENLLTEIELLKKL-----KHPHIVELKDFQWDEE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLNVLLHrqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTL--TDFDLSRS 176
Cdd:cd14121  69 HIYLIMEYCSGGDLSRFIR--SRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLklADFGFAQH 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LKkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVI 256
Cdd:cd14121 147 LK----------------------------------------------------------PNDEAHSLRGSPLYMAPEMI 168
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKE----TFRNVLMKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14121 169 LKKKYDARVDLWSVGVILYECLFGRAPFASRSFEEleekIRSSKPIEIPTRPELSADCRDLLLRLLQRDPDRRI 242
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
22-325 2.64e-23

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: 98.11  E-value: 2.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAhdvvSTSSSSSPFAVKLV-------PKSSASSLRrarwEIEVLRRLsvdsnQNPFLPRLLASF 94
Cdd:cd08224   3 EIEKKIGKGQFSVVYRA----RCLLDGRLVALKKVqifemmdAKARQDCLK----EIDLLQQL-----NHPNIIKYLASF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 -ESPEYFAwAVPYCSGGDLNVLL-HRQNDGV-FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:cd08224  70 iENNELNI-VLELADAGDLSRLIkHFKKQKRlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 172 DLSRSlkkplrphfyqpdpeliidrkksrsFSrliSPTAEknktglkktrsarvnpinrrktsfssgerSNSFVGTDEYV 251
Cdd:cd08224 149 GLGRF-------------------------FS---SKTTA-----------------------------AHSLVGTPYYM 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 252 SPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGkSKKETFrnVLMK---EPEFAGKPND-----LTDLIRRLLVKDPN 323
Cdd:cd08224 172 SPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYG-EKMNLY--SLCKkieKCEYPPLPADlysqeLRDLVAACIQPDPE 248

                ..
gi 15232374 324 RR 325
Cdd:cd08224 249 KR 250
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
108-326 4.76e-23

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 97.20  E-value: 4.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 108 SGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSgHVTLTDFDLSRSLKKplrphfyq 187
Cdd:cd14109  80 STIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQSRRLLR-------- 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 188 pdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGDGHDFAVDW 267
Cdd:cd14109 151 --------------------------------------------------GKLTTLIYGSPEFVSPEIVNSYPVTLATDM 180
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 268 WALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKP-----NDLTDLIRRLLVKDPNRRL 326
Cdd:cd14109 181 WSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPlgnisDDARDFIKKLLVYIPESRL 244
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
25-324 5.80e-23

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: 96.98  E-value: 5.80e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASS------LRRarwEIEVLRRLsvdsnQNPFLPRLLASFESPE 98
Cdd:cd14162   6 KTLGHGSYAVVKKAYST----KHKCKVAIKIVSKKKAPEdylqkfLPR---EIEVIKGL-----KHPNLICFYEAIETTS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLK 178
Cdd:cd14162  74 RVYIIMELAENGDL--LDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 KPlrphfyqPDPELIIdrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVIRG 258
Cdd:cd14162 152 KT-------KDGKPKL----------------------------------------------SETYCGSYAYASPEILRG 178
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 259 DGHD-FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVlMKEPEFAGKP---NDLTDLIRRLLVKDPNR 324
Cdd:cd14162 179 IPYDpFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV-QRRVVFPKNPtvsEECKDLILRMLSPVKKR 247
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
24-330 6.37e-23

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: 97.76  E-value: 6.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSvdsNQNpfLPRLLASFESPEYFAWA 103
Cdd:cd14166   8 MEVLGSGAFSEVYL----VKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIK---HEN--IVTLEDIYESTTHYYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDL-NVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI---QQSGHVTLTDFDLSRslkk 179
Cdd:cd14166  79 MQLVSGGELfDRILER---GVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptAEKNktGLKKTRsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRGD 259
Cdd:cd14166 152 ------------------------------MEQN--GIMSTA-----------------------CGTPGYVAPEVLAQK 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAgKP--NDLT----DLIRRLLVKDPNRRLGCHR 330
Cdd:cd14166 177 PYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFE-SPfwDDISesakDFIRHLLEKNPSKRYTCEK 252
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
70-326 8.30e-23

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: 96.63  E-value: 8.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGGDLnvllhrqndgvFS--SSVIRF-------YVAEIVCAL 140
Cdd:cd14095  48 EVAILRRVK-----HPNIVQLIEEYDTDTELYLVMELVKGGDL-----------FDaiTSSTKFterdasrMVTDLAQAL 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 141 EHLHTMGIAYRDLKPENILIQQSG----HVTLTDFDLSRSLKKPLrphfyqpdpeliidrkksrsfsrlisptaeknktg 216
Cdd:cd14095 112 KYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKEPL----------------------------------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 217 lkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKG--KSKKETFR 294
Cdd:cd14095 157 -------------------------FTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSpdRDQEELFD 211
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15232374 295 NVLMKEPEFAGKPND-----LTDLIRRLLVKDPNRRL 326
Cdd:cd14095 212 LILAGEFEFLSPYWDnisdsAKDLISRMLVVDPEKRY 248
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
26-329 1.63e-22

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: 96.33  E-value: 1.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARWEIEVLRRLSVDSNqnpfLPRLLASFESPEYFAWAVP 105
Cdd:cd14090   9 LLGEGAYASVQTCINLYTGKE----YAVKIIEKHPGHSRSRVFREVETLHQCQGHPN----ILQLIEYFEDDERFYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLnvLLHRQNDGVFS----SSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT---LTDFDLSRSLK 178
Cdd:cd14090  81 KMRGGPL--LSHIEKRVHFTeqeaSLVVR----DIASALDFLHDKGIAHRDLKPENILCESMDKVSpvkICDFDLGSGIK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kpLRPHFYQP--DPEliidrkksrsfsrLISPtaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVI 256
Cdd:cd14090 155 --LSSTSMTPvtTPE-------------LLTP------------------------------------VGSAEYMAPEVV 183
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 257 R---GDGH--DFAVDWWALGVLTYEMMYGETPFKGKSKKE----------TFRNVLMK----------EPEFAGKPNDLT 311
Cdd:cd14090 184 DafvGEALsyDKRCDLWSLGVILYIMLCGYPPFYGRCGEDcgwdrgeacqDCQELLFHsiqegeyefpEKEWSHISAEAK 263
                       330
                ....*....|....*...
gi 15232374 312 DLIRRLLVKDPNRRLGCH 329
Cdd:cd14090 264 DLISHLLVRDASQRYTAE 281
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
21-326 2.29e-22

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: 95.29  E-value: 2.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  21 IKALkiLGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASslrRARWEIE--VLRRLSvdsnqNPFLPRLLASFESPE 98
Cdd:cd14087   5 IKAL--IGRGSFSRVVR----VEHRVTRQPYAIKMIETKCRG---REVCESElnVLRRVR-----HTNIIQLIEVFETKE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDL-NVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH---VTLTDFDLS 174
Cdd:cd14087  71 RVYMVMELATGGELfDRIIAK---GSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RSLKKplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvNPINRRKTSfssgersnsfVGTDEYVSPE 254
Cdd:cd14087 148 STRKK----------------------------------------------GPNCLMKTT----------CGTPEYIAPE 171
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 255 VIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKP-----NDLTDLIRRLLVKDPNRRL 326
Cdd:cd14087 172 ILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPwpsvsNLAKDFIDRLLTVNPGERL 248
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
106-325 2.71e-22

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: 95.30  E-value: 2.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLL--HRQNDGVFSSSVIRFYVAEIVCALEHLHT-----MGIAYRDLKPENILIQQSGHVTLTDFDLSRSLk 178
Cdd:cd08217  82 YCEGGDLAQLIkkCKKENQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFLDSDNNVKLGDFGLARVL- 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinRRKTSFSSgersnSFVGTDEYVSPEVIRG 258
Cdd:cd08217 161 ---------------------------------------------------SHDSSFAK-----TYVGTPYYMSPELLNE 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374 259 DGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVlmKEPEFAGKPN----DLTDLIRRLLVKDPNRR 325
Cdd:cd08217 185 QSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKI--KEGKFPRIPSryssELNEVIKSMLNVDPDKR 253
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
20-326 3.38e-22

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: 94.99  E-value: 3.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  20 SIKALKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEY 99
Cdd:cd14190   5 SIHSKEVLGGGKFGKVHTCTE----KRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLN-----HRNLIQLYEAIETPNE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLnvlLHR--QNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENIL-IQQSGH-VTLTDFDLSR 175
Cdd:cd14190  76 IVLFMEYVEGGEL---FERivDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILcVNRTGHqVKIIDFGLAR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slkkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsaRVNPINRRKTSFssgersnsfvGTDEYVSPEV 255
Cdd:cd14190 153 ------------------------------------------------RYNPREKLKVNF----------GTPEFLSPEV 174
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLM-----KEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14190 175 VNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMgnwyfDEETFEHVSDEAKDFVSNLIIKERSARM 250
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
24-325 5.22e-22

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: 94.62  E-value: 5.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSssssPFAVKLVPKSSASS----LRRarwEIEVLRRLsvdsnQNPFLPRLLASFESpEY 99
Cdd:cd06609   6 LERIGKGSFGEVYKGIDKRTNQ----VVAIKVIDLEEAEDeiedIQQ---EIQFLSQC-----DSPYITKYYGSFLK-GS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAV-PYCSGGDLNVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLK 178
Cdd:cd06609  73 KLWIImEYCGGGSVLDLLKP---GPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvNPINRRKTsfssgersnsFVGTDEYVSPEVIRG 258
Cdd:cd06609 150 -----------------------------------------------STMSKRNT----------FVGTPFWMAPEVIKQ 172
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 259 DGHDFAVDWWALGVLTYEMMYGETPFkgkSKKETFRnVLMKEPEfaGKPNDLT---------DLIRRLLVKDPNRR 325
Cdd:cd06609 173 SGYDEKADIWSLGITAIELAKGEPPL---SDLHPMR-VLFLIPK--NNPPSLEgnkfskpfkDFVELCLNKDPKER 242
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
25-325 8.17e-22

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: 94.02  E-value: 8.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARWEIEVLRRLSVdsnQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd14074   9 ETLGRGHFAVVKLARHVFTGEK----VAVKVIDKTKLDDVSKAHLFQEVRCMKLV---QHPNVVRLYEVIDTQTKLYLIL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLNVLLHRQNDGVfSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI-QQSGHVTLTDFDLSRSlkkplrp 183
Cdd:cd14074  82 ELGDGGDMYDYIMKHENGL-NEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfYQPdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd14074 154 --FQP-------------------------------------------------GEKLETSCGSLAYSAPEILLGDEYDA 182
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 264 -AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL---MKEPEFAGKpnDLTDLIRRLLVKDPNRR 325
Cdd:cd14074 183 pAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMdckYTVPAHVSP--ECKDLIRRMLIRDPKKR 246
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
22-326 8.27e-22

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: 93.77  E-value: 8.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSS---ASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPE 98
Cdd:cd14186   4 KVLNLLGKGSFACVYRARSL----HTGLEVAIKMIDKKAmqkAGMVQRVRNEVEIHCQL-----KHPSILELYNYFEDSN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLNVLL-HRQNDgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd14186  75 YVYLVLEMCHNGEMSRYLkNRKKP--FTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 KKPLRPHFyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIR 257
Cdd:cd14186 153 KMPHEKHF---------------------------------------------------------TMCGTPNYISPEIAT 175
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE---PEFAGKpnDLTDLIRRLLVKDPNRRL 326
Cdd:cd14186 176 RSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADyemPAFLSR--EAQDLIHQLLRKNPADRL 245
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
21-325 1.13e-21

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: 93.33  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    21 IKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSLRRA-RWEIEVLRRLSvdsnqNPFLPRLLASFESPEY 99
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGENTKIKVAVKTLKEGADEEEREDfLEEASIMKKLD-----HPNIVKLLGVCTQGEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   100 FAWAVPYCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkk 179
Cdd:pfam07714  76 LYIVTEYMPGGDLLDFL-RKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDI-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   180 plrphfyqpdpeliidrkksrsfsrlisptaeKNKTGLKKTRSARVnPINrrktsfssgersnsfvgtdeYVSPEVIRGD 259
Cdd:pfam07714 153 --------------------------------YDDDYYRKRGGGKL-PIK--------------------WMAPESLKDG 179
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374   260 GHDFAVDWWALGVLTYEMM-YGETPFKGKSKKETFRNVL----MKEPEFAgkPNDLTDLIRRLLVKDPNRR 325
Cdd:pfam07714 180 KFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLEdgyrLPQPENC--PDELYDLMKQCWAYDPEDR 248
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
24-325 1.54e-21

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: 92.83  E-value: 1.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLA------HDVVstssssspfaVKLVPKSS--ASSLRRAR------WEIEVLRRLSVDSNQNpfLPR 89
Cdd:cd14004   5 LKEMGEGAYGQVNLAiykskgKEVV----------IKFIFKERilVDTWVRDRklgtvpLEIHILDTLNKRSHPN--IVK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  90 LLASFESPEYFAWAVP-YCSGGDLNVLLHRQN--DGVFSSSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILIQQSGHV 166
Cdd:cd14004  73 LLDFFEDDEFYYLVMEkHGSGMDLFDFIERKPnmDEKEAKYIFR----QVADAVKHLHDQGIVHRDIKDENVILDGNGTI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 167 TLTDFDLSRSLKkplRPHFYqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnSFVG 246
Cdd:cd14004 149 KLIDFGSAAYIK---SGPFD--------------------------------------------------------TFVG 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 247 TDEYVSPEVIRGD---GHDfaVDWWALGVLTYEMMYGETPF-------KGKSKketFRNVLMKepefagkpnDLTDLIRR 316
Cdd:cd14004 170 TIDYAAPEVLRGNpygGKE--QDIWALGVLLYTLVFKENPFynieeilEADLR---IPYAVSE---------DLIDLISR 235

                ....*....
gi 15232374 317 LLVKDPNRR 325
Cdd:cd14004 236 MLNRDVGDR 244
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
25-326 1.88e-21

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: 92.78  E-value: 1.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDvvstSSSSSPFAVKLV--PKSSASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAW 102
Cdd:cd14069   7 QTLGEGAFGEVFLAVN----RNTEEAVAVKFVdmKRAPGDCPENIKKEVCIQKMLS-----HKNVVRFYGHRREGEFQYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLnvlLHR-QNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrSLkkpl 181
Cdd:cd14069  78 FLEYASGGEL---FDKiEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLA-TV---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsFSRlisptaeKNKtglkktrsarvnpinrrktsfssgER-SNSFVGTDEYVSPEVIRGDG 260
Cdd:cd14069 150 --------------------FRY-------KGK------------------------ERlLNKMCGTLPYVAPELLAKKK 178
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 261 HDFA-VDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPNDLTD-----LIRRLLVKDPNRRL 326
Cdd:cd14069 179 YRAEpVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENKKTYLTPWKKIDtaalsLLRKILTENPNKRI 250
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
25-325 2.06e-21

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: 92.67  E-value: 2.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHD-----VVstssssspfAVKLVP--KSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESP 97
Cdd:cd06627   6 DLIGRGAFGSVYKGLNlntgeFV---------AIKQISleKIPKSDLKSVMGEIDLLKKL-----NHPNIVKYIGSVKTK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd06627  72 DSLYIILEYVENGSLASIIKKF--GKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 KkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIR 257
Cdd:cd06627 150 N---------------------------------------------------------EVEKDENSVVGTPYWMAPEVIE 172
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKG-KSKKETFRNVLMKEPEFagkPNDLTDLIRRLLV----KDPNRR 325
Cdd:cd06627 173 MSGVTTASDIWSVGCTVIELLTGNPPYYDlQPMAALFRIVQDDHPPL---PENISPELRDFLLqcfqKDPTLR 242
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
25-325 3.40e-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: 92.08  E-value: 3.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAhdvvSTSSSSSPFAVKLVP-----KSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEY 99
Cdd:cd06632   6 QLLGSGSFGSVYEG----FNGDTGDFFAVKEVSlvdddKKSRESVKQLEQEIALLSKL-----RHPNIVQYYGTEREEDN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKK 179
Cdd:cd06632  77 LYIFLEYVPGGSIHKLLQRY--GAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 PlrphfyqpdpeliidrkksrSFSRlisptaeknktglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIR-- 257
Cdd:cd06632 155 F--------------------SFAK--------------------------------------SFKGSPYWMAPEVIMqk 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVlMKEPEFAGKPNDLT----DLIRRLLVKDPNRR 325
Cdd:cd06632 177 NSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKI-GNSGELPPIPDHLSpdakDFIRLCLQRDPEDR 247
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
27-330 3.67e-21

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: 92.26  E-value: 3.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRA-RWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVP 105
Cdd:cd14169  11 LGEGAFSEVVLAQE----RGSQRLVALKCIPKKALRGKEAMvENEIAVLRRI-----NHENIVSLEDIYESPTHLYLAME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDL-NVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ---QSGHVTLTDFDLSRslkkpl 181
Cdd:cd14169  82 LVTGGELfDRIIER---GSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK------ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsFSSGERSNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd14169 153 -----------------------------------------------------IEAQGMLSTACGTPGYVAPELLEQKPY 179
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFaGKP--NDLT----DLIRRLLVKDPNRRLGCHR 330
Cdd:cd14169 180 GKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEF-DSPywDDISesakDFIRHLLERDPEKRFTCEQ 253
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
21-325 4.10e-21

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: 91.84  E-value: 4.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374     21 IKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSLRRA-RWEIEVLRRLsvdsnQNPFLPRLL--ASFESP 97
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDGKEVEVAVKTLKEDASEQQIEEfLREARIMRKL-----DHPNIVKLLgvCTEEEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374     98 EYFAwaVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:smart00221  76 LMIV--MEYMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    178 KkplrphfyqpdpeliidrkksrsfsrlisptaeknKTGLKKTRSARVnPINrrktsfssgersnsfvgtdeYVSPEVIR 257
Cdd:smart00221 154 Y-----------------------------------DDDYYKVKGGKL-PIR--------------------WMAPESLK 177
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374    258 GDGHDFAVDWWALGVLTYEMM-YGETPFKGKSKKETFRNV----LMKEPEfaGKPNDLTDLIRRLLVKDPNRR 325
Cdd:smart00221 178 EGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLkkgyRLPKPP--NCPPELYKLMLQCWAEDPEDR 248
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
51-326 7.34e-21

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: 91.62  E-value: 7.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRRARWEIEVLRRLSV-DSNQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDgvFSSSVI 129
Cdd:cd14194  33 YAAKFIKKRRTKSSRRGVSREDIEREVSIlKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKES--LTEEEA 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 130 RFYVAEIVCALEHLHTMGIAYRDLKPENILIqqsghvtltdfdLSRSLKKPlrphfyqpdpeliidRKKSRSFsrlispt 209
Cdd:cd14194 111 TEFLKQILNGVYYLHSLQIAHFDLKPENIML------------LDRNVPKP---------------RIKIIDF------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 210 aeknktGLkktrSARVNPINRRKTSFssgersnsfvGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSK 289
Cdd:cd14194 157 ------GL----AHKIDFGNEFKNIF----------GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTK 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15232374 290 KETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14194 217 QETLANVSavnyeFEDEYFSNTSALAKDFIRRLLVKDPKKRM 258
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
27-340 7.42e-21

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: 91.33  E-value: 7.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSSSSP-----FAVKLVPKSSASSLRRARweieVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd08222   8 LGSGNFGTVYLVSDLKATADEELKvlkeiSVGELQPDETVDANREAK----LLSKL-----DHPAIVKFHDSFVEKESFC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLN--VLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQsGHVTLTDFDLSRSLkk 179
Cdd:cd08222  79 IVTEYCEGGDLDdkISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFGISRIL-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsFSSGERSNSFVGTDEYVSPEVIRGD 259
Cdd:cd08222 156 -------------------------------------------------------MGTSDLATTFTGTPYYMSPEVLKHE 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPFKGKSkketFRNVLMK-----EPEFAGK-PNDLTDLIRRLLVKDPNRRLgchrGAA 333
Cdd:cd08222 181 GYNSKSDIWSLGCILYEMCCLKHAFDGQN----LLSVMYKivegeTPSLPDKySKELNAIYSRMLNKDPALRP----SAA 252

                ....*..
gi 15232374 334 EIKELAF 340
Cdd:cd08222 253 EILKIPF 259
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
24-325 8.18e-21

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: 91.17  E-value: 8.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstsSSSSPFAVKLVPKS---SASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYF 100
Cdd:cd14161   8 LETLGKGTYGRVKKARD-----SSGRLVAIKSIRKDrikDEQDLLHIRREIEIMSSLN-----HPHIISVYEVFENSSKI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDL-NVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkk 179
Cdd:cd14161  78 VIVMEYASRGDLyDYISERQR---LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLS----- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrpHFYQPDPELiidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGD 259
Cdd:cd14161 150 ----NLYNQDKFL-------------------------------------------------QTYCGSPLYASPEIVNGR 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 GHDFA-VDWWALGVLTYEMMYGETPFKGKSKKETFRNVL---MKEPEfagKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14161 177 PYIGPeVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISsgaYREPT---KPSDACGLIRWLLMVNPERR 243
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
20-326 8.85e-21

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: 91.13  E-value: 8.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  20 SIKALKILGKGATGTVflaHDVVSTSSSSSpFAVKLVPKSSASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEY 99
Cdd:cd14193   5 NVNKEEILGGGRFGQV---HKCEEKSSGLK-LAAKIIKARSQKEKEEVKNEIEVMNQLN-----HANLIQLYDAFESRND 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFyVAEIVCALEHLHTMGIAYRDLKPENILI--QQSGHVTLTDFDLSRSl 177
Cdd:cd14193  76 IVLVMEYVDGGELFDRIIDENYNLTELDTILF-IKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARR- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfYQPDPELiidrkksrsfsrlisptaeknktglkktrsaRVNpinrrktsfssgersnsfVGTDEYVSPEVIR 257
Cdd:cd14193 154 --------YKPREKL-------------------------------RVN------------------FGTPEFLAPEVVN 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14193 177 YEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILacqwdFEDEEFADISEEAKDFISKLLIKEKSWRM 250
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
25-331 9.08e-21

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: 91.24  E-value: 9.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRA-RWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWA 103
Cdd:cd14167   9 EVLGTGAFSEVVLAEE----KRTQKLVAIKCIAKKALEGKETSiENEIAVLHKI-----KHPNIVALDDIYESGGHLYLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDL-NVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENIL---IQQSGHVTLTDFDLSRslkk 179
Cdd:cd14167  80 MQLVSGGELfDRIVEK---GFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK---- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliIDrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGD 259
Cdd:cd14167 153 --------------IE----------------------------------------GSGSVMSTACGTPGYVAPEVLAQK 178
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFaGKP--NDLT----DLIRRLLVKDPNRRLGCHRG 331
Cdd:cd14167 179 PYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEF-DSPywDDISdsakDFIQHLMEKDPEKRFTCEQA 255
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
21-325 1.38e-20

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 90.28  E-value: 1.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374     21 IKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSLRRA-RWEIEVLRRLsvdsnQNPFLPRLL--ASFESP 97
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKVEVAVKTLKEDASEQQIEEfLREARIMRKL-----DHPNVVKLLgvCTEEEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374     98 EYFAwaVPYCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:smart00219  76 LYIV--MEYMEGGDLLSYL-RKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    178 KkplrphfyqpdpeliidrkksrsfsrlisptaeknKTGLKKTRSARVnPINrrktsfssgersnsfvgtdeYVSPEVIR 257
Cdd:smart00219 153 Y-----------------------------------DDDYYRKRGGKL-PIR--------------------WMAPESLK 176
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374    258 GDGHDFAVDWWALGVLTYEMM-YGETPFKGKSKKETFRNV----LMKEPEfaGKPNDLTDLIRRLLVKDPNRR 325
Cdd:smart00219 177 EGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLkngyRLPQPP--NCPPELYDLMLQCWAEDPEDR 247
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
27-326 1.88e-20

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: 90.01  E-value: 1.88e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSassLRR-------ARWEIEVLRRLsvdsnQNPFLPRLLASFESPE- 98
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCR----RAVKILKKRK---LRRipngeanVKREIQILRRL-----NHRNVIKLVDVLYNEEk 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 ---YFAwaVPYCSGGdLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd14119  69 qklYMV--MEYCVGG-LQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SLkkplrphfyqpdpeliiDRkksrsfsrlisptaeknktglkktrsarvnpinrrktsFSSGERSNSFVGTDEYVSPEV 255
Cdd:cd14119 146 AL-----------------DL--------------------------------------FAEDDTCTTSQGSPAFQPPEI 170
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 256 IRGDG--HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEF-AGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14119 171 ANGQDsfSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIpDDVDPDLQDLLRGMLEKDPEKRF 244
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
24-325 2.13e-20

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: 89.67  E-value: 2.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSSsspfAVKLVPKSSASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWA 103
Cdd:cd06613   5 IQRIGSGTYGDVYKARNIATGELA----AVKVIKLEPGDDFEIIQQEISMLKECR-----HPNIVAYFGSYLRRDKLWIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrp 183
Cdd:cd06613  76 MEYCGGGSLQDIYQVT--GPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVS--------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlisptAEKNKTglkktrsarvnpINRRktsfssgersNSFVGTDEYVSPEVI---RGDG 260
Cdd:cd06613 145 --------------------------AQLTAT------------IAKR----------KSFIGTPYWMAPEVAaveRKGG 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFkgkSKKETFRnVLMKEPEFAGKPNDLTD----------LIRRLLVKDPNRR 325
Cdd:cd06613 177 YDGKCDIWALGITAIELAELQPPM---FDLHPMR-ALFLIPKSNFDPPKLKDkekwspdfhdFIKKCLTKNPKKR 247
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
51-325 2.74e-20

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: 89.99  E-value: 2.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAV--KLVPKSS-----ASSLRRAR----WEIEVLRRLSVD--SNQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLH 117
Cdd:cd14197  22 FAVvrKCVEKDSgkefaAKFMRKRRkgqdCRMEIIHEIAVLelAQANPWVINLHEVYETASEMILVLEYAAGGEIFNQCV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 118 RQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQS---GHVTLTDFDLSRSLKkplrphfyqpdpelii 194
Cdd:cd14197 102 ADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILK---------------- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 195 drkksrsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLT 274
Cdd:cd14197 166 ------------------------------------------NSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLA 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 275 YEMMYGETPFKGKSKKETF-----RNVLMKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14197 204 YVMLTGISPFLGDDKQETFlnisqMNVSYSEEEFEHLSESAIDFIKTLLIKKPENR 259
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
19-341 3.43e-20

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: 89.34  E-value: 3.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAH-----DVVstssssspfAVKLVpkssasSLRRARWEIEVLRRLS--VDSNQNPFLPRLL 91
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYclpkkEKV---------AIKRI------DLEKCQTSMDELRKEIqaMSQCNHPNVVSYY 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  92 ASFESPEYFaWAV-PYCSGGD-LNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLT 169
Cdd:cd06610  66 TSFVVGDEL-WLVmPLLSGGSlLDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 170 DFDLSRSLKKPlrphfyqpdpeliidrkksrsfsrlisptaeknktglkKTRSARVnpinrRKTsfssgersnsFVGTDE 249
Cdd:cd06610 145 DFGVSASLATG--------------------------------------GDRTRKV-----RKT----------FVGTPC 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 250 YVSPEVIRGD-GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPefAGKPNDLT---------DLIRRLLV 319
Cdd:cd06610 172 WMAPEVMEQVrGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDP--PSLETGADykkysksfrKMISLCLQ 249
                       330       340
                ....*....|....*....|..
gi 15232374 320 KDPNRRlgchRGAAEIKELAFF 341
Cdd:cd06610 250 KDPSKR----PTAEELLKHKFF 267
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
51-326 4.96e-20

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: 89.25  E-value: 4.96e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRRARWEIEVLRRLSVDSN-QNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLhRQNDGVFSSSVI 129
Cdd:cd14196  33 YAAKFIKKRQSRASRRGVSREEIEREVSILRQvLHPNIITLHDVYENRTDVVLILELVSGGELFDFL-AQKESLSEEEAT 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 130 RFyVAEIVCALEHLHTMGIAYRDLKPENILIQQSG----HVTLTDFDLSRSLKKplrphfyqpdpeliidrkksrsfsrl 205
Cdd:cd14196 112 SF-IKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIED-------------------------- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 206 isptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFK 285
Cdd:cd14196 165 --------------------------------GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15232374 286 GKSKKETFRNVLMK----EPEFAGKPNDLT-DLIRRLLVKDPNRRL 326
Cdd:cd14196 213 GDTKQETLANITAVsydfDEEFFSHTSELAkDFIRKLLVKETRKRL 258
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
24-325 6.83e-20

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: 88.24  E-value: 6.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRR--ARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFA 101
Cdd:cd08529   5 LNKLGKGSFGVVYKVVRKVDGRV----YALKQIDISRMSRKMReeAIDEARVLSKLN-----SPYVIKYYDSFVDKGKLN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkpl 181
Cdd:cd08529  76 IVMEYAENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKIL---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrliSPTAEKNKTglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGH 261
Cdd:cd08529 152 -------------------------SDTTNFAQT----------------------------IVGTPYYLSPELCEDKPY 178
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL--MKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd08529 179 NEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVrgKYPPISASYSQDLSQLIDSCLTKDYRQR 244
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
51-326 7.83e-20

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: 88.93  E-value: 7.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRRARWEIEVLRRLSVDSNqnpfLPRLLASFESPEYFAWAVPYCSGGdlNVLLHRQNDGVFSSSVIR 130
Cdd:cd14174  30 YAVKIIEKNAGHSRSRVFREVETLYQCQGNKN----ILELIEFFEDDTRFYLVFEKLRGG--SILAHIQKRKHFNEREAS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT---LTDFDLSRSLKkplrphfyqpdpeliidrkksrsfsrlis 207
Cdd:cd14174 104 RVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSpvkICDFDLGSGVK----------------------------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 208 ptaeknktglkktrsarvnpINRRKTSFSSGERSNSfVGTDEYVSPEVI-----RGDGHDFAVDWWALGVLTYEMMYGET 282
Cdd:cd14174 155 --------------------LNSACTPITTPELTTP-CGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYP 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 283 PFKGK---------------SKKETFRNVLMKEPEFAGK-----PNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14174 214 PFVGHcgtdcgwdrgevcrvCQNKLFESIQEGKYEFPDKdwshiSSEAKDLISKLLVRDAKERL 277
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
51-325 1.01e-19

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: 88.06  E-value: 1.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSsasslRRAR-WEIEVLRRLSV--DSNQNPFLPRLLASFESPEYFAWAVPYCSGGDL-NVLLHRQNDGVFSS 126
Cdd:cd14198  36 YAAKFLKKR-----RRGQdCRAEILHEIAVleLAKSNPRVVNLHEVYETTSEIILILEYAAGGEIfNLCVPDLAEMVSEN 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 127 SVIRFyVAEIVCALEHLHTMGIAYRDLKPENIL---IQQSGHVTLTDFDLSRSLKkplrphfyqpdpeliidrkksrsfs 203
Cdd:cd14198 111 DIIRL-IRQILEGVYYLHQNNIVHLDLKPQNILlssIYPLGDIKIVDFGMSRKIG------------------------- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 204 rlisptaeknktglkktrsarvnpinrrktsfSSGERsNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETP 283
Cdd:cd14198 165 --------------------------------HACEL-REIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESP 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15232374 284 FKGKSKKETFRNVLM-----KEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14198 212 FVGEDNQETFLNISQvnvdySEETFSSVSQLATDFIQKLLVKNPEKR 258
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
51-326 1.08e-19

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: 87.93  E-value: 1.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRR--ARWEIEvlRRLSVDSN-QNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLhRQNDGVFSSS 127
Cdd:cd14105  33 YAAKFIKKRRSKASRRgvSREDIE--REVSILRQvLHPNIITLHDVFENKTDVVLILELVAGGELFDFL-AEKESLSEEE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 128 VIRFyVAEIVCALEHLHTMGIAYRDLKPENILIQQSG----HVTLTDFDLSRSLKkplrphfyqpdpeliidrkksrsfs 203
Cdd:cd14105 110 ATEF-LKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLAHKIE------------------------- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 204 rlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETP 283
Cdd:cd14105 164 ---------------------------------DGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15232374 284 FKGKSKKETFRNVLMKEPEFAGKPNDLT-----DLIRRLLVKDPNRRL 326
Cdd:cd14105 211 FLGDTKQETLANITAVNYDFDDEYFSNTselakDFIRQLLVKDPRKRM 258
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
27-326 1.09e-19

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: 87.81  E-value: 1.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVvstSSSSSPFAVKLVPKS----SASSLRRarwEIEVLRRLSvdsNQNpfLPRLLASFESPEYFAW 102
Cdd:cd14120   1 IGHGAFAVVFKGRHR---KKPDLPVAIKCITKKnlskSQNLLGK---EIKILKELS---HEN--VVALLDCQETSSSVYL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILiqqsghvtltdfdLSRSLKKplr 182
Cdd:cd14120  70 VMEYCNGGDLADYLQAK--GTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNIL-------------LSHNSGR--- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phfyQPDPELIIDRKKSRSFSRLIsptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDGHD 262
Cdd:cd14120 132 ----KPSPNDIRLKIADFGFARFL-----------------------------QDGMMAATLCGSPMYMAPEVIMSLQYD 178
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 263 FAVDWWALGVLTYEMMYGETPFKGKSKKEtFRNVLMKEPEFA-----GKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14120 179 AKADLWSIGTIVYQCLTGKAPFQAQTPQE-LKAFYEKNANLRpnipsGTSPALKDLLLGLLKRNPKDRI 246
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
27-326 1.99e-19

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: 87.96  E-value: 1.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRArwEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd14085  11 LGRGATSVVYRCRQ----KGTQKPYAVKKLKKTVDKKIVRT--EIGVLLRLS-----HPNIIKLKEIFETPTEISLVLEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDL-NVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH---VTLTDFDLSRslkkplr 182
Cdd:cd14085  80 VTGGELfDRIVEK---GYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSK------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phfyqpdpelIIDRKKSRSfsrlisptaeknktglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIRGDGHD 262
Cdd:cd14085 150 ----------IVDQQVTMK-----------------------------------------TVCGTPGYCAPEILRGCAYG 178
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 263 FAVDWWALGVLTYEMMYGETPF-KGKSKKETFRNVLMKEPEFAGKPND-----LTDLIRRLLVKDPNRRL 326
Cdd:cd14085 179 PEVDMWSVGVITYILLCGFEPFyDERGDQYMFKRILNCDYDFVSPWWDdvslnAKDLVKKLIVLDPKKRL 248
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
70-325 3.02e-19

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: 86.57  E-value: 3.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIA 149
Cdd:cd14113  53 ELGVLQSL-----QHPQLVGLLDTFETPTSYILVLEMADQGRL--LDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIA 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 150 YRDLKPENILIQQSGH---VTLTDFDLSRSLKKPlrPHFYQpdpeliidrkksrsfsrlisptaeknktglkktrsarvn 226
Cdd:cd14113 126 HLDLKPENILVDQSLSkptIKLADFGDAVQLNTT--YYIHQ--------------------------------------- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 227 pinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE---PE- 302
Cdd:cd14113 165 -----------------LLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDfsfPDd 227
                       250       260
                ....*....|....*....|....
gi 15232374 303 -FAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14113 228 yFKGVSQKAKDFVCFLLQMDPAKR 251
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
51-325 3.48e-19

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: 86.48  E-value: 3.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSaSSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIR 130
Cdd:cd14107  30 CAAKFIPLRS-STRARAFQERDILARLS-----HRRLTCLLDQFETRKTLILILELCSSEELLDRLFLK--GVVTEAEVK 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH--VTLTDFDLSRSLKkPLRPHFYQpdpeliidrkksrsfsrlisp 208
Cdd:cd14107 102 LYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQEIT-PSEHQFSK--------------------- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 209 taeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKS 288
Cdd:cd14107 160 ------------------------------------YGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGEN 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15232374 289 KKETFRNVLMKE-----PEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14107 204 DRATLLNVAEGVvswdtPEITHLSEDAKDFIKRVLQPDPEKR 245
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
24-326 3.68e-19

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


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 86.77  E-value: 3.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSssssPFAVKLVPKS------SASSLRrarwEIEVLRRLsvdsnQNPFLPRLLA----- 92
Cdd:cd07829   4 LEKLGEGTYGVVYKAKDKKTGE----IVALKKIRLDneeegiPSTALR----EISLLKEL-----KHPNIVKLLDvihte 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  93 -----SFESPEYfawavpycsggDLNVLLHRqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT 167
Cdd:cd07829  71 nklylVFEYCDQ-----------DLKKYLDK-RPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLK 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 168 LTDFDLSRSLKKPLRPHfyqpdpeliidrkksrsfsrlispTAEknktglkktrsarvnpinrrktsfssgersnsfVGT 247
Cdd:cd07829 139 LADFGLARAFGIPLRTY------------------------THE---------------------------------VVT 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 248 DEYVSPEVIRGDGH-DFAVDWWALGVLTYEMMYGETPFKGKSK---------------KETFRNV------LMKEPEFAG 305
Cdd:cd07829 162 LWYRAPEILLGSKHySTAVDIWSVGCIFAELITGKPLFPGDSEidqlfkifqilgtptEESWPGVtklpdyKPTFPKWPK 241
                       330       340       350
                ....*....|....*....|....*....|
gi 15232374 306 KP---------NDLTDLIRRLLVKDPNRRL 326
Cdd:cd07829 242 NDlekvlprldPEGIDLLSKMLQYNPAKRI 271
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
25-325 3.75e-19

