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Conserved domains on  [gi|1907195986|ref|XP_036010649|]
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SNF-related serine/threonine-protein kinase isoform X1 [Mus musculus]

Protein Classification

SNRK family serine/threonine-protein kinase( domain architecture ID 10197368)

SNRK family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to human SNF-related serine/threonine-protein kinase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
12-269 0e+00

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: 605.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14074     1 IAGLYDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKL 171
Cdd:cd14074    81 LELGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGEKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd14074   161 ETSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLI 240
                         250
                  ....*....|....*...
gi 1907195986 252 RDPKRRASLEEIESHPWL 269
Cdd:cd14074   241 RDPKKRASLEEIENHPWL 258
UBA_SNRK cd14339
UBA domain of SNF-related serine/threonine-protein kinase (SNRK) and similar proteins mainly ...
288-335 9.39e-22

UBA domain of SNF-related serine/threonine-protein kinase (SNRK) and similar proteins mainly found in metazoa; SNRK, also called Sucrose nonfermenting 1 (Snf1)-related kinase, is a serine/threonine kinase highly expressed in the testis. It is a distant member of the largely adenosine monophosphate (AMP)-activated protein kinase (AMPK) family. SNRK can be phosphorylated and activated by LKB1 and may mediate cellular effects regulated by LKB1. It is also involved in the regulation of colon cancer cell proliferation and beta-catenin signaling. It inhibits colon cancer cell proliferation through calcyclin-binding protein (CacyBP)-dependent reduction of beta-catenin. In addition to an N-terminal protein kinase domain, it harbors an ubiquitin-associated (UBA) domain, previously called SNF1 homology (SNH) domain which is conserved in other Snf1-related kinases, but not in any other protein kinase.


:

Pssm-ID: 270524  Cd Length: 48  Bit Score: 88.81  E-value: 9.39e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907195986 288 KNLSEEEHNSIIQRMVLGDIADRDAIVEALETNRYNHITATYFLLAER 335
Cdd:cd14339     1 ENLPEEEHELILQKMESGGIASREAILESLEKDAYDHITATYYLLAER 48
 
Name Accession Description Interval E-value
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
12-269 0e+00

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: 605.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14074     1 IAGLYDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKL 171
Cdd:cd14074    81 LELGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGEKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd14074   161 ETSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLI 240
                         250
                  ....*....|....*...
gi 1907195986 252 RDPKRRASLEEIESHPWL 269
Cdd:cd14074   241 RDPKKRASLEEIENHPWL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
16-269 4.66e-106

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 324.10  E-value: 4.66e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRE-RILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   96 DGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:smart00220  80 EGGDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPEN-ILLDEDGHVKLADFGLARQLDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  176 GSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQ-EANDSETLTMIMDCKYTVPPR---VSAGCRDLITRMLQ 251
Cdd:smart00220 158 GTPEYMAPEVLLGKGYG-KAVDIWSLGVILYELLTGKPPFPgDDQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLV 236
                          250
                   ....*....|....*...
gi 1907195986  252 RDPKRRASLEEIESHPWL 269
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
16-269 3.46e-66

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 218.27  E-value: 3.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYImKHEEGLNEDLAKKYFAQIVHAISychklhvvhrdlkpenvvffekqglvkltdfgfsnkfqPGKKLTTSC 175
Cdd:pfam00069  81 EGGSLFDLL-SEKGAFSEREAKFIMKQILEGLE--------------------------------------SGSSLTTFV 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY---TVPPRVSAGCRDLITRMLQR 252
Cdd:pfam00069 122 GTPWYMAPEVLGGNPYG-PKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafpELPSNLSEEAKDLLKKLLKK 200
                         250
                  ....*....|....*..
gi 1907195986 253 DPKRRASLEEIESHPWL 269
Cdd:pfam00069 201 DPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-263 8.01e-60

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 209.87  E-value: 8.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLF-QEVRCMKLVQHPNIVRLYEVIDTQTKLYL 90
Cdd:COG0515     5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFrREARALARLNHPNIVRVYDVGEEDGRPYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDYImKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSnKFQPGKK 170
Cdd:COG0515    85 VMEYVEGESLADLL-RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPAN-ILLTPDGRVKLIDFGIA-RALGGAT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LT---TSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP----PRVSAGCR 243
Cdd:COG0515   162 LTqtgTVVGTPGYMAPEQARGEPVD-PRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPselrPDLPPALD 240
                         250       260
                  ....*....|....*....|.
gi 1907195986 244 DLITRMLQRDPKRR-ASLEEI 263
Cdd:COG0515   241 AIVLRALAKDPEERyQSAAEL 261
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
16-273 2.76e-47

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 170.77  E-value: 2.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNeDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQpgKKLTTS 174
Cdd:PTZ00263  100 VVGGELFTHLRKAGRFPN-DVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL-DNKGHVKVTDFGFAKKVP--DRTFTL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDP 254
Cdd:PTZ00263  176 CGTPEYLAPEVIQSKGHGK-AVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDH 254
                         250       260
                  ....*....|....*....|....
gi 1907195986 255 -KRRASL----EEIESHPWLQGVD 273
Cdd:PTZ00263  255 tKRLGTLkggvADVKNHPYFHGAN 278
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
12-216 2.40e-26

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 114.12  E-value: 2.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdktKLDtLATGHLFQ-----EVRCM-KLVqHPNIVRLYEVIDTQ 85
Cdd:NF033483    5 LGGRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL---RPD-LARDPEFVarfrrEAQSAaSLS-HPNIVSVYDVGEDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  86 TKLYLILELGDGGDMFDYImkHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFG---- 160
Cdd:NF033483   80 GIPYIVMEYVDGRTLKDYI--REHGpLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL-ITKDGRVKVTDFGiara 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 161 FSNkfqpgkklTTSC------GSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQ 216
Cdd:NF033483  157 LSS--------TTMTqtnsvlGTVHYLSPEQARGGTVDARS-DIYSLGIVLYEMLTGRPPFD 209
UBA_SNRK cd14339
UBA domain of SNF-related serine/threonine-protein kinase (SNRK) and similar proteins mainly ...
288-335 9.39e-22

UBA domain of SNF-related serine/threonine-protein kinase (SNRK) and similar proteins mainly found in metazoa; SNRK, also called Sucrose nonfermenting 1 (Snf1)-related kinase, is a serine/threonine kinase highly expressed in the testis. It is a distant member of the largely adenosine monophosphate (AMP)-activated protein kinase (AMPK) family. SNRK can be phosphorylated and activated by LKB1 and may mediate cellular effects regulated by LKB1. It is also involved in the regulation of colon cancer cell proliferation and beta-catenin signaling. It inhibits colon cancer cell proliferation through calcyclin-binding protein (CacyBP)-dependent reduction of beta-catenin. In addition to an N-terminal protein kinase domain, it harbors an ubiquitin-associated (UBA) domain, previously called SNF1 homology (SNH) domain which is conserved in other Snf1-related kinases, but not in any other protein kinase.


Pssm-ID: 270524  Cd Length: 48  Bit Score: 88.81  E-value: 9.39e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907195986 288 KNLSEEEHNSIIQRMVLGDIADRDAIVEALETNRYNHITATYFLLAER 335
Cdd:cd14339     1 ENLPEEEHELILQKMESGGIASREAILESLEKDAYDHITATYYLLAER 48
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
38-258 3.67e-13

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 73.34  E-value: 3.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   38 TGEKVAVKVIdktKLDTLATGHLFQEVR-----CMKLvQHPNIVRLYEVIDTQ-TKLYLILELGDGGDMFDyIMKHEEGL 111
Cdd:TIGR03903    2 TGHEVAIKLL---RTDAPEEEHQRARFRretalCARL-YHPNIVALLDSGEAPpGLLFAVFEYVPGRTLRE-VLAADGAL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  112 NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL--VKLTDFGFSNkFQPG------KKLTTS---CGSLAY 180
Cdd:TIGR03903   77 PAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRphAKVLDFGIGT-LLPGvrdadvATLTRTtevLGTPTY 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  181 SAPEILLGdEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCR--DLITRMLQRDPKRRA 258
Cdd:TIGR03903  156 CAPEQLRG-EPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVSLPPWIAGHPlgQVLRKALNKDPRQRA 234
 
Name Accession Description Interval E-value
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
12-269 0e+00

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: 605.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14074     1 IAGLYDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKL 171
Cdd:cd14074    81 LELGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGEKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd14074   161 ETSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLI 240
                         250
                  ....*....|....*...
gi 1907195986 252 RDPKRRASLEEIESHPWL 269
Cdd:cd14074   241 RDPKKRASLEEIENHPWL 258
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
16-268 2.28e-140

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: 412.68  E-value: 2.28e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd14003    82 SGGELFDYIVNNG-RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENI-LLDKNGNLKIIDFGLSNEFRGGSLLKTFC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd14003   160 GTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPS 239
                         250
                  ....*....|...
gi 1907195986 256 RRASLEEIESHPW 268
Cdd:cd14003   240 KRITIEEILNHPW 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
16-268 3.55e-110