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


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 86.59  E-value: 3.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSssspFAVKLVP--KSSASSLRRARWEIEVLRRLSvdsnqNPFLPRllasfespeYFAW 102
Cdd:cd06626   6 NKIGEGTFGKVYTAVNLDTGEL----MAMKEIRfqDNDPKTIKEIADEMKVLEGLD-----HPNLVR---------YYGV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AV---------PYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDL 173
Cdd:cd06626  68 EVhreevyifmEYCQEGTLEELL--RHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGS 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SRSLKKPlrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrkTSFSSGERSNSFVGTDEYVSP 253
Cdd:cd06626 146 AVKLKNN----------------------------------------------------TTTMAPGEVNSLVGTPAYMAP 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVIRGD---GHDFAVDWWALGVLTYEMMYGETPFkgkskkETFRN-------VLMKEPEFAGKPNDLTDL----IRRLLV 319
Cdd:cd06626 174 EVITGNkgeGHGRAADIWSLGCVVLEMATGKRPW------SELDNewaimyhVGMGHKPPIPDSLQLSPEgkdfLSRCLE 247

                ....*.
gi 15232374 320 KDPNRR 325
Cdd:cd06626 248 SDPKKR 253
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
24-325 4.30e-19

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: 86.65  E-value: 4.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASS-LRRARWEIEVLRRLsvdsnQNPFLPRLLAS-FESPEYFA 101
Cdd:cd14046  11 LQVLGKGAFGQVVKVRNKLDGRY----YAIKKIKLRSESKnNSRILREVMLLSRL-----NHQHVVRYYQAwIERANLYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 wAVPYCSGGDLNVLLHRQN--DGVFSSSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKK 179
Cdd:cd14046  82 -QMEYCEKSTLRDLIDSGLfqDTDRLWRLFR----QILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 PLRpHFYQPdpeliidrkksrsfsrlisptaeknktGLKKTRSARvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGD 259
Cdd:cd14046 157 NVE-LATQD---------------------------INKSTSAAL-----------GSSGDLTGNVGTALYVAPEVQSGT 197
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 260 G--HDFAVDWWALGVLTYEMMYgetPFKGKSKK-ETFRNVLMKEPEFagkPNDL--------TDLIRRLLVKDPNRR 325
Cdd:cd14046 198 KstYNEKVDMYSLGIIFFEMCY---PFSTGMERvQILTALRSVSIEF---PPDFddnkhskqAKLIRWLLNHDPAKR 268
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
25-325 4.51e-19

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: 86.22  E-value: 4.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSAS---SLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd14188   7 KVLGKGGFAKCYEMTDLTTNKV----YAAKIIPHSRVSkphQREKIDKEIELHRIL-----HHKHVVQFYHYFEDKENIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQNdgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkpl 181
Cdd:cd14188  78 ILLEYCSRRSMAHILKARK--VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLA------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsARVNPI-NRRKTsfssgersnsFVGTDEYVSPEVIRGDG 260
Cdd:cd14188 149 -----------------------------------------ARLEPLeHRRRT----------ICGTPNYLSPEVLNKQG 177
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVlmKEPEFAgKPNDLT----DLIRRLLVKDPNRR 325
Cdd:cd14188 178 HGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCI--REARYS-LPSSLLapakHLIASMLSKNPEDR 243
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
25-332 4.76e-19

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: 87.03  E-value: 4.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSS----ASSLRRarwEIEVLRRLSVDSnqnpfLPRLLASFESPEYF 100
Cdd:cd14168  16 EVLGTGAFSEVVLAEE----RATGKLFAVKCIPKKAlkgkESSIEN---EIAVLRKIKHEN-----IVALEDIYESPNHL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILiqqsghvtltdfdlsrslkkp 180
Cdd:cd14168  84 YLVMQLVSGGELFDRIVEK--GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLL--------------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphFYQPDPELIIdrkksrsfsrLISptaeknKTGLKKTRsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDG 260
Cdd:cd14168 141 ----YFSQDEESKI----------MIS------DFGLSKME--------------GKGDVMSTACGTPGYVAPEVLAQKP 186
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK-----PNDLTDLIRRLLVKDPNRRLGCHRGA 332
Cdd:cd14168 187 YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPywddiSDSAKDFIRNLMEKDPNKRYTCEQAL 263
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
51-326 9.53e-19

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: 85.44  E-value: 9.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRR--ARWEIE----VLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDgvF 124
Cdd:cd14195  33 YAAKFIKKRRLSSSRRgvSREEIErevnILREI-----QHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKES--L 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 125 SSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQ----SGHVTLTDFDLSRSLKkplrphfyqpdpeliidrkksr 200
Cdd:cd14195 106 TEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDknvpNPRIKLIDFGIAHKIE---------------------- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 201 sfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYG 280
Cdd:cd14195 164 ------------------------------------AGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSG 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15232374 281 ETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14195 208 ASPFLGETKQETLTNISavnydFDEEYFSNTSELAKDFIRRLLVKDPKKRM 258
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
26-284 9.89e-19

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: 85.28  E-value: 9.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAHDVVSTSSssspFAVKLV--PKSSASSLRRAR-------WEIEVLRRLsvdsnQNPFLPRLLASFES 96
Cdd:cd06628   7 LIGSGSFGSVYLGMNASSGEL----MAVKQVelPSVSAENKDRKKsmldalqREIALLREL-----QHENIVQYLGSSSD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PEYFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd06628  78 ANHLNIFLEYVPGGSVATLL--NNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LkkplrphfyqpdpeliidrkksrsfsrlisptaEKNKTgLKKTRSARVnpinrrktsfssgersnSFVGTDEYVSPEVI 256
Cdd:cd06628 156 L---------------------------------EANSL-STKNNGARP-----------------SLQGSVFWMAPEVV 184
                       250       260
                ....*....|....*....|....*...
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd06628 185 KQTSYTRKADIWSLGCLVVEMLTGTHPF 212
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
25-326 1.18e-18

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: 84.91  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVvstsSSSSPFAVKLV--PKSSASSLRRARWEIEVLRRLSVDSnqnpfLPRLLASFESPEYFAW 102
Cdd:cd14097   7 RKLGQGSFGVVIEATHK----ETQTKWAIKKInrEKAGSSAVKLLEREVDILKHVNHAH-----IIHLEEVFETPKRMYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG-------HVTLTDFDLSR 175
Cdd:cd14097  78 VMELCEDGELKELLLRK--GFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slkkplrphfyqpdpeliidRKKSRSFSRLisptaeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEV 255
Cdd:cd14097 156 --------------------QKYGLGEDML------------------------------------QETCGTPIYMAPEV 179
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKP-NDLTD----LIRRLLVKDPNRRL 326
Cdd:cd14097 180 ISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVwQSVSDaaknVLQQLLKVDPAHRM 255
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
52-325 1.47e-18

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 84.63  E-value: 1.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLVPKSSASSLRRARwEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLnvLLHRQNDGVFSSSVIRF 131
Cdd:cd14115  22 AVKFVSKKMKKKEQAAH-EAALLQHL-----QHPQYITLHDTYESPTSYILVLELMDDGRL--LDYLMNHDELMEEKVAF 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 132 YVAEIVCALEHLHTMGIAYRDLKPENILIqqsghvtltdfdlsrSLKKPLrphfyqpdPEL-IIDRKKSrsfsrlispta 210
Cdd:cd14115  94 YIRDIMEALQYLHNCRVAHLDIKPENLLI---------------DLRIPV--------PRVkLIDLEDA----------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 211 eknktglkktrsarvnpinrrkTSFSSGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKK 290
Cdd:cd14115 140 ----------------------VQISGHRHVHHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKE 197
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15232374 291 ETFRNVLMKE----PE-FAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14115 198 ETCINVCRVDfsfpDEyFGDVSQAARDFINVILQEDPRRR 237
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
124-337 1.52e-18

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: 85.10  E-value: 1.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 124 FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSlkkplrphFYQPDPELiidrkksrsfs 203
Cdd:cd14118 112 LSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNE--------FEGDDALL----------- 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 204 rliSPTAeknktglkktrsarvnpinrrktsfssgersnsfvGTDEYVSPEVIRGDGHDF---AVDWWALGVLTYEMMYG 280
Cdd:cd14118 173 ---SSTA-----------------------------------GTPAFMAPEALSESRKKFsgkALDIWAMGVTLYCFVFG 214
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 281 ETPFKGKSKKETFRNVLMKEPEFAGKPN---DLTDLIRRLLVKDPNRRLGCHrgaaEIKE 337
Cdd:cd14118 215 RCPFEDDHILGLHEKIKTDPVVFPDDPVvseQLKDLILRMLDKNPSERITLP----EIKE 270
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
22-325 1.61e-18

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: 84.71  E-value: 1.61e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVvstsSSSSPFAVKLV---PKSSASS--LRRARWEIEVLRRLsvdsnQNPFLPRLLASFES 96
Cdd:cd06625   3 KQGKLLGQGAFGQVYLCYDA----DTGRELAVKQVeidPINTEASkeVKALECEIQLLKNL-----QHERIVQYYGCLQD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PEYFAWAVPYCSGGdlNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd06625  74 EKSLSIFMEYMPGG--SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LKkplrphfyqpdpeliidrkksrsfsrlisptAEKNKTGLKktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVI 256
Cdd:cd06625 152 LQ-------------------------------TICSSTGMK------------------------SVTGTPYWMSPEVI 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN---DLTDLIRRLLVKDPNRR 325
Cdd:cd06625 177 NGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPQLPPHvseDARDFLSLIFVRNKKQR 248
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
25-326 1.75e-18

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: 85.08  E-value: 1.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARWEIEVLRRLSVDSNqnpfLPRLLASFESPEYFAWAV 104
Cdd:cd14173   8 EVLGEGAYARVQTCINLITNKE----YAVKIIEKRPGHSRSRVFREVEMLYQCQGHRN----VLELIEFFEEEDKFYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLNVLLHRQNDgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT---LTDFDLSRSLKkpl 181
Cdd:cd14173  80 EKMRGGSILSHIHRRRH--FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSpvkICDFDLGSGIK--- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfYQPDPELIidrkksrSFSRLISPtaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRGDGH 261
Cdd:cd14173 155 ----LNSDCSPI-------STPELLTP------------------------------------CGSAEYMAPEVVEAFNE 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAV-----DWWALGVLTYEMMYGETPFKGKSKKET---------------FRNVLMKEPEFAGK-----PNDLTDLIRR 316
Cdd:cd14173 188 EASIydkrcDLWSLGVILYIMLSGYPPFVGRCGSDCgwdrgeacpacqnmlFESIQEGKYEFPEKdwahiSCAAKDLISK 267
                       330
                ....*....|
gi 15232374 317 LLVKDPNRRL 326
Cdd:cd14173 268 LLVRDAKQRL 277
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
22-325 2.66e-18

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: 83.72  E-value: 2.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKS--SASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEY 99
Cdd:cd14072   3 RLLKTIGKGNFAKVKLARHVLTGRE----VAIKIIDKTqlNPSSLQKLFREVRIMKILN-----HPNIVKLFEVIETEKT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDlnVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkk 179
Cdd:cd14072  74 LYLVMEYASGGE--VFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFS----- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrkTSFSSGERSNSFVGTDEYVSPEVIRGD 259
Cdd:cd14072 147 -----------------------------------------------------NEFTPGNKLDTFCGSPPYAAPELFQGK 173
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 GHDFA-VDWWALGVLTYEMMYGETPFKGKSKKETFRNVL---MKEPEFAGkpNDLTDLIRRLLVKDPNRR 325
Cdd:cd14072 174 KYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLrgkYRIPFYMS--TDCENLLKKFLVLNPSKR 241
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
27-328 3.28e-18

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 83.52  E-value: 3.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd14191  10 LGSGKFGQVFR----LVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCL-----HHPKLVQCVDAFEEKANIVMVLEM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDLNVLLHRQNDGVFSSSVIRfYVAEIVCALEHLHTMGIAYRDLKPENIL-IQQSG-HVTLTDFDLSRSLKkplrph 184
Cdd:cd14191  81 VSGGELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARRLE------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 185 fyqpdpeliidrkksrsfsrlisptaekNKTGLKktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIRGDGHDFA 264
Cdd:cd14191 154 ----------------------------NAGSLK------------------------VLFGTPEFVAPEVINYEPIGYA 181
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 265 VDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRLGC 328
Cdd:cd14191 182 TDMWSIGVICYILVSGLSPFMGDNDNETLANVTsatwdFDDEAFDEISDDAKDFISNLLKKDMKARLTC 250
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
27-328 3.45e-18

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: 84.30  E-value: 3.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVvstsSSSSPFAVKLVP------KSSASSLRrarwEIEVLRRLsvdsNQNPFLPRLLASFESPEYF 100
Cdd:cd07832   8 IGEGAHGIVFKAKDR----ETGETVALKKVAlrklegGIPNQALR----EIKALQAC----QGHPYVVKLRDVFPHGTGF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVLLHRQNDgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSlkkp 180
Cdd:cd07832  76 VLVFEYMLSSLSEVLRDEERP--LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARL---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfYQPDPEliidrkksrsfsRLISPTaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRG-D 259
Cdd:cd07832 150 -----FSEEDP------------RLYSHQ-----------------------------------VATRWYRAPELLYGsR 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-------MKE-PEFAGKP--NDLT------------------ 311
Cdd:cd07832 178 KYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLrtlgtpnEKTwPELTSLPdyNKITfpeskgirleeifpdcsp 257
                       330       340
                ....*....|....*....|
gi 15232374 312 ---DLIRRLLVKDPNRRLGC 328
Cdd:cd07832 258 eaiDLLKGLLVYNPKKRLSA 277
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
19-325 3.81e-18

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: 83.55  E-value: 3.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRArweieVLRRLSVD-SNQNPFLPRLLASFESP 97
Cdd:cd06605   1 DDLEYLGELGEGNGGVVSK----VRHRPSGQIMAVKVIRLEIDEALQKQ-----ILRELDVLhKCNSPYIVGFYGAFYSE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLH-TMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd06605  72 GDISICMEYMDGGSLDKILKEV--GRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQ 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LkkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarVNPInrrktsfssgerSNSFVGTDEYVSPEVI 256
Cdd:cd06605 150 L-----------------------------------------------VDSL------------AKTFVGTRSYMAPERI 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKgKSKKETFRNVL------MKEP-------EFAGkpnDLTDLIRRLLVKDPN 323
Cdd:cd06605 171 SGGKYTVKSDIWSLGLSLVELATGRFPYP-PPNAKPSMMIFellsyiVDEPppllpsgKFSP---DFQDFVSQCLQKDPT 246

                ..
gi 15232374 324 RR 325
Cdd:cd06605 247 ER 248
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
20-326 5.24e-18

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: 83.09  E-value: 5.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  20 SIKALKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEY 99
Cdd:cd14192   5 AVCPHEVLGGGRFGQVHKCTEL----STGLTLAAKIIKVKGAKEREEVKNEINIMNQLN-----HVNLIQLYDAFESKTN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFyVAEIVCALEHLHTMGIAYRDLKPENIL-IQQSGH-VTLTDFDLSRSl 177
Cdd:cd14192  76 LTLIMEYVDGGELFDRITDESYQLTELDAILF-TRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARR- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfYQPDPELiidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFssgersnsfvGTDEYVSPEVIR 257
Cdd:cd14192 154 --------YKPREKL---------------------------------------KVNF----------GTPEFLAPEVVN 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14192 177 YDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVnckwdFDAEAFENLSEEAKDFISRLLVKEKSCRM 250
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
25-327 7.59e-18

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: 82.44  E-value: 7.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLA-HDVVSTSsssspFAVKLVPKS--SASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFA 101
Cdd:cd14071   6 RTIGKGNFAVVKLArHRITKTE-----VAIKIIDKSqlDEENLKKIYREVQIMKMLN-----HPHIIKLYQVMETKDMLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkpl 181
Cdd:cd14071  76 LVTEYASNGEIFDYLAQH--GRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrkTSFSSGERSNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd14071 147 ---------------------------------------------------NFFKPGELLKTWCGSPPYAAPEVFEGKEY 175
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFA-VDWWALGVLTYEMMYGETPFKGKSKKETFRNVL---MKEPEFAGkpNDLTDLIRRLLVKDPNRRLG 327
Cdd:cd14071 176 EGPqLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLsgrFRIPFFMS--TDCEHLIRRMLVLDPSKRLT 243
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
25-284 7.92e-18

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: 82.46  E-value: 7.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAhdvvSTSSSSSPFAVKLVPKSSASSL--RRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAW 102
Cdd:cd14082   9 EVLGSGQFGIVYGG----KHRKTGRDVAIKVIDKLRFPTKqeSQLRNEVAILQQLS-----HPGVVNLECMFETPERVFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLNVLLHRQNdGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG---HVTLTDFDLSRslkk 179
Cdd:cd14082  80 VMEKLHGDMLEMILSSEK-GRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFAR---- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpelIIDRKksrSFSRlisptaeknktglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIRGD 259
Cdd:cd14082 155 -------------IIGEK---SFRR--------------------------------------SVVGTPAYLAPEVLRNK 180
                       250       260
                ....*....|....*....|....*
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd14082 181 GYNRSLDMWSVGVIIYVSLSGTFPF 205
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
22-377 9.28e-18

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: 83.34  E-value: 9.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSssssPFAVKLVPK--SSASSLRRARWEIEVLRRLsvdsnQNP--------FLPRLL 91
Cdd:cd07834   3 ELLKPIGSGAYGVVCSAYDKRTGR----KVAIKKISNvfDDLIDAKRILREIKILRHL-----KHEniiglldiLRPPSP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  92 ASFES----PEYFawavpycsGGDLNVLLHRQNDgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT 167
Cdd:cd07834  74 EEFNDvyivTELM--------ETDLHKVIKSPQP--LTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 168 LTDFDLSRSLkkplrphfyQPDPeliidrkksrsfsrlisptAEKNKTGlkktrsarvnpinrrktsfssgersnsFVGT 247
Cdd:cd07834 144 ICDFGLARGV---------DPDE-------------------DKGFLTE---------------------------YVVT 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 248 DEYVSPEVIRGDGH-DFAVDWWALGVLTYEMMYGETPFKGKS-----------------------KKETFRNVLMKEPEF 303
Cdd:cd07834 169 RWYRAPELLLSSKKyTKAIDIWSVGCIFAELLTRKPLFPGRDyidqlnlivevlgtpseedlkfiSSEKARNYLKSLPKK 248
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 304 AGKP---------NDLTDLIRRLLVKDPNRRLgchrGAAEIKELAFFAGVRWDLLTEVLRPPF-IPLRDDGELTVggFDI 373
Cdd:cd07834 249 PKKPlsevfpgasPEAIDLLEKMLVFNPKKRI----TADEALAHPYLAQLHDPEDEPVAKPPFdFPFFDDEELTI--EEL 322

                ....
gi 15232374 374 REHF 377
Cdd:cd07834 323 KELI 326
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
66-284 1.28e-17

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: 82.50  E-value: 1.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  66 RARW--EIEVLRRLSvdsNQNPFLPRLLasfeSPEYFAW--------AVPYCSGGDLNVLLHR-QNDGVFSSSVIRFYVA 134
Cdd:cd13989  37 RERWclEVQIMKKLN---HPNVVSARDV----PPELEKLspndlpllAMEYCSGGDLRKVLNQpENCCGLKESEVRTLLS 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 135 EIVCALEHLHTMGIAYRDLKPENILIQQSGhvtltdfdlSRSLKKplrphfyqpdpelIIDrkksrsfsrlisptaeknk 214
Cdd:cd13989 110 DISSAISYLHENRIIHRDLKPENIVLQQGG---------GRVIYK-------------LID------------------- 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 215 TGLKKtrsarvnpinrrktSFSSGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd13989 149 LGYAK--------------ELDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
16-326 1.47e-17

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: 81.83  E-value: 1.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVFLA-----HDVVSTSSSsspFAVKLVPKSSASSLRRarwEIEVLRRLsvdsnQNPFLPRL 90
Cdd:cd14117   3 FTIDDFDIGRPLGKGKFGNVYLArekqsKFIVALKVL---FKSQIEKEGVEHQLRR---EIEIQSHL-----RHPNILRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  91 LASFESPEYFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTD 170
Cdd:cd14117  72 YNYFHDRKRIYLILEYAPRGELYKEL--QKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIAD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 171 FDLSRSlkkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvNPINRRKTsfssgersnsFVGTDEY 250
Cdd:cd14117 150 FGWSVH-------------------------------------------------APSLRRRT----------MCGTLDY 170
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 251 VSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEF-AGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14117 171 LPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFpPFLSDGSRDLISKLLRYHPSERL 247
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
22-326 1.67e-17

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: 82.14  E-value: 1.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSssspFAVKLV----PKSSASSLRRarwEIEVLRRLSVDSNQNpfLPRLLASFESP 97
Cdd:cd06917   4 RRLELVGRGSYGAVYRGYHVKTGRV----VALKVLnldtDDDDVSDIQK---EVALLSQLKLGQPKN--IIKYYGSYLKG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQN-DGVFSSSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd06917  75 PSLWIIMDYCEGGSIRTLMRAGPiAERYIAVIMR----EVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAAS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LKkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpINRRKTSfssgersnSFVGTDEYVSPEVI 256
Cdd:cd06917 151 LN-------------------------------------------------QNSSKRS--------TFVGTPYWMAPEVI 173
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 257 R-GDGHDFAVDWWALGVLTYEMMYGETPFkgkSKKETFRNVLM----KEPEFAGK--PNDLTDLIRRLLVKDPNRRL 326
Cdd:cd06917 174 TeGKYYDTKADIWSLGITTYEMATGNPPY---SDVDALRAVMLipksKPPRLEGNgySPLLKEFVAACLDEEPKDRL 247
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
16-325 2.65e-17

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 81.72  E-value: 2.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRarweiEVLRRLSVDSN-QNPFLPRLLASF 94
Cdd:cd06620   2 LKNQDLETLKDLGAGNGGSVSK----VLHIPTGTIMAKKVIHIDAKSSVRK-----QILRELQILHEcHSPYIVSFYGAF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 --ESPEyFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTM-GIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:cd06620  73 lnENNN-IIICMEYMDCGSLDKILKKK--GPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 172 DLSRSLkkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarVNPInrrktsfssgerSNSFVGTDEYV 251
Cdd:cd06620 150 GVSGEL-----------------------------------------------INSI------------ADTFVGTSTYM 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 252 SPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLM---------------KEPEFAGKPNDLTDLIRR 316
Cdd:cd06620 171 SPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMgildllqrivnepppRLPKDRIFPKDLRDFVDR 250

                ....*....
gi 15232374 317 LLVKDPNRR 325
Cdd:cd06620 251 CLLKDPRER 259
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
52-326 2.91e-17

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: 80.84  E-value: 2.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLVPKS--SASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHrqNDGVFSSSVI 129
Cdd:cd14075  31 AIKILDKTklDQKTQRLLSREISSMEKL-----HHPNIIRLYEVVETLSKLHLVMEYASGGELYTKIS--TEGKLSESEA 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 130 RFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKplrphfyqpdpeliidrkksrsfsrlispt 209
Cdd:cd14075 104 KPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKR------------------------------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 210 aeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRgDGHDFA--VDWWALGVLTYEMMYGETPFKGK 287
Cdd:cd14075 154 ----------------------------GETLNTFCGSPPYAAPELFK-DEHYIGiyVDIWALGVLLYFMVTGVMPFRAE 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15232374 288 SKKETFRNVLMKE---PEFAgkPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14075 205 TVAKLKKCILEGTytiPSYV--SEPCQELIRGILQPVPSDRY 244
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
24-325 2.95e-17

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: 80.79  E-value: 2.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLahdvVSTSSSSSPFAVKLV--PKSSaSSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd08219   5 LRVVGEGSFGRALL----VQHVNSDQKYAMKEIrlPKSS-SAVEDSRKEAVLLAKM-----KHPNIVAFKESFEADGHLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPl 181
Cdd:cd08219  75 IVMEYCDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSP- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd08219 154 --------------------------------------------------------GAYACTYVGTPYYVPPEIWENMPY 177
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSkketFRNVLMKEPEFAGKP------NDLTDLIRRLLVKDPNRR 325
Cdd:cd08219 178 NNKSDIWSLGCILYELCTLKHPFQANS----WKNLILKVCQGSYKPlpshysYELRSLIKQMFKRNPRSR 243
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
27-284 3.88e-17

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 81.16  E-value: 3.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDvvstSSSSSPFAVKLVpKSSASSLRRARW--EIEVLRRLSvdsnqnpfLPRLLASFESPEYFA--- 101
Cdd:cd14038   2 LGTGGFGNVLRWIN----QETGEQVAIKQC-RQELSPKNRERWclEIQIMKRLN--------HPNVVAARDVPEGLQkla 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 ------WAVPYCSGGDLNVLLHR-QNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHvtltdfdls 174
Cdd:cd14038  69 pndlplLAMEYCQGGDLRKYLNQfENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQ--------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RSLKKplrphfyqpdpelIIDRKKSRSFSRlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPE 254
Cdd:cd14038 140 RLIHK-------------IIDLGYAKELDQ---------------------------------GSLCTSFVGTLQYLAPE 173
                       250       260       270
                ....*....|....*....|....*....|
gi 15232374 255 VIRGDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd14038 174 LLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
51-329 4.86e-17

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: 80.38  E-value: 4.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRR-ARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGGDL-NVLLHRQNdgvFSSSV 128
Cdd:cd14185  28 YAMKIIDKSKLKGKEDmIESEILIIKSLS-----HPNIVKLFEVYETEKEIYLILEYVRGGDLfDAIIESVK---FTEHD 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQ----SGHVTLTDFDLSRSLKKPLRphfyqpdpeliidrkksrsfsr 204
Cdd:cd14185 100 AALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHnpdkSTTLKLADFGLAKYVTGPIF---------------------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 205 lisptaeknktglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd14185 158 --------------------------------------TVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPF 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15232374 285 KG--KSKKETFRNVLMKEPEFAGKPND-----LTDLIRRLLVKDPNRRLGCH 329
Cdd:cd14185 200 RSpeRDQEELFQIIQLGHYEFLPPYWDniseaAKDLISRLLVVDPEKRYTAK 251
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
51-326 5.61e-17

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 80.40  E-value: 5.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVP----KSSASSLRRARW----EIEVLRRLSvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNdg 122
Cdd:cd14181  38 FAVKIIEvtaeRLSPEQLEEVRSstlkEIHILRQVS----GHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTEKV-- 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 123 VFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrslkkplrphfyqpdpeliidrkksrSF 202
Cdd:cd14181 112 TLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDF-----------------------------GF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 203 SRLISPtaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIR------GDGHDFAVDWWALGVLTYE 276
Cdd:cd14181 163 SCHLEP-----------------------------GEKLRELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFT 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 277 MMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14181 214 LLAGSPPFWHRRQMLMLRMIMegryqFSSPEWDDRSSTVKDLISRLLVVDPEIRL 268
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
51-326 5.98e-17

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 80.85  E-value: 5.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRRarwEIEVLRRlsvdSNQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDgvFSSSVIR 130
Cdd:cd14179  35 YAVKIVSKRMEANTQR---EIAALKL----CEGHPNIVKLHEVYHDQLHTFLVMELLKGGELLERIKKKQH--FSETEAS 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FYVAEIVCALEHLHTMGIAYRDLKPENILI---QQSGHVTLTDFDLSRslkkpLRPhfyqPDPELIidrkKSRSFsrlis 207
Cdd:cd14179 106 HIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFAR-----LKP----PDNQPL----KTPCF----- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 208 ptaeknktglkktrsarvnpinrrktsfssgersnsfvgTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGK 287
Cdd:cd14179 168 ---------------------------------------TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCH 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15232374 288 SKK-------ETFRNVLMKEPEFAGK-----PNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14179 209 DKSltctsaeEIMKKIKQGDFSFEGEawknvSQEAKDLIQGLLTVDPNKRI 259
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
25-325 6.28e-17

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: 79.89  E-value: 6.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHdVVSTSSSSSPFAVKLVPKSSASSLRRA-RWEIEVLRRLsvdsnQNPFLPRLL-ASFESPEYFAw 102
Cdd:cd00192   1 KKLGEGAFGEVYKGK-LKGGDGKTVDVAVKTLKEDASESERKDfLKEARVMKKL-----GHPNVVRLLgVCTEEEPLYL- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLNVLL--HRQNDGVFSSSVIRF-----YVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd00192  74 VMEYMEGGDLLDFLrkSRPVFPSPEPSTLSLkdllsFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SLkkplrphfyqpdpeliidrkksrsfsrlisptaeKNKTGLKKTRSARVnPInRrktsfssgersnsfvgtdeYVSPEV 255
Cdd:cd00192 154 DI----------------------------------YDDDYYRKKTGGKL-PI-R-------------------WMAPES 178
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMM-YGETPFKGKSKKETFRNVL----MKEPEFAgkPNDLTDLIRRLLVKDPNRR 325
Cdd:cd00192 179 LKDGIFTSKSDVWSFGVLLWEIFtLGATPYPGLSNEEVLEYLRkgyrLPKPENC--PDELYELMLSCWQLDPEDR 251
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
121-327 1.12e-16

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: 79.61  E-value: 1.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 121 DGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfyqpdpeliidrkksr 200
Cdd:cd14200 118 DKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQF----------------------- 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 201 sfsrlisptaEKNKTGLKKTrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRGDGHDF---AVDWWALGVLTYEM 277
Cdd:cd14200 175 ----------EGNDALLSST------------------------AGTPAFMAPETLSDSGQSFsgkALDVWAMGVTLYCF 220
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232374 278 MYGETPFKGKSKKETFRNVLMKEPEFAGKP---NDLTDLIRRLLVKDPNRRLG 327
Cdd:cd14200 221 VYGKCPFIDEFILALHNKIKNKPVEFPEEPeisEELKDLILKMLDKNPETRIT 273
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
22-326 1.16e-16

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


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 79.23  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSssspFAVKLVpKSSASSLRRARWEIEVLRRLSV-DSNQNPFLPRLLASFESPEYF 100
Cdd:cd14133   2 EVLEVLGKGTFGQVVKCYDLLTGEE----VALKII-KNNKDYLDQSLDEIRLLELLNKkDKADKYHIVRLKDVFYFKNHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSggdLNVL-LHRQNDGV-FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQqsghvtltdfDLSRSLK 178
Cdd:cd14133  77 CIVFELLS---QNLYeFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLA----------SYSRCQI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 KplrphfyqpdpelIIDrkksrsFSrlisptaeknktglkktrsarvnpinrrkTSFSSGERSNSFVGTDEYVSPEVIRG 258
Cdd:cd14133 144 K-------------IID------FG-----------------------------SSCFLTQRLYSYIQSRYYRAPEVILG 175
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 259 DGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLM---KEPEF---AGKPND--LTDLIRRLLVKDPNRRL 326
Cdd:cd14133 176 LPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGtigIPPAHmldQGKADDelFVDFLKKLLEIDPKERP 251
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
24-326 1.17e-16

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: 79.57  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstsSSSSPFAVKLVPKSSASSLRRARW--EIEVLRRLSvdsnqnpFLPRLLASFE----SP 97
Cdd:cd14131   6 LKQLGKGGSSKVYKVLN-----PKKKIYALKRVDLEGADEQTLQSYknEIELLKKLK-------GSDRIIQLYDyevtDE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQsGHVTLTDFDLSRSL 177
Cdd:cd14131  74 DDYLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKAI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyQPDpeliidrkksrsfsrlisptaeknktglkkTRSarvnpINRrktsfssgersNSFVGTDEYVSPEVIR 257
Cdd:cd14131 153 ---------QND------------------------------TTS-----IVR-----------DSQVGTLNYMSPEAIK 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 258 GDGHDFAV----------DWWALGVLTYEMMYGETPFK------GKSKKETFRNVLMKEPEFAGKpnDLTDLIRRLLVKD 321
Cdd:cd14131 178 DTSASGEGkpkskigrpsDVWSLGCILYQMVYGKTPFQhitnpiAKLQAIIDPNHEIEFPDIPNP--DLIDVMKRCLQRD 255

                ....*
gi 15232374 322 PNRRL 326
Cdd:cd14131 256 PKKRP 260
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
24-325 1.31e-16

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: 78.85  E-value: 1.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAhdvvSTSSSSSPFAVKLVP-KSSASSLRRarwEIEVLRRLsvdsnQNPFLPRLLASFESpEYFAW 102
Cdd:cd06612   8 LEKLGEGSYGSVYKA----IHKETGQVVAIKVVPvEEDLQEIIK---EISILKQC-----DSPYIVKYYGSYFK-NTDLW 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AV-PYCSGGDLNVLLHRQNDgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkpl 181
Cdd:cd06612  75 IVmEYCGAGSVSDIMKITNK-TLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVS------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfSRLISPTAEKnktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd06612 147 ---------------------GQLTDTMAKR-----------------------------NTVIGTPFWMAPEVIQEIGY 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFkgkSKKETFRNVLM---------KEPEFAGKpnDLTDLIRRLLVKDPNRR 325
Cdd:cd06612 177 NNKADIWSLGITAIEMAEGKPPY---SDIHPMRAIFMipnkppptlSDPEKWSP--EFNDFVKKCLVKDPEER 244
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
27-346 1.45e-16

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 78.91  E-value: 1.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSS---ASSLRrarwEIEVLRRLSVdsnqNPFLPRLLA-SFESPEYFAW 102
Cdd:cd13987   1 LGEGTYGKVLLAVH----KGSGTKMALKFVPKPStklKDFLR----EYNISLELSV----HPHIIKTYDvAFETEDYYVF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 AVPYCSGGDLNVLLHRQNdGVfSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG--HVTLTDFDLSRslkkp 180
Cdd:cd13987  69 AQEYAPYGDLFSIIPPQV-GL-PEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGLTR----- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaeknKTGLKKTRSARVNPinrrktsfssgersnsfvgtdeYVSPEVIRGDG 260
Cdd:cd13987 142 ---------------------------------RVGSTVKRVSGTIP----------------------YTAPEVCEAKK 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 261 HD-FAV----DWWALGVLTYEMMYGETPFKGKSKKETF--------RNVLMKEP-EFAGKPNDLTDLIRRLLVKDPNRRl 326
Cdd:cd13987 167 NEgFVVdpsiDVWAFGVLLFCCLTGNFPWEKADSDDQFyeefvrwqKRKNTAVPsQWRRFTPKALRMFKKLLAPEPERR- 245
                       330       340
                ....*....|....*....|
gi 15232374 327 gchrgaAEIKELAFFAGVRW 346
Cdd:cd13987 246 ------CSIKEVFKYLGDRW 259
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
52-326 1.52e-16

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: 78.96  E-value: 1.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLVPKSS-ASSLRRARWEIEVLRRLSvdsNQNpfLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDgvFSSSVIR 130
Cdd:cd14078  32 AIKIMDKKAlGDDLPRVKTEIEALKNLS---HQH--ICRLYHVIETDNKIFMVLEYCPGGELFDYIVAKDR--LSEDEAR 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLsrslkkplrphfyqpdpeliidrkksrsfsrlisptA 210
Cdd:cd14078 105 VFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGL------------------------------------C 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 211 EKNKTGLKktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEVIRGD---GHDfaVDWWALGVLTYEMMYGETPFKGK 287
Cdd:cd14078 149 AKPKGGMD--------------------HHLETCCGSPAYAAPELIQGKpyiGSE--ADVWSMGVLLYALLCGFLPFDDD 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15232374 288 SKKETFRNVL---MKEPEFAGKpnDLTDLIRRLLVKDPNRRL 326
Cdd:cd14078 207 NVMALYRKIQsgkYEEPEWLSP--SSKLLLDQMLQVDPKKRI 246
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
27-326 1.93e-16

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: 79.00  E-value: 1.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVflaHDVVSTSSSSSpFAVKLV--PKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd14086   9 LGKGAFSVV---RRCVQKSTGQE-FAAKIIntKKLSARDHQKLEREARICRLL-----KHPNIVRLHDSISEEGFHYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLnvllhrqndgvFSSSVIRFYVAE---------IVCALEHLHTMGIAYRDLKPENILI---QQSGHVTLTDFD 172
Cdd:cd14086  80 DLVTGGEL-----------FEDIVAREFYSEadashciqqILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 173 LSrslkkplrphfyqpdpeLIIDRKKSRSFSrlisptaeknktglkktrsarvnpinrrktsfssgersnsFVGTDEYVS 252
Cdd:cd14086 149 LA-----------------IEVQGDQQAWFG----------------------------------------FAGTPGYLS 171
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 253 PEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14086 172 PEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKagaydYPSPEWDTVTPEAKDLINQMLTVNPAKRI 250
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
110-326 2.01e-16

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 78.67  E-value: 2.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 110 GDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkplrphfyqpd 189
Cdd:cd14165  87 GDLLEFIKLR--GALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCL----------- 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 190 peliidrkksrsfsrlispTAEKNKTGLKKTrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDFAV-DWW 268
Cdd:cd14165 154 -------------------RDENGRIVLSKT-----------------------FCGSAAYAAPEVLQGIPYDPRIyDIW 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374 269 ALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN---DLTDLIRRLLVKDPNRRL 326
Cdd:cd14165 192 SLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNltsECKDLIYRLLQPDVSQRL 252
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
51-326 2.07e-16

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: 78.83  E-value: 2.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSsassLRRARWEIEVLRRLSvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDL--NVLLHRQndgvFSSSV 128
Cdd:cd14091  28 YAVKIIDKS----KRDPSEEIEILLRYG----QHPNIITLRDVYDDGNSVYLVTELLRGGELldRILRQKF----FSERE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH----VTLTDFDLSrslkKPLRphfyqpdpeliidrkksrsfsr 204
Cdd:cd14091  96 ASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFA----KQLR---------------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 205 lisptAEknkTGLKKTrsarvnPINrrktsfssgersnsfvgTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd14091 150 -----AE---NGLLMT------PCY-----------------TANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPF 198
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15232374 285 KgKSKKETFRNVL---------MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14091 199 A-SGPNDTPEVILarigsgkidLSGGNWDHVSDSAKDLVRKMLHVDPSQRP 248
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
84-326 2.23e-16

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 78.36  E-value: 2.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   84 NPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQS 163
Cdd:PHA03390  68 NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLL--KKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  164 -GHVTLTDFDLSRSLKKPlrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGErsn 242
Cdd:PHA03390 146 kDRIYLCDYGLCKIIGTP-------------------------------------------------------SCYD--- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  243 sfvGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKgKSKKETFRNVLMKE------PEFAGKPNDLTDLIRR 316
Cdd:PHA03390 168 ---GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFK-EDEDEELDLESLLKrqqkklPFIKNVSKNANDFVQS 243
                        250
                 ....*....|
gi 15232374  317 LLVKDPNRRL 326
Cdd:PHA03390 244 MLKYNINYRL 253
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
24-325 2.89e-16

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: 78.08  E-value: 2.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSS---SSSPFAVKLVPKSSASslrraRWEIEVLRRLsvdsnQNPFLPRLLASFESPEYF 100
Cdd:cd08225   5 IKKIGEGSFGKIYLAKAKSDSEHcviKEIDLTKMPVKEKEAS-----KKEVILLAKM-----KHPNIVTFFASFQENGRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT-LTDFDLSRSLKk 179
Cdd:cd08225  75 FIVMEYCDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAkLGDFGIARQLN- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGD 259
Cdd:cd08225 154 --------------------------------------------------------DSMELAYTCVGTPYYLSPEICQNR 177
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPFKGKSkketFRNVLMK------EPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd08225 178 PYNNKTDIWSLGCVLYELCTLKHPFEGNN----LHQLVLKicqgyfAPISPNFSRDLRSLISQLFKVSPRDR 245
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
106-325 3.94e-16

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: 77.47  E-value: 3.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkplrphf 185
Cdd:cd08221  80 YCNGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLD------- 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDGHDFAV 265
Cdd:cd08221 153 --------------------------------------------------SESSMAESIVGTPYYMSPELVQGVKYNFKS 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 266 DWWALGVLTYEMMygetpfkgkSKKETFR--------------NVLMKEPEFAgkpNDLTDLIRRLLVKDPNRR 325
Cdd:cd08221 183 DIWAVGCVLYELL---------TLKRTFDatnplrlavkivqgEYEDIDEQYS---EEIIQLVHDCLHQDPEDR 244
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
27-326 4.89e-16

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: 77.59  E-value: 4.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVflaHDVVSTSSSSSpFAVKLVpKSSASSLRRARWEIEVLRRLsvdsNQNPFLpRLLASFESPEYFAWAVPY 106
Cdd:cd14104   8 LGRGQFGIV---HRCVETSSKKT-YMAKFV-KVKGADQVLVKKEISILNIA----RHRNIL-RLHESFESHEELVMIFEF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDLnvlLHRQNDGVF--SSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ--QSGHVTLTDFDLSRSLKkplr 182
Cdd:cd14104  78 ISGVDI---FERITTARFelNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCtrRGSYIKIIEFGQSRQLK---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnPINRRKTSFSSGersnsfvgtdEYVSPEVIRGDGHD 262
Cdd:cd14104 151 --------------------------------------------PGDKFRLQYTSA----------EFYAPEVHQHESVS 176
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 263 FAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPND-----LTDLIRRLLVKDPNRRL 326
Cdd:cd14104 177 TATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKnisieALDFVDRLLVKERKSRM 245
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
24-325 4.97e-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: 77.47  E-value: 4.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSSSspfaVKLVPKSSASSLRR--ARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFA 101
Cdd:cd08220   5 IRVVGRGAYGTVYLCRRKDDNKLVI----IKQIPVEQMTKEERqaALNEVKVLSMLH-----HPNIIEYYESFLEDKALM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH-VTLTDFDLSRSLkkp 180
Cdd:cd08220  76 IVMEYAPGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKIL--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDG 260
Cdd:cd08220 153 -------------------------------------------------------SSKSKAYTVVGTPCYISPELCEGKP 177
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGkskkETFRNVLMK------EPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd08220 178 YNQKSDIWALGCVLYELASLKRAFEA----ANLPALVLKimrgtfAPISDRYSEELRHLILSMLHLDPNKR 244
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
24-325 5.54e-16

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: 77.16  E-value: 5.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRR--ARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd08218   5 IKKIGEGSFGKALL----VKSKEDGKQYVIKEINISKMSPKEReeSRKEVAVLSKM-----KHPNIVQYQESFEENGNLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkpl 181
Cdd:cd08218  76 IVMDYCDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLN--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd08218 153 ------------------------------------------------------STVELARTCIGTPYYLSPEICENKPY 178
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKetfrNVLMK------EPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd08218 179 NNKSDIWALGCVLYEMCTLKHAFEAGNMK----NLVLKiirgsyPPVPSRYSYDLRSLVSQLFKRNPRDR 244
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
17-327 7.42e-16

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: 77.04  E-value: 7.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  17 DLDSIKALKILGKGATGTVFLA--HDVvstsssssPFAVKLVPKSSASSLRRARWEIEvlrrLSVDSNQNPFLPRLLA-- 92
Cdd:cd13979   1 DWEPLRLQEPLGSGGFGSVYKAtyKGE--------TVAVKIVRRRRKNRASRQSFWAE----LNAARLRHENIVRVLAae 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  93 SFESPEYFAWAV-PYCSGGDLNVLLHRQNDGVFSSSVIRfYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:cd13979  69 TGTDFASLGLIImEYCGNGTLQQLIYEGSEPLPLAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 172 DLSRSLKKPLrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYV 251
Cdd:cd13979 148 GCSVKLGEGN------------------------------------------------------EVGTPRSHIGGTYTYR 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 252 SPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKsKKETFRNVLMKE--PEFAGKPNDLT-----DLIRRLLVKDPNR 324
Cdd:cd13979 174 APELLKGERVTPKADIYSFGITLWQMLTRELPYAGL-RQHVLYAVVAKDlrPDLSGLEDSEFgqrlrSLISRCWSAQPAE 252

                ...
gi 15232374 325 RLG 327
Cdd:cd13979 253 RPN 255
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
51-326 9.21e-16

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 76.88  E-value: 9.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLV---PKSSASS-----LRRARW-EIEVLRRLSVDSNqnpfLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNd 121
Cdd:cd14182  31 YAVKIIditGGGSFSPeevqeLREATLkEIDILRKVSGHPN----IIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKV- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 122 gVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrslkkplrphfyqpdpeliidrkksrS 201
Cdd:cd14182 106 -TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDF-----------------------------G 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 202 FSRLISPtaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIR------GDGHDFAVDWWALGVLTY 275
Cdd:cd14182 156 FSCQLDP-----------------------------GEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMY 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 276 EMMYGETPFKGKSKKETFRNVLMKE-----PEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14182 207 TLLAGSPPFWHRKQMLMLRMIMSGNyqfgsPEWDDRSDTVKDLISRFLVVQPQKRY 262
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
24-327 1.04e-15

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: 76.72  E-value: 1.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRR---------ARWEIEVLRRLSVDSNQN-PFLPRLLAS 93
Cdd:cd14077   6 VKTIGAGSMGKVKLAKHIRTGEK----CAIKIIPRASNAGLKKerekrlekeISRDIRTIREAALSSLLNhPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 FESPEYFAWAVPYCSGGD-LNVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFD 172
Cdd:cd14077  82 LRTPNHYYMLFEYVDGGQlLDYIISH---GKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 173 LSrslkkplrpHFYQPDPELiidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVS 252
Cdd:cd14077 159 LS---------NLYDPRRLL-------------------------------------------------RTFCGSLYFAA 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 253 PEVIRGD---GHDfaVDWWALGVLTYEMMYGETPF----------KGKSKKETFRNVLMKEpefagkpndLTDLIRRLLV 319
Cdd:cd14077 181 PELLQAQpytGPE--VDVWSFGVVLYVLVCGKVPFddenmpalhaKIKKGKVEYPSYLSSE---------CKSLISRMLV 249

                ....*...
gi 15232374 320 KDPNRRLG 327
Cdd:cd14077 250 VDPKKRAT 257
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
22-326 1.17e-15

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: 76.80  E-value: 1.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLA-----HDVVstssssspfAVKLVPKSSAS-----SLRrarwEIEVLRRLsvdsNQNPFLPRLL 91
Cdd:cd07830   2 KVIKQLGDGTFGSVYLArnketGELV---------AIKKMKKKFYSweecmNLR----EVKSLRKL----NEHPNIVKLK 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  92 ASF-ESPE-YFawaVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLT 169
Cdd:cd07830  65 EVFrENDElYF---VFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 170 DFDLSRSLKKplRPHFyqpdpeliidrkksrsfsrlispTAeknktglkktrsarvnpinrrktsfssgersnsFVGTDE 249
Cdd:cd07830 142 DFGLAREIRS--RPPY-----------------------TD---------------------------------YVSTRW 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 250 YVSPEVI-RGDGHDFAVDWWALGVLTYEMMYGETPFKGKS---------------KKETF-------RNVLMKEPEFAGK 306
Cdd:cd07830 164 YRAPEILlRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSeidqlykicsvlgtpTKQDWpegyklaSKLGFRFPQFAPT 243
                       330       340
                ....*....|....*....|....*....
gi 15232374 307 P---------NDLTDLIRRLLVKDPNRRL 326
Cdd:cd07830 244 SlhqlipnasPEAIDLIKDMLRWDPKKRP 272
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
25-325 1.21e-15

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: 76.51  E-value: 1.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSS-ASSLRRARWEIEVLRRLSVDsnqNPFLPRLLASFESPEYFAWA 103
Cdd:cd14187  13 RFLGKGGFAKCYEITDA----DTKEVFAGKIVPKSLlLKPHQKEKMSMEIAIHRSLA---HQHVVGFHGFFEDNDFVYVV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLnVLLHRQNDGVfSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkplrp 183
Cdd:cd14187  86 LELCRRRSL-LELHKRRKAL-TEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVE----- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd14187 159 ----------------------------------------------------YDGERKKTLCGTPNYIAPEVLSKKGHSF 186
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPNDL-TDLIRRLLVKDPNRR 325
Cdd:cd14187 187 EVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVaASLIQKMLQTDPTAR 249
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
17-344 1.55e-15

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: 76.61  E-value: 1.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  17 DLDSIKALKI---LGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRARWEIEVLRrlsvdSNQNPFLPRLLAS 93
Cdd:cd06644   7 DLDPNEVWEIigeLGDGAFGKVYKAKN----KETGALAAAKVIETKSEEELEDYMVEIEILA-----TCNHPYIVKLLGA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 FESPEYFAWAVPYCSGGDLNVLLHRQNDGVfSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDL 173
Cdd:cd06644  78 FYWDGKLWIMIEFCPGGAVDAIMLELDRGL-TEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SRSLKKPLrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSP 253
Cdd:cd06644 157 SAKNVKTL---------------------------------------------------------QRRDSFIGTPYWMAP 179
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVI-----RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN----DLTDLIRRLLVKDPNR 324
Cdd:cd06644 180 EVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQPSkwsmEFRDFLKTALDKHPET 259
                       330       340
                ....*....|....*....|
gi 15232374 325 RlgchRGAAEIKELAFFAGV 344
Cdd:cd06644 260 R----PSAAQLLEHPFVSSV 275
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
25-326 2.36e-15

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: 75.35  E-value: 2.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSS-ASSLRRARW--EIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd14189   7 RLLGKGGFARCYEMTDLATNKT----YAVKVIPHSRvAKPHQREKIvnEIELHRDL-----HHKHVVKFSHHFEDAENIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQNdgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLsrslkkpl 181
Cdd:cd14189  78 IFLELCSRKSLAHIWKARH--TLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGL-------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaeknktglkktrSARVNPINRRKtsfssgersNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd14189 148 ----------------------------------------AARLEPPEQRK---------KTICGTPNYLAPEVLLRQGH 178
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVlmKEPEFAgKPNDLT----DLIRRLLVKDPNRRL 326
Cdd:cd14189 179 GPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCI--KQVKYT-LPASLSlparHLLAGILKRNPGDRL 244
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
51-326 2.60e-15

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: 75.83  E-value: 2.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSasslRRARWEIEVLRRLSvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNdgVFSSSVIR 130
Cdd:cd14175  29 YAVKVIDKSK----RDPSEEIEILLRYG----QHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQK--FFSEREAS 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FYVAEIVCALEHLHTMGIAYRDLKPENIL-IQQSGH---VTLTDFDLSRSLKKplrphfyqpdpeliidrkksrsfsrli 206
Cdd:cd14175  99 SVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRA--------------------------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 207 sptaeknKTGLKKTRSARVNpinrrktsfssgersnsfvgtdeYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFkG 286
Cdd:cd14175 152 -------ENGLLMTPCYTAN-----------------------FVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPF-A 200
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15232374 287 KSKKETFRNVLMK--EPEFA---GKPNDLT----DLIRRLLVKDPNRRL 326
Cdd:cd14175 201 NGPSDTPEEILTRigSGKFTlsgGNWNTVSdaakDLVSKMLHVDPHQRL 249
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
25-299 2.96e-15

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: 75.50  E-value: 2.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVvstsSSSSPFAVKLV--PKSSA---SSLRRA-----RWEIEVLRRLsvdsnQNPFLPRLLASF 94
Cdd:cd06629   7 ELIGKGTYGRVYLAMNA----TTGEMLAVKQVelPKTSSdraDSRQKTvvdalKSEIDTLKDL-----DHPNIVQYLGFE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd06629  78 ETEDYFSIFLEYVPGGSIGSCLRKY--GKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGIS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RSLKkplrpHFYqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPE 254
Cdd:cd06629 156 KKSD-----DIY--------------------------------------------------GNNGATSMQGSVFWMAPE 180
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15232374 255 VI--RGDGHDFAVDWWALGVLTYEMMYGETPFkgkSKKETFRnVLMK 299
Cdd:cd06629 181 VIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPW---SDDEAIA-AMFK 223
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
24-175 3.28e-15

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: 75.39  E-value: 3.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVK--LVPKSSA----SSLRrarwEIEVLRRLsvDSNQNPFLPRLLASFESP 97
Cdd:cd07838   4 VAEIGEGAYGTVYKARDLQDGRF----VALKkvRVPLSEEgiplSTIR----EIALLKQL--ESFEHPNVVRLLDVCHGP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 ------------EYFAWavpycsggDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH 165
Cdd:cd07838  74 rtdrelkltlvfEHVDQ--------DLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQ 145
                       170
                ....*....|
gi 15232374 166 VTLTDFDLSR 175
Cdd:cd07838 146 VKLADFGLAR 155
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
17-325 4.29e-15

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 74.75  E-value: 4.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  17 DLDSIKALKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARWEIEVLRRLSvdsNQNpfLPRLLASFES 96
Cdd:cd06624   6 EYDESGERVVLGKGTFGVVYAARDLSTQVR----IAIKEIPERDSREVQPLHEEIALHSRLS---HKN--IVQYLGSVSE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PEYFAWAVPYCSGGDLNVLLhRQNDG--VFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQ-SGHVTLTDFDL 173
Cdd:cd06624  77 DGFFKIFMEQVPGGSLSALL-RSKWGplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SRSLkkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsARVNPInrrktsfssgerSNSFVGTDEYVSP 253
Cdd:cd06624 156 SKRL---------------------------------------------AGINPC------------TETFTGTLQYMAP 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVI-RGD-GHDFAVDWWALGVLTYEMMYGETPF--KGKSKKETFRNVLMKE-PEFagkPNDLTDLIRRLLVK----DPNR 324
Cdd:cd06624 179 EVIdKGQrGYGPPADIWSLGCTIIEMATGKPPFieLGEPQAAMFKVGMFKIhPEI---PESLSEEAKSFILRcfepDPDK 255

                .
gi 15232374 325 R 325
Cdd:cd06624 256 R 256
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
20-341 4.74e-15

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: 75.23  E-value: 4.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  20 SIKALKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSsasslRRAR-WEIEVLRRLsvdsnQNPFLPRLLASFESPE 98
Cdd:cd14137   5 SYTIEKVIGSGSFGVVYQAKLL----ETGEVVAIKKVLQD-----KRYKnRELQIMRRL-----KHPNIVKLKYFFYSSG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 yfawavpyCSGGD--LNVLL-------------HRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI-QQ 162
Cdd:cd14137  71 --------EKKDEvyLNLVMeympetlyrvirhYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdPE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 163 SGHVTLTDFDlsrSLKKPLRphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSN 242
Cdd:cd14137 143 TGVLKLCDFG---SAKRLVP-------------------------------------------------------GEPNV 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 243 SFVGTDEYVSPEVIRGDGH-DFAVDWWALG-VLTyEMMYGETPFKGKS---------------KKETFR--NVLMKEPEF 303
Cdd:cd14137 165 SYICSRYYRAPELIFGATDyTTAIDIWSAGcVLA-ELLLGQPLFPGESsvdqlveiikvlgtpTREQIKamNPNYTEFKF 243
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15232374 304 -------------AGKPNDLTDLIRRLLVKDPNRRLgchrGAAEIKELAFF 341
Cdd:cd14137 244 pqikphpwekvfpKRTPPDAIDLLSKILVYNPSKRL----TALEALAHPFF 290
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
106-291 5.65e-15

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: 74.66  E-value: 5.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG---------HVTLTDFDLSRS 176
Cdd:cd14202  82 YCNGGDLADYLHTM--RTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFARY 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LKkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVI 256
Cdd:cd14202 160 LQ----------------------------------------------------------NNMMAATLCGSPMYMAPEVI 181
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKE 291
Cdd:cd14202 182 MSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD 216
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
19-330 7.46e-15

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 74.38  E-value: 7.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVflahDVVSTSSSSSPFAVKLVPKSSASSLRRarweiEVLRRLSVD-SNQNPFLPRLLASF--E 95
Cdd:cd06621   1 DKIVELSSLGEGAGGSV----TKCRLRNTKTIFALKTITTDPNPDVQK-----QILRELEINkSCASPYIVKYYGAFldE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLH--RQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDL 173
Cdd:cd06621  72 QDSSIGIAMEYCEGGSLDSIYKkvKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SrslkkplrphfyqpdPELIidrkksrsfsrlisptaeknktglkktrsarvnpinrrkTSFSSgersnSFVGTDEYVSP 253
Cdd:cd06621 152 S---------------GELV---------------------------------------NSLAG-----TFTGTSYYMAP 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKK-----ETFRNVL-MKEPEFAGKPND-------LTDLIRRLLVK 320
Cdd:cd06621 173 ERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIVnMPNPELKDEPENgikwsesFKDFIEKCLEK 252
                       330
                ....*....|
gi 15232374 321 DPNRRLGCHR 330
Cdd:cd06621 253 DGTRRPGPWQ 262
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
27-342 8.51e-15

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: 74.01  E-value: 8.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSSsspfAVKLVPKSSASSLRRARWEIEVLrrlsvDSNQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFA----AAKIIQIESEEELEDFMVEIDIL-----SECKHPNIVGLYEAYFYENKLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLrphfy 186
Cdd:cd06611  84 CDGGALDSIM-LELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTL----- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 187 qpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEVI-----RGDGH 261
Cdd:cd06611 158 ----------------------------------------------------QKRDTFIGTPYWMAPEVVacetfKDNPY 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN----DLTDLIRRLLVKDPNRRLGChrgaAEIKE 337
Cdd:cd06611 186 DYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQPSkwssSFNDFLKSCLVKDPDDRPTA----AELLK 261

                ....*
gi 15232374 338 LAFFA 342
Cdd:cd06611 262 HPFVS 266
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
27-325 9.44e-15

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: 73.91  E-value: 9.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSSsspfAVKLVPKSSASSLRRARWEIEVLRrlsvdSNQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd06643  13 LGDGAFGKVYKAQNKETGILA----AAKVIDTKSEEELEDYMVEIDILA-----SCDHPNIVKLLDAFYYENNLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDLN-VLLHRQNDgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplrphf 185
Cdd:cd06643  84 CAGGAVDaVMLELERP--LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSA---------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yqpdpeliidrkksrsfsrlisptaeknktglKKTRSArvnpinrrktsfssgERSNSFVGTDEYVSPEVI-----RGDG 260
Cdd:cd06643 152 --------------------------------KNTRTL---------------QRRDSFIGTPYWMAPEVVmcetsKDRP 184
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN----DLTDLIRRLLVKDPNRR 325
Cdd:cd06643 185 YDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQPSrwspEFKDFLRKCLEKNVDAR 253
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
70-325 9.80e-15

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: 73.91  E-value: 9.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLL---HRQNDGVFSSSVIRFYVaEIVCALEHLHTM 146
Cdd:cd08228  52 EIDLLKQLN-----HPNVIKYLDSFIEDNELNIVLELADAGDLSQMIkyfKKQKRLIPERTVWKYFV-QLCSAVEHMHSR 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 147 GIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplrphFYQpdpeliidrkksrsfsrlisptaeknktglKKTRSArvn 226
Cdd:cd08228 126 RVMHRDIKPANVFITATGVVKLGDLGLGR---------FFS------------------------------SKTTAA--- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 227 pinrrktsfssgersNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGK 306
Cdd:cd08228 164 ---------------HSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPL 228
                       250       260
                ....*....|....*....|....
gi 15232374 307 PND-----LTDLIRRLLVKDPNRR 325
Cdd:cd08228 229 PTEhysekLRELVSMCIYPDPDQR 252
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
25-326 1.03e-14

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: 73.48  E-value: 1.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFlahdVVSTSSSSSPFAVKLVPKSsasslRRARWEIEVLRRLS--------VDSNQNPFLPR--LLASF 94
Cdd:cd14089   7 QVLGLGINGKVL----ECFHKKTGEKFALKVLRDN-----PKARREVELHWRASgcphivriIDVYENTYQGRkcLLVVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEyfawavpycsGGDLNVLLHRQNDGVFS----SSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILI---QQSGHVT 167
Cdd:cd14089  78 ECME----------GGELFSRIQERADSAFTereaAEIMR----QIGSAVAHLHSMNIAHRDLKPENLLYsskGPNAILK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 168 LTDFDLSRslkkplrphfyqpdpelIIDRKKSrsfsrLISPTAeknktglkktrsarvnpinrrktsfssgersnsfvgT 247
Cdd:cd14089 144 LTDFGFAK-----------------ETTTKKS-----LQTPCY------------------------------------T 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 248 DEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPF---KGKSKKETFRNVLMK------EPEFAGKPNDLTDLIRRLL 318
Cdd:cd14089 166 PYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnHGLAISPGMKKRIRNgqyefpNPEWSNVSEEAKDLIRGLL 245

                ....*...
gi 15232374 319 VKDPNRRL 326
Cdd:cd14089 246 KTDPSERL 253
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
51-326 1.24e-14

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: 74.29  E-value: 1.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSasslRRARWEIEVLRRLSvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNdgVFSSSVIR 130
Cdd:cd14176  47 FAVKIIDKSK----RDPTEEIEILLRYG----QHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQK--FFSEREAS 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FYVAEIVCALEHLHTMGIAYRDLKPENIL-IQQSGH---VTLTDFDLSRSLKKplrphfyqpdpeliidrkksrsfsrli 206
Cdd:cd14176 117 AVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRA--------------------------- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 207 sptaeknKTGLKKTRSARVNpinrrktsfssgersnsfvgtdeYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFkG 286
Cdd:cd14176 170 -------ENGLLMTPCYTAN-----------------------FVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPF-A 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15232374 287 KSKKETFRNVLMK--EPEFA-------GKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14176 219 NGPDDTPEEILARigSGKFSlsggywnSVSDTAKDLVSKMLHVDPHQRL 267
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
24-329 1.41e-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: 1.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLA-----HDVVstssssspfAVK--LVPKSSASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFES 96
Cdd:cd07833   6 LGVVGEGAYGVVLKCrnkatGEIV---------AIKkfKESEDDEDVKKTALREVKVLRQLR-----HENIVNLKEAFRR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PEYFAWAVPYCsggDLNVL--LHRQNDGVfSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd07833  72 KGRLYLVFEYV---ERTLLelLEASPGGL-PPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RSLKKPLRPHFyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPE 254
Cdd:cd07833 148 RALTARPASPL--------------------------------------------------------TDYVATRWYRAPE 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 255 VIRGDG-HDFAVDWWALGVLTYEMMYGETPFKGKSKKE---TFRNVL------------------------MKEPE---- 302
Cdd:cd07833 172 LLVGDTnYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDqlyLIQKCLgplppshqelfssnprfagvafpePSQPEsler 251
                       330       340
                ....*....|....*....|....*....
gi 15232374 303 -FAGKPND-LTDLIRRLLVKDPNRRLGCH 329
Cdd:cd07833 252 rYPGKVSSpALDFLKACLRMDPKERLTCD 280
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
25-325 1.58e-14

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: 73.47  E-value: 1.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLS--------VDSNQNPFLPRllasfes 96
Cdd:cd14037   9 KYLAEGGFAHVYLVKT----SNGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSghknivgyIDSSANRSGNG------- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 peyfAWAV----PYCSGGDL-NVLLHRQNDGVFSSSVIRFY--VAEIVCALEHLHTMgIAYRDLKPENILIQQSGHVTLT 169
Cdd:cd14037  78 ----VYEVlllmEYCKGGGViDLMNQRLQTGLTESEILKIFcdVCEAVAAMHYLKPP-LIHRDLKVENVLISDSGNYKLC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 170 DFDlsrSLKKPLRPhfyqpdpeliidrkksrsfsrlisPTAEKNKTGLKKTrsarvnpINRRKTSfssgersnsfvgtdE 249
Cdd:cd14037 153 DFG---SATTKILP------------------------PQTKQGVTYVEED-------IKKYTTL--------------Q 184
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 250 YVSPEVI---RGDGHDFAVDWWALGVLTYEMMYGETPFkGKSKKETFRNVLMKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14037 185 YRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPF-EESGQLAILNGNFTFPDNSRYSKRLHKLIRYMLEEDPEKR 262
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
27-318 1.69e-14

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: 73.04  E-value: 1.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARWEIEVLRRlsvdsNQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd06647  15 IGQGASGTVYTAIDVATGQE----VAIKQMNLQQQPKKELIINEILVMRE-----NKNPNIVNYLDSYLVGDELWVVMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDL-NVLLHRQNDGVFSSSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrslkkplrphf 185
Cdd:cd06647  86 LAGGSLtDVVTETCMDEGQIAAVCR----ECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yqpdpeliidrkksrSFSRLISPTAEKNKTglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDFAV 265
Cdd:cd06647 148 ---------------GFCAQITPEQSKRST----------------------------MVGTPYWMAPEVVTRKAYGPKV 184
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15232374 266 DWWALGVLTYEMMYGETPFKGKSK-KETFRNVLMKEPEFAGkPNDLTDLIRRLL 318
Cdd:cd06647 185 DIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQN-PEKLSAIFRDFL 237
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
24-325 1.87e-14

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: 73.12  E-value: 1.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSSsspfAVK---LVPKSS----ASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFE- 95
Cdd:cd13990   5 LNLLGKGGFSEVYKAFDLVEQRYV----ACKihqLNKDWSeekkQNYIKHALREYEIHKSL-----DHPRIVKLYDVFEi 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTM--GIAYRDLKPENILI---QQSGHVTLTD 170
Cdd:cd13990  76 DTDSFCTVLEYCDGNDLDFYLKQH--KSIPEREARSIIMQVVSALKYLNEIkpPIIHYDLKPGNILLhsgNVSGEIKITD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 171 FDLSRslkkplrphfyqpdpeliidrkksrsfsrlISPTAEKNKTGLKKTRsarvnpinrrktsfssgersnSFVGTDEY 250
Cdd:cd13990 154 FGLSK------------------------------IMDDESYNSDGMELTS---------------------QGAGTYWY 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 251 VSPEV-IRGDGH---DFAVDWWALGVLTYEMMYGETPF--KGKSKKETFRNVLMK--EPEFAGKP---NDLTDLIRRLLV 319
Cdd:cd13990 183 LPPECfVVGKTPpkiSSKVDVWSVGVIFYQMLYGRKPFghNQSQEAILEENTILKatEVEFPSKPvvsSEAKDFIRRCLT 262

                ....*.
gi 15232374 320 KDPNRR 325
Cdd:cd13990 263 YRKEDR 268
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
51-326 1.95e-14

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 73.12  E-value: 1.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSasslRRARWEIEVLRRLSvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNdgVFSSSVIR 130
Cdd:cd14178  31 YAVKIIDKSK----RDPSEEIEILLRYG----QHPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQK--CFSEREAS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FYVAEIVCALEHLHTMGIAYRDLKPENIL-IQQSGH---VTLTDFDLSRSLKKplrphfyqpdpeliidrkksrsfsrli 206
Cdd:cd14178 101 AVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRA--------------------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 207 sptaeknKTGLKKTRSARVNpinrrktsfssgersnsfvgtdeYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFkG 286
Cdd:cd14178 154 -------ENGLLMTPCYTAN-----------------------FVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPF-A 202
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15232374 287 KSKKETFRNVLMK--EPEFA---GKPNDLT----DLIRRLLVKDPNRRL 326
Cdd:cd14178 203 NGPDDTPEEILARigSGKYAlsgGNWDSISdaakDIVSKMLHVDPHQRL 251
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
24-325 2.01e-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: 72.47  E-value: 2.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRR--ARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd08223   5 LRVIGKGSYGEVWL----VRHKRDRKQYVIKKLNLKNASKRERkaAEQEAKLLSKL-----KHPNIVSYKESFEGEDGFL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 W-AVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkp 180
Cdd:cd08223  76 YiVMGFCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLE-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDG 260
Cdd:cd08223 154 -------------------------------------------------------SSSDMATTLIGTPYYMSPELFSNKP 178
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKE-TFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRR 325
Cdd:cd08223 179 YNHKSDVWALGCCVYEMATLKHAFNAKDMNSlVYKILEGKLPPMPKQySPELGELIKAMLHQDPEKR 245
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
70-326 2.65e-14

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: 72.73  E-value: 2.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIA 149
Cdd:cd14201  55 EIKILKEL-----QHENIVALYDVQEMPNSVFLVMEYCNGGDLADYL--QAKGTLSEDTIRVFLQQIAAAMRILHSKGII 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 150 YRDLKPENILIQQSGhvtltdfdlsrslkkplrphfyqpdpeliidRKKSrsfsrlisptaekNKTGLKktrsarvnpIN 229
Cdd:cd14201 128 HRDLKPQNILLSYAS-------------------------------RKKS-------------SVSGIR---------IK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 230 RRKTSFSSGERSN----SFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKK------ETFRNVLMK 299
Cdd:cd14201 155 IADFGFARYLQSNmmaaTLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQdlrmfyEKNKNLQPS 234
                       250       260
                ....*....|....*....|....*..
gi 15232374 300 EPEFAGKpnDLTDLIRRLLVKDPNRRL 326
Cdd:cd14201 235 IPRETSP--YLADLLLGLLQRNQKDRM 259
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
109-326 3.00e-14

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: 72.33  E-value: 3.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 109 GGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI---QQSGHVTLTDFDLSR--SLKKPLRP 183
Cdd:cd14172  85 GGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKetTVQNALQT 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 HFYQPdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnsfvgtdEYVSPEVIRGDGHDF 263
Cdd:cd14172 165 PCYTP------------------------------------------------------------YYVAPEVLGPEKYDK 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 264 AVDWWALGVLTYEMMYGETPFKGKSKKETF----RNVLMKE-----PEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14172 185 SCDMWSLGVIMYILLCGFPPFYSNTGQAISpgmkRRIRMGQygfpnPEWAEVSEEAKQLIRHLLKTDPTERM 256
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
109-326 3.39e-14

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: 72.60  E-value: 3.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 109 GGDLnvLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH---VTLTDFDLSRslkkpLRPHF 185
Cdd:cd14180  85 GGEL--LDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFAR-----LRPQG 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 YQPdpeliidrkksrsfsrLISPTAeknktglkktrsarvnpinrrktsfssgersnsfvgTDEYVSPEVIRGDGHDFAV 265
Cdd:cd14180 158 SRP----------------LQTPCF------------------------------------TLQYAAPELFSNQGYDESC 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 266 DWWALGVLTYEMMYGETPFKGKSKKETFRNVL-----MKEPEFA-------GKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14180 186 DLWSLGVILYTMLSGQVPFQSKRGKMFHNHAAdimhkIKEGDFSlegeawkGVSEEAKDLVRGLLTVDPAKRL 258
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
139-325 5.06e-14

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: 71.70  E-value: 5.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 139 ALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlrphfyqpdpeliidrkksrsfsrlisptaeknktglk 218
Cdd:cd06648 115 ALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKE-------------------------------------- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 219 ktrsarvnpINRRKtsfssgersnSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLM 298
Cdd:cd06648 157 ---------VPRRK----------SLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRD 217
                       170       180       190
                ....*....|....*....|....*....|.
gi 15232374 299 KEPEFAGKPND----LTDLIRRLLVKDPNRR 325
Cdd:cd06648 218 NEPPKLKNLHKvsprLRSFLDRMLVRDPAQR 248
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
25-328 5.93e-14

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: 71.59  E-value: 5.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVvstsSSSSPFAVKLVP-----KSSASSLRRARWEIEVLRRLSVDSnqnpfLPRLLASFESPE- 98
Cdd:cd06653   8 KLLGRGAFGEVYLCYDA----DTGRELAVKQVPfdpdsQETSKEVNALECEIQLLKNLRHDR-----IVQYYGCLRDPEe 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 -YFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRsl 177
Cdd:cd06653  79 kKLSIFVEYMPGGSVKDQL--KAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinRRKTSFSSGERSNSFVGTDEYVSPEVIR 257
Cdd:cd06653 155 ----------------------------------------------------RIQTICMSGTGIKSVTGTPYWMSPEVIS 182
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPF-KGKSKKETFRnvLMKEPEFAGKPNDLT----DLIRRLLVKDPNRRLGC 328
Cdd:cd06653 183 GEGYGRKADVWSVACTVVEMLTEKPPWaEYEAMAAIFK--IATQPTKPQLPDGVSdacrDFLRQIFVEEKRRPTAE 256
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
27-175 6.28e-14

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: 71.33  E-value: 6.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARW--EIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAV 104
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGM----VAIKCLHSSPNCIEERKALlkEAEKMERAR-----HSYVLPLLGVCVERRSLGLVM 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 105 PYCSGGDLNVLLHRQNDGVFSSSVIRFyVAEIVCALEHLHTM--GIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd13978  72 EYMENGSLKSLLEREIQDVPWSLRFRI-IHEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLSK 143
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
51-326 6.83e-14

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: 71.80  E-value: 6.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLV--------PKSSASSLRRarwEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNV-LLHRQND 121
Cdd:cd14094  31 FAVKIVdvakftssPGLSTEDLKR---EASICHML-----KHPHIVELLETYSSDGMLYMVFEFMDGADLCFeIVKRADA 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 122 G-VFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI---QQSGHVTLTDFDLSRSLkkplrphfyqpdPELiidrk 197
Cdd:cd14094 103 GfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL------------GES----- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 198 ksrsfsrlisptaeknktglkktrsarvnpinrrkTSFSSGErsnsfVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEM 277
Cdd:cd14094 166 -----------------------------------GLVAGGR-----VGTPHFMAPEVVKREPYGKPVDVWGCGVILFIL 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15232374 278 MYGETPFKGkSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14094 206 LSGCLPFYG-TKERLFEGIIkgkykMNPRQWSHISESAKDLVRRMLMLDPAERI 258
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
25-325 7.18e-14