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: 335.22  E-value: 3.55e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHeEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEK--QGLVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd05117    82 TGGELFDRIVKK-GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdpDSPIKIIDFGLAKIFEEGEKLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSAGCRDLITRM 249
Cdd:cd05117   161 VCGTPYYVAPEVLKGKGYG-KKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPewknVSEEAKDLIKRL 239
                         250
                  ....*....|....*....
gi 1907195986 250 LQRDPKRRASLEEIESHPW 268
Cdd:cd05117   240 LVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
16-269 4.66e-106

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 324.10  E-value: 4.66e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRE-RILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   96 DGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:smart00220  80 EGGDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPEN-ILLDEDGHVKLADFGLARQLDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  176 GSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQ-EANDSETLTMIMDCKYTVPPR---VSAGCRDLITRMLQ 251
Cdd:smart00220 158 GTPEYMAPEVLLGKGYG-KAVDIWSLGVILYELLTGKPPFPgDDQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLV 236
                          250
                   ....*....|....*...
gi 1907195986  252 RDPKRRASLEEIESHPWL 269
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
16-269 1.51e-99

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: 307.40  E-value: 1.51e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd14071    82 SNGEIFDYLAQHGR-MSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL-DANMNIKIADFGFSNFFKPGELLKTWC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd14071   160 GSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPS 239
                         250
                  ....*....|....
gi 1907195986 256 RRASLEEIESHPWL 269
Cdd:cd14071   240 KRLTIEQIKKHKWM 253
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
14-269 2.19e-94

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: 294.18  E-value: 2.19e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTL-ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd14079     2 GNYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLdMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFQPGKKLT 172
Cdd:cd14079    82 EYVSGGELFDYIVQKG-RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENL-LLDSNMNVKIADFGLSNIMRDGEFLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQR 252
Cdd:cd14079   160 TSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVV 239
                         250
                  ....*....|....*..
gi 1907195986 253 DPKRRASLEEIESHPWL 269
Cdd:cd14079   240 DPLKRITIPEIRQHPWF 256
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
16-269 5.12e-94

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: 292.89  E-value: 5.12e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd14072    82 SGGEVFDYLVAHGR-MKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLL-LDADMNIKIADFGFSNEFTPGNKLDTFC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd14072   160 GSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPS 239
                         250
                  ....*....|....
gi 1907195986 256 RRASLEEIESHPWL 269
Cdd:cd14072   240 KRGTLEQIMKDRWM 253
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
14-269 4.43e-90

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: 282.61  E-value: 4.43e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDT--LATGhLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14081     1 GPYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKesVLMK-VEREIAIMKLIEHPNVLKLYDVYENKKYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFQPGKKL 171
Cdd:cd14081    80 LEYVSGGELFDYLVKKG-RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENL-LLDEKNNIKIADFGMASLQPEGSLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd14081   158 ETSCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLE 237
                         250
                  ....*....|....*...
gi 1907195986 252 RDPKRRASLEEIESHPWL 269
Cdd:cd14081   238 VNPEKRITIEEIKKHPWF 255
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
14-269 2.38e-89

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: 280.76  E-value: 2.38e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd14075     2 GFYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYImkHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLT 172
Cdd:cd14075    82 YASGGELYTKI--STEGkLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAEN-VFYASNNCVKVGDFGFSTHAKRGETLN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQR 252
Cdd:cd14075   159 TFCGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQP 238
                         250
                  ....*....|....*..
gi 1907195986 253 DPKRRASLEEIESHPWL 269
Cdd:cd14075   239 VPSDRYSIDEIKNSEWL 255
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
16-270 1.29e-87

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: 276.28  E-value: 1.29e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRrEIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKFqPGKKLTTS 174
Cdd:cd14007    82 APNGELYKELKKQKR-FDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSN-GELKLADFGWSVHA-PSNRRKTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDP 254
Cdd:cd14007   159 CGTLDYLPPEMVEGKEYD-YKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDP 237
                         250
                  ....*....|....*.
gi 1907195986 255 KRRASLEEIESHPWLQ 270
Cdd:cd14007   238 SKRLSLEQVLNHPWIK 253
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
12-269 6.63e-86

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: 271.95  E-value: 6.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLAtgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYL 90
Cdd:cd14078     1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALgDDLP--RVKTEIEALKNLSHQHICRLYHVIETDNKIFM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNKFQPGKK 170
Cdd:cd14078    79 VLEYCPGGELFDYIVAKDR-LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNL-KLIDFGLCAKPKGGMD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 --LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITR 248
Cdd:cd14078   157 hhLETCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQ 236
                         250       260
                  ....*....|....*....|.
gi 1907195986 249 MLQRDPKRRASLEEIESHPWL 269
Cdd:cd14078   237 MLQVDPKKRITVKELLNHPWV 257
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
16-268 7.57e-84

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: 266.58  E-value: 7.57e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVaREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFS---NKFQPGKKL 171
Cdd:cd14663    82 VTGGELFSKIAKNGR-LKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDED-GNLKISDFGLSalsEQFRQDGLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd14663   160 HTTCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILD 239
                         250
                  ....*....|....*..
gi 1907195986 252 RDPKRRASLEEIESHPW 268
Cdd:cd14663   240 PNPSTRITVEQIMASPW 256
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
22-269 1.63e-82

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: 263.26  E-value: 1.63e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKL------------DTLATGHLFQEVRCMKLVQHPNIVRLYEVID--TQTK 87
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLrkrregkndrgkIKNALDDVRREIAIMKKLDHPNIVRLYEVIDdpESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGGDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQ 166
Cdd:cd14008    81 LYLVLEYCEGGPVMELDSGDRvPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPEN-LLLTADGTVKISDFGVSEMFE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGK-KLTTSCGSLAYSAPEILLGD--EYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK--YTVPPRVSAG 241
Cdd:cd14008   160 DGNdTLQKTAGTPAFLAPELCDGDskTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNdeFPIPPELSPE 239
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 242 CRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14008   240 LKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
16-269 4.55e-82

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: 262.12  E-value: 4.55e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLA--RHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKApKDFLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFQPGKKLT 172
Cdd:cd14080    82 EYAEHGDLLEYIQKRG-ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENI-LLDSNNNVKLSDFGFARLCPDDDGDV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TS---CGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV---SAGCRDLI 246
Cdd:cd14080   160 LSktfCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSVkklSPECKDLI 239
                         250       260
                  ....*....|....*....|...
gi 1907195986 247 TRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14080   240 DQLLEPDPTKRATIEEILNHPWL 262
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
22-268 9.19e-79

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: 252.82  E-value: 9.19e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDM 100
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEiIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYiMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKF-QPGKKLTTSCGSLA 179
Cdd:cd05123    81 FSH-LSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL-DSDGHIKLTDFGLAKELsSDGDRTYTFCGTPE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 180 YSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKRR-- 257
Cdd:cd05123   159 YLAPEVLLGKGYG-KAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRlg 237
                         250
                  ....*....|..
gi 1907195986 258 -ASLEEIESHPW 268
Cdd:cd05123   238 sGGAEEIKAHPF 249
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
22-268 2.52e-77

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: 249.06  E-value: 2.52e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHeEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF--FEKQGLVKLTDFGFSNKFQPGKKLTTSCGSLA 179
Cdd:cd14009    81 QYIRKR-GRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstSGDDPVLKIADFGFARSLQPASMAETLCGSPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 180 YSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC----KYTVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd14009   160 YMAPEILQFQKYDAKA-DLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSdaviPFPIAAQLSPDCKDLLRRLLRRDPA 238
                         250
                  ....*....|...
gi 1907195986 256 RRASLEEIESHPW 268
Cdd:cd14009   239 ERISFEEFFAHPF 251
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
16-269 2.55e-77

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: 249.23  E-value: 2.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIeDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd14073    83 ASGGELYDYISERRR-LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILL-DQNGNAKIADFGLSNLYSKDKLLQTF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCrDLITRMLQRDP 254
Cdd:cd14073   161 CGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPSDAS-GLIRWMLTVNP 239
                         250
                  ....*....|....*
gi 1907195986 255 KRRASLEEIESHPWL 269
Cdd:cd14073   240 KRRATIEDIANHWWV 254
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
14-269 3.82e-77

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: 249.29  E-value: 3.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKT-------------KLDTLATGHLFQEVRCMKLVQHPNIVRLYE 80
Cdd:cd14077     1 GNWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRAsnaglkkerekrlEKEISRDIRTIREAALSSLLNHPHICRLRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  81 VIDTQTKLYLILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFG 160
Cdd:cd14077    81 FLRTPNHYYMLFEYVDGGQLLDYIISHGK-LKEKQARKFARQIASALDYLHRNSIVHRDLKIENILI-SKSGNIKIIDFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 FSNKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSA 240
Cdd:cd14077   159 LSNLYDPRRLLRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSS 238
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 241 GCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14077   239 ECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
16-269 3.18e-76

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: 246.44  E-value: 3.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKApEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSN---KFQPGKK- 170
Cdd:cd14162    82 AENGDLLDYIRKNG-ALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLL-DKNNNLKITDFGFARgvmKTKDGKPk 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 -LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMImDCKYTVP--PRVSAGCRDLIT 247
Cdd:cd14162   160 lSETYCGSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV-QRRVVFPknPTVSEECKDLIL 238
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLqRDPKRRASLEEIESHPWL 269
Cdd:cd14162   239 RML-SPVKKRITIEEIKRDPWF 259
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
22-267 9.61e-72

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: 232.93  E-value: 9.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLAtGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLL-EELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTSCG--SLA 179
Cdd:cd00180    80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPEN-ILLDSDGTVKLADFGLAKDLDSDDSLLKTTGgtTPP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 180 YSAPEILLGDEYDAPAVDIWSLGVILFmlvcgqppfqeandsetltmIMDCkytvpprvsagCRDLITRMLQRDPKRRAS 259
Cdd:cd00180   159 YYAPPELLGGRYYGPKVDIWSLGVILY--------------------ELEE-----------LKDLIRRMLQYDPKKRPS 207

                  ....*...
gi 1907195986 260 LEEIESHP 267
Cdd:cd00180   208 AKELLEHL 215
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
16-267 1.70e-69

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: 228.50  E-value: 1.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEG---LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKL- 171
Cdd:cd08215    82 DGGDLAQKIKKQKKKgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQN-IFLTKDGVVKLGDFGISKVLESTTDLa 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY-TVPPRVSAGCRDLITRML 250
Cdd:cd08215   161 KTVVGTPYYLSPELCENKPYNYKS-DIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYpPIPSQYSSELRDLVNSML 239
                         250
                  ....*....|....*..
gi 1907195986 251 QRDPKRRASLEEIESHP 267
Cdd:cd08215   240 QKDPEKRPSANEILSSP 256
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
16-269 5.50e-68

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: 224.66  E-value: 5.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQT-KLYLILE 93
Cdd:cd14165     3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKApDDFVEKFLPRELEILARLNHKSIIKTYEIFETSDgKVYIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYImKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFS---NKFQPGKK 170
Cdd:cd14165    83 LGVQGDLLEFI-KLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL-DKDFNIKLTDFGFSkrcLRDENGRI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 L--TTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV--SAGCRDLI 246
Cdd:cd14165   161 VlsKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKnlTSECKDLI 240
                         250       260
                  ....*....|....*....|...
gi 1907195986 247 TRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14165   241 YRLLQPDVSQRLCIDEVLSHPWL 263
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
16-269 6.07e-68

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: 224.52  E-value: 6.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYImKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ-PGKK--LT 172
Cdd:cd14069    83 SGGELFDKI-EPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLL-LDENDNLKISDFGLATVFRyKGKErlLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMI-MDCK---YTVPPRVSAGCRDLITR 248
Cdd:cd14069   161 KMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDwKENKktyLTPWKKIDTAALSLLRK 240
                         250       260
                  ....*....|....*....|.
gi 1907195986 249 MLQRDPKRRASLEEIESHPWL 269
Cdd:cd14069   241 ILTENPNKRITIEDIKKHPWY 261
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
16-268 5.91e-67

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: 221.82  E-value: 5.91e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDtlATGHLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCK--GKEHMIEnEVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNEDlAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSNKFQpgKKL 171
Cdd:cd14095    80 VKGGDLFDAITSSTKFTERD-ASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDgskSLKLADFGLATEVK--EPL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQ-EANDSETL-TMIMDCKYTVPP----RVSAGCRDL 245
Cdd:cd14095   157 FTVCGTPTYVAPEILAETGYGL-KVDIWAAGVITYILLCGFPPFRsPDRDQEELfDLILAGEFEFLSpywdNISDSAKDL 235
                         250       260
                  ....*....|....*....|...
gi 1907195986 246 ITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd14095   236 ISRMLVVDPEKRYSAGQVLDHPW 258
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
16-269 7.80e-67

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: 222.27  E-value: 7.80e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLdTLATGHLFQ-------EVRCMKLVQHPNIVRLYEVIDTQTKL 88
Cdd:cd14084     8 YIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKF-TIGSRREINkprnietEIEILKKLSHPCIIKIEDFFDAEDDY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF--EKQGLVKLTDFGFSNKFQ 166
Cdd:cd14084    87 YIVLELMEGGELFDRVVS-NKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSsqEEECLIKITDFGLSKILG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKKLTTSCGSLAYSAPEILL--GDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLT-MIMDCKYTVPP----RVS 239
Cdd:cd14084   166 ETSLMKTLCGTPTYLAPEVLRsfGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKeQILSGKYTFIPkawkNVS 245
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 240 AGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14084   246 EEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
Pkinase pfam00069
Protein kinase domain;
16-269 3.46e-66

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 218.27  E-value: 3.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYImKHEEGLNEDLAKKYFAQIVHAISychklhvvhrdlkpenvvffekqglvkltdfgfsnkfqPGKKLTTSC 175
Cdd:pfam00069  81 EGGSLFDLL-SEKGAFSEREAKFIMKQILEGLE--------------------------------------SGSSLTTFV 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY---TVPPRVSAGCRDLITRMLQR 252
Cdd:pfam00069 122 GTPWYMAPEVLGGNPYG-PKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafpELPSNLSEEAKDLLKKLLKK 200
                         250
                  ....*....|....*..
gi 1907195986 253 DPKRRASLEEIESHPWL 269
Cdd:pfam00069 201 DPSKRLTATQALQHPWF 217
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
24-273 4.55e-65

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: 217.08  E-value: 4.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  24 RGHFAVVKLARHVFTGEKVAVKVIDKTKLDTL-ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFD 102
Cdd:cd05579     3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKnQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 103 yIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFS-------NKFQPGKKLTTS- 174
Cdd:cd05579    83 -LLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNIL-IDANGHLKLTDFGLSkvglvrrQIKLSIQKKSNGa 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 --------CGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP--PRVSAGCRD 244
Cdd:cd05579   161 pekedrriVGTPDYLAPEILLGQGHG-KTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPedPEVSDEAKD 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 245 LITRMLQRDPKRRA---SLEEIESHPWLQGVD 273
Cdd:cd05579   240 LISKLLTPDPEKRLgakGIEEIKNHPFFKGID 271
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-292 1.37e-64

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: 217.55  E-value: 1.37e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKT---LGRGHFAVVKLARHVFTGEKVAVKVIDKtKLDTLatghlfQEVRCMKLVQ-HPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14092     5 YELDLReeaLGDGSFSVCRKCVHKKTGQEFAVKIVSR-RLDTS------REVQLLRLCQgHPNIVKLHEVFQDELHTYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE--KQGLVKLTDFGFSNKFQPGK 169
Cdd:cd14092    78 MELLRGGELLERIRKKKR-FTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDedDDAEIKIVDFGFARLKPENQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILLGD----EYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC-----------KYTV 234
Cdd:cd14092   157 PLKTPCFTLPYAAPEVLKQAlstqGYDE-SCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRiksgdfsfdgeEWKN 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 235 pprVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGVDPSPATkyniPLVSYKNLSE 292
Cdd:cd14092   236 ---VSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSST----PLMTPGVLSS 286
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
16-268 5.76e-64

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: 213.77  E-value: 5.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLAtghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14083     5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALkgkeDSLE-----NEIAVLRKIKHPNIVQLLDIYESKSHLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMkhEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF--EKQGLVKLTDFGFSnKFQPG 168
Cdd:cd14083    80 MELVTGGELFDRIV--EKGsYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYspDEDSKIMISDFGLS-KMEDS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTV-PP---RVSAGCRD 244
Cdd:cd14083   157 GVMSTACGTPGYVAPEVLAQKPY-GKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFdSPywdDISDSAKD 235
                         250       260
                  ....*....|....*....|....
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd14083   236 FIRHLMEKDPNKRYTCEQALEHPW 259
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
16-269 1.51e-62

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: 209.81  E-value: 1.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVfTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIkDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd14161    84 ASRGDLYDYISERQR-LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL-DANGNIKIADFGLSNLYNQDKFLQTY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCrDLITRMLQRDP 254
Cdd:cd14161   162 CGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSDAC-GLIRWLLMVNP 240
                         250
                  ....*....|....*
gi 1907195986 255 KRRASLEEIESHPWL 269
Cdd:cd14161   241 ERRATLEDVASHWWV 255
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
22-273 2.84e-62

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: 209.39  E-value: 2.84e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDM 100
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIvQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYImkHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFQPGKKLTTSCGSLA 179
Cdd:cd05572    81 WTIL--RDRGlFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENL-LLDSNGYVKLVDFGFAKKLGSGRKTWTFCGTPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 180 YSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDS--ETLTMIMDCKYTV--PPRVSAGCRDLITRMLQRDPK 255
Cdd:cd05572   158 YVAPEIILNKGYDF-SVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGIDKIefPKYIDKNAKNLIKQLLRRNPE 236
                         250       260
                  ....*....|....*....|...
gi 1907195986 256 RR-----ASLEEIESHPWLQGVD 273
Cdd:cd05572   237 ERlgylkGGIRDIKKHKWFEGFD 259
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
20-269 8.10e-62