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 72.98  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   25 KILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSVD-----SNQNPFLPRLLASFESPEY 99
Cdd:PTZ00283  38 RVLGSGATGTVLCAKRV----SDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDffsivKCHEDFAKKDPRNPENVLM 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  100 FAWAVPYCSGGDLnvllhRQNDGVFSSSVIRFYVAE-------IVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFd 172
Cdd:PTZ00283 114 IALVLDYANAGDL-----RQEIKSRAKTNRTFREHEagllfiqVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDF- 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  173 lsrslkkplrphfyqpdpeliidrkksrSFSRLISPTAeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVS 252
Cdd:PTZ00283 188 ----------------------------GFSKMYAATV--------------------------SDDVGRTFCGTPYYVA 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374  253 PEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMK--EPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:PTZ00283 214 PEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGryDPLPPSISPEMQEIVTALLSSDPKRR 288
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
27-284 8.05e-14

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 71.49  E-value: 8.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDvvstSSSSSPFAVKLVpKSSASSLRRARW--EIEVLRRLSvdsnqnpfLPRLLASFESPEYFAW-- 102
Cdd:cd14039   1 LGTGGFGNVCLYQN----QETGEKIAIKSC-RLELSVKNKDRWchEIQIMKKLN--------HPNVVKACDVPEEMNFlv 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 103 ------AVPYCSGGDLNVLLHRQND--GVFSSSVIRFyVAEIVCALEHLHTMGIAYRDLKPENILIQQSGhvtltdfdlS 174
Cdd:cd14039  68 ndvpllAMEYCSGGDLRKLLNKPENccGLKESQVLSL-LSDIGSGIQYLHENKIIHRDLKPENIVLQEIN---------G 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RSLKKplrphfyqpdpelIIDRKKSRSFSRlisptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPE 254
Cdd:cd14039 138 KIVHK-------------IIDLGYAKDLDQ---------------------------------GSLCTSFVGTLQYLAPE 171
                       250       260       270
                ....*....|....*....|....*....|
gi 15232374 255 VIRGDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd14039 172 LFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
pknD PRK13184
serine/threonine-protein kinase PknD;
24-325 8.17e-14

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 73.27  E-value: 8.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKS-SASSLRRARWEIEVlrRLSVDSNQNPFLPrlLASFES---PEY 99
Cdd:PRK13184   7 IRLIGKGGMGEVYLAYDPVCSRR----VALKKIREDlSENPLLKKRFLREA--KIAADLIHPGIVP--VYSICSdgdPVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  100 FAwaVPYCSGGDLNVLLH--RQNDGVFSSSVIRFYVA-------EIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTD 170
Cdd:PRK13184  79 YT--MPYIEGYTLKSLLKsvWQKESLSKELAEKTSVGaflsifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  171 FDLSRSLKKplrphfyQPDPELIIDrkksrsfsrlisptaeknktglkktrsarvnpINRRKTSFSSGERSNSFVGTDEY 250
Cdd:PRK13184 157 WGAAIFKKL-------EEEDLLDID--------------------------------VDERNICYSSMTIPGKIVGTPDY 197
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374  251 VSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPF-KGKSKKETFRNVLMKEPEFAGK---PNDLTDLIRRLLVKDPNRR 325
Cdd:PRK13184 198 MAPERLLGVPASESTDIYALGVILYQMLTLSFPYrRKKGRKISYRDVILSPIEVAPYreiPPFLSQIAMKALAVDPAER 276
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
25-341 1.10e-13

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: 70.37  E-value: 1.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSSsspfAVKLVPKSSASSLR---RARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFA 101
Cdd:cd14079   8 KTLGVGSFGKVKLAEHELTGHKV----AVKILNRQKIKSLDmeeKIRREIQILKLFR-----HPHIIRLYEVIETPTDIF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLhRQNDGVFSSSVIRFYvAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkpl 181
Cdd:cd14079  79 MVMEYVSGGELFDYI-VQKGRLSEDEARRFF-QQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMR--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpDPELIidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSfssgersnsfVGTDEYVSPEVIrgDGH 261
Cdd:cd14079 154 -------DGEFL--------------------------------------KTS----------CGSPNYAAPEVI--SGK 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 262 DFA---VDWWALGVLTYEMMYGETPFKGKSKKETFRNVlmKEPEFAgKPNDLT----DLIRRLLVKDPNRRLGCHrgaaE 334
Cdd:cd14079 177 LYAgpeVDVWSCGVILYALLCGSLPFDDEHIPNLFKKI--KSGIYT-IPSHLSpgarDLIKRMLVVDPLKRITIP----E 249

                ....*..
gi 15232374 335 IKELAFF 341
Cdd:cd14079 250 IRQHPWF 256
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
132-288 1.12e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.52  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  132 YVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfyqpdpeliidrkksrsfsrlisptae 211
Cdd:NF033483 112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARAL---------------------------------- 157
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374  212 knktglkktrsarvnpinrrktSFSSGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKS 288
Cdd:NF033483 158 ----------------------SSTTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
22-175 1.24e-13

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: 70.36  E-value: 1.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASslRRARWEIEVLRRLSvdsnQNPFLPRLLASFESPEYfA 101
Cdd:cd14017   3 KVVKKIGGGGFGEIYKVRDVVDGEE----VAMKVESKSQPK--QVLKMEVAVLKKLQ----GKPHFCRLIGCGRTERY-N 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 102 WAVPYCSGGDLNVLLHRQNDGVFS-SSVIRFYVAeIVCALEHLHTMGIAYRDLKPENILI----QQSGHVTLTDFDLSR 175
Cdd:cd14017  72 YIVMTLLGPNLAELRRSQPRGKFSvSTTLRLGIQ-ILKAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYILDFGLAR 149
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
24-180 1.41e-13

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: 70.18  E-value: 1.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSssssPFAVKLVPKSSASSLrrARWEIEVLRRLsvdsNQNPFLPRLLASFESPEYFAWA 103
Cdd:cd14016   5 VKKIGSGSFGEVYLGIDLKTGE----EVAIKIEKKDSKHPQ--LEYEAKVYKLL----QGGPGIPRLYWFGQEGDYNVMV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCsGGDLNVLLhRQNDGVFS-SSVIRfyVA-EIVCALEHLHTMGIAYRDLKPENILI---QQSGHVTLTDFDLSRSLK 178
Cdd:cd14016  75 MDLL-GPSLEDLF-NKCGRKFSlKTVLM--LAdQMISRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLAKKYR 150

                ..
gi 15232374 179 KP 180
Cdd:cd14016 151 DP 152
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
94-325 1.73e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 71.97  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   94 FESPEYFAWAVPYCSGGDLNVLL-HRQNDGV-FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:PTZ00267 134 FKSDDKLLLIMEYGSGGDLNKQIkQRLKEHLpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDF 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  172 dlsrslkkplrphfyqpdpeliidrkksrsfsrlisptaeknktGLKKTRSARVnpinrrktsfsSGERSNSFVGTDEYV 251
Cdd:PTZ00267 214 --------------------------------------------GFSKQYSDSV-----------SLDVASSFCGTPYYL 238
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374  252 SPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMK--EPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:PTZ00267 239 APELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGkyDPFPCPVSSGMKALLDPLLSKNPALR 314
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
81-326 1.74e-13

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 70.01  E-value: 1.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  81 SNQNPFLPRLLASFESPEYFAWAVPYCSGGDLnvlLHRQ-NDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENIL 159
Cdd:cd14665  52 SLRHPNIVRFKEVILTPTHLAIVMEYAAGGEL---FERIcNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 160 IQQSghvtltdfdlsrslkkplrphfyqPDPEL-IIDRKKSRSfSRLISptaeknktglkktrsarvnpinrrktsfssg 238
Cdd:cd14665 129 LDGS------------------------PAPRLkICDFGYSKS-SVLHS------------------------------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 239 eRSNSFVGTDEYVSPEVIRGDGHDFAV-DWWALGVLTYEMMYGETPFKGKSKKETFR-------NVLMKEPEFAGKPNDL 310
Cdd:cd14665 153 -QPKSTVGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDPEEPRNFRktiqrilSVQYSIPDYVHISPEC 231
                       250
                ....*....|....*.
gi 15232374 311 TDLIRRLLVKDPNRRL 326
Cdd:cd14665 232 RHLISRIFVADPATRI 247
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
27-286 2.69e-13

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: 69.06  E-value: 2.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAhdvvstSSSSSPFAVKLVPKSSASslrrarwEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd14059   1 LGSGAQGAVFLG------KFRGEEVAVKKVRDEKET-------DIKHLRKL-----NHPNIIKFKGVCTQAPCYCILMEY 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDLNVLLHRQNdgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfy 186
Cdd:cd14059  63 CPYGQLYEVLRAGR--EITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL--------- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 187 qpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssGERSN--SFVGTDEYVSPEVIRGDGHDFA 264
Cdd:cd14059 132 ---------------------------------------------------SEKSTkmSFAGTVAWMAPEVIRNEPCSEK 160
                       250       260
                ....*....|....*....|..
gi 15232374 265 VDWWALGVLTYEMMYGETPFKG 286
Cdd:cd14059 161 VDIWSFGVVLWELLTGEIPYKD 182
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
124-326 3.65e-13

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: 69.61  E-value: 3.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 124 FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlrphfyqpdpeliidrkksrsfS 203
Cdd:cd14199 123 LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGS----------------------D 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 204 RLISPTaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRGDGHDF---AVDWWALGVLTYEMMYG 280
Cdd:cd14199 181 ALLTNT-----------------------------------VGTPAFMAPETLSETRKIFsgkALDVWAMGVTLYCFVFG 225
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15232374 281 ETPFKGK---SKKETFRNVLMKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14199 226 QCPFMDErilSLHSKIKTQPLEFPDQPDISDDLKDLLFRMLDKNPESRI 274
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
27-326 3.87e-13

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 68.80  E-value: 3.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASS------LRRARWEIEVLRRLSVDSNqnPFLPRLLASFESPEYF 100
Cdd:cd14005   8 LGKGGFGTVYSGVRI----RDGLPVAVKFVPKSRVTEwamingPVPVPLEIALLLKASKPGV--PGVIRLLDWYERPDGF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGG-DLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ-QSGHVTLTDFDLSRSLK 178
Cdd:cd14005  82 LLIMERPEPCqDLFDFITER--GALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGALLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 KplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinRRKTSFSsgersnsfvGTDEYVSPEVIR- 257
Cdd:cd14005 160 D--------------------------------------------------SVYTDFD---------GTRVYSPPEWIRh 180
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPFkgKSKKETFRNVLMKEPefaGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14005 181 GRYHGRPATVWSLGILLYDMLCGDIPF--ENDEQILRGNVLFRP---RLSKECCDLISRCLQFDPSKRP 244
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
70-325 5.75e-13

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: 68.48  E-value: 5.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLSvdsnQNPFLPRLLASFESPEYFA-----WAV-PYCSGG---DLNVLLHRQNDGVfSSSVIRFYVAEIVCAL 140
Cdd:cd06608  52 EINILRKFS----NHPNIATFYGAFIKKDPPGgddqlWLVmEYCGGGsvtDLVKGLRKKGKRL-KEEWIAYILRETLRGL 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 141 EHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSlkkplrphfyqpdpeliidrkksrsfsrlisptaeknktgLKKT 220
Cdd:cd06608 127 AYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQ----------------------------------------LDST 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 221 RSARvnpinrrktsfssgersNSFVGTDEYVSPEVIRGD-----GHDFAVDWWALGVLTYEMMYGETPF-KGKSKKETF- 293
Cdd:cd06608 167 LGRR-----------------NTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGITAIELADGKPPLcDMHPMRALFk 229
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15232374 294 --RNV--LMKEPEFAGKpnDLTDLIRRLLVKDPNRR 325
Cdd:cd06608 230 ipRNPppTLKSPEKWSK--EFNDFISECLIKNYEQR 263
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
22-326 5.76e-13

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: 68.26  E-value: 5.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARwEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd14662   3 ELVKDIGSGNFGVARLMRNKETKEL----VAVKYIERGLKIDENVQR-EIINHRSL-----RHPNIIRFKEVVLTPTHLA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLnvlLHR-QNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQS--GHVTLTDFDLSRSlk 178
Cdd:cd14662  73 IVMEYAAGGEL---FERiCNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKS-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kplrphfyqpdpeliidrkksrsfSRLISptaeknktglkktrsarvnpinrrktsfssgeRSNSFVGTDEYVSPEVIRG 258
Cdd:cd14662 148 ------------------------SVLHS--------------------------------QPKSTVGTPAYIAPEVLSR 171
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 259 DGHDFAV-DWWALGVLTYEMMYGETPFKGKSKKETFRN-------VLMKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14662 172 KEYDGKVaDVWSCGVTLYVMLVGAYPFEDPDDPKNFRKtiqrimsVQYKIPDYVRVSQDCRHLLSRIFVANPAKRI 247
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
127-326 9.82e-13

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: 68.20  E-value: 9.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 127 SVIRFYvaEIVCALEHLHTMGIAYRDLKPENILIQQSGH-VTLTDFDLSRSLKKplrphfyqpDPELIIDRKksrsfsrl 205
Cdd:cd13974 134 ALVIFY--DVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVS---------EDDLLKDQR-------- 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 206 isptaeknktglkktrsarvnpinrrktsfssgersnsfvGTDEYVSPEVIRGDGH-DFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd13974 195 ----------------------------------------GSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPF 234
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15232374 285 KGKSKKETFRNVlmKEPEFAgKPND------LTDLIRRLLVKDPNRRL 326
Cdd:cd13974 235 YDSIPQELFRKI--KAAEYT-IPEDgrvsenTVCLIRKLLVLNPQKRL 279
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
51-318 1.01e-12

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 67.75  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRR-ARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNvllhrqnDGVFSSSVI 129
Cdd:cd14184  29 FALKIIDKAKCCGKEHlIENEVSILRRV-----KHPNIIMLIEEMDTPAELYLVMELVKGGDLF-------DAITSSTKY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 130 -----RFYVAEIVCALEHLHTMGIAYRDLKPENILI----QQSGHVTLTDFDLSRSLKKPLRphfyqpdpeliidrkksr 200
Cdd:cd14184  97 terdaSAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEGPLY------------------ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 201 sfsrlisptaeknktglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYG 280
Cdd:cd14184 159 ------------------------------------------TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCG 196
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15232374 281 ETPFKGKS--KKETFRNVLMKEPEFAGkP--NDLTDLIRRLL 318
Cdd:cd14184 197 FPPFRSENnlQEDLFDQILLGKLEFPS-PywDNITDSAKELI 237
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
26-325 1.02e-12

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: 67.57  E-value: 1.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAHDVVSTSSssspFAVKLVPK------SSASSLRRARWEIEVLRRLSVDSNqNPFLPRLLASFESPEY 99
Cdd:cd14101   7 LLGKGGFGTVYAGHRISDGLQ----VAIKQISRnrvqqwSKLPGVNPVPNEVALLQSVGGGPG-HRGVIRLLDWFEIPEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAvpycsggdLNVLLHRQN-------DGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ-QSGHVTLTDF 171
Cdd:cd14101  82 FLLV--------LERPQHCQDlfdyiteRGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 172 DLSRSLKKplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYV 251
Cdd:cd14101 154 GSGATLKD-----------------------------------------------------------SMYTDFDGTRVYS 174
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 252 SPE-VIRGDGHDFAVDWWALGVLTYEMMYGETPFkgkskkETFRNVLMKEPEFAGK-PNDLTDLIRRLLVKDPNRR 325
Cdd:cd14101 175 PPEwILYHQYHALPATVWSLGILLYDMVCGDIPF------ERDTDILKAKPSFNKRvSNDCRSLIRSCLAYNPSDR 244
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
136-326 1.20e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 68.10  E-value: 1.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 136 IVCALEHLHTMGIAYRDLKPENILiqqsghvtLTDFDLSRSLKkplrphfyqpdpelIIDRkksrSFSRLiSPTAEKNKT 215
Cdd:cd14092 108 LVSAVSFMHSKGVVHRDLKPENLL--------FTDEDDDAEIK--------------IVDF----GFARL-KPENQPLKT 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 216 glkktrsarvnPinrrktsfssgersnsfVGTDEYVSPEVIRGD----GHDFAVDWWALGVLTYEMMYGETPFKGKSKKE 291
Cdd:cd14092 161 -----------P-----------------CFTLPYAAPEVLKQAlstqGYDESCDLWSLGVILYTMLSGQVPFQSPSRNE 212
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15232374 292 TFRNVLMK---------EPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14092 213 SAAEIMKRiksgdfsfdGEEWKNVSSEAKSLIQGLLTVDPSKRL 256
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
27-175 1.29e-12

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: 67.68  E-value: 1.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHdvvstSSSSSPFAVK-LVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVP 105
Cdd:cd14066   1 IGSGGFGTVYKGV-----LENGTVVAVKrLNEMNCAASKKEFLTELEMLGRL-----RHPNLVRLLGYCLESDEKLLVYE 70
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 106 YCSGGDLNVLLHRQNDGVFSSSVIRFYVA-EIVCALEHLHTMG---IAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd14066  71 YMPNGSLEDRLHCHKGSPPLPWPQRLKIAkGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLAR 144
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
27-284 1.67e-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: 67.44  E-value: 1.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSssspfavklVPKSSASSLRRARWEIEVLRRLSVDSNQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd06654  28 IGQGASGTVYTAMDVATGQE---------VAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDL-NVLLHRQNDGVFSSSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrslkkplrphf 185
Cdd:cd06654  99 LAGGSLtDVVTETCMDEGQIAAVCR----ECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-------------- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yqpdpeliidrkksrSFSRLISPTAEKNKTglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDFAV 265
Cdd:cd06654 161 ---------------GFCAQITPEQSKRST----------------------------MVGTPYWMAPEVVTRKAYGPKV 197
                       250
                ....*....|....*....
gi 15232374 266 DWWALGVLTYEMMYGETPF 284
Cdd:cd06654 198 DIWSLGIMAIEMIEGEPPY 216
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
51-292 1.85e-12

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: 66.77  E-value: 1.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPkSSASSLRRARWEIEVLRRLSVDsnqnpflpRLLASFE---SPEYFAWAVPYCSGGDLnvlLHRQNDGV-FSS 126
Cdd:cd14111  31 FPAKIVP-YQAEEKQGVLQEYEILKSLHHE--------RIMALHEayiTPRYLVLIAEFCSGKEL---LHSLIDRFrYSE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 127 SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfyqpdpeliidrkksrsfsrli 206
Cdd:cd14111  99 DDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSF----------------------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 207 sptaeknktglkktrsarvNPINRRKTSfssgersnSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKG 286
Cdd:cd14111 150 -------------------NPLSLRQLG--------RRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFED 202

                ....*.
gi 15232374 287 KSKKET 292
Cdd:cd14111 203 QDPQET 208
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
27-284 1.96e-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: 1.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd06655  27 IGQGASGTVFTAIDVATGQE----VAIKQINLQKQPKKELIINEILVMKEL-----KNPNIVNFLDSFLVGDELFVVMEY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDL-NVLLHRQNDGVFSSSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrslkkplrphf 185
Cdd:cd06655  98 LAGGSLtDVVTETCMDEAQIAAVCR----ECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDF-------------- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yqpdpeliidrkksrSFSRLISPTAEKNKTglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDFAV 265
Cdd:cd06655 160 ---------------GFCAQITPEQSKRST----------------------------MVGTPYWMAPEVVTRKAYGPKV 196
                       250
                ....*....|....*....
gi 15232374 266 DWWALGVLTYEMMYGETPF 284
Cdd:cd06655 197 DIWSLGIMAIEMVEGEPPY 215
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
24-328 2.45e-12

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: 67.21  E-value: 2.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSssssPFAVK---LVPKSSA------SSLRrarwEIEVLRRLsvdsnQNPFLPRLLASF 94
Cdd:cd07841   5 GKKLGEGTYAVVYKARDKETGR----IVAIKkikLGERKEAkdginfTALR----EIKLLQEL-----KHPNIIGLLDVF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEYFAWAVPYCSGgDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd07841  72 GHKSNINLVFEFMET-DLEKVI-KDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RSLKKPLRPHFYQpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPE 254
Cdd:cd07841 150 RSFGSPNRKMTHQ---------------------------------------------------------VVTRWYRAPE 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 255 VIRGDGH-DFAVDWWALGVLTYEMM------YGE---------------------------------TPFKGKSKKETFR 294
Cdd:cd07841 173 LLFGARHyGVGVDMWSVGCIFAELLlrvpflPGDsdidqlgkifealgtpteenwpgvtslpdyvefKPFPPTPLKQIFP 252
                       330       340       350
                ....*....|....*....|....*....|....
gi 15232374 295 NVlmkepefagkPNDLTDLIRRLLVKDPNRRLGC 328
Cdd:cd07841 253 AA----------SDDALDLLQRLLTLNPNKRITA 276
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
18-326 2.46e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 67.75  E-value: 2.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  18 LDSIKALKILGKGATGTVFLAHDVVSTSssssPFAVKLV--PKSSASSLRRARWEIEVLRRLS---VDSNQNPFLP-RLL 91
Cdd:cd07876  20 LKRYQQLKPIGSGAQGIVCAAFDTVLGI----NVAVKKLsrPFQNQTHAKRAYRELVLLKCVNhknIISLLNVFTPqKSL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  92 ASFESpeyfAWAVPYCSGGDLNVLLHRQNDgvfsSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:cd07876  96 EEFQD----VYLVMELMDANLCQVIHMELD----HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDF 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 172 DLSRSlkkplrphfyqpdpeliidrkKSRSFsrLISPtaeknktglkktrsarvnpinrrktsfssgersnsFVGTDEYV 251
Cdd:cd07876 168 GLART---------------------ACTNF--MMTP-----------------------------------YVVTRYYR 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 252 SPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSK----------------------KETFRNVLMKEPEFAG---- 305
Cdd:cd07876 190 APEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHidqwnkvieqlgtpsaefmnrlQPTVRNYVENRPQYPGisfe 269
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15232374 306 -----------------KPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd07876 270 elfpdwifpseserdklKTSQARDLLSKMLVIDPDKRI 307
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
51-325 2.50e-12

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 66.96  E-value: 2.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSasslRRARWEIEVLRRLSvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNdgVFSSSVIR 130
Cdd:cd14177  32 FAVKIIDKSK----RDPSEEIEILMRYG----QHPNIITLKDVYDDGRYVYLVTELMKGGELLDRILRQK--FFSEREAS 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FYVAEIVCALEHLHTMGIAYRDLKPENIL-IQQSGH---VTLTDFDLSRSLKKplrphfyqpDPELiidrkksrsfsrLI 206
Cdd:cd14177 102 AVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRG---------ENGL------------LL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 207 SPTAEKNktglkktrsarvnpinrrktsfssgersnsfvgtdeYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFkG 286
Cdd:cd14177 161 TPCYTAN------------------------------------FVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPF-A 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15232374 287 KSKKETFRNVLMK--EPEFA---GKPNDLT----DLIRRLLVKDPNRR 325
Cdd:cd14177 204 NGPNDTPEEILLRigSGKFSlsgGNWDTVSdaakDLLSHMLHVDPHQR 251
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
27-325 4.90e-12

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: 66.28  E-value: 4.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARWEIEVLRRlsvdsNQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd06656  27 IGQGASGTVYTAIDIATGQE----VAIKQMNLQQQPKKELIINEILVMRE-----NKNPNIVNYLDSYLVGDELWVVMEY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDL-NVLLHRQNDGVFSSSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrslkkplrphf 185
Cdd:cd06656  98 LAGGSLtDVVTETCMDEGQIAAVCR----ECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-------------- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yqpdpeliidrkksrSFSRLISPTAEKNKTglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDFAV 265
Cdd:cd06656 160 ---------------GFCAQITPEQSKRST----------------------------MVGTPYWMAPEVVTRKAYGPKV 196
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 266 DWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPNDLT----DLIRRLLVKDPNRR 325
Cdd:cd06656 197 DIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSavfrDFLNRCLEMDVDRR 260
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
126-328 5.97e-12

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: 65.91  E-value: 5.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 126 SSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlrphfyqpdpeliidrkksrsfsrl 205
Cdd:cd07846  99 ESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP------------------------- 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 206 isptaeknktglkktrsarvnpinrrktsfssGERSNSFVGTDEYVSPEVIRGD-GHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd07846 154 --------------------------------GEVYTDYVATRWYRAPELLVGDtKYGKAVDVWAVGCLVTEMLTGEPLF 201
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 285 KGKSKKETF--------------RNVLMKEPEFAG---------KPND---------LTDLIRRLLVKDPNRRLGC 328
Cdd:cd07846 202 PGDSDIDQLyhiikclgnliprhQELFQKNPLFAGvrlpevkevEPLErrypklsgvVIDLAKKCLHIDPDKRPSC 277
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
25-177 6.11e-12

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: 65.52  E-value: 6.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFlahDVVSTSSSSSPFAVKL--VPKSSASSLRRARWEIEVLRRLSVDSNqnPFLPRLLASFESPEYFAW 102
Cdd:cd14052   6 ELIGSGEFSQVY---KVSERVPTGKVYAVKKlkPNYAGAKDRLRRLEEVSILRELTLDGH--DNIVQLIDSWEYHGHLYI 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 103 AVPYCSGGDLNVLLHRQND-GVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd14052  81 QTELCENGSLDVFLSELGLlGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVW 156
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
24-326 6.12e-12

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: 66.16  E-value: 6.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVvstsSSSSPFAVK--LVPKSSASSLRRARWEIEVLRRL---SVDSNQNPFLPRllasfESPE 98
Cdd:cd07851  20 LSPVGSGAYGQVCSAFDT----KTGRKVAIKklSRPFQSAIHAKRTYRELRLLKHMkheNVIGLLDVFTPA-----SSLE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YF--AWAVPYCSGGDLNVLLHRQndgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd07851  91 DFqdVYLVTHLMGADLNNIVKCQ---KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARH 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 lkkplrphfyqpdpeliidrkksrsfsrlisptAEKNKTGlkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVI 256
Cdd:cd07851 168 ---------------------------------TDDEMTG---------------------------YVATRWYRAPEIM 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 257 RGDGH-DFAVDWWALGVLTYEMMYGETPFKG-----------------------KSKKETFRNVLMKEPE---------F 303
Cdd:cd07851 188 LNWMHyNQTVDIWSVGCIMAELLTGKTLFPGsdhidqlkrimnlvgtpdeellkKISSESARNYIQSLPQmpkkdfkevF 267
                       330       340
                ....*....|....*....|...
gi 15232374 304 AGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd07851 268 SGANPLAIDLLEKMLVLDPDKRI 290
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
51-303 6.89e-12

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: 65.40  E-value: 6.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRRA-RWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVI 129
Cdd:cd14183  34 YALKIINKSKCRGKEHMiQNEVSILRRV-----KHPNIVLLIEEMDMPTELYLVMELVKGGDLFDAITSTNKYTERDASG 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 130 RFYvaEIVCALEHLHTMGIAYRDLKPENILIQQ----SGHVTLTDFDLSRSLKKPLRphfyqpdpeliidrkksrsfsrl 205
Cdd:cd14183 109 MLY--NLASAIKYLHSLNIVHRDIKPENLLVYEhqdgSKSLKLGDFGLATVVDGPLY----------------------- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 206 isptaeknktglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFK 285
Cdd:cd14183 164 -------------------------------------TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFR 206
                       250       260
                ....*....|....*....|
gi 15232374 286 GKSKKET--FRNVLMKEPEF 303
Cdd:cd14183 207 GSGDDQEvlFDQILMGQVDF 226
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
22-325 8.52e-12

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: 65.39  E-value: 8.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSssssPFAVKLVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLAS----FESP 97
Cdd:cd13986   3 RIQRLLGEGGFSFVYLVEDLSTGR----LYALKKILCHSKEDVKEAMREIENYRLF-----NHPNILRLLDSqivkEAGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAV-PYCSGGDL-NVLLHRQNDGVF-SSSVIRFYVAEIVCALEHLHTM---GIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:cd13986  74 KKEVYLLlPYYKRGSLqDEIERRLVKGTFfPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 172 DLSRSLKKPLRphfyqpdpeliidrkkSRSFSRLISPTAEKNktglkktrsarvnpinrrktsfssgersnsfvGTDEYV 251
Cdd:cd13986 154 GSMNPARIEIE----------------GRREALALQDWAAEH--------------------------------CTMPYR 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 252 SPEVIRGDGH---DFAVDWWALGVLTYEMMYGETPF-----KGKSKKETFRNVLMKEPEFAGKPNDLTDLIRRLLVKDPN 323
Cdd:cd13986 186 APELFDVKSHctiDEKTDIWSLGCTLYALMYGESPFerifqKGDSLALAVLSGNYSFPDNSRYSEELHQLVKSMLVVNPA 265

                ..
gi 15232374 324 RR 325
Cdd:cd13986 266 ER 267
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
90-325 8.60e-12

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: 65.44  E-value: 8.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  90 LLASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRF--------------YVAEIVCALEHLHTMGIAYRDLKP 155
Cdd:cd08229  77 LLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFkkqkrlipektvwkYFVQLCSALEHMHSRRVMHRDIKP 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 156 ENILIQQSGHVTLTDFDLSRslkkplrphFYQpdpeliidrkksrsfsrlisptaeknktglKKTRSArvnpinrrktsf 235
Cdd:cd08229 157 ANVFITATGVVKLGDLGLGR---------FFS------------------------------SKTTAA------------ 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 236 ssgersNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPND-----L 310
Cdd:cd08229 186 ------HSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDhyseeL 259
                       250
                ....*....|....*
gi 15232374 311 TDLIRRLLVKDPNRR 325
Cdd:cd08229 260 RQLVNMCINPDPEKR 274
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
25-284 1.51e-11

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: 64.37  E-value: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSssspFAVKLV------PKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPE 98
Cdd:cd06630   6 PLLGTGAFSSCYQARDVKTGTL----MAVKQVsfcrnsSSEQEEVVEAIREEIRMMARL-----NHPNIVRMLGATQHKS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG-HVTLTDFDlsrsl 177
Cdd:cd06630  77 HFNIFVEWMAGGSVASLLSKY--GAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFG----- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrkksrSFSRLISPTaeknkTGlkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIR 257
Cdd:cd06630 150 -----------------------AAARLASKG-----TG--------------------AGEFQGQLLGTIAFMAPEVLR 181
                       250       260
                ....*....|....*....|....*..
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd06630 182 GEQYGRSCDVWSVGCVIIEMATAKPPW 208
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
27-325 1.60e-11

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: 63.94  E-value: 1.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSssspFAVK--LVPKSSASSLRRARWEIEVLRRLSvdsnQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd13997   8 IGSGSFSEVFKVRSKVDGCL----YAVKksKKPFRGPKERARALREVEAHAALG----QHPNIVRYYSSWEEGGHLYIQM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLNVLLHRQN-DGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkPLRP 183
Cdd:cd13997  80 ELCENGSLQDALEELSpISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRL--ETSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 HFYQPDPeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnsfvgtdEYVSPEVIRGD-GHD 262
Cdd:cd13997 158 DVEEGDS----------------------------------------------------------RYLAPELLNENyTHL 179
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 263 FAVDWWALGVLTYEMMYG-ETPFKGKSKKEtFRNVLMKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd13997 180 PKADIFSLGVTVYEAATGePLPRNGQQWQQ-LRQGKLPLPPGLVLSQELTRLLKVMLDPDPTRR 242
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
51-296 1.93e-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: 63.78  E-value: 1.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVP---KSSASSLRrarwEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNdgVFSSS 127
Cdd:cd14110  31 LAAKIIPykpEDKQLVLR----EYQVLRRLS-----HPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAERN--SYSEA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 128 VIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDlsrslkkplRPHFYQPDPELIIDRKKSrsfsrLIS 207
Cdd:cd14110 100 EVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLG---------NAQPFNQGKVLMTDKKGD-----YVE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 208 PTAeknktglkktrsarvnpinrrktsfssgersnsfvgtdeyvsPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGK 287
Cdd:cd14110 166 TMA------------------------------------------PELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSD 203

                ....*....
gi 15232374 288 SKKETFRNV 296
Cdd:cd14110 204 LNWERDRNI 212
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
25-284 1.97e-11

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: 63.91  E-value: 1.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVvstsSSSSPFAVKLV---PKSSASS--LRRARWEIEVLRRLSVDsnqnpflpRLLASF----E 95
Cdd:cd06652   8 KLLGQGAFGRVYLCYDA----DTGRELAVKQVqfdPESPETSkeVNALECEIQLLKNLLHE--------RIVQYYgclrD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPE-YFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd06652  76 PQErTLSIFMEYMPGGSIKDQL--KSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGAS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RSLKkplrphfyqpdpeliidrkksrsfsrlispTAEKNKTGLKktrsarvnpinrrktsfssgersnSFVGTDEYVSPE 254
Cdd:cd06652 154 KRLQ------------------------------TICLSGTGMK------------------------SVTGTPYWMSPE 179
                       250       260       270
                ....*....|....*....|....*....|
gi 15232374 255 VIRGDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd06652 180 VISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
52-325 2.69e-11

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: 63.68  E-value: 2.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLVPKssasslRRARWEIEVLRRLSVDSN-----QNPFLPRLLASFESPEYFAWAVPYCSGGDLnvlLHRQNDGV-FS 125
Cdd:cd14070  31 AIKVIDK------KKAKKDSYVTKNLRREGRiqqmiRHPNITQLLDILETENSYYLVMELCPGGNL---MHRIYDKKrLE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 126 SSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlrphfyqpdpeliidrkksrsfsrl 205
Cdd:cd14070 102 EREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGIL------------------------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 206 isptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFK 285
Cdd:cd14070 157 ------------------------------GYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFT 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15232374 286 GK--SKKETFRNVLMKE--PEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14070 207 VEpfSLRALHQKMVDKEmnPLPTDLSPGAISFLRSLLEPDPLKR 250
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
21-284 2.95e-11

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: 63.74  E-value: 2.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  21 IKALKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRA-RWEIEVLRRlsVDSnqnPFLPRLLASFESPEY 99
Cdd:cd06619   3 IQYQEILGHGNGGTVYKAYHLLTRRI----LAVKVIPLDITVELQKQiMSELEILYK--CDS---PYIIGFYGAFFVENR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLlhrqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkk 179
Cdd:cd06619  74 ISICTEFMDGGSLDVY------RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQL-- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarVNPInrrktsfssgerSNSFVGTDEYVSPEVIRGD 259
Cdd:cd06619 146 ---------------------------------------------VNSI------------AKTYVGTNAYMAPERISGE 168
                       250       260
                ....*....|....*....|....*
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd06619 169 QYGIHSDVWSLGISFMELALGRFPY 193
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
24-326 5.60e-11

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: 62.50  E-value: 5.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLA-HDVVSTSSSSSPFAVKLVPKSS---ASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEY 99
Cdd:cd14076   6 GRTLGEGEFGKVKLGwPLPKANHRSGVQVAIKLIRRDTqqeNCQTSKIMREINILKGLT-----HPNIVRLLDVLKTKKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDL--NVLLHRQndgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSl 177
Cdd:cd14076  81 IGIVLEFVSGGELfdYILARRR----LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANT- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphFYQPDPELIidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSfssgersnsfVGTDEYVSPEVIR 257
Cdd:cd14076 156 -------FDHFNGDLM--------------------------------------STS----------CGSPCYAAPELVV 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 258 GDG--HDFAVDWWALGVLTYEMMYGETPF-------KGKSKKETFR---NVLMKEPEFAgKPNDlTDLIRRLLVKDPNRR 325
Cdd:cd14076 181 SDSmyAGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRyicNTPLIFPEYV-TPKA-RDLLRRILVPNPRKR 258

                .
gi 15232374 326 L 326
Cdd:cd14076 259 I 259
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
24-326 6.55e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 63.30  E-value: 6.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   24 LKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRR--ARwEIEVLRrlSVDsnqNPFLPRLLASFESpeyfa 101
Cdd:PLN00034  79 VNRIGSGAGGTVYK----VIHRPTGRLYALKVIYGNHEDTVRRqiCR-EIEILR--DVN---HPNVVKCHDMFDH----- 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  102 wavpycsGGDLNVLL----------HRQNDGVFSSSVIRfyvaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:PLN00034 144 -------NGEIQVLLefmdggslegTHIADEQFLADVAR----QILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADF 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  172 DLSRSLKKPLRPhfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgerSNSFVGTDEYV 251
Cdd:PLN00034 213 GVSRILAQTMDP---------------------------------------------------------CNSSVGTIAYM 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  252 SPEVIRGDGHD-----FAVDWWALGVLTYEMMYGETPFkGKSKKETFRNVL----MKEPEFA--GKPNDLTDLIRRLLVK 320
Cdd:PLN00034 236 SPERINTDLNHgaydgYAGDIWSLGVSILEFYLGRFPF-GVGRQGDWASLMcaicMSQPPEApaTASREFRHFISCCLQR 314

                 ....*.
gi 15232374  321 DPNRRL 326
Cdd:PLN00034 315 EPAKRW 320
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
23-368 1.63e-10