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: 208.18  E-value: 8.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKtklDTLATGH----LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14099     7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPK---SSLTKPKqrekLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYImKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFQ-PGKKLTTS 174
Cdd:cd14099    84 SNGSLMELL-KRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNL-FLDENMNVKIGDFGLAARLEyDGERKKTL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR--VSAGCRDLITRMLQR 252
Cdd:cd14099   162 CGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHlsISDEAKDLIRSMLQP 241
                         250
                  ....*....|....*..
gi 1907195986 253 DPKRRASLEEIESHPWL 269
Cdd:cd14099   242 DPTKRPSLDEILSHPFF 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
16-268 1.83e-61

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: 207.33  E-value: 1.83e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKvAGNDKNLQLFQrEINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHeEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG-LVKLTDFGFSNKFQPGKKLT 172
Cdd:cd14098    82 YVEGGDLMDFIMAW-GAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPvIVKISDFGLAKVIHTGTFLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPA-----VDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP----RVSAGCR 243
Cdd:cd14098   161 TFCGTMAYLAPEILMSKEQNLQGgysnlVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPlvdfNISEEAI 240
                         250       260
                  ....*....|....*....|....*
gi 1907195986 244 DLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd14098   241 DFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
16-263 5.26e-61

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: 205.90  E-value: 5.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVID-KTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRpELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYImKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd14014    82 VEGGSLADLL-RERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPAN-ILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 --CGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY----TVPPRVSAGCRDLITR 248
Cdd:cd14014   160 svLGTPAYMAPEQARGGPVD-PRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppsPLNPDVPPALDAIILR 238
                         250
                  ....*....|....*.
gi 1907195986 249 MLQRDPKRR-ASLEEI 263
Cdd:cd14014   239 ALAKDPEERpQSAAEL 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
15-269 8.78e-61

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: 205.13  E-value: 8.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLAtgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKE--SILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd05122    79 CSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD-GEVKLIDFGLSAQLSDGKTRNTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD---CKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd05122   158 VGTPYWMAPEVIQGKPYG-FKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATngpPGLRNPKKWSKEFKDFLKKCLQ 236
                         250
                  ....*....|....*...
gi 1907195986 252 RDPKRRASLEEIESHPWL 269
Cdd:cd05122   237 KDPEKRPTAEQLLKHPFI 254
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
20-268 4.94e-60

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: 203.99  E-value: 4.94e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDK---TKLDtlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05581     7 KPLGEGSYSTVVLAKEKETGKEYAIKVLDKrhiIKEK--KVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFG---------------- 160
Cdd:cd05581    85 NGDLLEYIRKYGS-LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDED-MHIKITDFGtakvlgpdsspestkg 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 --FSNKFQPGKKLTTSCGSLAYSAPEiLLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV 238
Cdd:cd05581   163 daDSQIAYNQARAASFVGTAEYVSPE-LLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPENF 241
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907195986 239 SAGCRDLITRMLQRDPKRR------ASLEEIESHPW 268
Cdd:cd05581   242 PPDAKDLIQKLLVLDPSKRlgvnenGGYDELKAHPF 277
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-263 8.01e-60

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 209.87  E-value: 8.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLF-QEVRCMKLVQHPNIVRLYEVIDTQTKLYL 90
Cdd:COG0515     5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFrREARALARLNHPNIVRVYDVGEEDGRPYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDYImKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSnKFQPGKK 170
Cdd:COG0515    85 VMEYVEGESLADLL-RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPAN-ILLTPDGRVKLIDFGIA-RALGGAT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LT---TSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP----PRVSAGCR 243
Cdd:COG0515   162 LTqtgTVVGTPGYMAPEQARGEPVD-PRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPselrPDLPPALD 240
                         250       260
                  ....*....|....*....|.
gi 1907195986 244 DLITRMLQRDPKRR-ASLEEI 263
Cdd:COG0515   241 AIVLRALAKDPEERyQSAAEL 261
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-271 1.00e-59

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: 203.20  E-value: 1.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14169     1 INSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRG-KEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMkhEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF---FEKQGLVkLTDFGFSnKFQP 167
Cdd:cd14169    80 MELVTGGELFDRII--ERGsYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYatpFEDSKIM-ISDFGLS-KIEA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP----RVSAGCR 243
Cdd:cd14169   156 QGMLSTACGTPGYVAPELLEQKPY-GKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSpywdDISESAK 234
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 244 DLITRMLQRDPKRRASLEEIESHPWLQG 271
Cdd:cd14169   235 DFIRHLLERDPEKRFTCEQALQHPWISG 262
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
22-268 4.19e-59

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: 200.19  E-value: 4.19e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHlfqEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLR---EISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ-GLVKLTDFGFSNKFQPGKKLTTSCGSLAY 180
Cdd:cd14006    78 DRLAERGS-LSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPsPQIKIIDFGLARKLNPGEELKEIFGTPEF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP----RVSAGCRDLITRMLQRDPKR 256
Cdd:cd14006   157 VAPEIVNGEPV-SLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEeyfsSVSQEAKDFIRKLLVKEPRK 235
                         250
                  ....*....|..
gi 1907195986 257 RASLEEIESHPW 268
Cdd:cd14006   236 RPTAQEALQHPW 247
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-271 1.14e-58

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: 199.87  E-value: 1.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14167     1 IRDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEG-KETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMkhEEGL-NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF--EKQGLVKLTDFGFSNKFQPG 168
Cdd:cd14167    80 MQLVSGGELFDRIV--EKGFyTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYslDEDSKIMISDFGLSKIEGSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP----RVSAGCRD 244
Cdd:cd14167   158 SVMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSpywdDISDSAKD 236
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPWLQG 271
Cdd:cd14167   237 FIQHLMEKDPEKRFTCEQALQHPWIAG 263
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
16-269 2.51e-58

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: 198.68  E-value: 2.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKT-KLDTLATGHLFQEVRCMKLVQHPNIVRLYEVID-TQTKLYLILE 93
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSgGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLEsADGKIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMkHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfekQGL-VKLTDFGFSNKF-QPGKKL 171
Cdd:cd14163    82 LAEDGDVFDCVL-HGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL---QGFtLKLTDFGFAKQLpKGGREL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 T-TSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMiMDCKYTVPPR--VSAGCRDLITR 248
Cdd:cd14163   158 SqTFCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQ-QQKGVSLPGHlgVSRTCQDLLKR 236
                         250       260
                  ....*....|....*....|.
gi 1907195986 249 MLQRDPKRRASLEEIESHPWL 269
Cdd:cd14163   237 LLEPDMVLRPSIEEVSWHPWL 257
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
16-273 3.16e-58

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: 199.34  E-value: 3.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLA-TGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKqVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFqpgKKLT-T 173
Cdd:cd05580    83 VPGGELFSLLRR-SGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLL-DSDGHIKITDFGFAKRV---KDRTyT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd05580   158 LCGTPEYLAPEIILSKGHGK-AVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVD 236
                         250       260
                  ....*....|....*....|....*
gi 1907195986 254 P-KRRASL----EEIESHPWLQGVD 273
Cdd:cd05580   237 LtKRLGNLkngvEDIKNHPWFAGID 261
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
16-269 3.47e-58

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: 198.73  E-value: 3.47e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATG------HLFQEVRCMKLVQ-HPNIVRLYEVIDTQTKL 88
Cdd:cd14093     5 YEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEaeelreATRREIEILRQVSgHPNIIELHDVFESPTFI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPG 168
Cdd:cd14093    85 FLVFELCRKGELFDYLTEVVT-LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILL-DDNLNVKISDFGFATRLDEG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGDEYD-APA----VDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP-PR---VS 239
Cdd:cd14093   163 EKLRELCGTPGYLAPEVLKCSMYDnAPGygkeVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGsPEwddIS 242
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 240 AGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14093   243 DTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
16-269 7.00e-58

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: 198.81  E-value: 7.00e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHV-FTGEKVAVKVIDKTKLDTLATG-----HLFQEVRCMKLVQHPNIVRLYEVIDTQTKLY 89
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAVPLrNTGKPVAIKVVRKADLSSDNLKgssraNILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF----FEKQ-------------- 151
Cdd:cd14096    83 IVLELADGGEIFHQIVRLTY-FSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipFIPSivklrkadddetkv 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 152 --------------GLVKLTDFGFSNKFQPgKKLTTSCGSLAYSAPEIlLGDEYDAPAVDIWSLGVILFMLVCGQPPFQE 217
Cdd:cd14096   162 degefipgvggggiGIVKLADFGLSKQVWD-SNTKTPCGTVGYTAPEV-VKDERYSKKVDMWALGCVLYTLLCGFPPFYD 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 218 aNDSETLTM-IMDCKYT-VPP---RVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14096   240 -ESIETLTEkISRGDYTfLSPwwdEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
22-269 1.06e-57

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: 196.71  E-value: 1.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATG--HLFQEVRCMKLVQHPNIVRLYEVI--DTQTKLYLILELGDG 97
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIPNGeaNVKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVMEYCVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 G--DMFDyiMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFG---FSNKFQPGKKLT 172
Cdd:cd14119    81 GlqEMLD--SAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLL-TTDGTLKISDFGvaeALDLFAEDDTCT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDE-YDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd14119   158 TSQGSPAFQPPEIANGQDsFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLE 237
                         250
                  ....*....|....*...
gi 1907195986 252 RDPKRRASLEEIESHPWL 269
Cdd:cd14119   238 KDPEKRFTIEQIRQHPWF 255
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
15-269 1.95e-57