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 61.84  E-value: 1.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  23 ALKILGKGATGTVFLAHDV-----VSTSSSSSPFAVKLVPKssasslrRARWEIEVLRRLSvDSNQNPFLPRLLA--SFE 95
Cdd:cd07879  19 SLKQVGSGAYGSVCSAIDKrtgekVAIKKLSRPFQSEIFAK-------RAYRELTLLKHMQ-HENVIGLLDVFTSavSGD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLHRqndgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd07879  91 EFQDFYLVMPYMQTDLQKIMGHP-----LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLAR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SlkkplrphfyqpdpeliidrkksrsfsrlisptAEKNKTGlkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEV 255
Cdd:cd07879 166 H---------------------------------ADAEMTG---------------------------YVVTRWYRAPEV 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 IRGDGH-DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVL----MKEPEFAGKPNDL-------------------- 310
Cdd:cd07879 186 ILNWMHyNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILkvtgVPGPEFVQKLEDKaaksyikslpkyprkdfstl 265
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 311 --------TDLIRRLLVKDPNRRLgchrGAAEIKELAFFAGVRwDLLTEVLRPPFIPLRDDGELTV 368
Cdd:cd07879 266 fpkaspqaVDLLEKMLELDVDKRL----TATEALEHPYFDSFR-DADEETEQQPYDDSLENEKLSV 326
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
19-368 1.66e-10

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: 61.89  E-value: 1.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHDV-----VSTSSSSSPFAVKLVPKssasslrRARWEIEVLRRL---SVDSNQNPFLPRL 90
Cdd:cd07880  15 DRYRDLKQVGSGAYGTVCSALDRrtgakVAIKKLYRPFQSELFAK-------RAYRELRLLKHMkheNVIGLLDVFTPDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  91 laSFESPEYFAWAVPYCsGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTD 170
Cdd:cd07880  88 --SLDRFHDFYLVMPFM-GTDLGKLMKHEK---LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 171 FDLSRslkkplrphfyQPDPELiidrkksrsfsrlisptaeknkTGlkktrsarvnpinrrktsfssgersnsFVGTDEY 250
Cdd:cd07880 162 FGLAR-----------QTDSEM----------------------TG---------------------------YVVTRWY 181
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 251 VSPEVIRGDGH-DFAVDWWALGVLTYEMMYGETPFKG-----------------------KSKKETFRNVLMKEPEFAGK 306
Cdd:cd07880 182 RAPEVILNWMHyTQTVDIWSVGCIMAEMLTGKPLFKGhdhldqlmeimkvtgtpskefvqKLQSEDAKNYVKKLPRFRKK 261
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 307 pnDLTDLIR-----------RLLVKDPNRRLgchrGAAEIKELAFFAGVRwDLLTEVLRPPFIPLRDDGELTV 368
Cdd:cd07880 262 --DFRSLLPnanplavnvleKMLVLDAESRI----TAAEALAHPYFEEFH-DPEDETEAPPYDDSFDEVDQSL 327
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
111-192 1.85e-10

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: 61.43  E-value: 1.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 111 DLNVLLHRqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLRPHF----- 185
Cdd:cd07840  89 DLTGLLDN-PEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKENNADYtnrvi 167
                        90
                ....*....|
gi 15232374 186 ---YQPdPEL 192
Cdd:cd07840 168 tlwYRP-PEL 176
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
24-320 2.13e-10

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: 61.72  E-value: 2.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSVD------------SNQNPFLPRLL 91
Cdd:cd07854  10 LRPLGCGSNGLVFSAVD----SDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDnivkvyevlgpsGSDLTEDVGSL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  92 ASFESpeyfAWAVPYCSGGDLNVLLhrqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHV-TLTD 170
Cdd:cd07854  86 TELNS----VYIVQEYMETDLANVL---EQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 171 FDLSRslkkplrphfyqpdpelIIDRKKSRsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVgTDEY 250
Cdd:cd07854 159 FGLAR-----------------IVDPHYSH------------------------------------KGYLSEGLV-TKWY 184
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374 251 VSPE-VIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPefAGKPNDLTDLIRRLLVK 320
Cdd:cd07854 185 RSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVP--VVREEDRNELLNVIPSF 253
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
129-326 2.37e-10

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: 61.42  E-value: 2.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkplrphfyqpdpeliiDRKKSRSFSRLisp 208
Cdd:cd07852 109 KQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLS----------------QLEEDDENPVL--- 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 209 taeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGDGH-DFAVDWWALGVLTYEMMYGETPFKGK 287
Cdd:cd07852 170 ---------------------------------TDYVATRWYRAPEILLGSTRyTKGVDMWSVGCILGEMLLGKPLFPGT 216
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 288 S------------------------------------KKETFRNVLMkepeFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd07852 217 StlnqlekiievigrpsaediesiqspfaatmleslpPSRPKSLDEL----FPKASPDALDLLKKLLVFNPNKRL 287
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
19-186 2.45e-10

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: 61.23  E-value: 2.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHDVVSTSSSsspfAVKLVPKSSA--SSLRRARWEIEVLRRLSVDSnqnpfLPRLLASFES 96
Cdd:cd07855   5 DRYEPIETIGSGAYGVVCSAIDTKSGQKV----AIKKIPNAFDvvTTAKRTLRELKILRHFKHDN-----IIAIRDILRP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PeyfawaVPYCSGGDLNVL-------LHR--QNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT 167
Cdd:cd07855  76 K------VPYADFKDVYVVldlmesdLHHiiHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELK 149
                       170       180
                ....*....|....*....|
gi 15232374 168 LTDFDLSRSL-KKPLRPHFY 186
Cdd:cd07855 150 IGDFGMARGLcTSPEEHKYF 169
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
17-325 2.45e-10

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


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 60.85  E-value: 2.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  17 DLDSIKALKILGKGATGTV----FLAHDVVstssssspFAVKLVPKSS-ASSLRRarweieVLRRLSV--DSNQNPFLPR 89
Cdd:cd06618  13 DLNDLENLGEIGSGTCGQVykmrHKKTGHV--------MAVKQMRRSGnKEENKR------ILMDLDVvlKSHDCPYIVK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  90 LLASFESpEYFAWAVPYCSGGDLNVLLHRQNdGVFSSSVIRFYVAEIVCALEHLHTM-GIAYRDLKPENILIQQSGHVTL 168
Cdd:cd06618  79 CYGYFIT-DSDVFICMELMSTCLDKLLKRIQ-GPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 169 TDFDLSrslkkplrphfyqpdpeliidrkksrsfSRLISPTAeknktglkKTRSArvnpinrrktsfssgersnsfvGTD 248
Cdd:cd06618 157 CDFGIS----------------------------GRLVDSKA--------KTRSA----------------------GCA 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 249 EYVSPEVI---RGDGHDFAVDWWALGVLTYEMMYGETPFKG-KSKKETFRNVLMKE-PEFAGKPN---DLTDLIRRLLVK 320
Cdd:cd06618 179 AYMAPERIdppDNPKYDIRADVWSLGISLVELATGQFPYRNcKTEFEVLTKILNEEpPSLPPNEGfspDFCSFVDLCLTK 258

                ....*
gi 15232374 321 DPNRR 325
Cdd:cd06618 259 DHRYR 263
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
104-278 2.56e-10

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: 60.60  E-value: 2.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLNVLLHRQNDGVFSSSVIRFyVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlrp 183
Cdd:cd14154  69 TEYIPGGTLKDVLKDMARPLPWAQRVRF-AKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEE--- 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdPELIIDRKKSRSFSRLISPTAEKNKTglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDF 263
Cdd:cd14154 145 ------RLPSGNMSPSETLRHLKSPDRKKRYT----------------------------VVGNPYWMAPEMLNGRSYDE 190
                       170
                ....*....|....*
gi 15232374 264 AVDWWALGVLTYEMM 278
Cdd:cd14154 191 KVDIFSFGIVLCEII 205
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
24-326 2.66e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 61.28  E-value: 2.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSSssspFAVKLV--PKSSASSLRRARWEIeVLRRLSVDSNqnpfLPRLLASF---ESPE 98
Cdd:cd07850   5 LKPIGSGAQGIVCAAYDTVTGQN----VAIKKLsrPFQNVTHAKRAYREL-VLMKLVNHKN----IIGLLNVFtpqKSLE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFA--WAVPYCSGGDLNVLLHRQNDgvfsSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrs 176
Cdd:cd07850  76 EFQdvYLVMELMDANLCQVIQMDLD----HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 lkkplrphfyqpdpeliidRKKSRSFsrLISPtaeknktglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVI 256
Cdd:cd07850 150 -------------------RTAGTSF--MMTP-----------------------------------YVVTRYYRAPEVI 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSK----------------------KETFRNVLMKEPEFAG--------- 305
Cdd:cd07850 174 LGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHidqwnkiieqlgtpsdefmsrlQPTVRNYVENRPKYAGysfeelfpd 253
                       330       340       350
                ....*....|....*....|....*....|....
gi 15232374 306 -------------KPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd07850 254 vlfppdseehnklKASQARDLLSKMLVIDPEKRI 287
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
27-301 2.67e-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: 60.97  E-value: 2.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDvvstSSSSSPFAVKLV-PKSSASSLRRARWEIEVLRRLSvdsNQNpfLPRLLASFE--SPEYFAWA 103
Cdd:cd13988   1 LGQGATANVFRGRH----KKTGDLYAVKVFnNLSFMRPLDVQMREFEVLKKLN---HKN--IVKLFAIEEelTTRHKVLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDL-NVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENIL--IQQSGHVT--LTDFDLSRSLK 178
Cdd:cd13988  72 MELCPCGSLyTVLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSVykLTDFGAARELE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfsSGERSNSFVGTDEYVSPE---- 254
Cdd:cd13988 152 ----------------------------------------------------------DDEQFVSLYGTEEYLHPDmyer 173
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 255 -VIRGD-GHDFA--VDWWALGVLTYEMMYGETPFK----GKSKKETFRNVLMKEP 301
Cdd:cd13988 174 aVLRKDhQKKYGatVDLWSIGVTFYHAATGSLPFRpfegPRRNKEVMYKIITGKP 228
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
50-325 2.75e-10

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


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 60.26  E-value: 2.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  50 PFAVKLVPKSSASS------LRRarwEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRqnDGV 123
Cdd:cd14164  27 KVAIKIVDRRRASPdfvqkfLPR---ELSILRRV-----NHPNIVQMFECIEVANGRLYIVMEAAATDLLQKIQE--VHH 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 124 FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG-HVTLTDFDLSRSLKKPlrphfyqpdPELiidrkksrsf 202
Cdd:cd14164  97 IPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDY---------PEL---------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 203 srlisptaeknktglkktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVIRGDGHDF-AVDWWALGVLTYEMMYGE 281
Cdd:cd14164 158 --------------------------------------STTFCGSRAYTPPEVILGTPYDPkKYDVWSLGVVLYVMVTGT 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232374 282 TPFKG---------KSKKETFRNVLMKEPEFAgkpndltdLIRRLLVKDPNRR 325
Cdd:cd14164 200 MPFDEtnvrrlrlqQRGVLYPSGVALEEPCRA--------LIRTLLQFNPSTR 244
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
22-336 3.93e-10

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: 60.20  E-value: 3.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSasslRRARWEIEVLRRLsvdsnQNPFLPRLLASFESP---- 97
Cdd:cd14047   9 KEIELIGSGGFGQVFKAKHRIDGKT----YAIKRVKLNN----EKAEREVKALAKL-----DHPNIVRYNGCWDGFdydp 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 ------------EYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH 165
Cdd:cd14047  76 etsssnssrsktKCLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 166 VTLTDFDLSRSLKKPlrphfyqpdpeliIDRKKSRsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnsfv 245
Cdd:cd14047 156 VKIGDFGLVTSLKND-------------GKRTKSK--------------------------------------------- 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 246 GTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETpfKGKSKKETFRNVLMKE--PEFAGKPNDLTDLIRRLLVKDPN 323
Cdd:cd14047 178 GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCD--SAFEKSKFWTDLRNGIlpDIFDKRYKIEKTIIKKMLSKKPE 255
                       330
                ....*....|...
gi 15232374 324 RRlgCHrgAAEIK 336
Cdd:cd14047 256 DR--PN--ASEIL 264
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
129-341 5.12e-10

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 59.87  E-value: 5.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKkplrphfyqpdpeliiDRKKSRSFSRLisp 208
Cdd:cd05576 115 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVE----------------DSCDSDAIENM--- 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 209 taeknktglkktrsarvnpinrrktsfssgersnsfvgtdeYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGeTPFKGKS 288
Cdd:cd05576 176 -----------------------------------------YCAPEVGGISEETEACDWWSLGALLFELLTG-KALVECH 213
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15232374 289 KKETFRNVLMKEPEFAGKPndLTDLIRRLLVKDPNRRLGC-HRGAAEIKELAFF 341
Cdd:cd05576 214 PAGINTHTTLNIPEWVSEE--ARSLLQQLLQFNPTERLGAgVAGVEDIKSHPFF 265
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
102-284 5.77e-10

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 59.64  E-value: 5.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAV-PYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkp 180
Cdd:cd06636  95 WLVmEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--- 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpdpeliiDRKksrsfsrlisptaeknktglkktrsarvnpINRRktsfssgersNSFVGTDEYVSPEVIRGD- 259
Cdd:cd06636 172 --------------DRT------------------------------VGRR----------NTFIGTPYWMAPEVIACDe 197
                       170       180
                ....*....|....*....|....*....
gi 15232374 260 ----GHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd06636 198 npdaTYDYRSDIWSLGITAIEMAEGAPPL 226
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
25-326 5.83e-10

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: 60.05  E-value: 5.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFlahdVVSTSSSSSPFAVKLVPKSSasslrRARWEIEVLRRLSvdsnQNPFLPRLLASFE----SPEYF 100
Cdd:cd14170   8 QVLGLGINGKVL----QIFNKRTQEKFALKMLQDCP-----KARREVELHWRAS----QCPHIVRIVDVYEnlyaGRKCL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI---QQSGHVTLTDFDLSrsl 177
Cdd:cd14170  75 LIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYtskRPNAILKLTDFGFA--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrKKSRSFSRLISPTAeknktglkktrsarvnpinrrktsfssgersnsfvgTDEYVSPEVIR 257
Cdd:cd14170 152 -------------------KETTSHNSLTTPCY------------------------------------TPYYVAPEVLG 176
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPF---------KGKSKKETFRNVLMKEPEFAGKPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd14170 177 PEKYDKSCDMWSLGVIMYILLCGYPPFysnhglaisPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRM 254
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
24-293 5.94e-10

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: 59.87  E-value: 5.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHD-----VVstssssspfAVKLVpKSSASSLRRARWEIEVLRRL-SVDSNQNPFLPRLLASFESP 97
Cdd:cd14210  18 LSVLGKGSFGQVVKCLDhktgqLV---------AIKII-RNKKRFHQQALVEVKILKHLnDNDPDDKHNIVRYKDSFIFR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFawavpyCS-----GGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTdfd 172
Cdd:cd14210  88 GHL------CIvfellSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIK--- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 173 lsrslkkplrphfyqpdpelIIDrkksrsfsrlisptaeknktglkktrsarvnpinrrktsFSS----GERSNSFVGTD 248
Cdd:cd14210 159 --------------------VID---------------------------------------FGSscfeGEKVYTYIQSR 179
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15232374 249 EYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETF 293
Cdd:cd14210 180 FYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQL 224
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
21-328 7.11e-10

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: 59.70  E-value: 7.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  21 IKALKILGKGATGTVFLAHDVVSTSSSSSPFAVK-LVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESP-- 97
Cdd:cd05038   6 LKFIKQLGEGHFGSVELCRYDPLGDNTGEQVAVKsLQPSGEEQHMSDFKREIEILRTL-----DHEYIVKYKGVCESPgr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 -------EYfawaVPYcsgGDLNVLLHRQNDGVFSSSVIRFyvAEIVC-ALEHLHTMGIAYRDLKPENILIQQSGHVTLT 169
Cdd:cd05038  81 rslrlimEY----LPS---GSLRDYLQRHRDQIDLKRLLLF--ASQICkGMEYLGSQRYIHRDLAARNILVESEDLVKIS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 170 DFDLSRSLkkPLRPHFYqpdpeliidrkksrsfsrlisptaeknktglkKTRSARVNPInrrktsfssgersnsfvgtdE 249
Cdd:cd05038 152 DFGLAKVL--PEDKEYY--------------------------------YVKEPGESPI--------------------F 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 250 YVSPEVIRGDGHDFAVDWWALGVLTYEMM-YGEtpfKGKSKKETFrnvlMKEPEFAGKPNDLTDLIRRLlvkDPNRRLGC 328
Cdd:cd05038 178 WYAPECLRESRFSSASDVWSFGVTLYELFtYGD---PSQSPPALF----LRMIGIAQGQMIVTRLLELL---KSGERLPR 247
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
24-325 7.24e-10

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: 59.30  E-value: 7.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVpkssasSLRRARWEIE-VLRRLSVDSN-QNPFLPRLLASFESPEYFA 101
Cdd:cd06642   9 LERIGKGSFGEVYKGID----NRTKEVVAIKII------DLEEAEDEIEdIQQEITVLSQcDSPYITRYYGSYLKGTKLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLhrqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkpl 181
Cdd:cd06642  79 IIMEYLGGGSALDLL---KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQL---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaekNKTGLKKtrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd06642 152 -------------------------------TDTQIKR----------------------NTFVGTPFWMAPEVIKQSAY 178
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFkgkSKKETFRNVLM----KEPEFAGK-PNDLTDLIRRLLVKDPNRR 325
Cdd:cd06642 179 DFKADIWSLGITAIELAKGEPPN---SDLHPMRVLFLipknSPPTLEGQhSKPFKEFVEACLNKDPRFR 244
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
18-326 1.02e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 59.72  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  18 LDSIKALKILGKGATGTVFLAHDVVSTSSssspFAVKLV--PKSSASSLRRARWEIEVLRRLS---VDSNQNPFLP-RLL 91
Cdd:cd07874  16 LKRYQNLKPIGSGAQGIVCAAYDAVLDRN----VAIKKLsrPFQNQTHAKRAYRELVLMKCVNhknIISLLNVFTPqKSL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  92 ASFESpeyfAWAVPYCSGGDLNVLLHRQNDgvfsSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:cd07874  92 EEFQD----VYLVMELMDANLCQVIQMELD----HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 172 DLSRSlkkplrphfyqpdpeliidrkKSRSFsrLISPtaeknktglkktrsarvnpinrrktsfssgersnsFVGTDEYV 251
Cdd:cd07874 164 GLART---------------------AGTSF--MMTP-----------------------------------YVVTRYYR 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 252 SPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKG----------------------KSKKETFRNVLMKEPEFAG---- 305
Cdd:cd07874 186 APEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGrdyidqwnkvieqlgtpcpefmKKLQPTVRNYVENRPKYAGltfp 265
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15232374 306 -----------------KPNDLTDLIRRLLVKDPNRRL 326
Cdd:cd07874 266 klfpdslfpadsehnklKASQARDLLSKMLVIDPAKRI 303
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
52-321 1.04e-09

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 58.85  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLVPKSSASSLRRARW---EIEVLRRLsvDSNQNPFLPRLLASFESPEYFAWAVpyCSGGDlnVLLHRQNDGVFSSSV 128
Cdd:cd14163  29 AIKIIDKSGGPEEFIQRFlprELQIVERL--DHKNIIHVYEMLESADGKIYLVMEL--AEDGD--VFDCVLHGGPLPEHR 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQqSGHVTLTDFdlsrslkkplrphfyqpdpeliidrkksrSFSRLIsp 208
Cdd:cd14163 103 AKALFRQLVEAIRYCHGCGVAHRDLKCENALLQ-GFTLKLTDF-----------------------------GFAKQL-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 209 taeknktglkktrsarvnPINRRktsfssgERSNSFVGTDEYVSPEVIRGDGHDFAV-DWWALGVLTYEMMYGETPFKGK 287
Cdd:cd14163 151 ------------------PKGGR-------ELSQTFCGSTAYAAPEVLQGVPHDSRKgDIWSMGVVLYVMLCAQLPFDDT 205
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15232374 288 SKKETF--RNVLMKEPEFAGKPNDLTDLIRRLLVKD 321
Cdd:cd14163 206 DIPKMLcqQQKGVSLPGHLGVSRTCQDLLKRLLEPD 241
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
22-328 1.21e-09

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


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 59.34  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVvsTSSSSSPFAVKLVPK--SSASSLRRARWEIEVLRRLSVDSNQNpflprLLASFESPEY 99
Cdd:cd07857   3 ELIKELGQGAYGIVCSARNA--ETSEEETVAIKKITNvfSKKILAKRALRELKLLRHFRGHKNIT-----CLYDMDIVFP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYC----SGGDLNVLLHrqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd07857  76 GNFNELYLyeelMEADLHQIIR--SGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLAR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SlkkplrphfyqpdpeliidrkksrsfsrlISPTAEKNKTGLKKtrsarvnpinrrktsfssgersnsFVGTDEYVSPEV 255
Cdd:cd07857 154 G-----------------------------FSENPGENAGFMTE------------------------YVATRWYRAPEI 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 256 -IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKS---------------KKETFR--------NVLMKEPEFAGKP---- 307
Cdd:cd07857 181 mLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDyvdqlnqilqvlgtpDEETLSrigspkaqNYIRSLPNIPKKPfesi 260
                       330       340
                ....*....|....*....|....*.
gi 15232374 308 -----NDLTDLIRRLLVKDPNRRLGC 328
Cdd:cd07857 261 fpnanPLALDLLEKLLAFDPTKRISV 286
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
19-325 1.27e-09

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: 58.87  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHDVVSTSSSsspfAVKLV-PKSSASSLRRARWEIevLRRLSVDSNQNPFLPRLLASFESP 97
Cdd:cd06638  18 DTWEIIETIGKGTYGKVFKVLNKKNGSKA----AVKILdPIHDIDEEIEAEYNI--LKALSDHPNVVKFYGMYYKKDVKN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAV-PYCSGGDLNVL----LHRQNDgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFD 172
Cdd:cd06638  92 GDQLWLVlELCNGGSVTDLvkgfLKRGER--MEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 173 LSRSLKKplrphfyqpdpeliidrkksrsfSRLisptaeknktglkktrsarvnpinRRKTSfssgersnsfVGTDEYVS 252
Cdd:cd06638 170 VSAQLTS-----------------------TRL------------------------RRNTS----------VGTPFWMA 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 253 PEVIRGD-----GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKP----NDLTDLIRRLLVKDPN 323
Cdd:cd06638 193 PEVIACEqqldsTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPTLHQPelwsNEFNDFIRKCLTKDYE 272

                ..
gi 15232374 324 RR 325
Cdd:cd06638 273 KR 274
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
132-326 1.30e-09

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 58.63  E-value: 1.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 132 YVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH---VTLTDFDLSRSLKKPLR-PHF--YQPDPELIIDRKKSRsfsrl 205
Cdd:cd14171 114 YTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGFAKVDQGDLMtPQFtpYYVAPQVLEAQRRHR----- 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 206 isptaeKNKTGLKKTRSarvnpinrrktsfssgersnsfvgtdEYVspevirgdgHDFAVDWWALGVLTYEMMYGETPFK 285
Cdd:cd14171 189 ------KERSGIPTSPT--------------------------PYT---------YDKSCDMWSLGVIIYIMLCGYPPFY 227
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15232374 286 GKSKKETFRNVlMKEPEFAGK---PND--------LTDLIRRLLVKDPNRRL 326
Cdd:cd14171 228 SEHPSRTITKD-MKRKIMTGSyefPEEewsqisemAKDIVRKLLCVDPEERM 278
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
25-284 1.56e-09

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: 58.56  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSSSSPfAVKLVPKSSASS--LRRARWEIEVLRRLSVDsnqnpflpRLLASF-----ESP 97
Cdd:cd06651  13 KLLGQGAFGRVYLCYDVDTGRELAAK-QVQFDPESPETSkeVSALECEIQLLKNLQHE--------RIVQYYgclrdRAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLhrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRsl 177
Cdd:cd06651  84 KTLTIFMEYMPGGSVKDQL--KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 kkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinRRKTSFSSGERSNSFVGTDEYVSPEVIR 257
Cdd:cd06651 160 ----------------------------------------------------RLQTICMSGTGIRSVTGTPYWMSPEVIS 187
                       250       260
                ....*....|....*....|....*..
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd06651 188 GEGYGRKADVWSLGCTVVEMLTEKPPW 214
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
70-328 1.84e-09

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: 58.15  E-value: 1.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCsggDLNVL--LHRQNDGVfSSSVIRFYVAEIVCALEHLHTMG 147
Cdd:cd07847  50 EIRMLKQL-----KHPNLVNLIEVFRRKRKLHLVFEYC---DHTVLneLEKNPRGV-PEHLIKKIIWQTLQAVNFCHKHN 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 148 IAYRDLKPENILIQQSGHVTLTDFdlsrslkkplrphfyqpdpeliidrkksrSFSRLISPTaeknktglkktrsarvnp 227
Cdd:cd07847 121 CIHRDVKPENILITKQGQIKLCDF-----------------------------GFARILTGP------------------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 228 inrrktsfssGERSNSFVGTDEYVSPEVIRGD-GHDFAVDWWALGVLTYEMMYGETPFKGKS------------------ 288
Cdd:cd07847 154 ----------GDDYTDYVATRWYRAPELLVGDtQYGPPVDVWAIGCVFAELLTGQPLWPGKSdvdqlylirktlgdlipr 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15232374 289 ------KKETFRNVLMKEPE--------FAGKPNDLTDLIRRLLVKDPNRRLGC 328
Cdd:cd07847 224 hqqifsTNQFFKGLSIPEPEtrepleskFPNISSPALSFLKGCLQMDPTERLSC 277
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
107-325 2.49e-09

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: 57.90  E-value: 2.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDLNVLLHRQNdGVFSSSVIRFYVAEIVCALEHLHT-MGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrphf 185
Cdd:cd08528  94 APLGEHFSSLKEKN-EHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDFGLA----------- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yqpdpeliidRKKSRSFSRLisptaeknktglkktrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGDGHDFAV 265
Cdd:cd08528 162 ----------KQKGPESSKM------------------------------------TSVVGTILYSCPEIVQNEPYGEKA 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 266 DWWALGVLTYEMMYGETPFKGkskkETFRNVLMK--EPEFAGKP-----NDLTDLIRRLLVKDPNRR 325
Cdd:cd08528 196 DIWALGCILYQMCTLQPPFYS----TNMLTLATKivEAEYEPLPegmysDDITFVIRSCLTPDPEAR 258
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
24-293 2.54e-09

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: 58.35  E-value: 2.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVVSTSssssPFAVKLV--PKSSASSLRRARWEIEVLRRLSVDSnqnpfLPRLLASFESPEYFA 101
Cdd:cd07856  15 LQPVGMGAFGLVCSARDQLTGQ----NVAVKKImkPFSTPVLAKRTYRELKLLKHLRHEN-----IISLSDIFISPLEDI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSlkkpl 181
Cdd:cd07856  86 YFVTELLGTDLHRLLTSRP---LEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI----- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqPDPELiidrkksrsfsrlisptaeknkTGlkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEV-IRGDG 260
Cdd:cd07856 158 ------QDPQM----------------------TG---------------------------YVSTRYYRAPEImLTWQK 182
                       250       260       270
                ....*....|....*....|....*....|...
gi 15232374 261 HDFAVDWWALGVLTYEMMYGETPFKGKSKKETF 293
Cdd:cd07856 183 YDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQF 215
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
24-308 2.76e-09

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: 58.14  E-value: 2.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLV--PKSSASSLRRARWEIEVLRRLSvdsNQNPF-LPRLLASFESPEYF 100
Cdd:cd07878  20 LTPVGSGAYGSVCSAYDT----RLRQKVAVKKLsrPFQSLIHARRTYRELRLLKHMK---HENVIgLLDVFTPATSIENF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 --AWAVPYCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslk 178
Cdd:cd07878  93 neVYLVTNLMGADLNNIVKCQK---LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLAR--- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 kplrphfyQPDPELiidrkksrsfsrlisptaeknkTGlkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRG 258
Cdd:cd07878 167 --------QADDEM----------------------TG---------------------------YVATRWYRAPEIMLN 189
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15232374 259 DGH-DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLmkepEFAGKPN 308
Cdd:cd07878 190 WMHyNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIM----EVVGTPS 236
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
102-284 3.00e-09

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: 57.81  E-value: 3.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAV-PYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKP 180
Cdd:cd06637  85 WLVmEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 LrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEVIRGD- 259
Cdd:cd06637 165 V---------------------------------------------------------GRRNTFIGTPYWMAPEVIACDe 187
                       170       180
                ....*....|....*....|....*....
gi 15232374 260 ----GHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd06637 188 npdaTYDFKSDLWSLGITAIEMAEGAPPL 216
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
106-325 3.97e-09

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: 57.30  E-value: 3.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLHRQNDGVFSS--SVIRFYVAEI--VC-----ALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrs 176
Cdd:cd06659  87 YLVGEELWVLMEYLQGGALTDivSQTRLNEEQIatVCeavlqALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDF----- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 lkkplrphfyqpdpeliidrkksrSFSRLISPTAEKNKtglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVI 256
Cdd:cd06659 162 ------------------------GFCAQISKDVPKRK----------------------------SLVGTPYWMAPEVI 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPND----LTDLIRRLLVKDPNRR 325
Cdd:cd06659 190 SRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKaspvLRDFLERMLVRDPQER 262
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
19-342 4.35e-09

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 57.74  E-value: 4.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHDVvstsSSSSPFAVKLV--PKSSASSLRRARWEIEVLRRL---SVDSNQNPFLP-RLLA 92
Cdd:cd07877  17 ERYQNLSPVGSGAYGSVCAAFDT----KTGLRVAVKKLsrPFQSIIHAKRTYRELRLLKHMkheNVIGLLDVFTPaRSLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  93 SFESpeyfAWAVPYCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFD 172
Cdd:cd07877  93 EFND----VYLVTHLMGADLNNIVKCQK---LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 173 LSRslkkplrphfyQPDPELiidrkksrsfsrlisptaeknkTGlkktrsarvnpinrrktsfssgersnsFVGTDEYVS 252
Cdd:cd07877 166 LAR-----------HTDDEM----------------------TG---------------------------YVATRWYRA 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 253 PEVIRGDGH-DFAVDWWALGVLTYEMMYGETPFKG-----------------------KSKKETFRNVLMKEPE------ 302
Cdd:cd07877 186 PEIMLNWMHyNQTVDIWSVGCIMAELLTGRTLFPGtdhidqlklilrlvgtpgaellkKISSESARNYIQSLTQmpkmnf 265
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 15232374 303 ---FAGKPNDLTDLIRRLLVKDPNRRLgchrGAAEIKELAFFA 342
Cdd:cd07877 266 anvFIGANPLAVDLLEKMLVLDSDKRI----TAAQALAHAYFA 304
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
22-283 4.41e-09

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: 57.00  E-value: 4.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVvstsSSSSPFAVKLVpkssasSLRRARWEIE-VLRRLSVDSN-QNPFLPRLLASFESPEY 99
Cdd:cd06641   7 TKLEKIGKGSFGEVFKGIDN----RTQKVVAIKII------DLEEAEDEIEdIQQEITVLSQcDSPYVTKYYGSYLKDTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPYCSGGDLNVLLHrqnDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkk 179
Cdd:cd06641  77 LWIIMEYLGGGSALDLLE---PGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQL-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliidrkksrsfsrlisptaekNKTGLKKtrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGD 259
Cdd:cd06641 152 ---------------------------------TDTQIKR----------------------N*FVGTPFWMAPEVIKQS 176
                       250       260
                ....*....|....*....|....
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETP 283
Cdd:cd06641 177 AYDSKADIWSLGITAIELARGEPP 200
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
99-326 4.53e-09

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 57.57  E-value: 4.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAV-PYCSGGDLN-VLLHRQNDGVFSSSvirfYVAEIVCALEHLHTMGIAYRDLKPENILI-QQSGHVTL--TDFDL 173
Cdd:cd13977 108 CYLWFVmEFCDGGDMNeYLLSRRPDRQTNTS----FMLQLSSALAFLHRNQIVHRDLKPDNILIsHKRGEPILkvADFGL 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SRSLKkplrphfyqpdpeliidrkksrsfsrlisptaeknKTGLKKTRSARVNpinrrKTSFSSGersnsfVGTDEYVSP 253
Cdd:cd13977 184 SKVCS-----------------------------------GSGLNPEEPANVN-----KHFLSSA------CGSDFYMAP 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVirGDGHDFA-VDWWALGVLTYEMMYGETPFKGKSKKETFRN-------------VLMKEPEF---------AGKPNDL 310
Cdd:cd13977 218 EV--WEGHYTAkADIFALGIIIWAMVERITFRDGETKKELLGTyiqqgkeivplgeALLENPKLelqiplkkkKSMNDDM 295
                       250
                ....*....|....*.
gi 15232374 311 TDLIRRLLVKDPNRRL 326
Cdd:cd13977 296 KQLLRDMLAANPQERP 311
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
135-325 5.66e-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: 56.51  E-value: 5.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 135 EIVCALEHLHTMGIAYRDLKPENILIQQS-----GHVTLTDFDLSRSLkkplrphfyqpdpeliiDRKKSrSFSRLISPT 209
Cdd:cd13982 107 QIASGLAHLHSLNIVHRDLKPQNILISTPnahgnVRAMISDFGLCKKL-----------------DVGRS-SFSRRSGVA 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 210 aeknktglkktrsarvnpinrrktsfssgersnsfvGTDEYVSPEVIRGDGHD---FAVDWWALG-VLTYEMMYGETPFK 285
Cdd:cd13982 169 ------------------------------------GTSGWIAPEMLSGSTKRrqtRAVDIFSLGcVFYYVLSGGSHPFG 212
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15232374 286 GKSKKEtfRNV------LMKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd13982 213 DKLERE--ANIlkgkysLDKLLSLGEHGPEAQDLIERMIDFDPEKR 256
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
124-326 6.39e-09

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: 56.51  E-value: 6.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 124 FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQsGHVTLTDFDLSRSLkkplrphfYQPDPeliidrkksrsFS 203
Cdd:cd07831  97 LPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFGSCRGI--------YSKPP-----------YT 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 204 RLISptaeknktglkkTRSarvnpinrrktsfssgersnsfvgtdeYVSPEVIRGDG-HDFAVDWWALGVLTYEMMYGET 282
Cdd:cd07831 157 EYIS------------TRW---------------------------YRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFP 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 283 PFKGK------------------SKKETFRNVLMKEPEFAGK------------PNDLTDLIRRLLVKDPNRRL 326
Cdd:cd07831 198 LFPGTneldqiakihdvlgtpdaEVLKKFRKSRHMNYNFPSKkgtglrkllpnaSAEGLDLLKKLLAYDPDERI 271
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
22-326 8.03e-09

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 56.80  E-value: 8.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDvvstSSSSSPFAVKL---VPKSSASslrrARWEIEVLRRLSVDSNQNPFL-PRLLasfesp 97
Cdd:cd14134  15 KILRLLGEGTFGKVLECWD----RKRKRYVAVKIirnVEKYREA----AKIEIDVLETLAEKDPNGKSHcVQLR------ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYC-----SGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFD 172
Cdd:cd14134  81 DWFDYRGHMCivfelLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYNPK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 173 LSRSLKKPLRPHFYqpdpelIIDrkksrsFSrlisptaeknktglkktrSArvnpinrrktSFSSGERSnSFVGTDEYVS 252
Cdd:cd14134 161 KKRQIRVPKSTDIK------LID------FG------------------SA----------TFDDEYHS-SIVSTRHYRA 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 253 PEVIRGDGHDFAVDWWALGVLTYEMMYGETPF---------------------------KGKSKKETFRNVLMKEPEFA- 304
Cdd:cd14134 200 PEVILGLGWSYPCDVWSIGCILVELYTGELLFqthdnlehlammerilgplpkrmirraKKGAKYFYFYHGRLDWPEGSs 279
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15232374 305 --------GKPND------------LTDLIRRLLVKDPNRRL 326
Cdd:cd14134 280 sgrsikrvCKPLKrlmllvdpehrlLFDLIRKMLEYDPSKRI 321
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
24-175 1.09e-08

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: 56.08  E-value: 1.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVK------LVPKSSASSLRRarwEIEVLRRlsvdSNQNPFLPrLLASFESP 97
Cdd:cd14026   2 LRYLSRGAFGTVSRARH----ADWRVTVAIKclkldsPVGDSERNCLLK---EAEILHK----ARFSYILP-ILGICNEP 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVA-EIVCALEHLHTMG--IAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd14026  70 EFLGIVTEYMTNGSLNELLHEKDIYPDVAWPLRLRILyEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLS 149

                .
gi 15232374 175 R 175
Cdd:cd14026 150 K 150
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
15-326 1.25e-08

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: 55.81  E-value: 1.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  15 ILDLDSIKALKILGKGATGTVF--LAHDVVSTSSSSsPFAVKLVPKSSASSLRrarweIEVLRRLSVDSNQN-PFLPRLL 91
Cdd:cd05032   2 ELPREKITLIRELGQGSFGMVYegLAKGVVKGEPET-RVAIKTVNENASMRER-----IEFLNEASVMKEFNcHHVVRLL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  92 --ASFESP-----EYFAWavpycsgGDLNVLLH------RQNDGVFSSSVIRFY--VAEIVCALEHLHTMGIAYRDLKPE 156
Cdd:cd05032  76 gvVSTGQPtlvvmELMAK-------GDLKSYLRsrrpeaENNPGLGPPTLQKFIqmAAEIADGMAYLAAKKFVHRDLAAR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 157 NILIQQSGHVTLTDFDLSRSLkkplrphfYQPDPeliidrkksrsfsrlisptaeknktgLKKTRSARVnPInrrktsfs 236
Cdd:cd05032 149 NCMVAEDLTVKIGDFGMTRDI--------YETDY--------------------------YRKGGKGLL-PV-------- 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 237 sgersnsfvgtdEYVSPEVIRGDGHDFAVDWWALGVLTYEMM-YGETPFKGKSKKETFRNVL----MKEPEfaGKPNDLT 311
Cdd:cd05032 186 ------------RWMAPESLKDGVFTTKSDVWSFGVVLWEMAtLAEQPYQGLSNEEVLKFVIdgghLDLPE--NCPDKLL 251
                       330
                ....*....|....*
gi 15232374 312 DLIRRLLVKDPNRRL 326
Cdd:cd05032 252 ELMRMCWQYNPKMRP 266
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
29-340 1.30e-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: 55.44  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  29 KGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSLRRarwEIEVLRRL--SVDSNQNPFLPRLLAS--FESPEYFAWAV 104
Cdd:cd14012   3 ESPSGTFYLVYEVVLDNSKKPGKFLTSQEYFKTSNGKK---QIQLLEKEleSLKKLRHPNLVSYLAFsiERRGRSDGWKV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 ----PYCSGGDLNVLLHRqndgVFSSSV--IRFYVAEIVCALEHLHTMGIAYRDLKPENILI---QQSGHVTLTDFdlsr 175
Cdd:cd14012  80 ylltEYAPGGSLSELLDS----VGSVPLdtARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDY---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 slkkplrphFYQPDPELIIDRKKSRSF--SRLISPtaEKNKTGLKKTrsarvnpinrRKTsfssgersnsfvgtdeyvsp 253
Cdd:cd14012 152 ---------SLGKTLLDMCSRGSLDEFkqTYWLPP--ELAQGSKSPT----------RKT-------------------- 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 evirgdghdfavDWWALGVLTYEMMYGETPFKGKSKKETFRNVLmkepefaGKPNDLTDLIRRLLVKDPNRRLgchrGAA 333
Cdd:cd14012 191 ------------DVWDLGLLFLQMLFGLDVLEKYTSPNPVLVSL-------DLSASLQDFLSKCLSLDPKKRP----TAL 247

                ....*..
gi 15232374 334 EIKELAF 340
Cdd:cd14012 248 ELLPHEF 254
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
25-312 1.56e-08

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: 55.79  E-value: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSSsspfAVKLVpKSSASSLRRARWEIEVLRRL-SVDSNQNPFLPRLLasfespEYFAWA 103
Cdd:cd14226  19 SLIGKGSFGQVVKAYDHVEQEWV----AIKII-KNKKAFLNQAQIEVRLLELMnKHDTENKYYIVRLK------RHFMFR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDL---NV--LLHRQNDGVFSSSVIRFYVAEIVCALEHLHT--MGIAYRDLKPENILIQQSghvtltdfdlSRS 176
Cdd:cd14226  88 NHLCLVFELlsyNLydLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTpeLSIIHCDLKPENILLCNP----------KRS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LKKplrphfyqpdpelIIDrkksrsFSrlisptaeknktglkktrsarvnpinrrkTSFSSGERSNSFVGTDEYVSPEVI 256
Cdd:cd14226 158 AIK-------------IID------FG-----------------------------SSCQLGQRIYQYIQSRFYRSPEVL 189
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETfrnvLMKEPEFAG-KPNDLTD 312
Cdd:cd14226 190 LGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQ----MNKIVEVLGmPPVHMLD 242
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
70-178 1.62e-08

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: 55.23  E-value: 1.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLSvdsnqNPFLPRLL-ASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVaEIVCALEHLH--TM 146
Cdd:cd14064  41 EVSILCRLN-----HPCVIQFVgACLDDPSQFAIVTQYVSGGSLFSLLHEQKRVIDLQSKLIIAV-DVAKGMEYLHnlTQ 114
                        90       100       110
                ....*....|....*....|....*....|..
gi 15232374 147 GIAYRDLKPENILIQQSGHVTLTDFDLSRSLK 178
Cdd:cd14064 115 PIIHRDLNSHNILLYEDGHAVVADFGESRFLQ 146
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
15-178 1.78e-08

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: 55.46  E-value: 1.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  15 ILDLDSIKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLV-----PKSSASSLRRArweievlrrLSVDSNQNPFLPR 89
Cdd:cd05110   3 ILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILnettgPKANVEFMDEA---------LIMASMDHPHLVR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  90 LLASFESP--EYFAWAVPYcsgGDLNVLLHRQNDGVFSSSVIRFYVaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT 167
Cdd:cd05110  74 LLGVCLSPtiQLVTQLMPH---GCLLDYVHEHKDNIGSQLLLNWCV-QIAKGMMYLEERRLVHRDLAARNVLVKSPNHVK 149
                       170
                ....*....|.
gi 15232374 168 LTDFDLSRSLK 178
Cdd:cd05110 150 ITDFGLARLLE 160
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
27-175 1.92e-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: 55.35  E-value: 1.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHD-----VVSTSSSSSPFAVKLVPKSSASslrrarwEIEVLRRLsvDSNQNPFLPRLL----ASFESP 97
Cdd:cd07863   8 IGVGAYGTVYKARDphsghFVALKSVRVQTNEDGLPLSTVR-------EVALLKRL--EAFDHPNIVRLMdvcaTSRTDR 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd07863  79 ETKVTLVFEHVDQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLAR 156
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
128-360 1.96e-08

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 55.81  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  128 VIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH-VTLTDFDLSRSLkkplrphfyqpdpeliidrkksrsfsrli 206
Cdd:PTZ00036 171 LVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNL----------------------------- 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  207 sptaeknktglkktrsarvnpinrrktsfSSGERSNSFVGTDEYVSPEVIRGD-GHDFAVDWWALGVLTYEMMYGETPFK 285
Cdd:PTZ00036 222 -----------------------------LAGQRSVSYICSRFYRAPELMLGAtNYTTHIDLWSLGCIIAEMILGYPIFS 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  286 GKSKKETFRNVL----------MKE--PEFA------------------GKPNDLTDLIRRLLVKDPNRRLgchrgaAEI 335
Cdd:PTZ00036 273 GQSSVDQLVRIIqvlgtptedqLKEmnPNYAdikfpdvkpkdlkkvfpkGTPDDAINFISQFLKYEPLKRL------NPI 346
                        250       260
                 ....*....|....*....|....*
gi 15232374  336 KELAffagvrwDLLTEVLRPPFIPL 360
Cdd:PTZ00036 347 EALA-------DPFFDDLRDPCIKL 364
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
26-325 2.07e-08

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: 54.93  E-value: 2.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLA----HDVVSTSSSSSPFAV-----------KLVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRL 90
Cdd:cd14000   1 LLGDGGFGSVYRAsykgEPVAVKIFNKHTSSNfanvpadtmlrHLRATDAMKNFRLLRQELTVLSHL-----HHPSIVYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  91 LASFESPeyFAWAVPYCSGGDLNVLLhRQNDGVFSS---SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIqqsghvt 167
Cdd:cd14000  76 LGIGIHP--LMLVLELAPLGSLDHLL-QQDSRSFASlgrTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLV------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 168 ltdfdlsrslkkplrphFYQPDPELIIDRKKSRSFSRLISPTAEKnktglkktrsarvnpinrrktsfssgersnSFVGT 247
Cdd:cd14000 146 -----------------WTLYPNSAIIIKIADYGISRQCCRMGAK------------------------------GSEGT 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 248 DEYVSPEVIRGD-GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPND-----LTDLIRRLLVKD 321
Cdd:cd14000 179 PGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLRPPLKQYECapwpeVEVLMKKCWKEN 258

                ....
gi 15232374 322 PNRR 325
Cdd:cd14000 259 PQQR 262
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
70-278 2.08e-08

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: 54.95  E-value: 2.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLhRQNDGVFSSSVIRFyVAEIVCALEHLHTMGIA 149
Cdd:cd14222  40 EVKVMRSLD-----HPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFL-RADDPFPWQQKVSF-AKGIASGMAYLHSMSII 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 150 YRDLKPENILIQQSGHVTLTDFDLSRslkkplrphfyqpdpeLIIDRKKsrsfsrliSPTAEKNKTglkKTRSARVNPIN 229
Cdd:cd14222 113 HRDLNSHNCLIKLDKTVVVADFGLSR----------------LIVEEKK--------KPPPDKPTT---KKRTLRKNDRK 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15232374 230 RRKTsfssgersnsFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMM 278
Cdd:cd14222 166 KRYT----------VVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
51-324 2.96e-08

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: 54.52  E-value: 2.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPkSSASSLRRARWEIEVLRRLSVDSnqnpfLPRLLASFESPEYFAWAVPYCSGgdlNVLLHRQNDGVFSSSVIR 130
Cdd:cd14108  30 FAAKFIP-VRAKKKTSARRELALLAELDHKS-----IVRFHDAFEKRRVVIIVTELCHE---ELLERITKRPTVCESEVR 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FYVAEIVCALEHLHTMGIAYRDLKPENILI--QQSGHVTLTDFDLSRSLkKPLRPHFYQpdpeliidrkksrsfsrlisp 208
Cdd:cd14108 101 SYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQEL-TPNEPQYCK--------------------- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 209 taeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKS 288
Cdd:cd14108 159 ------------------------------------YGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGEN 202
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15232374 289 KKETFR-----NVLMKEPEFAGKPNDLTDLIRRLLVKDPNR 324
Cdd:cd14108 203 DRTTLMnirnyNVAFEESMFKDLCREAKGFIIKVLVSDRLR 243
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
15-177 2.96e-08

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: 54.65  E-value: 2.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  15 ILDLDSIKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSLRRarweiEVLRRLSVDSN-QNPFLPRLLAS 93
Cdd:cd05109   3 ILKETELKKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANK-----EILDEAYVMAGvGSPYVCRLLGI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 --FESPEYFAWAVPYcsGGDLNVLlhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:cd05109  78 clTSTVQLVTQLMPY--GCLLDYV--RENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDF 153

                ....*.
gi 15232374 172 DLSRSL 177
Cdd:cd05109 154 GLARLL 159
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
127-182 3.35e-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: 54.60  E-value: 3.35e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 127 SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLR 182
Cdd:cd07835  99 PLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGVPVR 154
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
24-283 3.57e-08

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: 54.29  E-value: 3.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVpkssasSLRRARWEIE-VLRRLSVDSN-QNPFLPRLLASFESPEYFA 101
Cdd:cd06640   9 LERIGKGSFGEVFKGID----NRTQQVVAIKII------DLEEAEDEIEdIQQEITVLSQcDSPYVTKYYGSYLKGTKLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkpl 181
Cdd:cd06640  79 IIMEYLGGGSALDLLRA---GPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQL---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 182 rphfyqpdpeliidrkksrsfsrlisptaekNKTGLKKtrsarvnpinrrktsfssgersNSFVGTDEYVSPEVIRGDGH 261
Cdd:cd06640 152 -------------------------------TDTQIKR----------------------NTFVGTPFWMAPEVIQQSAY 178
                       250       260
                ....*....|....*....|..
gi 15232374 262 DFAVDWWALGVLTYEMMYGETP 283
Cdd:cd06640 179 DSKADIWSLGITAIELAKGEPP 200
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
19-291 4.85e-08

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 54.29  E-value: 4.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFlahdVVSTSSSSSPFAVKLVPKSSASSLRRarweiEVLRRLSVDSNQN-PFLPRLLASFESP 97
Cdd:cd06650   5 DDFEKISELGAGNGGVVF----KVSHKPSGLVMARKLIHLEIKPAIRN-----QIIRELQVLHECNsPYIVGFYGAFYSD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHL-HTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd06650  76 GEISICMEHMDGGSLDQVLKKA--GRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LkkplrphfyqpdpeliIDrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEVI 256
Cdd:cd06650 154 L----------------ID-------------------------------------------SMANSFVGTRSYMSPERL 174
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15232374 257 RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKE 291
Cdd:cd06650 175 QGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKE 209
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
121-341 5.31e-08

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 53.87  E-value: 5.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 121 DGVFSSSVIRFYVAEIVCALEHLH-TMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKP--LRPHFYQPDPELIIDrk 197
Cdd:cd14011 108 DYKLYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQAtdQFPYFREYDPNLPPL-- 185
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 198 ksrsfsrlisptaeknktglkktrsARVNPinrrktsfssgersnsfvgtdEYVSPEVIRGDGHDFAVDWWALGVLTYEM 277
Cdd:cd14011 186 -------------------------AQPNL---------------------NYLAPEYILSKTCDPASDMFSLGVLIYAI 219
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 278 MY-GETPFKGKSKKETFRNVL-----MKEPEFAGKPNDLTDLIRRLLVKDPNRRLGCHrgaaEIKELAFF 341
Cdd:cd14011 220 YNkGKPLFDCVNNLLSYKKNSnqlrqLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAE----QLSKIPFF 285
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
136-325 5.57e-08

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 53.58  E-value: 5.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 136 IVCALEHLHT-MGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfyqpdpeliIDrkksrsfsrlisptaeknk 214
Cdd:cd06617 112 IVKALEYLHSkLSVIHRDVKPSNVLINRNGQVKLCDFGISGYL----------------VD------------------- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 215 tGLKKTRSArvnpinrrktsfssgersnsfvGTDEYVSPEVIRGD----GHDFAVDWWALGVLTYEMMYGETPFKG-KSK 289
Cdd:cd06617 157 -SVAKTIDA----------------------GCKPYMAPERINPElnqkGYDVKSDVWSLGITMIELATGRFPYDSwKTP 213
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15232374 290 KETFRNVLmKEPEFAgKPN-----DLTDLIRRLLVKDPNRR 325
Cdd:cd06617 214 FQQLKQVV-EEPSPQ-LPAekfspEFQDFVNKCLKKNYKER 252
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
27-325 5.93e-08

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: 53.51  E-value: 5.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSSsspfAVKLVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd06645  19 IGSGTYGDVYKARNVNTGELA----AIKVIKLEPGEDFAVVQQEIIMMKDC-----KHSNIVAYFGSYLRRDKLWICMEF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSlkkplrphfy 186
Cdd:cd06645  90 CGGGSLQDIYHVT--GPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQ---------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 187 qpdpeliidrkksrsfsrlISPTAEKNKtglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVI---RGDGHDF 263
Cdd:cd06645 158 -------------------ITATIAKRK----------------------------SFIGTPYWMAPEVAaveRKGGYNQ 190
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 264 AVDWWALGVLTYEMMYGETP-FKGKSKKETFrnvLMKEPEFagKPNDLTD----------LIRRLLVKDPNRR 325
Cdd:cd06645 191 LCDIWAVGITAIELAELQPPmFDLHPMRALF---LMTKSNF--QPPKLKDkmkwsnsfhhFVKMALTKNPKKR 258
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
21-288 6.19e-08

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: 53.51  E-value: 6.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  21 IKALKILGKGATGTVFLAH---DVvstssssspfAVKLVP------------KSSASSLRRARWEIEVLrrlsvdsnqnp 85
Cdd:cd14063   2 LEIKEVIGKGRFGRVHRGRwhgDV----------AIKLLNidylneeqleafKEEVAAYKNTRHDNLVL----------- 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  86 flprLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDgVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIqQSGH 165
Cdd:cd14063  61 ----FMGACMDPPHLAIVTSLCKGRTLYSLIHERKE-KFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGR 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 166 VTLTDFDLSrSLKKPLRPhfYQPDPELIIDRkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnsfv 245
Cdd:cd14063 135 VVITDFGLF-SLSGLLQP--GRREDTLVIPN------------------------------------------------- 162
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232374 246 GTDEYVSPEVIR--------GDGHDF--AVDWWALGVLTYEMMYGETPFKGKS 288
Cdd:cd14063 163 GWLCYLAPEIIRalspdldfEESLPFtkASDVYAFGTVWYELLAGRWPFKEQP 215
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
65-326 7.44e-08

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: 53.11  E-value: 7.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  65 RRARWEIEVLRRLsvdsnQNPFLPRLLASFES-PEYFAWaVPYCSGGDLNVLLHRQndGVFS----SSVIRfyvaEIVCA 139
Cdd:cd14088  44 KAAKNEINILKMV-----KHPNILQLVDVFETrKEYFIF-LELATGREVFDWILDQ--GYYSerdtSNVIR----QVLEA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 140 LEHLHTMGIAYRDLKPENILI---QQSGHVTLTDFDLSrslkkplrphfyqpdpeliidrkksrsfsrlisptaeKNKTG 216
Cdd:cd14088 112 VAYLHSLKIVHRNLKLENLVYynrLKNSKIVISDFHLA-------------------------------------KLENG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 217 LKKtrsarvNPinrrktsfssgersnsfVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSK------- 289
Cdd:cd14088 155 LIK------EP-----------------CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEeddyenh 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15232374 290 -KETFRNVLMKEPEFaGKP--NDLT----DLIRRLLVKDPNRRL 326
Cdd:cd14088 212 dKNLFRKILAGDYEF-DSPywDDISqaakDLVTRLMEVEQDQRI 254
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
26-285 7.71e-08

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; 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). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 53.04  E-value: 7.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSsasslRRARW----------EIEVLRRLSVDSNQnpfLPRLLASFE 95
Cdd:cd14102   7 VLGSGGFGTVYAGSRI----ADGLPVAVKHVVKE-----RVTEWgtlngvmvplEIVLLKKVGSGFRG---VIKLLDWYE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAV--PYCSGGDLNVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ-QSGHVTLTDFD 172
Cdd:cd14102  75 RPDGFLIVMerPEPVKDLFDFITEK---GALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 173 LSRSLKKPLrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgerSNSFVGTDEYVS 252
Cdd:cd14102 152 SGALLKDTV-----------------------------------------------------------YTDFDGTRVYSP 172
                       250       260       270
                ....*....|....*....|....*....|....
gi 15232374 253 PEVIRGDG-HDFAVDWWALGVLTYEMMYGETPFK 285
Cdd:cd14102 173 PEWIRYHRyHGRSATVWSLGVLLYDMVCGDIPFE 206
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
129-291 9.47e-08

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: 53.09  E-value: 9.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlrphfyqpdpeliidrkksrsfsrlisp 208
Cdd:cd07871 105 VKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVP---------------------------- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 209 taeknktglKKTRSARVNPINRRKtsfssgerSNSFVGTDEYVSPevirgdghdfaVDWWALGVLTYEMMYGETPFKGKS 288
Cdd:cd07871 157 ---------TKTYSNEVVTLWYRP--------PDVLLGSTEYSTP-----------IDMWGVGCILYEMATGRPMFPGST 208

                ...
gi 15232374 289 KKE 291
Cdd:cd07871 209 VKE 211
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
27-177 1.03e-07

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: 53.07  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTV----------FLAHDVVSTSSSSSP--FAVKLVpKSSASSLRRARW--EIEVLRRLsvdsnQNPFLPRLLA 92
Cdd:cd05095  13 LGEGQFGEVhlceaegmekFMDKDFALEVSENQPvlVAVKML-RADANKNARNDFlkEIKIMSRL-----KDPNIIRLLA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  93 SFESPEYFAWAVPYCSGGDLNVLLHRQ----------NDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQ 162
Cdd:cd05095  87 VCITDDPLCMITEYMENGDLNQFLSRQqpegqlalpsNALTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGK 166
                       170
                ....*....|....*
gi 15232374 163 SGHVTLTDFDLSRSL 177
Cdd:cd05095 167 NYTIKIADFGMSRNL 181
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
26-283 1.09e-07

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: 52.82  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAhdvvsTSSSSSPFAVKLVPKSSASSLR------RARWEIEVLRRLSvDSNQNPFLPRLLaSFESPEY 99
Cdd:cd06631   8 VLGKGAYGTVYCG-----LTSTGQLIAVKQVELDTSDKEKaekeyeKLQEEVDLLKTLK-HVNIVGYLGTCL-EDNVVSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAVPycsGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkk 179
Cdd:cd06631  81 FMEFVP---GGSIASILARF--GALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRL-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 180 plrphfyqpdpeliIDRKKSRSFSRLisptaeknktgLKKTRsarvnpinrrktsfssgersnsfvGTDEYVSPEVIRGD 259
Cdd:cd06631 154 --------------CINLSSGSQSQL-----------LKSMR------------------------GTPYWMAPEVINET 184
                       250       260
                ....*....|....*....|....
gi 15232374 260 GHDFAVDWWALGVLTYEMMYGETP 283
Cdd:cd06631 185 GHGRKSDIWSIGCTVFEMATGKPP 208
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
18-318 1.10e-07

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 53.97  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    18 LDSIKALKILGKGATGTVFLahdvVSTSSSSSPFAVKLVPKSSASSLRRARW--EIEVLRRLSvDSNQNPFLPRLLASFE 95
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFL----VKHKRTQEFFCWKAISYRGLKEREKSQLviEVNVMRELK-HKNIVRYIDRFLNKAN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374    96 SPEYFAwaVPYCSGGDL--NVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMG-------IAYRDLKPENIL----IQQ 162
Cdd:PTZ00266   87 QKLYIL--MEFCDAGDLsrNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFlstgIRH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   163 SGHVTLTDFDLSRSlkkplrphfyqpdpeliidrkksrsfsrlisPTAEKNKTGLKKtrsarvnpinrrktSFSSGERSN 242
Cdd:PTZ00266  165 IGKITAQANNLNGR-------------------------------PIAKIGDFGLSK--------------NIGIESMAH 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   243 SFVGTDEYVSPEVI--RGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEF--AGKPNDLTDLIRRLL 318
Cdd:PTZ00266  200 SCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHKANNFSQLISELKRGPDLpiKGKSKELNILIKNLL 279
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
27-175 1.18e-07

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: 52.73  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSLRRARwEIEVLRRLsvDSNQNPFLPRLL----ASFESPEYFAW 102
Cdd:cd07862   9 IGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIR-EVAVLRHL--ETFEHPNVVRLFdvctVSRTDRETKLT 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 103 AVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd07862  86 LVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLAR 158
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
25-161 1.25e-07

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 52.74  E-value: 1.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVvSTSSSSSPFAVKLVPKSSasslrraRWEI----EVLRRLSVDSNQNPFLP------RLLASF 94
Cdd:cd13981   6 KELGEGGYASVYLAKDD-DEQSDGSLVALKVEKPPS-------IWEFyicdQLHSRLKNSRLRESISGahsahlFQDESI 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374  95 ESPEYFawavPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ 161
Cdd:cd13981  78 LVMDYS----SQGTLLDVVNKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLR 140
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
135-325 1.52e-07

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: 52.51  E-value: 1.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 135 EIVCALEHLHTMGIAYRDLKPENILIQQSG-HVTLTDFDLSRslkkplrphfyqpdPELIIDRKKSRSFSRLISPTaekn 213
Cdd:cd14049 128 QLLEGVTYIHSMGIVHRDLKPRNIFLHGSDiHVRIGDFGLAC--------------PDILQDGNDSTTMSRLNGLT---- 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 214 ktglkktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMygeTPFKGKSKK-ET 292
Cdd:cd14049 190 ---------------------------HTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---QPFGTEMERaEV 239
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15232374 293 FRNVLMKE-PE-FAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14049 240 LTQLRNGQiPKsLCKRWPVQAKYIKLLTSTEPSER 274
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
91-325 1.59e-07

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: 52.34  E-value: 1.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  91 LASFESPEYFAWAVPYCSGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTD 170
Cdd:cd06646  72 FGSYLSREKLWICMEYCGGGSLQDIYHVT--GPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLAD 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 171 FDLSRSlkkplrphfyqpdpeliidrkksrsfsrlISPTAEKNKtglkktrsarvnpinrrktsfssgersnSFVGTDEY 250
Cdd:cd06646 150 FGVAAK-----------------------------ITATIAKRK----------------------------SFIGTPYW 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 251 VSPEVI---RGDGHDFAVDWWALGVLTYEMMYGETP-FKGKSKKETFrnvLMKEPEFagKPNDLTD----------LIRR 316
Cdd:cd06646 173 MAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALF---LMSKSNF--QPPKLKDktkwsstfhnFVKI 247

                ....*....
gi 15232374 317 LLVKDPNRR 325
Cdd:cd06646 248 SLTKNPKKR 256
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
139-325 1.79e-07

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: 52.35  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 139 ALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlrphfyqpdpeliidrkksrsfsrlisptaeknktglk 218
Cdd:cd06658 130 ALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKE-------------------------------------- 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 219 ktrsarvnpINRRKtsfssgersnSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLM 298
Cdd:cd06658 172 ---------VPKRK----------SLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRD 232
                       170       180       190
                ....*....|....*....|....*....|.
gi 15232374 299 KEPEFAGKPNDLTDLIRR----LLVKDPNRR 325
Cdd:cd06658 233 NLPPRVKDSHKVSSVLRGfldlMLVREPSQR 263
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
19-325 1.80e-07

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 52.16  E-value: 1.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAhdvvstssSSSPFAVKLVPKSSASSLRRARW-----EIEVLRRLSvdsnqNPFLPRLLAS 93
Cdd:cd06622   1 DEIEVLDELGKGNYGSVYKV--------LHRPTGVTMAMKEIRLELDESKFnqiimELDILHKAV-----SPYIVDFYGA 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 F--ESPEYFAwaVPYCSGGDLNVLL-HRQNDGVFSSSVIRFYVAEIVCALEHL-HTMGIAYRDLKPENILIQQSGHVTLT 169
Cdd:cd06622  68 FfiEGAVYMC--MEYMDAGSLDKLYaGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLC 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 170 DFDLSRSLKKPLrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsARVNpinrrktsfssgersnsfVGTDE 249
Cdd:cd06622 146 DFGVSGNLVASL-----------------------------------------AKTN------------------IGCQS 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 250 YVSPEVIRGDG------HDFAVDWWALGVLTYEMMYGETPFkgksKKETFRNVLMK------------EPEFAGkpnDLT 311
Cdd:cd06622 167 YMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPY----PPETYANIFAQlsaivdgdpptlPSGYSD---DAQ 239
                       330
                ....*....|....
gi 15232374 312 DLIRRLLVKDPNRR 325
Cdd:cd06622 240 DFVAKCLNKIPNRR 253
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
129-376 2.01e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 52.74  E-value: 2.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSlkkplrphfyqpdpeliidrkKSRSFsrLISP 208
Cdd:cd07875 128 MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART---------------------AGTSF--MMTP 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 209 taeknktglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKG-- 286
Cdd:cd07875 185 -----------------------------------YVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGtd 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 287 --------------------KSKKETFRNVLMKEPEFAG---------------------KPNDLTDLIRRLLVKDPNRR 325
Cdd:cd07875 230 hidqwnkvieqlgtpcpefmKKLQPTVRTYVENRPKYAGysfeklfpdvlfpadsehnklKASQARDLLSKMLVIDASKR 309
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15232374 326 LGCHRGAAEIkelafFAGVRWDLLTEVLRPPFIPlrdDGELtvggfDIREH 376
Cdd:cd07875 310 ISVDEALQHP-----YINVWYDPSEAEAPPPKIP---DKQL-----DEREH 347
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
28-290 2.56e-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: 51.90  E-value: 2.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  28 GKGATGTVFLAhdVVSTSSSSSPFAVKLV--PKS-----SASSLRrarwEIEVLRRLS---VDSNQNPFLP----RLLAS 93
Cdd:cd07842   9 GRGTYGRVYKA--KRKNGKDGKEYAIKKFkgDKEqytgiSQSACR----EIALLRELKhenVVSLVEVFLEhadkSVYLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 FESPEYFAWAVpycsggdlnVLLHRQNDGV-FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI----QQSGHVTL 168
Cdd:cd07842  83 FDYAEHDLWQI---------IKFHRQAKRVsIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 169 TDFDLSRSLKKPLRPhFYQPDPeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgersnsFVGTD 248
Cdd:cd07842 154 GDLGLARLFNAPLKP-LADLDP-----------------------------------------------------VVVTI 179
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15232374 249 EYVSPEVIRGDGH-DFAVDWWALGVLTYEMMYGETPFKGKSKK 290
Cdd:cd07842 180 WYRAPELLLGARHyTKAIDIWAIGCIFAELLTLEPIFKGREAK 222
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
15-177 2.76e-07

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: 51.65  E-value: 2.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  15 ILDLDSIKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSAsslRRARWEI--EVLRRLSVDsnqNPFLPRLLA 92
Cdd:cd05057   3 IVKETELEKGKVLGSGAFGTVYKGVWIPEGEKVKIPVAIKVLREETG---PKANEEIldEAYVMASVD---HPHLVRLLG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  93 SFESPEY--FAWAVPYCSggdlnvLLH--RQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTL 168
Cdd:cd05057  77 ICLSSQVqlITQLMPLGC------LLDyvRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKI 150

                ....*....
gi 15232374 169 TDFDLSRSL 177
Cdd:cd05057 151 TDFGLAKLL 159
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
26-285 3.60e-07

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: 51.12  E-value: 3.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASSLRR----ARWEIEVLRRLSVDSNQNPFLpRLLASFESPEYFA 101
Cdd:cd14100   7 LLGSGGFGSVYSGIRV----ADGAPVAIKHVEKDRVSEWGElpngTRVPMEIVLLKKVGSGFRGVI-RLLDWFERPDSFV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAV--PYCSGGDLNVLLHRqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ-QSGHVTLTDFDLSRSLK 178
Cdd:cd14100  82 LVLerPEPVQDLFDFITER---GALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 KPLrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVI-- 256
Cdd:cd14100 159 DTV-----------------------------------------------------------YTDFDGTRVYSPPEWIrf 179
                       250       260       270
                ....*....|....*....|....*....|
gi 15232374 257 -RGDGHDFAVdwWALGVLTYEMMYGETPFK 285
Cdd:cd14100 180 hRYHGRSAAV--WSLGILLYDMVCGDIPFE 207
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
106-286 3.65e-07

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: 51.24  E-value: 3.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHT---MGIAYRDLKPENILIQQS------GHVTL--TDFDLS 174
Cdd:cd14061  74 YARGGALNRVLAGRK---IPPHVLVDWAIQIARGMNYLHNeapVPIIHRDLKSSNILILEAienedlENKTLkiTDFGLA 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RSLkkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkkTRSARVnpinrrktsfssgersnSFVGTDEYVSPE 254
Cdd:cd14061 151 REW------------------------------------------HKTTRM-----------------SAAGTYAWMAPE 171
                       170       180       190
                ....*....|....*....|....*....|..
gi 15232374 255 VIRGDGHDFAVDWWALGVLTYEMMYGETPFKG 286
Cdd:cd14061 172 VIKSSTFSKASDVWSYGVLLWELLTGEVPYKG 203
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-279 3.82e-07

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: 51.03  E-value: 3.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  18 LDSIKALKILGKGATGTVFLAHDVVSTSSssspFAVK--LVPKSSASSLRRARwEIEVLRRLsvdsnQNPFLPRLLASFE 95
Cdd:cd14048   5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCN----YAVKriRLPNNELAREKVLR-EVRALAKL-----DHPGIVRYFNAWL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 S--PE---------YFAWAVPYCSGGDLNVLLHRQNDGVFSS-SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQS 163
Cdd:cd14048  75 ErpPEgwqekmdevYLYIQMQLCRKENLKDWMNRRCTMESRElFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 164 GHVTLTDFDLSrslkkplrPHFYQPDPEliidrkksrsFSRLISPTAEKNKTGLkktrsarvnpinrrktsfssgersns 243
Cdd:cd14048 155 DVVKVGDFGLV--------TAMDQGEPE----------QTVLTPMPAYAKHTGQ-------------------------- 190
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15232374 244 fVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMY 279
Cdd:cd14048 191 -VGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIY 225
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
125-182 4.17e-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: 50.97  E-value: 4.17e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 125 SSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLR 182
Cdd:cd07860  98 PLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVR 155
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
106-325 4.60e-07

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: 50.74  E-value: 4.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphf 185
Cdd:cd05063  87 YMENGALDKYL-RDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVL-------- 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yQPDPEliidrkksrsfsrlisptaeknktGLKKTRSARVnPInrrktsfssgersnsfvgtdEYVSPEVIRGDGHDFAV 265
Cdd:cd05063 158 -EDDPE------------------------GTYTTSGGKI-PI--------------------RWTAPEAIAYRKFTSAS 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 266 DWWALGVLTYEMM-YGETPFKGKSKKETFR--NVLMKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd05063 192 DVWSFGIVMWEVMsFGERPYWDMSNHEVMKaiNDGFRLPAPMDCPSAVYQLMLQCWQQDRARR 254
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
27-182 4.93e-07

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: 50.89  E-value: 4.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLA-----HDVVSTSSSSSPFAVKLVPkssASSLRrarwEIEVLRRLsvdsnQNPFLPRLLASFESPEYFA 101
Cdd:cd07839   8 IGEGTYGTVFKAknretHEIVALKRVRLDDDDEGVP---SSALR----EICLLKEL-----KHKNIVRLYDVLHSDKKLT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGgDLNVLLHRQNdGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPL 181
Cdd:cd07839  76 LVFEYCDQ-DLKKYFDSCN-GDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPV 153

                .
gi 15232374 182 R 182
Cdd:cd07839 154 R 154
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
106-286 5.23e-07

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 51.30  E-value: 5.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  106 YCSGGDLNV---LLHRQNDGVFSSSvIRFYVAEIVC-------ALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:PTZ00024  89 YVEGDFINLvmdIMASDLKKVVDRK-IRLTESQVKCillqilnGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLAR 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  176 SlkkplrphfYQPDPeliidrkksrsfsrlISPTAEKNKTGLKKtrsarvnpinrrktsfssgERSNSFVGTDEYVSPEV 255
Cdd:PTZ00024 168 R---------YGYPP---------------YSDTLSKDETMQRR-------------------EEMTSKVVTLWYRAPEL 204
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15232374  256 IRG-DGHDFAVDWWALGVLTYEMMYGETPFKG 286
Cdd:PTZ00024 205 LMGaEKYHFAVDMWSVGCIFAELLTGKPLFPG 236
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
22-171 6.02e-07

Catalytic domain of the Dual-specificity protein kinase, YAK1; 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 proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 50.71  E-value: 6.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSSsspfAVKLVpKSSASSLRRARWEIEVLRRLS--VDSNQNPFLPRLLASFEspey 99
Cdd:cd14212   2 LVLDLLGQGTFGQVVKCQDLKTNKLV----AVKVL-KNKPAYFRQAMLEIAILTLLNtkYDPEDKHHIVRLLDHFM---- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 fawavpYCS---------GGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQ--SGHVTL 168
Cdd:cd14212  73 ------HHGhlcivfellGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNldSPEIKL 146

                ...
gi 15232374 169 TDF 171
Cdd:cd14212 147 IDF 149
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
25-339 6.13e-07

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: 50.59  E-value: 6.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSVDSNQNPFLPrllASFESPE------ 98
Cdd:cd14036   6 RVIAEGGFAFVYEAQDV----GTGKEYALKRLLSNEEEKNKAIIQEINFMKKLSGHPNIVQFCS---AASIGKEesdqgq 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 -YFAWAVPYCSGGDLNVLLHRQNDGVFS-SSVIR-FYvaEIVCALEHLHTMG--IAYRDLKPENILIQQSGHVTLTDFDL 173
Cdd:cd14036  79 aEYLLLTELCKGQLVDFVKKVEAPGPFSpDTVLKiFY--QTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SRSLkkPLRPHFyqpdpeliidrkksrsfsrliSPTAEKnktglkktRSARVNPINRRKTSFssgersnsfvgtdeYVSP 253
Cdd:cd14036 157 ATTE--AHYPDY---------------------SWSAQK--------RSLVEDEITRNTTPM--------------YRTP 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 254 EVIrgdghDF--------AVDWWALGVLTYEMMYGETPFKgKSKKETFRNVLMKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14036 192 EMI-----DLysnypigeKQDIWALGCILYLLCFRKHPFE-DGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEER 265
                       330
                ....*....|....
gi 15232374 326 LGCHRGAAEIKELA 339
Cdd:cd14036 266 LSITEIVEQLQELA 279
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
195-326 6.26e-07

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 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: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 50.04  E-value: 6.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 195 DRKKSRSFSRLISPTAEKNKTGLK----KTRSARVNPINRRKTSFSSGERSNSFVGTDE----------YVSPEVIRGDG 260
Cdd:cd14022  83 EEEAARLFYQIASAVAHCHDGGLVlrdlKLRKFVFKDEERTRVKLESLEDAYILRGHDDslsdkhgcpaYVSPEILNTSG 162
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 261 H--DFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVlmKEPEFaGKPNDLTD----LIRRLLVKDPNRRL 326
Cdd:cd14022 163 SysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQF-NIPETLSPkakcLIRSILRREPSERL 231
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
27-173 6.69e-07