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: 197.26  E-value: 1.95e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14086     2 EYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKFQPGKKLT 172
Cdd:cd14086    82 VTGGELFEDIVAREF-YSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSkgAAVKLADFGLAIEVQGDQQAW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TS-CGSLAYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP----RVSAGCRDLIT 247
Cdd:cd14086   161 FGfAGTPGYLSPEVLRKDPYGKP-VDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKDLIN 239
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14086   240 QMLTVNPAKRITAAEALKHPWI 261
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
22-268 2.48e-57

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: 195.58  E-value: 2.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARH-VFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDM 100
Cdd:cd14121     3 LGSGTYATVYKAYRkSGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF-FEKQGLVKLTDFGFSNKFQPGKKLTTSCGSLA 179
Cdd:cd14121    83 SRFIRSRRT-LPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLsSRYNPVLKLADFGFAQHLKPNDEAHSLRGSPL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 180 YSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK-YTVP--PRVSAGCRDLITRMLQRDPKR 256
Cdd:cd14121   162 YMAPEMILKKKYDA-RVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPtrPELSADCRDLLLRLLQRDPDR 240
                         250
                  ....*....|..
gi 1907195986 257 RASLEEIESHPW 268
Cdd:cd14121   241 RISFEEFFAHPF 252
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
16-268 7.02e-57

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: 194.60  E-value: 7.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDK-TKLDTlatgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERgLKIDE----NVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG-LVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd14662    78 AAGGELFERICNAGR-FSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPApRLKICDFGYSKSSVLHSQPKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEAND----SETLTMIMDCKYTVPP--RVSAGCRDLIT 247
Cdd:cd14662   157 TVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDpknfRKTIQRIMSVQYKIPDyvRVSQDCRHLLS 236
                         250       260
                  ....*....|....*....|.
gi 1907195986 248 RMLQRDPKRRASLEEIESHPW 268
Cdd:cd14662   237 RIFVANPAKRITIPEIKNHPW 257
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
16-269 2.26e-56

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: 193.22  E-value: 2.26e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGH----LFQEVRCMKLV---QHPNIVRLYEVIDTQTKL 88
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINgpvpVPLEIALLLKAskpGVPGVIRLLDWYERPDGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGG-DMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGfsnkfqP 167
Cdd:cd14005    82 LLIMERPEPCqDLFDFITERGA-LSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEVKLIDFG------C 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTS-----CGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQeaNDSEtltmIMDCKYTVPPRVSAGC 242
Cdd:cd14005   155 GALLKDSvytdfDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFE--NDEQ----ILRGNVLFRPRLSKEC 228
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 243 RDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14005   229 CDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
16-273 2.55e-56

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: 196.35  E-value: 2.55e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTklDTLA---TGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd05573     3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKS--DMLKreqIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLT 172
Cdd:cd05573    81 EYMPGGDLMNLLIKYDV-FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNIL-LDADGHIKLADFGLCTKMNKSGDRE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 ------------------------------TSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILF-MLVcGQPPFQEANDS 221
Cdd:cd05573   159 sylndsvntlfqdnvlarrrphkqrrvraySAVGTPDYIAPEVLRGTGYG-PECDWWSLGVILYeMLY-GFPPFYSDSLV 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 222 ETLTMIMDCK--YTVP--PRVSAGCRDLITRMLqRDPKRR-ASLEEIESHPWLQGVD 273
Cdd:cd05573   237 ETYSKIMNWKesLVFPddPDVSPEAIDLIRRLL-CDPEDRlGSAEEIKAHPFFKGID 292
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
16-283 3.98e-56

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: 193.62  E-value: 3.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLatghlfQEVRC-MKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPS------EEIEIlLRYGQHPNIITLRDVYDDGNSVYLVTEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL---VKLTDFGFSnkfqpgKKL 171
Cdd:cd14091    76 LRGGELLDRILRQKF-FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpesLRICDFGFA------KQL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 T-------TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEA-NDS--ETLTMIMDCKYTVP----PR 237
Cdd:cd14091   149 RaengllmTPCYTANFVAPEVLKKQGYDA-ACDIWSLGVLLYTMLAGYTPFASGpNDTpeVILARIGSGKIDLSggnwDH 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907195986 238 VSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGVDPSPATKYNIP 283
Cdd:cd14091   228 VSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDP 273
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
16-268 6.67e-56

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: 192.09  E-value: 6.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLATghlfqEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLkgkeDMIES-----EILIIKSLSHPNIVKLFEVYETEKEIYLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEGLNEDlAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF---FEKQGLVKLTDFGFSNKFQpg 168
Cdd:cd14185    77 LEYVRGGDLFDAIIESVKFTEHD-AALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnPDKSTTLKLADFGLAKYVT-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPF--QEANDSETLTMIMDCKYT-VPP---RVSAGC 242
Cdd:cd14185   154 GPIFTVCGTPTYVAPEILSEKGY-GLEVDMWAAGVILYILLCGFPPFrsPERDQEELFQIIQLGHYEfLPPywdNISEAA 232
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 243 RDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd14185   233 KDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
14-269 8.75e-56

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: 191.95  E-value: 8.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDK--TKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14070     2 GSYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKkkAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKFQP---G 168
Cdd:cd14070    82 MELCPGGNLMHRIYDKKR-LEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN-IKLIDFGLSNCAGIlgyS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQ-EANDSETL--TMIMDCKYTVPPRVSAGCRDL 245
Cdd:cd14070   160 DPFSTQCGSPAYAAPELLARKKY-GPKVDVWSIGVNMYAMLTGTLPFTvEPFSLRALhqKMVDKEMNPLPTDLSPGAISF 238
                         250       260
                  ....*....|....*....|....
gi 1907195986 246 ITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14070   239 LRSLLEPDPLKRPNIKQALANRWL 262
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-271 8.90e-56

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: 192.51  E-value: 8.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14166     1 IRETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSS--LENEIAVLKRIKHENIVTLEDIYESTTHYYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMkhEEGL-NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF--EKQGLVKLTDFGFSNKFQPG 168
Cdd:cd14166    79 MQLVSGGELFDRIL--ERGVyTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLtpDENSKIMITDFGLSKMEQNG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KkLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP----RVSAGCRD 244
Cdd:cd14166   157 I-MSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESpfwdDISESAKD 234
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPWLQG 271
Cdd:cd14166   235 FIRHLLEKNPSKRYTCEKALSHPWIIG 261
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
14-269 9.51e-56

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: 191.93  E-value: 9.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLDKTLGRGHFAVVKLARHV-----FTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTK 87
Cdd:cd14076     1 GPYILGRTLGEGEFGKVKLGWPLpkanhRSGVQVAIKLIRRDTQqENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVkLTDFGFSNKFQP 167
Cdd:cd14076    81 IGIVLEFVSGGELFDYILARRR-LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLV-ITDFGFANTFDH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 --GKKLTTSCGSLAYSAPEILLGDE-YDAPAVDIWSLGVILFMLVCGQPPFQE-------ANDSETLTMIMDCKYTVPPR 237
Cdd:cd14076   159 fnGDLMSTSCGSPCYAAPELVVSDSmYAGRKADIWSCGVILYAMLAGYLPFDDdphnpngDNVPRLYRYICNTPLIFPEY 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 238 VSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14076   239 VTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
11-269 1.61e-55

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: 191.55  E-value: 1.61e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  11 KIAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATG----HLFQEVRCMKLVQHPNIVRLYEVIDTQT 86
Cdd:cd14105     2 NVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRGvsreDIEREVSILRQVLHPNIITLHDVFENKT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 KLYLILELGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEK---QGLVKLTDFGFSN 163
Cdd:cd14105    82 DVVLILELVAGGELFDFLAE-KESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKnvpIPRIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV----S 239
Cdd:cd14105   161 KIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEA-DMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYfsntS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 240 AGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14105   240 ELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
16-269 2.23e-55

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: 190.55  E-value: 2.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGH-LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14116     7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHqLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSnKFQPGKKLTTS 174
Cdd:cd14116    87 APLGTVYRELQKLSK-FDEQRTATYITELANALSYCHSKRVIHRDIKPENLLL-GSAGELKIADFGWS-VHAPSSRRTTL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDP 254
Cdd:cd14116   164 CGTLDYLPPEMIEGRMHDE-KVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNP 242
                         250
                  ....*....|....*
gi 1907195986 255 KRRASLEEIESHPWL 269
Cdd:cd14116   243 SQRPMLREVLEHPWI 257
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
22-269 4.55e-55

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: 190.39  E-value: 4.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIdktKLDTLATGhlFQ-----EVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd07829     7 LGEGTYGVVYKAKDKKTGEIVALKKI---RLDNEEEG--IPstalrEISLLKELKHPNIVKLLDVIHTENKLYLVFEYCD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQ-PGKKLTTSC 175
Cdd:cd07829    82 Q-DLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQN-LLINRDGVLKLADFGLARAFGiPLRTYTHEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM------------------DCKYTVP-- 235
Cdd:cd07829   160 VTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFqilgtpteeswpgvtklpDYKPTFPkw 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907195986 236 ---------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07829   240 pkndlekvlPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
16-269 7.60e-55

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: 188.98  E-value: 7.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdktKLDTLATGHLFQEVRCMKLV----QHPNIVRLYEVIDTQ--TKLY 89
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI---KNDFRHPKAALREIKLLKHLndveGHPNIVKLLDVFEHRggNHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGdGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPgK 169
Cdd:cd05118    78 LVFELM-GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLKLADFGLARSFTS-P 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPprvsagCRDLITRM 249
Cdd:cd05118   156 PYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGTPE------ALDLLSKM 229
                         250       260
                  ....*....|....*....|
gi 1907195986 250 LQRDPKRRASLEEIESHPWL 269
Cdd:cd05118   230 LKYDPAKRITASQALAHPYF 249
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
16-273 1.04e-54

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: 189.92  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLA-TGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14209     3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKqVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQpgKKLTTS 174
Cdd:cd14209    83 VPGGEMFSHLRRIGR-FSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLL-IDQQGYIKVTDFGFAKRVK--GRTWTL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDP 254
Cdd:cd14209   159 CGTPEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 237
                         250       260
                  ....*....|....*....|....
gi 1907195986 255 KRR-----ASLEEIESHPWLQGVD 273
Cdd:cd14209   238 TKRfgnlkNGVNDIKNHKWFATTD 261
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
16-268 1.63e-54

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: 188.27  E-value: 1.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDK-TKLDTlatgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERgEKIDE----NVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG-LVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd14665    78 AAGGELFERICNAGR-FSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPApRLKICDFGYSKSSVLHSQPKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEAND----SETLTMIMDCKYTVPP--RVSAGCRDLIT 247
Cdd:cd14665   157 TVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEprnfRKTIQRILSVQYSIPDyvHISPECRHLIS 236
                         250       260
                  ....*....|....*....|.
gi 1907195986 248 RMLQRDPKRRASLEEIESHPW 268
Cdd:cd14665   237 RIFVADPATRITIPEIRNHEW 257
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
20-269 2.55e-54

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: 187.73  E-value: 2.55e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKFQ---PGKKLTTSCG 176
Cdd:cd06606    86 LAS-LLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSD-GVVKLADFGCAKRLAeiaTGEGTKSLRG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAvDIWSLG-VILFMLvCGQPPFQEANDSETLTM-IMDCKYT--VPPRVSAGCRDLITRMLQR 252
Cdd:cd06606   164 TPYWMAPEVIRGEGYGRAA-DIWSLGcTVIEMA-TGKPPWSELGNPVAALFkIGSSGEPppIPEHLSEEAKDFLRKCLQR 241
                         250
                  ....*....|....*..
gi 1907195986 253 DPKRRASLEEIESHPWL 269
Cdd:cd06606   242 DPKKRPTADELLQHPFL 258
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
20-273 3.31e-53

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: 186.84  E-value: 3.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEK---VAVKVIDKTKLDTLA--TGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05584     2 KVLGKGGYGKVFQVRKTTGSDKgkiFAMKVLKKASIVRNQkdTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFdyIMKHEEGL-NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLT 172
Cdd:cd05584    82 LSGGELF--MHLEREGIfMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILL-DAQGHVKLTDFGLCKEsIHDGTVTH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQR 252
Cdd:cd05584   159 TFCGTIEYMAPEILTRSGHGK-AVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKR 237
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 253 DPKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05584   238 NVSSRlgsgpGDAEEIKAHPFFRHIN 263
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
22-269 4.66e-53

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: 183.97  E-value: 4.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDRED--VRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG-LVKLTDFGFSNKFQPGKKLTTSCGSLAY 180
Cdd:cd14103    79 ERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGnQIKIIDFGLARKYDPDKKLKVLFGTPEF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILlgdEYDA--PAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY----TVPPRVSAGCRDLITRMLQRDP 254
Cdd:cd14103   159 VAPEVV---NYEPisYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWdfddEAFDDISDEAKDFISKLLVKDP 235
                         250
                  ....*....|....*
gi 1907195986 255 KRRASLEEIESHPWL 269
Cdd:cd14103   236 RKRMSAAQCLQHPWL 250
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
16-269 5.22e-53

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: 184.45  E-value: 5.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATG----HLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14194     7 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGvsreDIEREVSILKEIQHPNVITLHEVYENKTDVILI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEK---QGLVKLTDFGFSNKFQPG 168
Cdd:cd14194    87 LELVAGGELFDFLAE-KESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRnvpKPRIKIIDFGLAHKIDFG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEIL----LGDEydapaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP----PRVSA 240
Cdd:cd14194   166 NEFKNIFGTPEFVAPEIVnyepLGLE-----ADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEdeyfSNTSA 240
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 241 GCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14194   241 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-292 1.06e-52

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: 184.64  E-value: 1.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKT---KLDTLATGHLFQevrcmklVQHPNIVRLYEVIDTQTKL 88
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTvdkKIVRTEIGVLLR-------LSHPNIIKLKEIFETPTEI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFDYIMkhEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE--KQGLVKLTDFGFSNKF 165
Cdd:cd14085    74 SLVLELVTGGELFDRIV--EKGyYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpaPDAPLKIADFGLSKIV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGKKLTTSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPF-QEANDSETLTMIMDCKYT-VPP---RVSA 240
Cdd:cd14085   152 DQQVTMKTVCGTPGYCAPEILRGCAYG-PEVDMWSVGVITYILLCGFEPFyDERGDQYMFKRILNCDYDfVSPwwdDVSL 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 241 GCRDLITRMLQRDPKRRASLEEIESHPWLQGvdpsPATKYNIPLVSYKNLSE 292
Cdd:cd14085   231 NAKDLVKKLIVLDPKKRLTTQQALQHPWVTG----KAANFAHMDTAQKKLQE 278
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
22-268 1.47e-52

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: 183.33  E-value: 1.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKL--------------DTLATG-------HLFQEVRCMKLVQHPNIVRLYE 80
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLlkqagffrrppprrKPGALGkpldpldRVYREIAILKKLDHPNVVKLVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  81 VID--TQTKLYLILELGDGGDMFDYIMkhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTD 158
Cdd:cd14118    82 VLDdpNEDNLYMVFELVDKGAVMEVPT--DNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGD-DGHVKIAD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 159 FGFSNKFQPGK-KLTTSCGSLAYSAPEILLG--DEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP 235
Cdd:cd14118   159 FGVSNEFEGDDaLLSSTAGTPAFMAPEALSEsrKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFP 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907195986 236 --PRVSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd14118   239 ddPVVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
16-267 4.95e-52

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: 181.59  E-value: 4.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYE-VIDTQ-TKLYLILE 93
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDrIVDRAnTTLYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKH-EEG--LNEDLAKKYFAQIVHAISYCHKLH-----VVHRDLKPENVvFFEKQGLVKLTDFGFSNKF 165
Cdd:cd08217    82 YCEGGDLAQLIKKCkKENqyIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANI-FLDSDNNVKLGDFGLARVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGKKLTTSC-GSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYT-VPPRVSAGCR 243
Cdd:cd08217   161 SHDSSFAKTYvGTPYYMSPELLNEQSYD-EKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPrIPSRYSSELN 239
                         250       260
                  ....*....|....*....|....
gi 1907195986 244 DLITRMLQRDPKRRASLEEIESHP 267
Cdd:cd08217   240 EVIKSMLNVDPDKRPSVEELLQLP 263
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
16-268 7.62e-52

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: 181.00  E-value: 7.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKldTLATGHLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14184     3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAK--CCGKEHLIEnEVSILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNEDLAKKYFaQIVHAISYCHKLHVVHRDLKPENVVFFE---KQGLVKLTDFGFSNKFQpgKKL 171
Cdd:cd14184    81 VKGGDLFDAITSSTKYTERDASAMVY-NLASALKYLHGLCIVHRDIKPENLLVCEypdGTKSLKLGDFGLATVVE--GPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEAND--SETLTMIMDCKYTVPP----RVSAGCRDL 245
Cdd:cd14184   158 YTVCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRSENNlqEDLFDQILLGKLEFPSpywdNITDSAKEL 236
                         250       260
                  ....*....|....*....|...
gi 1907195986 246 ITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd14184   237 ISHMLQVNVEARYTAEQILSHPW 259
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
20-269 1.05e-51

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: 180.66  E-value: 1.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL--DTLAT----GHLFQEVRCMKLVQ---HPNIVRLYEVIDTQTKLYL 90
Cdd:cd14004     6 KEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERIlvDTWVRdrklGTVPLEIHILDTLNkrsHPNIVKLLDFFEDDEFYYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILEL-GDGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK 169
Cdd:cd14004    86 VMEKhGSGMDLFDFIERKP-NMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVIL-DGNGTIKLIDFGSAAYIKSGP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 kLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDsetltmIMDCKYTVPPRVSAGCRDLITRM 249
Cdd:cd14004   164 -FDTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYAVSEDLIDLISRM 236
                         250       260
                  ....*....|....*....|
gi 1907195986 250 LQRDPKRRASLEEIESHPWL 269
Cdd:cd14004   237 LNRDVGDRPTIEELLTDPWL 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
20-273 1.54e-51