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 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: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 50.30  E-value: 6.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLA---HDVVSTSSSSSPFAVK-LVPKSSASslrRARWEIEVLRRLSVDSNQNPflprLLASFESPEYFAW 102
Cdd:cd14019   9 IGEGTFSSVYKAedkLHDLYDRNKGRLVALKhIYPTSSPS---RILNELECLERLGGSNNVSG----LITAFRNEDQVVA 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 103 AVPYCSGGDLNVLLHRqndgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI-QQSGHVTLTDFDL 173
Cdd:cd14019  82 VLPYIEHDDFRDFYRK-----MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYnRETGKGVLVDFGL 148
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
27-291 7.45e-07

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: 50.08  E-value: 7.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHdvvstssSSSPFAVKL--VPKSSASSLRRARWEIEVLRRLSVDsnqNPFLprLLASFESPEyFAWAV 104
Cdd:cd14062   1 IGSGSFGTVYKGR-------WHGDVAVKKlnVTDPTPSQLQAFKNEVAVLRKTRHV---NILL--FMGYMTKPQ-LAIVT 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLNVLLHRQnDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrph 184
Cdd:cd14062  68 QWCEGSSLYKHLHVL-ETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLA---------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 185 fyqpdpeliidrkksrsfsrlispTAeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEVIR---GDGH 261
Cdd:cd14062 137 ------------------------TV---------------------KTRWSGSQQFEQPTGSILWMAPEVIRmqdENPY 171
                       250       260       270
                ....*....|....*....|....*....|
gi 15232374 262 DFAVDWWALGVLTYEMMYGETPFKGKSKKE 291
Cdd:cd14062 172 SFQSDVYAFGIVLYELLTGQLPYSHINNRD 201
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
19-325 7.76e-07

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: 50.38  E-value: 7.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFlahdVVSTSSSSSPFAVKLV-PKSSASSLRRARWEIevLRRLSvdsnQNPFLPRLLASFesp 97
Cdd:cd06639  22 DTWDIIETIGKGTYGKVY----KVTNKKDGSLAAVKILdPISDVDEEIEAEYNI--LRSLP----NHPNVVKFYGMF--- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 eyfaWAVPYCSGGDLNVLLHRQNDGVFS--------------SSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQS 163
Cdd:cd06639  89 ----YKADQYVGGQLWLVLELCNGGSVTelvkgllkcgqrldEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 164 GHVTLTDFDLSRSLKkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrSARVnpinRRKTSfssgersns 243
Cdd:cd06639 165 GGVKLVDFGVSAQLT-------------------------------------------SARL----RRNTS--------- 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 244 fVGTDEYVSPEVIRGD-----GHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKEPEFAGKPN----DLTDLI 314
Cdd:cd06639 189 -VGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPPPTLLNPEkwcrGFSHFI 267
                       330
                ....*....|.
gi 15232374 315 RRLLVKDPNRR 325
Cdd:cd06639 268 SQCLIKDFEKR 278
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
27-191 9.44e-07

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: 50.23  E-value: 9.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVvstsSSSSPFAVKL---VPKssasslRRARWEIEVLRRLsvdsNQNPFLPRLLASF--ESPEYFA 101
Cdd:cd14132  26 IGRGKYSEVFEGINI----GNNEKVVIKVlkpVKK------KKIKREIKILQNL----RGGPNIVKLLDVVkdPQSKTPS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLhrqndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH-VTLTDFDLSrslkkp 180
Cdd:cd14132  92 LIFEYVNNTDFKTLY-----PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLA------ 160
                       170
                ....*....|.
gi 15232374 181 lrpHFYQPDPE 191
Cdd:cd14132 161 ---EFYHPGQE 168
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
115-325 1.06e-06

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


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 49.99  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 115 LLHRQNDGVFSSSViRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfyqpdpelii 194
Cdd:cd07848  89 LLEEMPNGVPPEKV-RSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNL----------------- 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 195 drkksrsfsrlisptaeknktglkktrsarvnpinrrktsfSSGERSN--SFVGTDEYVSPEVIRGDGHDFAVDWWALGV 272
Cdd:cd07848 151 -----------------------------------------SEGSNANytEYVATRWYRSPELLLGAPYGKAVDMWSVGC 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 273 LTYEMMYGETPFKGKSKKE---TFRNVL-------MK----EPEFAG-------KPNDLT------------DLIRRLLV 319
Cdd:cd07848 190 ILGELSDGQPLFPGESEIDqlfTIQKVLgplpaeqMKlfysNPRFHGlrfpavnHPQSLErrylgilsgvllDLMKNLLK 269

                ....*.
gi 15232374 320 KDPNRR 325
Cdd:cd07848 270 LNPTDR 275
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
136-325 1.06e-06

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: 50.06  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 136 IVCALEHL-HTMGIAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrphfyqpdpeliidrkksrsfSRLISPTAeknk 214
Cdd:cd06616 118 TVKALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGIS----------------------------GQLVDSIA---- 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 215 tglkKTRSARVNPinrrktsfssgersnsfvgtdeYVSPEVI----RGDGHDFAVDWWALGVLTYEMMYGETPF-KGKSK 289
Cdd:cd06616 166 ----KTRDAGCRP----------------------YMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPYpKWNSV 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15232374 290 KETFRNVLMKEP---------EFAgkpNDLTDLIRRLLVKDPNRR 325
Cdd:cd06616 220 FDQLTQVVKGDPpilsnseerEFS---PSFVNFVNLCLIKDESKR 261
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
21-186 1.10e-06

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: 49.89  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  21 IKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSVDsnqnpFLPRLLASFESP--E 98
Cdd:cd05081   6 LKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSD-----FIVKYRGVSYGPgrR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLNVLLHRqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLk 178
Cdd:cd05081  81 SLRLVMEYLPSGCLRDFLQR-HRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLL- 158

                ....*...
gi 15232374 179 kPLRPHFY 186
Cdd:cd05081 159 -PLDKDYY 165
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
88-334 1.30e-06

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: 49.67  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  88 PRLLASFE----SPEYFAWAVPYCSGGDLNVLLHRQNdgVFSSSVIRFYVAEIVCALEHLHTMG--IAYRDLKPENILI- 160
Cdd:cd14041  70 PRIVKLYDyfslDTDSFCTVLEYCEGNDLDFYLKQHK--LMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLv 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 161 --QQSGHVTLTDFDLSRslkkplrphfyqpdpelIIDRKKSRSFSRLisptaeknktglkktrsarvnpinrrktsfssg 238
Cdd:cd14041 148 ngTACGEIKITDFGLSK-----------------IMDDDSYNSVDGM--------------------------------- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 239 ERSNSFVGTDEYVSPE--VIRGDGHDFA--VDWWALGVLTYEMMYGETPF-KGKSKKETFR-NVLMK--EPEFAGKPN-- 308
Cdd:cd14041 178 ELTSQGAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFYQCLYGRKPFgHNQSQQDILQeNTILKatEVQFPPKPVvt 257
                       250       260
                ....*....|....*....|....*..
gi 15232374 309 -DLTDLIRRLLVKDPNRRLGCHRGAAE 334
Cdd:cd14041 258 pEAKAFIRRCLAYRKEDRIDVQQLACD 284
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
26-160 1.52e-06

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: 49.18  E-value: 1.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAhdvvstSSSSSPFAVKLVPKSSasSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEyfAWAVP 105
Cdd:cd14068   1 LLGDGGFGSVYRA------VYRGEDVAVKIFNKHT--SFRLLRQELVVLSHL-----HHPSLVALLAAGTAPR--MLVME 65
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 106 YCSGGDLNVLLHRQNDGVFSS--SVIRFYVAEivcALEHLHTMGIAYRDLKPENILI 160
Cdd:cd14068  66 LAPKGSLDALLQQDNASLTRTlqHRIALHVAD---GLRYLHSAMIIYRDLKPHNVLL 119
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
70-278 1.61e-06

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: 49.18  E-value: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFyVAEIVCALEHLHTMGIA 149
Cdd:cd14221  40 EVKVMRCL-----EHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSHYPWSQRVSF-AKDIASGMAYLHSMNII 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 150 YRDLKPENILIQQSGHVTLTDFDLSRslkkplrphfyqpdpeLIIDRKKSrsfsrlisptAEKNKTGLKKTRSARVnpin 229
Cdd:cd14221 114 HRDLNSHNCLVRENKSVVVADFGLAR----------------LMVDEKTQ----------PEGLRSLKKPDRKKRY---- 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15232374 230 rrktsfssgersnSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMM 278
Cdd:cd14221 164 -------------TVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
15-177 1.62e-06

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: 49.64  E-value: 1.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  15 ILDLDSIKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASslrRARWEI--EVLRRLSVDsnqNPFLPRLLA 92
Cdd:cd05108   3 ILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSP---KANKEIldEAYVMASVD---NPHVCRLLG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  93 S--FESPEYFAWAVPYcsGGDLNVLlhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTD 170
Cdd:cd05108  77 IclTSTVQLITQLMPF--GCLLDYV--REHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITD 152

                ....*..
gi 15232374 171 FDLSRSL 177
Cdd:cd05108 153 FGLAKLL 159
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
124-291 1.89e-06

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: 49.29  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 124 FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLRPhfyqpdpeliidrkksrsfs 203
Cdd:cd07845 105 FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKP-------------------- 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 204 rlISPTaeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRG-DGHDFAVDWWALGVLTYEMMYGET 282
Cdd:cd07845 165 --MTPK-----------------------------------VVTLWYRAPELLLGcTTYTTAIDMWAVGCILAELLAHKP 207

                ....*....
gi 15232374 283 PFKGKSKKE 291
Cdd:cd07845 208 LLPGKSEIE 216
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
136-325 1.95e-06

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: 49.25  E-value: 1.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 136 IVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlrphfyqpdpeliidrkksrsfsrlisptaeknkt 215
Cdd:cd06657 125 VLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE----------------------------------- 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 216 glkktrsarvnpINRRKtsfssgersnSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRN 295
Cdd:cd06657 170 ------------VPRRK----------SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKM 227
                       170       180       190
                ....*....|....*....|....*....|....
gi 15232374 296 VLMKEPEFAGKPNDLTDLIR----RLLVKDPNRR 325
Cdd:cd06657 228 IRDNLPPKLKNLHKVSPSLKgfldRLLVRDPAQR 261
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
130-329 1.96e-06

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 49.17  E-value: 1.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 130 RFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFdlsrSLKKPlrphFYQPDPeliidrkksrsfsrlispt 209
Cdd:cd13980 100 KWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDF----ASFKP----TYLPED------------------- 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 210 aeknktglkktrsarvNP--------INRRKTSFSSGERsnsFVGTDEYVSPEVIRGDGHDFAVDWWALG-VLTYEMMYG 280
Cdd:cd13980 153 ----------------NPadfsyffdTSRRRTCYIAPER---FVDALTLDAESERRDGELTPAMDIFSLGcVIAELFTEG 213
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 281 ETPF------KGKSKKETFRNVLMKepefaGKPNDLTDLIRRLLVKDPNRRLGCH 329
Cdd:cd13980 214 RPLFdlsqllAYRKGEFSPEQVLEK-----IEDPNIRELILHMIQRDPSKRLSAE 263
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
119-180 1.98e-06

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: 49.19  E-value: 1.98e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 119 QNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKP 180
Cdd:cd07870  90 QHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIP 151
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
106-286 2.59e-06

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: 48.50  E-value: 2.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIA---YRDLKPENILIQQSghvtLTDFDLSRSLKKplr 182
Cdd:cd14145  86 FARGGPLNRVLSGKR---IPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEK----VENGDLSNKILK--- 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phfyqpdpelIIDRKKSRSFSRLISPTAeknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRGDGHD 262
Cdd:cd14145 156 ----------ITDFGLAREWHRTTKMSA----------------------------------AGTYAWMAPEVIRSSMFS 191
                       170       180
                ....*....|....*....|....
gi 15232374 263 FAVDWWALGVLTYEMMYGETPFKG 286
Cdd:cd14145 192 KGSDVWSYGVLLWELLTGEVPFRG 215
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
130-341 2.83e-06

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: 48.64  E-value: 2.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 130 RFYVAEIVCALEHLHTMGIAYRDLKPENILIQqsghvtltdfdlsrslkkplrphfYQPD--PELIIdrkksrsfSRLIS 207
Cdd:cd14018 141 RVMILQLLEGVDHLVRHGIAHRDLKSDNILLE------------------------LDFDgcPWLVI--------ADFGC 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 208 PTAEKNkTGLKktrsarvnpinrrkTSFSSGERSNSfvGTDEYVSPEVIRGDGHDFAV------DWWALGVLTYEMMYGE 281
Cdd:cd14018 189 CLADDS-IGLQ--------------LPFSSWYVDRG--GNACLMAPEVSTAVPGPGVVinyskaDAWAVGAIAYEIFGLS 251
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 282 TPFKGKSKKeTFRNVLMKEPEF----AGKPNDLTDLIRRLLVKDPNRRLGChRGAAEIKELAFF 341
Cdd:cd14018 252 NPFYGLGDT-MLESRSYQESQLpalpSAVPPDVRQVVKDLLQRDPNKRVSA-RVAANVLHLSLW 313
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
111-288 3.24e-06

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: 48.46  E-value: 3.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 111 DLNVLLHrqNDGV-FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplrpHFYQPD 189
Cdd:cd07866 100 DLSGLLE--NPSVkLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLAR--------PYDGPP 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 190 PeliidrkksrsfsrlisptaeKNKTGlkktrsarvNPINRRKTSfssgersnSFVGTDEYVSPEVIRGD-GHDFAVDWW 268
Cdd:cd07866 170 P---------------------NPKGG---------GGGGTRKYT--------NLVVTRWYRPPELLLGErRYTTAVDIW 211
                       170       180
                ....*....|....*....|
gi 15232374 269 ALGVLTYEMMYGETPFKGKS 288
Cdd:cd07866 212 GIGCVFAEMFTRRPILQGKS 231
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
111-198 4.52e-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: 47.99  E-value: 4.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 111 DLNVLLHRqNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLRP------- 183
Cdd:cd07843  91 DLKSLMET-MKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGSPLKPytqlvvt 169
                        90
                ....*....|....*
gi 15232374 184 HFYQPdPELIIDRKK 198
Cdd:cd07843 170 LWYRA-PELLLGAKE 183
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
21-319 5.34e-06

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: 47.70  E-value: 5.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  21 IKALKILGKGATGTVFLAH---DVvstssssspfAVKL--VPKSSASSLRRARWEIEVLRRlsvdSNQNPFLprLLASFE 95
Cdd:cd14150   2 VSMLKRIGTGSFGTVFRGKwhgDV----------AVKIlkVTEPTPEQLQAFKNEMQVLRK----TRHVNIL--LFMGFM 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLHrQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd14150  66 TRPNFAIITQWCEGSSLYRHLH-VTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAT 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SlkkplrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrKTSFSSGERSNSFVGTDEYVSPEV 255
Cdd:cd14150 145 V-------------------------------------------------------KTRWSGSQQVEQPSGSILWMAPEV 169
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 256 IR---GDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETF-----RNVLmkEPEFAGKPNDLTDLIRRLLV 319
Cdd:cd14150 170 IRmqdTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIifmvgRGYL--SPDLSKLSSNCPKAMKRLLI 239
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
22-296 5.85e-06

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 47.72  E-value: 5.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFL-----AHDVVstssssspfAVKLVpKSSASSLRRARWEIEVLRRLSVDSNQNPFLPRLLASFES 96
Cdd:cd14229   3 EVLDFLGRGTFGQVVKcwkrgTNEIV---------AVKIL-KNHPSYARQGQIEVGILARLSNENADEFNFVRAYECFQH 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  97 PEYFAWAVPYCSGGDLNVLlhRQNDgvFSS---SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILiqqsghvtltdfdl 173
Cdd:cd14229  73 RNHTCLVFEMLEQNLYDFL--KQNK--FSPlplKVIRPILQQVATALKKLKSLGLIHADLKPENIM-------------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 srsLKKPLRphfyQPdpeliidrkksrsfsrlisptaeknktglkktrsARVNPINRRKTSFSSGERSNSFVGTDEYVSP 253
Cdd:cd14229 135 ---LVDPVR----QP----------------------------------YRVKVIDFGSASHVSKTVCSTYLQSRYYRAP 173
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15232374 254 EVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNV 296
Cdd:cd14229 174 EIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYI 216
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
121-182 6.95e-06

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: 47.41  E-value: 6.95e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 121 DGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLR 182
Cdd:cd07861  95 GKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVR 156
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
27-322 7.19e-06

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 47.60  E-value: 7.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSsssPFAVKLVpKSSASSLRRARWEIEVLRRLS-VDSNQNPFLPRLLASFESPEYFAwAVP 105
Cdd:cd14135   8 LGKGVFSNVVRARDLARGNQ---EVAIKII-RNNELMHKAGLKELEILKKLNdADPDDKKHCIRLLRHFEHKNHLC-LVF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLHRQNDGV-FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT-LTDFDlsrslkkplrp 183
Cdd:cd14135  83 ESLSMNLREVLKKYGKNVgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTLkLCDFG----------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 184 hfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgerSNSFVGTDE---------YVSPE 254
Cdd:cd14135 152 ---------------------------------------------------------SASDIGENEitpylvsrfYRAPE 174
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 255 VIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRnvLMKepEFAGKPNdlTDLIRRLLVKDP 322
Cdd:cd14135 175 IILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLK--LMM--DLKGKFP--KKMLRKGQFKDQ 236
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
26-284 7.62e-06

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: 47.22  E-value: 7.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAHDvvstSSSSSPFA---VKLVpKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESP--EYF 100
Cdd:cd13983   8 VLGRGSFKTVYRAFD----TEEGIEVAwneIKLR-KLPKAERQRFKQEIEILKSL-----KHPNIIKFYDSWESKskKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGGDLNVllHRQNDGVFSSSVIRFYVAEIVCALEHLHTMG--IAYRDLKPENILIQ-QSGHVTLTDFDLSRSL 177
Cdd:cd13983  78 IFITELMTSGTLKQ--YLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 KKplrphfyqpdpeliidrkksrSFSRlisptaeknktglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIr 257
Cdd:cd13983 156 RQ---------------------SFAK--------------------------------------SVIGTPEFMAPEMY- 175
                       250       260
                ....*....|....*....|....*..
gi 15232374 258 GDGHDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd13983 176 EEHYDEKVDIYAFGMCLLEMATGEYPY 202
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
29-326 7.64e-06

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: 46.93  E-value: 7.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  29 KGATGTVFLAHDVvstsSSSSPFAVKLVPkssASSLRRARWEIEVLRRlsvdsNQNpfLPRLLASFESPEYFAWAVPYCS 108
Cdd:cd13995  14 RGAFGKVYLAQDT----KTKKRMACKLIP---VEQFKPSDVEIQACFR-----HEN--IAELYGALLWEETVHLFMEAGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 109 GGdlNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQqSGHVTLTDFDLSRSLKKPLrphfYQP 188
Cdd:cd13995  80 GG--SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFM-STKAVLVDFGLSVQMTEDV----YVP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 189 dpeliidrkksrsfsrlisptaeknktglKKTRsarvnpinrrktsfssgersnsfvGTDEYVSPEVIRGDGHDFAVDWW 268
Cdd:cd13995 153 -----------------------------KDLR------------------------GTEIYMSPEVILCRGHNTKADIY 179
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 269 ALGVLTYEMMYGETPFKGKSKKETFRNVLM----KEPEFAGKPNDLTDLIRRL----LVKDPNRRL 326
Cdd:cd13995 180 SLGATIIHMQTGSPPWVRRYPRSAYPSYLYiihkQAPPLEDIAQDCSPAMRELleaaLERNPNHRS 245
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
21-177 8.81e-06

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: 46.93  E-value: 8.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  21 IKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLSVDSnqnpflprlLASFESPEYF 100
Cdd:cd14205   6 LKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDN---------IVKYKGVCYS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 A------WAVPYCSGGDLNVLLHRQNDGVFSSSVIRfYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd14205  77 AgrrnlrLIMEYLPYGSLRDYLQKHKERIDHIKLLQ-YTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLT 155

                ...
gi 15232374 175 RSL 177
Cdd:cd14205 156 KVL 158
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
20-180 8.82e-06

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


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 46.55  E-value: 8.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  20 SIKALKILGKGATGTVFLAHDvvstssSSSPFAVKLV-PKSSASSLRRarwEIEVLRRLsvdsNQNPFLPRLLASfeSPE 98
Cdd:COG2112  41 LIGGLRLLGKGYRGVVFLGKL------GGKKVALKIRrTDSPRPSLKK---EAEILKKA----NGAGVGPKLYDY--GRD 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAvpYCSGGDLnvllhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDL-KPENILIQQSGHVTLTDFDLSRSL 177
Cdd:COG2112 106 FLVME--YIEGEPL-----KDWLENLDKEELRKVIRELLEAAYLLDRIGIDHGELsRPGKHVIVDKGRPYIIDFESASIS 178

                ...
gi 15232374 178 KKP 180
Cdd:COG2112 179 RKP 181
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
111-196 8.94e-06

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: 47.36  E-value: 8.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 111 DLNVLLhrQNDGV-FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR--SLKKPLRPH--- 184
Cdd:cd07865 104 DLAGLL--SNKNVkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARafSLAKNSQPNryt 181
                        90
                ....*....|....*....
gi 15232374 185 ------FYQPdPELII-DR 196
Cdd:cd07865 182 nrvvtlWYRP-PELLLgER 199
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
19-325 1.02e-05

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: 46.96  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHdvvstSSSSSPFAVKLVpKSSASSLRRARWEIEVLRRLSVDSnqnpfLPRLLASFESPE 98
Cdd:cd05072   7 ESIKLVKKLGAGQFGEVWMGY-----YNNSTKVAVKTL-KPGTMSVQAFLEEANLMKTLQHDK-----LVRLYAVVTKEE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGGDLNVLLHRQNDG-VFSSSVIRFyVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd05072  76 PIYIITEYMAKGSLLDFLKSDEGGkVLLPKLIDF-SAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 178 KKplrphfyqpdpeliiDRKKSRSFSRLisptaeknktglkktrsarvnPInrrktsfssgersnsfvgtdEYVSPEVIR 257
Cdd:cd05072 155 ED---------------NEYTAREGAKF---------------------PI--------------------KWTAPEAIN 178
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 258 GDGHDFAVDWWALGVLTYEMM-YGETPFKGKSKKETF----RNVLMKEPEFAgkPNDLTDLIRRLLVKDPNRR 325
Cdd:cd05072 179 FGSFTIKSDVWSFGILLYEIVtYGKIPYPGMSNSDVMsalqRGYRMPRMENC--PDELYDIMKTCWKEKAEER 249
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
148-291 1.02e-05

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 47.05  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 148 IAYRDLKPENILIQQSGHVTLTDFDLSrslkkplrphfyqpdpeliidrkksrsfSRLISPTAeknktglkktrsarvnp 227
Cdd:cd06615 121 IMHRDVKPSNILVNSRGEIKLCDFGVS----------------------------GQLIDSMA----------------- 155
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 228 inrrktsfssgersNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKE 291
Cdd:cd06615 156 --------------NSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKE 205
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
129-194 1.09e-05

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: 46.92  E-value: 1.09e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLRPH-------FYQPdPELII 194
Cdd:cd07873 102 VKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYsnevvtlWYRP-PDILL 173
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
105-191 1.47e-05

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: 46.52  E-value: 1.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLNVLLHRQ-NDGvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL----KK 179
Cdd:cd08216  79 PLMAYGSCRDLLKTHfPEG-LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMvkhgKR 157
                        90
                ....*....|..
gi 15232374 180 PLRPHFYQPDPE 191
Cdd:cd08216 158 QRVVHDFPKSSE 169
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
124-194 1.72e-05

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: 46.33  E-value: 1.72e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 124 FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL-KKPLRPH-------FYQPdPELII 194
Cdd:cd07864 113 FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLYnSEESRPYtnkvitlWYRP-PELLL 190
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
52-177 1.72e-05

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: 46.12  E-value: 1.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLVpKSSASSLRRARW--EIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLL----------HRQ 119
Cdd:cd05097  48 AVKML-RADVTKTARNDFlkEIKIMSRL-----KNPNIIRLLGVCVSDDPLCMITEYMENGDLNQFLsqreiestftHAN 121
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 120 NDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd05097 122 NIPSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKIADFGMSRNL 179
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
51-187 2.19e-05

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 45.65  E-value: 2.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  51 FAVKLVPKSSASSLRrARW-----EIEVLRRlsvdsNQNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFS 125
Cdd:cd14160  19 YAVKLFKQEKKMQWK-KHWkrflsELEVLLL-----FQHPNILELAAYFTETEKFCLVYPYMQNGTLFDRLQCHGVTKPL 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 126 SSVIRFYVAE-IVCALEHLHTM---GIAYRDLKPENILIQQSGHVTLTDFDLSRslkkpLRPHFYQ 187
Cdd:cd14160  93 SWHERINILIgIAKAIHYLHNSqpcTVICGNISSANILLDDQMQPKLTDFALAH-----FRPHLED 153
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
127-210 2.27e-05

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 46.60  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  127 SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLS---------RSLKKPLRPHfYQPDPELIIDRK 197
Cdd:PLN03224 309 NVIKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDFGAAvdmctginfNPLYGMLDPR-YSPPEELVMPQS 387
                         90
                 ....*....|....*..
gi 15232374  198 KSRS----FSRLISPTA 210
Cdd:PLN03224 388 CPRApapaMAALLSPFA 404
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
118-181 2.30e-05

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: 45.93  E-value: 2.30e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 118 RQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPL 181
Cdd:cd07836  91 HGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPV 154
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
67-291 2.41e-05

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 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: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 45.77  E-value: 2.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  67 ARWEIEVLRRLSVDSNQNPFLPRLLAsfespEYFAWAVPYCS-----GGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALE 141
Cdd:cd14214  57 ARLEINVLKKIKEKDKENKFLCVLMS-----DWFNFHGHMCIafellGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALK 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 142 HLHTMGIAYRDLKPENILIQQSGHVTLTDfdlsrslkkplrphfyqpdpeliidrkksrsfsrlisptaEKNKTGLKKTR 221
Cdd:cd14214 132 FLHENQLTHTDLKPENILFVNSEFDTLYN----------------------------------------ESKSCEEKSVK 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 222 SARVNPINRRKTSFSSgERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKE 291
Cdd:cd14214 172 NTSIRVADFGSATFDH-EHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENRE 240
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
16-325 2.50e-05

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: 45.44  E-value: 2.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVFLAHdVVSTSSSSSPFAVKLVpKSSASSLRRarweIEVLRRLSVDSN-QNPFLPRLLASF 94
Cdd:cd05033   1 IDASYVTIEKVIGGGEFGEVCSGS-LKLPGKKEIDVAIKTL-KSGYSDKQR----LDFLTEASIMGQfDHPNVIRLEGVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEYFAWAVPYCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd05033  75 TKSRPVMIVTEYMENGSLDKFL-RENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RSLKkplrphfyqpDPELIIDRKKSRSFSRLISPTAeknktglkktrsarvnpINRRKtsFSSgersnsfvgtdeyvspe 254
Cdd:cd05033 154 RRLE----------DSEATYTTKGGKIPIRWTAPEA-----------------IAYRK--FTS----------------- 187
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 255 virgdghdfAVDWWALGVLTYEMM-YGETPFKGKSKKEtfrnvLMKEPEFA---GKPNDLTDLIRRLLV----KDPNRR 325
Cdd:cd05033 188 ---------ASDVWSFGIVMWEVMsYGERPYWDMSNQD-----VIKAVEDGyrlPPPMDCPSALYQLMLdcwqKDRNER 252
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
24-291 2.54e-05

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; 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. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. 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. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 45.85  E-value: 2.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVpKSSASSLRRARWEIEVL---RRLSVDSNQNpflprllaSFESPEYF 100
Cdd:cd14225  48 LEVIGKGSFGQVVKALD----HKTNEHVAIKII-RNKKRFHHQALVEVKILdalRRKDRDNSHN--------VIHMKEYF 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYC-----SGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd14225 115 YFRNHLCitfelLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSIKVIDFGS 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 176 SLKKPLRPHFYqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpINRRktsFssgersnsfvgtdeYVSPEV 255
Cdd:cd14225 195 SCYEHQRVYTY-----------------------------------------IQSR---F--------------YRSPEV 216
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15232374 256 IRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKE 291
Cdd:cd14225 217 ILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVE 252
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
123-194 2.76e-05

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 45.75  E-value: 2.76e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 123 VFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLRPH-------FYQPdPELII 194
Cdd:cd07872 100 IMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYsnevvtlWYRP-PDVLL 177
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
60-193 2.84e-05

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: 45.46  E-value: 2.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  60 SASSLRRARWEIEVLRRLSVDsNQNPFLPrllASFESPEYFA-WAvpYCSGGDLNVLLHRQN---DGVFSSSVIRfyvaE 135
Cdd:cd13992  36 SRTEKRTILQELNQLKELVHD-NLNKFIG---ICINPPNIAVvTE--YCTRGSLQDVLLNREikmDWMFKSSFIK----D 105
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 136 IVCALEHLHTMGIAYR-DLKPENILIQQSGHVTLTDFDLSRSLKK---------PLRPHFYQPDPELI 193
Cdd:cd13992 106 IVKGMNYLHSSSIGYHgRLKSSNCLVDSRWVVKLTDFGLRNLLEEqtnhqldedAQHKKLLWTAPELL 173
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
24-194 3.11e-05

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; 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 DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 45.89  E-value: 3.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDvvstSSSSSPFAVKLVpKSSASSLRRARWEI---EVLRRLSVDSNQNpfLPRLLASFESPEYF 100
Cdd:cd14224  70 LKVIGKGSFGQVVKAYD----HKTHQHVALKMV-RNEKRFHRQAAEEIrilEHLKKQDKDNTMN--VIHMLESFTFRNHI 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAVPYCSGgDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH--VTLTDFDLS---- 174
Cdd:cd14224 143 CMTFELLSM-NLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSScyeh 221
                       170       180
                ....*....|....*....|
gi 15232374 175 RSLKKPLRPHFYQPdPELII 194
Cdd:cd14224 222 QRIYTYIQSRFYRA-PEVIL 240
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
139-277 3.14e-05

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: 45.13  E-value: 3.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 139 ALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDlSRSLKKPlrphfyqpdpeliidrkksrsfsrlisptaeknktglk 218
Cdd:cd06607 113 GLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG-SASLVCP-------------------------------------- 153
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 219 ktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVIRG--DGH-DFAVDWWALGVLTYEM 277
Cdd:cd06607 154 ----------------------ANSFVGTPYWMAPEVILAmdEGQyDGKVDVWSLGITCIEL 193
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
129-180 3.42e-05

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: 45.45  E-value: 3.42e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKP 180
Cdd:cd07869 105 VKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVP 156
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
27-296 3.60e-05

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: 45.12  E-value: 3.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAhdvvsTSSSSSPFAVKLVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd05148  14 LGSGYFGEVWEG-----LWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRL-----RHKHLISLFAVCSVGEPVYIITEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 CSGGDLNVLLhRQNDG--VFSSSVIRF--YVAEIVCALEHLHtmgIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPlr 182
Cdd:cd05148  84 MEKGSLLAFL-RSPEGqvLPVASLIDMacQVAEGMAYLEEQN---SIHRDLAARNILVGEDLVCKVADFGLARLIKED-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phFYQPDPELIIdrkksrsfSRLISPTAeknktglkktrsarvnpINRRKTSFSSgersnsfvgtdeyvspevirgdghd 262
Cdd:cd05148 158 --VYLSSDKKIP--------YKWTAPEA-----------------ASHGTFSTKS------------------------- 185
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15232374 263 favDWWALGVLTYEMM-YGETPFKGKSKKETFRNV 296
Cdd:cd05148 186 ---DVWSFGILLYEMFtYGQVPYPGMNNHEVYDQI 217
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
106-325 3.62e-05

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: 45.02  E-value: 3.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIA---YRDLKPENILIQQSG------HVTL--TDFDLS 174
Cdd:cd14147  83 YAAGGPLSRALAGRR---VPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLQPIenddmeHKTLkiTDFGLA 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 175 RslkkplrphfyqpdpeliidrkksrsfsrlisptaEKNKTglkktrsarvnpinrrkTSFSSGersnsfvGTDEYVSPE 254
Cdd:cd14147 160 R-----------------------------------EWHKT-----------------TQMSAA-------GTYAWMAPE 180
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 255 VIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE---PEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14147 181 VIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKltlPIPSTCPEPFAQLMADCWAQDPHRR 254
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
25-195 3.74e-05

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 45.06  E-value: 3.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSlrrarWEIEvlRRLSVDSN-QNPFLPRLLASFE---SPEYF 100
Cdd:cd14055   1 KLVGKGRFAEVWKAKLKQNASGQYETVAVKIFPYEEYAS-----WKNE--KDIFTDASlKHENILQFLTAEErgvGLDRQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AWAV-PYCSGGDLNVLLHRQndgVFSSSVIRFYVAEIVCALEHLHT---------MGIAYRDLKPENILIQQSGHVTLTD 170
Cdd:cd14055  74 YWLItAYHENGSLQDYLTRH---ILSWEDLCKMAGSLARGLAHLHSdrtpcgrpkIPIAHRDLKSSNILVKNDGTCVLAD 150
                       170       180
                ....*....|....*....|....*
gi 15232374 171 FDLSRSLkkplrphfyqpDPELIID 195
Cdd:cd14055 151 FGLALRL-----------DPSLSVD 164
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
130-314 4.07e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 45.45  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  130 RFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLRPHFYqpdpeliidrkksrsfsrlispt 209
Cdd:PHA03210 270 RAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAFDY----------------------- 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  210 aeknktglkktrsarvnpinrrktsfssgersnSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGE-TPFKGKS 288
Cdd:PHA03210 327 ---------------------------------GWVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLSHDfCPIGDGG 373
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15232374  289 KK------ETFRNVLMKEPEFAGKPNDLTDLI 314
Cdd:PHA03210 374 GKpgkqllKIIDSLSVCDEEFPDPPCKLFDYI 405
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
125-328 4.17e-05

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: 45.51  E-value: 4.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 125 SSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRslkkplrphFYQPDPELIIdrkksrsfsr 204
Cdd:cd07853 101 SSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLAR---------VEEPDESKHM---------- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 205 lispTAEknktglkktrsarvnpinrrktsfssgersnsfVGTDEYVSPEVIRGDGH-DFAVDWWALGVLTYEMMYGETP 283
Cdd:cd07853 162 ----TQE---------------------------------VVTQYYRAPEILMGSRHyTSAVDIWSVGCIFAELLGRRIL 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 284 FKG----------------------KSKKETFRNVLMKEPEfagKPNDLT--------------DLIRRLLVKDPNRRLG 327
Cdd:cd07853 205 FQAqspiqqldlitdllgtpsleamRSACEGARAHILRGPH---KPPSLPvlytlssqatheavHLLCRMLVFDPDKRIS 281

                .
gi 15232374 328 C 328
Cdd:cd07853 282 A 282
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
24-284 4.91e-05

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: 45.04  E-value: 4.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASSlrRARW-----EIEVLRRLsvdsnQNPFLPRLLASFESpE 98
Cdd:cd06635  30 LREIGHGSFGAVYFARDV----RTSEVVAIKKMSYSGKQS--NEKWqdiikEVKFLQRI-----KHPNSIEYKGCYLR-E 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAV-PYCSGGDLNVL-LHRQNDGVFSSSVIRFYVAEivcALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDlSRS 176
Cdd:cd06635  98 HTAWLVmEYCLGSASDLLeVHKKPLQEIEIAAITHGALQ---GLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-SAS 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LKKPlrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVI 256
Cdd:cd06635 174 IASP------------------------------------------------------------ANSFVGTPYWMAPEVI 193
                       250       260       270
                ....*....|....*....|....*....|.
gi 15232374 257 RG--DG-HDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd06635 194 LAmdEGqYDGKVDVWSLGITCIELAERKPPL 224
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
52-177 5.45e-05

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: 44.64  E-value: 5.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVK-LVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASFESPEYFAWAVPYCSGGDLN-VLLHRQNDGVFSS--- 126
Cdd:cd05051  50 AVKmLRPDASKNAREDFLKEVKIMSQL-----KDPNIVRLLGVCTRDEPLCMIVEYMENGDLNqFLQKHEAETQGASatn 124
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 127 ------SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd05051 125 sktlsyGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIKIADFGMSRNL 181
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
27-171 5.48e-05

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: 42.81  E-value: 5.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVVSTSSssspFAVKLVPKSSASSLRRARWEIEVLRRLSvdsNQNPFLPRLLASFESPEYFAWAVPY 106
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIG----VAVKIGDDVNNEEGEDLESEMDILRRLK---GLELNIPKVLVTEDVDGPNILLMEL 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 107 CSGGDLN-VLLHRQNDGVFSSSVIRFYVAeivcALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:cd13968  74 VKGGTLIaYTQEEELDEKDVESIMYQLAE----CMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDF 135
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
106-325 5.51e-05