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: 180.48  E-value: 1.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd06623     7 KVLGQGSSGVVYKVRHKPTGKIYALKKI-HVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDyIMKHEEGLNEDLAKKYFAQIVHAISYCH-KLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLT-TSCGS 177
Cdd:cd06623    86 LAD-LLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLL-INSKGEVKIADFGISKVLENTLDQCnTFVGT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMI----MDCKYTVPP-RVSAGCRDLITRMLQR 252
Cdd:cd06623   164 VTYMSPERIQGESYSYAA-DIWSLGLTLLECALGKFPFLPPGQPSFFELMqaicDGPPPSLPAeEFSPEFRDFISACLQK 242
                         250       260
                  ....*....|....*....|.
gi 1907195986 253 DPKRRASLEEIESHPWLQGVD 273
Cdd:cd06623   243 DPKKRPSAAELLQHPFIKKAD 263
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
12-269 7.26e-51

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: 178.70  E-value: 7.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKT-LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQ-HPNIVRLYEVIDTQTKLY 89
Cdd:cd14106     5 INEVYTVESTpLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELCKdCPRVVNLHEVYETRSELI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKFQP 167
Cdd:cd14106    85 LILELAAGGELQT-LLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFplGDIKLCDFGISRVIGE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTSCGSLAYSAPEILlgdEYDaP---AVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSA 240
Cdd:cd14106   164 GEEIREILGTPDYVAPEIL---SYE-PislATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEElfkdVSP 239
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 241 GCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14106   240 LAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
22-267 8.05e-51

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: 177.95  E-value: 8.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHV-FTGEKVAVKVIDKTKLDTLATgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDM 100
Cdd:cd14120     1 IGHGAFAVVFKGRHRkKPDLPVAIKCITKKNLSKSQN-LLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYImkHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG--------LVKLTDFGFSNKFQPGKKL 171
Cdd:cd14120    80 ADYL--QAKGtLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndiRLKIADFGFARFLQDGMMA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQeANDSETLTMIMDCKYTVPPRVSAGC----RDLIT 247
Cdd:cd14120   158 ATLCGSPMYMAPEVIMSLQYDAKA-DLWSIGTIVYQCLTGKAPFQ-AQTPQELKAFYEKNANLRPNIPSGTspalKDLLL 235
                         250       260
                  ....*....|....*....|
gi 1907195986 248 RMLQRDPKRRASLEEIESHP 267
Cdd:cd14120   236 GLLKRNPKDRIDFEDFFSHP 255
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
22-269 1.30e-50

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: 177.88  E-value: 1.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKV--AVKVIDKTKLDTLATGHlfqEVRCMK------LVQHPNIVRLYEV-IDTQTKLYLIL 92
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSGVlyAVKEYRRRDDESKRKDY---VKRLTSeyiissKLHHPNIVKVLDLcQDLHGKWCLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKF--QPGKK 170
Cdd:cd13994    78 EYCPGGDLFTLIEK-ADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILL-DEDGVLKLTDFGTAEVFgmPAEKE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTS---CGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSE------TLTMIMDCKYTVPPRVS-- 239
Cdd:cd13994   156 SPMSaglCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRSAKKSDsaykayEKSGDFTNGPYEPIENLlp 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 240 AGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd13994   236 SECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
16-269 6.54e-50

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: 175.49  E-value: 6.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd06627     2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHeEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTS- 174
Cdd:cd06627    82 ENGSLASIIKKF-GKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANIL-TTKDGLVKLADFGVATKLNEVEKDENSv 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYT-VPPRVSAGCRDLITRMLQRD 253
Cdd:cd06627   160 VGTPYWMAPEVIEMSGVTT-ASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPpLPENISPELRDFLLQCFQKD 238
                         250
                  ....*....|....*.
gi 1907195986 254 PKRRASLEEIESHPWL 269
Cdd:cd06627   239 PTLRPSAKELLKHPWL 254
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
20-273 9.71e-50

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: 177.51  E-value: 9.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQEVRC-MKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd05575     1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAiLKRNEVKHIMAERNVlLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLTTSCG 176
Cdd:cd05575    81 GELFFHLQR-ERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILL-DSQGHVVLTDFGLCKEgIEPSDTTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKR 256
Cdd:cd05575   159 TPEYLAPEVLRKQPYDR-TVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTK 237
                         250       260
                  ....*....|....*....|.
gi 1907195986 257 R----ASLEEIESHPWLQGVD 273
Cdd:cd05575   238 RlgsgNDFLEIKNHSFFRPIN 258
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
16-270 1.14e-49

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: 175.44  E-value: 1.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGH-LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14117     8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHqLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSnKFQPGKKLTTS 174
Cdd:cd14117    88 APRGELYKELQKHGR-FDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYK-GELKIADFGWS-VHAPSLRRRTM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDP 254
Cdd:cd14117   165 CGTLDYLPPEMIEGRTHDE-KVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHP 243
                         250
                  ....*....|....*.
gi 1907195986 255 KRRASLEEIESHPWLQ 270
Cdd:cd14117   244 SERLPLKGVMEHPWVK 259
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-271 2.22e-49

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: 175.62  E-value: 2.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGhLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14168     8 IKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNHLYLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMkhEEGL-NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKFQPG 168
Cdd:cd14168    87 MQLVSGGELFDRIV--EKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDeeSKIMISDFGLSKMEGKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP----RVSAGCRD 244
Cdd:cd14168   165 DVMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSpywdDISDSAKD 243
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPWLQG 271
Cdd:cd14168   244 FIRNLMEKDPNKRYTCEQALRHPWIAG 270
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
16-262 2.46e-49

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: 174.46  E-value: 2.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATG----HLF-QEVRCMKLV-QHPNIVRLYEVIDTQTKLY 89
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNdfqkLPQlREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEGLNED-LAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSnkfqpg 168
Cdd:cd13993    82 IVLEYCPNGDLFEAITENRIYVGKTeLIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGTVKLCDFGLA------ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 kklTTS-------CGSLAYSAPEIL-----LGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK----Y 232
Cdd:cd13993   156 ---TTEkismdfgVGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGIILLNLTFGRNPWKIASESDPIFYDYYLNspnlF 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 233 TVPPRVSAGCRDLITRMLQRDPKRRASLEE 262
Cdd:cd13993   233 DVILPMSDDFYNLLRQIFTVNPNNRILLPE 262
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
16-270 4.80e-49

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: 173.95  E-value: 4.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLfQEVR---------CMKLVQHPNIVRLYEVIDTQT 86
Cdd:cd14182     5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEEV-QELReatlkeidiLRKVSGHPNIIQLKDTYETNT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 KLYLILELGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKFQ 166
Cdd:cd14182    84 FFFLVFDLMKKGELFDYLTE-KVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN-IKLTDFGFSCQLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKKLTTSCGSLAYSAPEIL---LGDEYD--APAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM--DCKYTVPP--R 237
Cdd:cd14182   162 PGEKLREVCGTPGYLAPEIIecsMDDNHPgyGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMsgNYQFGSPEwdD 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907195986 238 VSAGCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14182   242 RSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
22-272 8.02e-49

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: 172.96  E-value: 8.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVF---TGEKVAVKVIDKTKLDTLA--TGHLFQEVRCMKLV-QHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd05583     2 LGTGAYGKVFLVRKVGghdAGKLYAMKVLKKATIVQKAktAEHTMTERQVLEAVrQSPFLVTLHYAFQTDAKLHLILDYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTS- 174
Cdd:cd05583    82 NGGELFTHLYQREH-FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENIL-LDSEGHVVLTDFGLSKEFLPGENDRAYs 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 -CGSLAYSAPEILLGDE--YDApAVDIWSLGVILFMLVCGQPPFQ---EAND-SETLTMIMDCKYTVPPRVSAGCRDLIT 247
Cdd:cd05583   160 fCGTIEYMAPEVVRGGSdgHDK-AVDWWSLGVLTYELLTGASPFTvdgERNSqSEISKRILKSHPPIPKTFSAEAKDFIL 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 248 RMLQRDPKRR-----ASLEEIESHPWLQGV 272
Cdd:cd05583   239 KLLEKDPKKRlgagpRGAHEIKEHPFFKGL 268
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
20-273 8.65e-49

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: 174.72  E-value: 8.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05599     7 KVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEmLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEFLPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSCGSL 178
Cdd:cd05599    87 DMMTLLMKKDT-LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLL-LDARGHIKLSDFGLCTGLKKSHLAYSTVGTP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYDApAVDIWSLGVILF-MLVcGQPPFQEANDSETLTMIMDCKYTV--PP--RVSAGCRDLITRMLQrD 253
Cdd:cd05599   165 DYIAPEVFLQKGYGK-ECDWWSLGVIMYeMLI-GYPPFCSDDPQETCRKIMNWRETLvfPPevPISPEAKDLIERLLC-D 241
                         250       260
                  ....*....|....*....|...
gi 1907195986 254 PKRRA---SLEEIESHPWLQGVD 273
Cdd:cd05599   242 AEHRLganGVEEIKSHPFFKGVD 264
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
16-270 1.39e-48