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: 44.47  E-value: 5.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 106 YCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphf 185
Cdd:cd05066  86 YMENGSLDAFL-RKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVL-------- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 186 yQPDPEliidrkksrsfsrlisptaeknktGLKKTRSARVnPInrrktsfssgersnsfvgtdEYVSPEVIRGDGHDFAV 265
Cdd:cd05066 157 -EDDPE------------------------AAYTTRGGKI-PI--------------------RWTAPEAIAYRKFTSAS 190
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 266 DWWALGVLTYEMM-YGETPFKGKSKKETFRNVL--MKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd05066 191 DVWSYGIVMWEVMsYGERPYWEMSNQDVIKAIEegYRLPAPMDCPAALHQLMLDCWQKDRNER 253
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
246-326 5.67e-05

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 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: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 44.27  E-value: 5.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 246 GTDEYVSPEVIRGDG--HDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVlmKEPEFAgKPNDLTD----LIRRLLV 319
Cdd:cd14023 148 GCPAYVSPEILNTTGtySGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFC-IPDHVSPkarcLIRSLLR 224

                ....*..
gi 15232374 320 KDPNRRL 326
Cdd:cd14023 225 REPSERL 231
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
27-337 5.83e-05

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: 44.42  E-value: 5.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  27 LGKGATGTVFLAHDVvstsSSSSPFAVKLVPkssassLRRARWEiEVLRRLSVDSnqnpflPRLLASFESPEYFAWAVPY 106
Cdd:cd13991  14 IGRGSFGEVHRMEDK----QTGFQCAVKKVR------LEVFRAE-ELMACAGLTS------PRVVPLYGAVREGPWVNIF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 107 C---SGGDLNVLLHRQndGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSG-HVTLTDFDLSRSLkkplr 182
Cdd:cd13991  77 MdlkEGGSLGQLIKEQ--GCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECL----- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 183 phfyQPDpeliidrkksrsfsrlisptaeknktGLKKtrsarvnpinrrktsfsSGERSNSFVGTDEYVSPEVIRGDGHD 262
Cdd:cd13991 150 ----DPD--------------------------GLGK-----------------SLFTGDYIPGTETHMAPEVVLGKPCD 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 263 FAVDWWALGVLTYEMMYGETPFkgkskKETFRNVL----MKEP----EFAGKPNDLT-DLIRRLLVKDPNRRLgchrGAA 333
Cdd:cd13991 183 AKVDVWSSCCMMLHMLNGCHPW-----TQYYSGPLclkiANEPpplrEIPPSCAPLTaQAIQAGLRKEPVHRA----SAA 253

                ....
gi 15232374 334 EIKE 337
Cdd:cd13991 254 ELRR 257
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
52-177 6.84e-05

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: 44.54  E-value: 6.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLV-PKSSASSLRRARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLL--HRQNDG------ 122
Cdd:cd05096  50 AVKILrPDANKNARNDFLKEVKILSRLK-----DPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLssHHLDDKeengnd 124
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 123 ---------VFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd05096 125 avppahclpAISYSSLLHVALQIASGMKYLSSLNFVHRDLATRNCLVGENLTIKIADFGMSRNL 188
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
50-177 7.87e-05

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: 43.98  E-value: 7.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  50 PFAVKLVpKSSASSLRRARWEIEVLRRLSVdSNQNpFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHR------QNDGV 123
Cdd:cd05043  36 EVLVKTV-KDHASEIQVTMLLQESSLLYGL-SHQN-LLPILHVCIEDGEKPMVLYPYMNWGNLKLFLQQcrlseaNNPQA 112
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15232374 124 FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd05043 113 LSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDL 166
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
19-182 9.93e-05

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 44.06  E-value: 9.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAHDVVSTssssspfavKLVpkssasSLRRARWEIE-------VLRRLSVDS--NQNPFLPR 89
Cdd:cd07837   1 DAYEKLEKIGEGTYGKVYKARDKNTG---------KLV------ALKKTRLEMEeegvpstALREVSLLQmlSQSIYIVR 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  90 LLA---SFESPEYFAWAVPYCSGGDLNVLLHRQNDGV---FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI-QQ 162
Cdd:cd07837  66 LLDvehVEENGKPLLYLVFEYLDTDLKKFIDSYGRGPhnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVdKQ 145
                       170       180
                ....*....|....*....|
gi 15232374 163 SGHVTLTDFDLSRSLKKPLR 182
Cdd:cd07837 146 KGLLKIADLGLGRAFTIPIK 165
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
250-326 1.10e-04

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB 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: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 43.57  E-value: 1.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 250 YVSPEVIRGDGH--DFAVDWWALGVLTYEMMYGETPFKGKSKKETF---RNVLMKEPEFAGKPNDLtdLIRRLLVKDPNR 324
Cdd:cd13976 152 YVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFakiRRGQFAIPETLSPRARC--LIRSLLRREPSE 229

                ..
gi 15232374 325 RL 326
Cdd:cd13976 230 RL 231
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
66-173 1.43e-04

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: 43.42  E-value: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  66 RARWEIEV-LRRLSVDSNQNPFLPRL------------------LASFESPEYFAWAVPYCSGGDLNVLLhRQNDGVFSS 126
Cdd:cd14152  18 RGRWHGEVaIRLLEIDGNNQDHLKLFkkevmnyrqtrhenvvlfMGACMHPPHLAIITSFCKGRTLYSFV-RDPKTSLDI 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15232374 127 SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIqQSGHVTLTDFDL 173
Cdd:cd14152  97 NKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGL 142
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
111-176 1.63e-04

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 43.45  E-value: 1.63e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232374 111 DLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd07849  93 DLYKLIKTQH---LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARI 155
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
19-296 1.99e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 43.15  E-value: 1.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFL-----AHDVVstssssspfAVKLVpKSSASSLRRARWEIEVLRRLSVDSNQNPFLPRLLAS 93
Cdd:cd14227  15 NTYEVLEFLGRGTFGQVVKcwkrgTNEIV---------AIKIL-KNHPSYARQGQIEVSILARLSTESADDYNFVRAYEC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 FESPEYFAWAVPYCSGgDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIqqsghvtltdFDL 173
Cdd:cd14227  85 FQHKNHTCLVFEMLEQ-NLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIML----------VDP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 174 SRslkkplrphfyQPDPELIIDRKKSRSFSRLISPTaeknktglkktrsarvnpinrrktsfssgersnsFVGTDEYVSP 253
Cdd:cd14227 154 SR-----------QPYRVKVIDFGSASHVSKAVCST----------------------------------YLQSRYYRAP 188
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15232374 254 EVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNV 296
Cdd:cd14227 189 EIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYI 231
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
243-286 2.06e-04

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: 42.72  E-value: 2.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15232374 243 SFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKG 286
Cdd:cd14146 170 SAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRG 213
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
136-203 2.32e-04

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: 42.64  E-value: 2.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 136 IVCALEHLHT--MG------IAYRDLKPENILIQQSGHVTLTDFDLS---RSLKKPLRPHF--------YQPdPELIIDR 196
Cdd:cd14056 101 AASGLAHLHTeiVGtqgkpaIAHRDLKSKNILVKRDGTCCIADLGLAvryDSDTNTIDIPPnprvgtkrYMA-PEVLDDS 179

                ....*..
gi 15232374 197 KKSRSFS 203
Cdd:cd14056 180 INPKSFE 186
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
100-286 2.56e-04

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 42.55  E-value: 2.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 100 FAWAV-PYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLK 178
Cdd:cd08226  73 WLWVIsPFMAYGSARGLLKTYFPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMV 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 KPLRPHFYQPD-PEliidrkksrsFSRLISPtaeknktglkktrsarvnpinrrktsfssgersnsfvgtdeYVSPEVIR 257
Cdd:cd08226 153 TNGQRSKVVYDfPQ----------FSTSVLP-----------------------------------------WLSPELLR 181
                       170       180       190
                ....*....|....*....|....*....|.
gi 15232374 258 GD--GHDFAVDWWALGVLTYEMMYGETPFKG 286
Cdd:cd08226 182 QDlhGYNVKSDIYSVGITACELARGQVPFQD 212
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
104-325 2.89e-04

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: 42.21  E-value: 2.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 104 VPYCSGGDLN--VLLHRQNDGVFSSSV---IRFYVaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLK 178
Cdd:cd05074  96 LPFMKHGDLHtfLLMSRIGEEPFTLPLqtlVRFMI-DIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKIY 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 KPlrphfyqpdpeliiDRKKSRSFSRLisptaeknktglkktrsarvnPInrrktsfssgersnsfvgtdEYVSPEVIRG 258
Cdd:cd05074 175 SG--------------DYYRQGCASKL---------------------PV--------------------KWLALESLAD 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 259 DGHDFAVDWWALGVLTYEMM-YGETPFKGKSKKETFR-----NVLMKEPEFagkPNDLTDLIRRLLVKDPNRR 325
Cdd:cd05074 200 NVYTTHSDVWAFGVTMWEIMtRGQTPYAGVENSEIYNylikgNRLKQPPDC---LEDVYELMCQCWSPEPKCR 269
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
25-325 3.01e-04

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: 42.47  E-value: 3.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAHDV-VSTSSSSSPFAVKLVPKSSASSLRRARW-EIEVLRRLSVDSNqnpfLPRLLA--SFESPEYF 100
Cdd:cd05055  41 KTLGAGAFGKVVEATAYgLSKSDAVMKVAVKMLKPTAHSSEREALMsELKIMSHLGNHEN----IVNLLGacTIGGPILV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 101 AwaVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKp 180
Cdd:cd05055 117 I--TEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMN- 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 181 lrphfyqpDPELIidrkkSRSFSRLisptaeknktglkktrsarvnPInrrktsfssgersnsfvgtdEYVSPEVIRGDG 260
Cdd:cd05055 194 --------DSNYV-----VKGNARL---------------------PV--------------------KWMAPESIFNCV 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374 261 HDFAVDWWALGVLTYEMM-YGETPFKGKSKKETFRNVL-----MKEPEFAgkPNDLTDLIRRLLVKDPNRR 325
Cdd:cd05055 220 YTFESDVWSYGILLWEIFsLGSNPYPGMPVDSKFYKLIkegyrMAQPEHA--PAEIYDIMKTCWDADPLKR 288
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
52-201 3.02e-04

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: 42.24  E-value: 3.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLVPKSSASSLRRARW-EIEVLRRLSvdsnqNPFLPRLLASFESpEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIR 130
Cdd:cd05115  35 AIKVLKQGNEKAVRDEMMrEAQIMHQLD-----NPYIVRMIGVCEA-EALMLVMEMASGGPLNKFLSGKKDEITVSNVVE 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 131 FyVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL-------------KKPLRphFYQpdPELIIDRK 197
Cdd:cd05115 109 L-MHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALgaddsyykarsagKWPLK--WYA--PECINFRK 183

                ....*
gi 15232374 198 -KSRS 201
Cdd:cd05115 184 fSSRS 188
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
111-182 3.15e-04

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 42.50  E-value: 3.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374  111 DLNVLLHRQNDGVFSSS--VIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGH-VTLTDFDLSRSLKKPLR 182
Cdd:PLN00009  84 DLDLKKHMDSSPDFAKNprLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLARAFGIPVR 158
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
70-278 3.17e-04

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: 42.09  E-value: 3.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVfsSSVIRFYVA-EIVCALEHLHTMGI 148
Cdd:cd14065  38 EVKLMRRLS-----HPNILRFIGVCVKDNKLNFITEYVNGGTLEELLKSMDEQL--PWSQRVSLAkDIASGMAYLHSKNI 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 149 AYRDLKPENILIQQSG---HVTLTDFDLSRSLkkplrPHFYQPDPeliiDRKKsrsfsrlisptaeknktglkktrsarv 225
Cdd:cd14065 111 IHRDLNSKNCLVREANrgrNAVVADFGLAREM-----PDEKTKKP----DRKK--------------------------- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232374 226 nPINrrktsfssgersnsFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMM 278
Cdd:cd14065 155 -RLT--------------VVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII 192
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
129-182 3.26e-04

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 42.37  E-value: 3.26e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15232374 129 IRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKPLR 182
Cdd:cd07844 100 VRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSK 153
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
70-278 3.67e-04

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: 41.74  E-value: 3.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  70 EIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRFyVAEIVCALEHLHTMGIA 149
Cdd:cd14156  38 EISLLQKLS-----HPNIVRYLGICVKDEKLHPILEYVSGGCLEELLAREELPLSWREKVEL-ACDISRGMVYLHSKNIY 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 150 YRDLKPENILIQQSGHV---TLTDFDLSRSLKkplrphfyqpdpELiidrkksrsfsrlisptaeknktglkktrsarvn 226
Cdd:cd14156 112 HRDLNSKNCLIRVTPRGreaVVTDFGLAREVG------------EM---------------------------------- 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15232374 227 PINrrktsfsSGERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMM 278
Cdd:cd14156 146 PAN-------DPERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
72-291 3.90e-04

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 42.34  E-value: 3.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  72 EVLRRLSVDSNQN-PFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQND------GVFSSSVIRFyvaeiVCALEHLH 144
Cdd:cd06649  49 QIIRELQVLHECNsPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRipeeilGKVSIAVLRG-----LAYLREKH 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 145 TmgIAYRDLKPENILIQQSGHVTLTDFDLSRSLkkplrphfyqpdpeliIDrkksrsfsrlisptaeknktglkktrsar 224
Cdd:cd06649 124 Q--IMHRDVKPSNILVNSRGEIKLCDFGVSGQL----------------ID----------------------------- 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232374 225 vnpinrrktsfssgERSNSFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKE 291
Cdd:cd06649 157 --------------SMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKE 209
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
83-285 4.63e-04

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: 41.51  E-value: 4.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  83 QNPFLPRLLASFESPEYFAWAVPYCSGGDLNVLLHRQNdgvFSSSVIRFYVAEIVCALEHLHT---MGIAYRDLKPENIL 159
Cdd:cd14148  51 QHPNIIALRGVCLNPPHLCLVMEYARGGALNRALAGKK---VPPHVLVNWAVQIARGMNYLHNeaiVPIIHRDLKSSNIL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 160 IQQ--------SGHVTLTDFDLSRslkkplrphfyqpdpeliidrkksrsfsrlisptaEKNKTglkktrsarvnpinrr 231
Cdd:cd14148 128 ILEpienddlsGKTLKITDFGLAR-----------------------------------EWHKT---------------- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15232374 232 kTSFSSGersnsfvGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFK 285
Cdd:cd14148 157 -TKMSAA-------GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYR 202
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
19-296 4.65e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 42.00  E-value: 4.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVflahDVVSTSSSSSPFAVKLVpKSSASSLRRARWEIEVLRRLSVDSNQNPFLPRLLASFESPE 98
Cdd:cd14228  15 NSYEVLEFLGRGTFGQV----AKCWKRSTKEIVAIKIL-KNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAVPYCSGgDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILiqqsghvtltdfdlsrsLK 178
Cdd:cd14228  90 HTCLVFEMLEQ-NLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIM-----------------LV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 179 KPLRphfyQPDPELIIDRKKSRSFSRLISPTaeknktglkktrsarvnpinrrktsfssgersnsFVGTDEYVSPEVIRG 258
Cdd:cd14228 152 DPVR----QPYRVKVIDFGSASHVSKAVCST----------------------------------YLQSRYYRAPEIILG 193
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15232374 259 DGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNV 296
Cdd:cd14228 194 LPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYI 231
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
243-325 7.48e-04

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: 40.71  E-value: 7.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 243 SFVGTDEYVSPEVIRGDGHDFAVDWWALGVLTYEMMYGETPFKGKSKKETFRNVLMKE-----PEFAgkPNDLTDLIRRL 317
Cdd:cd14060 144 SLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNerptiPSSC--PRSFAELMRRC 221

                ....*...
gi 15232374 318 LVKDPNRR 325
Cdd:cd14060 222 WEADVKER 229
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
128-171 7.67e-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: 41.27  E-value: 7.67e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15232374 128 VIRFYVAEIVCALEHLHTMGIAYRDLKPENILI-QQSGHVTLTDF 171
Cdd:cd14013 121 IIKSIMRQILVALRKLHSTGIVHRDVKPQNIIVsEGDGQFKIIDL 165
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
139-325 7.85e-04

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: 40.75  E-value: 7.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 139 ALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDlsrslkkplrphfyqpdpeLIIDRKKSrsfsrlisptaeknktglk 218
Cdd:cd14050 112 GLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFG-------------------LVVELDKE------------------- 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 219 ktrsarvnpinrrktsfssgERSNSFVGTDEYVSPEVIRGDGHDFAvDWWALGVLTYEMM-YGETPFKGKSKKEtFRNVL 297
Cdd:cd14050 154 --------------------DIHDAQEGDPRYMAPELLQGSFTKAA-DIFSLGITILELAcNLELPSGGDGWHQ-LRQGY 211
                       170       180
                ....*....|....*....|....*...
gi 15232374 298 MKEPEFAGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd14050 212 LPEEFTAGLSPELRSIIKLMMDPDPERR 239
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
22-175 8.92e-04

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; 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. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 40.78  E-value: 8.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSssspfaVKLVPKSSASSLRRARWEIEVLRRLSVDSNQNPFLprllaSFESPEYFA 101
Cdd:cd14130   3 KVLKKIGGGGFGEIYEAMDLLTREN------VALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFI-----GCGRNEKFN 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374 102 WAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENI----LIQQSGHVTLTDFDLSR 175
Cdd:cd14130  72 YVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR 149
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
127-176 1.04e-03

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: 40.56  E-value: 1.04e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15232374 127 SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRS 176
Cdd:cd14027  90 SVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASF 139
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
96-173 1.08e-03

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: 40.38  E-value: 1.08e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232374  96 SPEYFAWAVPYCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIqQSGHVTLTDFDL 173
Cdd:cd14153  67 SPPHLAIITSLCKGRTLYSVV-RDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGL 142
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
25-175 1.09e-03

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: 40.37  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  25 KILGKGATGTVFLAhdvvsTSSSSSPFAVKLVPKSSASSLR-RARWEIEVLRRLSvdsnqNPFLPRLLASFESPEYFAWA 103
Cdd:cd05085   2 ELLGKGNFGEVYKG-----TLKDKTPVAVKTCKEDLPQELKiKFLSEARILKQYD-----HPNIVKLIGVCTQRQPIYIV 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374 104 VPYCSGGDLNVLLHRQNDGVFSSSVIRFYVaEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd05085  72 MELVPGGDFLSFLRKKKDELKTKQLVKFSL-DAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSR 142
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
52-325 1.22e-03

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: 40.21  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  52 AVKLVPKSSASSlrRARWEIEVLRRLsvdsnQNPFLPRLLASFEsPEYFAWAVPYCSGGDlnVLLHRQNDGVFSSSVIRF 131
Cdd:cd14112  34 AVKIFEVSDEAS--EAVREFESLRTL-----QHENVQRLIAAFK-PSNFAYLVMEKLQED--VFTRFSSNDYYSEEQVAT 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 132 YVAEIVCALEHLHTMGIAYRDLKPENILIQ--QSGHVTLTDFDlsrslkkplrphfyqpdpeliidrkksrsfsrlispt 209
Cdd:cd14112 104 TVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFG------------------------------------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 210 aeknktglkktRSARVNPINRRKTSFSSgersnsfvgtdEYVSPEVIRGDGHDFA-VDWWALGVLTYEMMYGETPFKG-- 286
Cdd:cd14112 147 -----------RAQKVSKLGKVPVDGDT-----------DWASPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFTSey 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15232374 287 KSKKETFRNVLMKEPEFAGKPNDLTD----LIRRLLVKDPNRR 325
Cdd:cd14112 205 DDEEETKENVIFVKCRPNLIFVEATQealrFATWALKKSPTRR 247
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
127-194 1.29e-03

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 40.44  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 127 SVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ----QSGHVTLTDFDLSRSLKKPLRP---------HFYQPDPELI 193
Cdd:cd07867 109 SMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPladldpvvvTFWYRAPELL 188

                .
gi 15232374 194 I 194
Cdd:cd07867 189 L 189
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
130-175 1.43e-03

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: 40.53  E-value: 1.43e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15232374 130 RFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd07859 106 QFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLAR 151
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
15-186 1.70e-03

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: 39.94  E-value: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  15 ILDLDSIKALKILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSAsslrRARWEIEVLRRLSVDSNQNPFLPRLLASF 94
Cdd:cd05111   3 IFKETELRKLKVLGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQDRSG----RQSFQAVTDHMLAIGSLDHAYIVRLLGIC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEyFAWAVPYCSGGDLnvLLH-RQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDL 173
Cdd:cd05111  79 PGAS-LQLVTQLLPLGSL--LDHvRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGV 155
                       170
                ....*....|...
gi 15232374 174 SRSLKKPLRPHFY 186
Cdd:cd05111 156 ADLLYPDDKKYFY 168
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
21-178 1.89e-03

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: 39.91  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  21 IKALKILGKGATGTVFLAHDVVSTSSSSSPFAVK-LVPKSSASSLRRARWEIEVLRRLSvdsNQNPFLPRLLASFESPEY 99
Cdd:cd05079   6 LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKsLKPESGGNHIADLKKEIEILRNLY---HENIVKYKGICTEDGGNG 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232374 100 FAWAVPYCSGGDLNVLLHRQNDGVFSSSVIRfYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLK 178
Cdd:cd05079  83 IKLIMEFLPSGSLKEYLPRNKNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 160
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
130-175 1.96e-03

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: 40.05  E-value: 1.96e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15232374 130 RFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd07858 111 QYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLAR 156
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
16-325 2.31e-03

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: 39.71  E-value: 2.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVFLAH--DVVSTSSSSSPFAVKLVpKSSASS--LRRARWEIEVLRRLSvdsnQNPFLPRLL 91
Cdd:cd05053   9 LPRDRLTLGKPLGEGAFGQVVKAEavGLDNKPNEVVTVAVKML-KDDATEkdLSDLVSEMEMMKMIG----KHKNIINLL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  92 A--SFESPEYFAwaVPYCSGGDLNVLL--HRQNDGVFSSSVIR---------------FYVAEivcALEHLHTMGIAYRD 152
Cdd:cd05053  84 GacTQDGPLYVV--VEYASKGNLREFLraRRPPGEEASPDDPRvpeeqltqkdlvsfaYQVAR---GMEYLASKKCIHRD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 153 LKPENILIQQSGHVTLTDFDLSRSLKKplrphfyqpdpeliIDRKKSRSFSRLisptaeknktglkktrsarvnPInrrk 232
Cdd:cd05053 159 LAARNVLVTEDNVMKIADFGLARDIHH--------------IDYYRKTTNGRL---------------------PV---- 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 233 tsfssgersnsfvgtdEYVSPEVIRGDGHDFAVDWWALGVLTYEMM-YGETPFKGKSKKETFRnvLMKEPEFAGKP---- 307
Cdd:cd05053 200 ----------------KWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELFK--LLKEGHRMEKPqnct 261
                       330
                ....*....|....*...
gi 15232374 308 NDLTDLIRRLLVKDPNRR 325
Cdd:cd05053 262 QELYMLMRDCWHEVPSQR 279
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
266-325 2.35e-03

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: 39.19  E-value: 2.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232374 266 DWWALGVLTYEMM-YGETPFKGKSKKETFRNVL----MKEPEfaGKPNDLTDLIRRLLVKDPNRR 325
Cdd:cd05034 175 DVWSFGILLYEIVtYGRVPYPGMTNREVLEQVErgyrMPKPP--GCPDELYDIMLQCWKKEPEER 237
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
19-175 2.68e-03

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: 39.60  E-value: 2.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  19 DSIKALKILGKGATGTVFLAhdVVSTSSSSSPFAVKLVPK-SSASSLRRARWEIEVLRRLSvdsnQNPFLPRLLASFESP 97
Cdd:cd05089   2 EDIKFEDVIGEGNFGQVIKA--MIKKDGLKMNAAIKMLKEfASENDHRDFAGELEVLCKLG----HHPNIINLLGACENR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  98 EYFAWAVPYCSGGDLNVLLHR----QNDGVF-----------SSSVIRFyVAEIVCALEHLHTMGIAYRDLKPENILIQQ 162
Cdd:cd05089  76 GYLYIAIEYAPYGNLLDFLRKsrvlETDPAFakehgtastltSQQLLQF-ASDVAKGMQYLSEKQFIHRDLAARNVLVGE 154
                       170
                ....*....|...
gi 15232374 163 SGHVTLTDFDLSR 175
Cdd:cd05089 155 NLVSKIADFGLSR 167
Haspin_kinase pfam12330
Haspin like kinase domain; This family represents the haspin-like kinase domains.
123-175 2.88e-03

Haspin like kinase domain; This family represents the haspin-like kinase domains.


Pssm-ID: 432484 [Multi-domain]  Cd Length: 369  Bit Score: 39.40  E-value: 2.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15232374   123 VFSSSVIRFYVAEIVCALEHlhtmgiayRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:pfam12330 215 IFWQCVKILYVAETKFQFEH--------RDLHWGHILVDKNLNVTLIDYTLAR 259
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
26-175 2.95e-03

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: 39.25  E-value: 2.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  26 ILGKGATGTVFLAhdVVSTSSSSSPFAVKLVPK-SSASSLRRARWEIEVLRRLSvdsnQNPFLPRLLASFESPEYFAWAV 104
Cdd:cd05047   2 VIGEGNFGQVLKA--RIKKDGLRMDAAIKRMKEyASKDDHRDFAGELEVLCKLG----HHPNIINLLGACEHRGYLYLAI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 105 PYCSGGDLNVLLHR----QNDGVF----------SSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTD 170
Cdd:cd05047  76 EYAPHGNLLDFLRKsrvlETDPAFaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 155

                ....*
gi 15232374 171 FDLSR 175
Cdd:cd05047 156 FGLSR 160
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
106-178 3.17e-03

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: 39.08  E-value: 3.17e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232374 106 YCSGGDLNVLLhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLK 178
Cdd:cd05065  86 FMENGALDSFL-RQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLE 157
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
139-171 3.46e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 39.21  E-value: 3.46e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 15232374  139 ALEHLHTMGIAYRDLKPENILIQQSGHVTLTDF 171
Cdd:PHA03212 194 AIQYLHENRIIHRDIKAENIFINHPGDVCLGDF 226
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
107-177 3.47e-03

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: 38.94  E-value: 3.47e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232374 107 CSGGDLNVLLHRQNDGVFSSSVIrFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSL 177
Cdd:cd05056  88 APLGELRSYLQVNKYSLDLASLI-LYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYM 157
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
18-175 4.06e-03

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: 38.90  E-value: 4.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  18 LDSIKALKILGKGATGTVFLAHDVVSTSSSSS-PFAVKLVPKSSASSLRRA-RWEIEVLRRLsvdsnQNPFLPRLLASFE 95
Cdd:cd05048   4 LSAVRFLEELGEGAFGKVYKGELLGPSSEESAiSVAIKTLKENASPKTQQDfRREAELMSDL-----QHPNIVCLLGVCT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  96 SPEYFAWAVPYCSGGDLN--VLLHRQNDGVFSSSVIR-----------FYVA-EIVCALEHLHTMGIAYRDLKPENILIQ 161
Cdd:cd05048  79 KEQPQCMLFEYMAHGDLHefLVRHSPHSDVGVSSDDDgtassldqsdfLHIAiQIAAGMEYLSSHHYVHRDLAARNCLVG 158
                       170
                ....*....|....
gi 15232374 162 QSGHVTLTDFDLSR 175
Cdd:cd05048 159 DGLTVKISDFGLSR 172
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
128-194 4.24e-03

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 38.89  E-value: 4.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 128 VIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQ----QSGHVTLTDFDLSRSLKKPLRP---------HFYQPDPELII 194
Cdd:cd07868 125 MVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPladldpvvvTFWYRAPELLL 204
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
22-177 4.29e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; 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. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 38.50  E-value: 4.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  22 KALKILGKGATGTVFLAHDVVSTSSssspfaVKLVPKSSASSLRRARWEIEVLRRLSVDSNQNPFLprllaSFESPEYFA 101
Cdd:cd14129   3 KVLRKIGGGGFGEIYDALDLLTREN------VALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFI-----GCGRNDRFN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 102 WAVPYCSGGDLNVLLHRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI----QQSGHVTLTDFDLSRSL 177
Cdd:cd14129  72 YVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQF 151
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
25-159 4.36e-03

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 39.39  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374   25 KILGKGATGTVFLAHDVVSTSSSSSPFAVKLVPKSSASSLrrarWEIEVLRRL---SVDSNQNPFLPRLLASFESPEYFA 101
Cdd:PLN03225 138 KKLGEGAFGVVYKASLVNKQSKKEGKYVLKKATEYGAVEI----WMNERVRRAcpnSCADFVYGFLEPVSSKKEDEYWLV 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  102 WA---------------VPY-------CSGGDLNVLLHRQNdgvfssSVIRFYVAEIVCALEHLHTMGIAYRDLKPENIL 159
Cdd:PLN03225 214 WRyegestladlmqskeFPYnvepyllGKVQDLPKGLEREN------KIIQTIMRQILFALDGLHSTGIVHRDVKPQNII 287
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
132-175 4.47e-03

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: 37.63  E-value: 4.47e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15232374 132 YVAEIVCALEHLHTMGIAYRDLKPENILIqQSGHVTLTDFDLSR 175
Cdd:COG3642  56 LLRELGRLLARLHRAGIVHGDLTTSNILV-DDGGVYLIDFGLAR 98
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
118-325 4.63e-03

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: 38.48  E-value: 4.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 118 RQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSRSLKKplRPHFYQpdpeliidrk 197
Cdd:cd05040  89 RKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQ--NEDHYV---------- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 198 ksrsfsrlispTAEKnktglkktrsarvnpinrRKTSFSsgersnsfvgtdeYVSPEVIRGDGHDFAVDWWALGVLTYEM 277
Cdd:cd05040 157 -----------MQEH------------------RKVPFA-------------WCAPESLKTRKFSHASDVWMFGVTLWEM 194
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15232374 278 M-YGETPFKGKSKKETFRNV-----LMKEPEFAgkPNDLTDLIRRLLVKDPNRR 325
Cdd:cd05040 195 FtYGEEPWLGLNGSQILEKIdkegeRLERPDDC--PQDIYNVMLQCWAHKPADR 246
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
136-174 4.76e-03

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: 38.58  E-value: 4.76e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15232374 136 IVCALEHLHTM--------GIAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd14142 111 AASGLVHLHTEifgtqgkpAIAHRDLKSKNILVKSNGQCCIADLGLA 157
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
20-325 4.91e-03

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: 38.60  E-value: 4.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  20 SIKALKILGKGATGTVFLAH-DVVSTSSSSSPFAVKLVPK----SSASSLRRarwEIEVLRRLSvdsnqNPFLPRLLASF 94
Cdd:cd05046   6 NLQEITTLGRGEFGEVFLAKaKGIEEEGGETLVLVKALQKtkdeNLQSEFRR---ELDMFRKLS-----HKNVVRLLGLC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEYFAWAVPYCSGGDLNVLLHRQNDGV-------FSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVT 167
Cdd:cd05046  78 REAEPHYMILEYTDLGDLKQFLRATKSKDeklkpppLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 168 LTDFDLSRslkkplrphfyqpdpeliiDRKKSRSFsrlisptaeknktglkKTRSARVnPInrrktsfssgersnsfvgt 247
Cdd:cd05046 158 VSLLSLSK-------------------DVYNSEYY----------------KLRNALI-PL------------------- 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 248 dEYVSPEVIRGDGHDFAVDWWALGVLTYEMM-YGETPFKGKSKKETFRNVLMKEPEF---AGKPNDLTDLIRRLLVKDPN 323
Cdd:cd05046 183 -RWLAPEAVQEDDFSTKSDVWSFGVLMWEVFtQGELPFYGLSDEEVLNRLQAGKLELpvpEGCPSRLYKLMTRCWAVNPK 261

                ..
gi 15232374 324 RR 325
Cdd:cd05046 262 DR 263
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
99-160 5.16e-03

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: 38.54  E-value: 5.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232374  99 YFAWAV--------PYCSGGDLNVLL--HRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILI 160
Cdd:cd14051  66 YSAWAEddhmiiqnEYCNGGSLADAIseNEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFI 137
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
24-284 5.46e-03

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: 38.47  E-value: 5.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  24 LKILGKGATGTVFLAHDVvstsSSSSPFAVKLVPKSSASSlrRARW-----EIEVLRRLsvdsnQNPFLPRLLASFESpE 98
Cdd:cd06634  20 LREIGHGSFGAVYFARDV----RNNEVVAIKKMSYSGKQS--NEKWqdiikEVKFLQKL-----RHPNTIEYRGCYLR-E 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  99 YFAWAV-PYCSGGDLNVL-LHRQNDGVFSSSVIRFYVAEivcALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDlSRS 176
Cdd:cd06634  88 HTAWLVmEYCLGSASDLLeVHKKPLQEVEIAAITHGALQ---GLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG-SAS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 177 LKKPlrphfyqpdpeliidrkksrsfsrlisptaeknktglkktrsarvnpinrrktsfssgerSNSFVGTDEYVSPEVI 256
Cdd:cd06634 164 IMAP------------------------------------------------------------ANSFVGTPYWMAPEVI 183
                       250       260       270
                ....*....|....*....|....*....|.
gi 15232374 257 RG--DG-HDFAVDWWALGVLTYEMMYGETPF 284
Cdd:cd06634 184 LAmdEGqYDGKVDVWSLGITCIELAERKPPL 214
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
112-175 5.97e-03

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: 38.30  E-value: 5.97e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232374 112 LNVLlhRQNDGVFSSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENILIQQSGHVTLTDFDLSR 175
Cdd:cd05114  87 LNYL--RQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTR 148
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
234-325 6.52e-03

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 38.38  E-value: 6.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 234 SFSSGERSNSFVGTDEYVSPEV----------IRGDGH-DFAVDWWALGVLTYEMmygetpFKGKSKKETFRNVLMKEPE 302
Cdd:cd14020 158 SFKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSETEcTSAVDLWSLGIVLLEM------FSGMKLKHTVRSQEWKDNS 231
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15232374 303 -------FAGK--------PNDLTDLIRRLLVKDPNRR 325
Cdd:cd14020 232 saiidhiFASNavvnpaipAYHLRDLIKSMLHNDPGKR 269
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
15-175 7.62e-03

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: 38.05  E-value: 7.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  15 ILDLDSIKALKILGKGATGTVFLAHdvVSTSSSSSPFAVKLVPK-SSASSLRRARWEIEVLRRLSvdsnQNPFLPRLLAS 93
Cdd:cd05088   3 VLEWNDIKFQDVIGEGNFGQVLKAR--IKKDGLRMDAAIKRMKEyASKDDHRDFAGELEVLCKLG----HHPNIINLLGA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  94 FESPEYFAWAVPYCSGGDLNVLLHR----QNDGVF----------SSSVIRFYVAEIVCALEHLHTMGIAYRDLKPENIL 159
Cdd:cd05088  77 CEHRGYLYLAIEYAPHGNLLDFLRKsrvlETDPAFaianstastlSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNIL 156
                       170
                ....*....|....*.
gi 15232374 160 IQQSGHVTLTDFDLSR 175
Cdd:cd05088 157 VGENYVAKIADFGLSR 172
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
137-174 7.68e-03

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: 37.84  E-value: 7.68e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15232374 137 VCALEHLHTM--------GIAYRDLKPENILIQQSGHVTLTDFDLS 174
Cdd:cd14144 102 ACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLA 147
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
250-326 7.72e-03

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


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 37.99  E-value: 7.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374 250 YVSPEVIRGDGH-DFAVDWWALGVLTYEMMY-GETPFKGKSKKEtfrnvlmKEPEFAGK-----PN--DLTDLIRRLLVK 320
Cdd:cd05077 178 WIAPECVEDSKNlSIAADKWSFGTTLWEICYnGEIPLKDKTLAE-------KERFYEGQcmlvtPSckELADLMTHCMNY 250

                ....*.
gi 15232374 321 DPNRRL 326
Cdd:cd05077 251 DPNQRP 256
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
16-194 7.74e-03

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: 38.07  E-value: 7.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  16 LDLDSIKALKILGKGATGTVFLAHDVVSTSSSSSPFAVK-LVPKSSASSLRRARWEIEVLRRLsvdsnQNPFLPRLLASF 94
Cdd:cd05090   2 LPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQLVAIKtLKDYNNPQQWNEFQQEASLMTEL-----HHPNIVCLLGVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232374  95 ESPEYFAWAVPYCSGGDLNVLL-----------HRQNDGVFSSSVIR---FYVA-EIVCALEHLHTMGIAYRDLKPENIL 159
Cdd:cd05090  77 TQEQPVCMLFEFMNQGDLHEFLimrsphsdvgcSSDEDGTVKSSLDHgdfLHIAiQIAAGMEYLSSHFFVHKDLAARNIL 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15232374 160 IQQSGHVTLTDFDLSRSL---------KKPLRPHFYQPdPELII 194
Cdd:cd05090 157 VGEQLHVKISDLGLSREIyssdyyrvqNKSLLPIRWMP-PEAIM 199
 
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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