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: 172.49  E-value: 1.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATG----HLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGvsreEIEREVNILREIQHPNIITLHDIFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSNKFQPG 168
Cdd:cd14195    87 LELVSGGELFDFLAE-KESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnpRIKLIDFGIAHKIEAG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEIL----LGDEydapaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSA 240
Cdd:cd14195   166 NEFKNIFGTPEFVAPEIVnyepLGLE-----ADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEyfsnTSE 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 241 GCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14195   241 LAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
16-269 5.23e-48

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: 171.31  E-value: 5.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKT------------KLDTLATGHLFQEVRcmklvQHPNIVRLYEVID 83
Cdd:cd14181    12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTaerlspeqleevRSSTLKEIHILRQVS-----GHPSIITLIDSYE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  84 TQTKLYLILELGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSN 163
Cdd:cd14181    87 SSTFIFLVFDLMRRGELFDYLTE-KVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL-DDQLHIKLSDFGFSC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQPGKKLTTSCGSLAYSAPEILLG--DEYD---APAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTV-PPR 237
Cdd:cd14181   165 HLEPGEKLRELCGTPGYLAPEILKCsmDETHpgyGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFsSPE 244
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907195986 238 ---VSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14181   245 wddRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
22-263 6.29e-48

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: 169.64  E-value: 6.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVftGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFS-NKFQPGKKLTTSCGSLAY 180
Cdd:cd13999    79 DLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLN-ILLDENFTVKIADFGLSrIKNSTTEKMTGVVGTPRW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSEtLTMIMDCKYTVPPrVSAGC----RDLITRMLQRDPKR 256
Cdd:cd13999   158 MAPEVLRGEPYT-EKADVYSFGIVLWELLTGEVPFKELSPIQ-IAAAVVQKGLRPP-IPPDCppelSKLIKRCWNEDPEK 234

                  ....*..
gi 1907195986 257 RASLEEI 263
Cdd:cd13999   235 RPSFSEI 241
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
15-269 7.16e-48

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: 170.42  E-value: 7.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14097     2 IYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfeKQGLV--------KLTDFGFSNKFQ 166
Cdd:cd14097    82 CEDGEL-KELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILV--KSSIIdnndklniKVTDFGLSVQKY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKK--LTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMI----MDCKYTVPPRVSA 240
Cdd:cd14097   159 GLGEdmLQETCGTPIYMAPEVISAHGY-SQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIrkgdLTFTQSVWQSVSD 237
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 241 GCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14097   238 AAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
11-269 9.33e-48

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: 170.14  E-value: 9.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  11 KIAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDT----LATGHLFQEVRCMKLVQHPNIVRLYEVIDTQT 86
Cdd:cd14196     2 KVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgVSREEIEREVSILRQVLHPNIITLHDVYENRT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 KLYLILELGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSN 163
Cdd:cd14196    82 DVVLILELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpipHIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQPGKKLTTSCGSLAYSAPEIlLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VS 239
Cdd:cd14196   161 EIEDGVEFKNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEffshTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 240 AGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14196   240 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-270 1.10e-47

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: 171.38  E-value: 1.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLD---KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTkldtlATGHLFQEVRCMKLVQ-HPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14179     6 YELDlkdKPLGEGSFSICRKCLHKKTNQEYAVKIVSKR-----MEANTQREIAALKLCEgHPNIVKLHEVYHDQLHTFLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEK--QGLVKLTDFGFSNKFQPGK 169
Cdd:cd14179    81 MELLKGGELLERIKKKQH-FSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDEsdNSEIKIIDFGFARLKPPDN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 K-LTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD-----------CKYTVPPR 237
Cdd:cd14179   160 QpLKTPCFTLHYAAPELLNYNGYDE-SCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSAEEimkkikqgdfsFEGEAWKN 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907195986 238 VSAGCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14179   239 VSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQ 271
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
16-269 1.50e-47

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: 168.88  E-value: 1.50e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDT-LATGHLFQEVRCMKLVQHPNIVRLYEVID-TQTKLYLILE 93
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPdFVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGgDMFDYImkHEEGL-NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKL- 171
Cdd:cd14164    82 AAAT-DLLQKI--QEVHHiPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRKIKIADFGFARFVEDYPELs 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd14164   159 TTFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSGVALEEPCRALIRTLLQ 238
                         250
                  ....*....|....*...
gi 1907195986 252 RDPKRRASLEEIESHPWL 269
Cdd:cd14164   239 FNPSTRPSIQQVAGNSWL 256
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
16-269 2.26e-47

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: 168.87  E-value: 2.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKtklDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIET---KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEGLNEDlAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKL--TDFGFSN--KFQPGKKL 171
Cdd:cd14087    80 TGGELFDRIIAKGSFTERD-ATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKImiTDFGLAStrKKGPNCLM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSAGCRDLIT 247
Cdd:cd14087   159 KTTCGTPEYIAPEILLRKPY-TQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEpwpsVSNLAKDFID 237
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14087   238 RLLTVNPGERLSATQALKHPWI 259
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
16-273 2.76e-47

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 170.77  E-value: 2.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNeDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQpgKKLTTS 174
Cdd:PTZ00263  100 VVGGELFTHLRKAGRFPN-DVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL-DNKGHVKVTDFGFAKKVP--DRTFTL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDP 254
Cdd:PTZ00263  176 CGTPEYLAPEVIQSKGHGK-AVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDH 254
                         250       260
                  ....*....|....*....|....
gi 1907195986 255 -KRRASL----EEIESHPWLQGVD 273
Cdd:PTZ00263  255 tKRLGTLkggvADVKNHPYFHGAN 278
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
22-269 3.48e-47

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: 169.01  E-value: 3.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATG---HLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGg 98
Cdd:cd07835     7 IGEGTYGVVYKARDKLTGEIVALK---KIRLETEDEGvpsTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFLDL- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKH-EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ-PGKKLTTSCG 176
Cdd:cd07835    83 DLKKYMDSSpLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLL-IDTEGALKLADFGLARAFGvPVRTYTHEVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFqeANDSE---------TL-----------TMIMDCKYTVP- 235
Cdd:cd07835   162 TLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLF--PGDSEidqlfrifrTLgtpdedvwpgvTSLPDYKPTFPk 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907195986 236 ----------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07835   240 warqdlskvvPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-285 1.20e-46

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: 168.51  E-value: 1.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLD---KTLGRGHFAVVKLARHVFTGEKVAVKVIDKtKLDTLATghlfQEVRCMKLVQ-HPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14180     5 YELDleePALGEGSFSVCRKCRHRQSGQEYAVKIISR-RMEANTQ----REVAALRLCQsHPNIVALHEVLHDQYHTYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEK--QGLVKLTDFGFSNKF-QPG 168
Cdd:cd14180    80 MELLRGGELLDRIKKKAR-FSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADEsdGAVLKVIDFGFARLRpQGS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEAND-------SETLTMIMDCKYTVPPR---- 237
Cdd:cd14180   159 RPLQTPCFTLQYAAPELFSNQGYDE-SCDLWSLGVILYTMLSGQVPFQSKRGkmfhnhaADIMHKIKEGDFSLEGEawkg 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907195986 238 VSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGVDPSPATKYNIPLV 285
Cdd:cd14180   238 VSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTPLMTPDV 285
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
16-269 1.29e-46

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: 167.64  E-value: 1.29e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLD--KTLGRGHFAVVKLARHVFTGEKVAVKV-IDKTKLDTLATGHlfqeVRCmklVQHPNIVRLYEVI---------- 82
Cdd:cd14171     6 YEVNwtQKLGTGISGPVRVCVKKSTGERFALKIlLDRPKARTEVRLH----MMC---SGHPNIVQIYDVYansvqfpges 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  83 DTQTKLYLILELGDGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEK--QGLVKLTDFG 160
Cdd:cd14171    79 SPRARLLIVMELMEGGELFDRISQHR-HFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNseDAPIKLCDFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 FSnKFQPGkKLTTSCGSLAYSAPEILLGDE-----------------YDApAVDIWSLGVILFMLVCGQPPFQEANDSET 223
Cdd:cd14171   158 FA-KVDQG-DLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpytYDK-SCDMWSLGVIIYIMLCGYPPFYSEHPSRT 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907195986 224 LT-----MIMDCKYTVPPR----VSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14171   235 ITkdmkrKIMTGSYEFPEEewsqISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
16-269 1.91e-46

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: 165.89  E-value: 1.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTL-ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKdSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd05578    82 LLGGDL-RYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDE-QGHVHITDFNIATKLTDGTLATST 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFqEANDS----ETLTMIMDCKYTVPPRVSAGCRDLITRML 250
Cdd:cd05578   160 SGTKPYMAPEVFMRAGYSF-AVDWWSLGVTAYEMLRGKRPY-EIHSRtsieEIRAKFETASVLYPAGWSEEAIDLINKLL 237
                         250       260
                  ....*....|....*....|
gi 1907195986 251 QRDPKRRAS-LEEIESHPWL 269
Cdd:cd05578   238 ERDPQKRLGdLSDLKNHPYF 257
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
20-273 2.64e-46

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: 167.78  E-value: 2.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKtklDTLATghlFQEVRCM---KLV-----QHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd05570     1 KVLGKGSFGKVMLAERKKTDELYAIKVLKK---EVIIE---DDDVECTmteKRVlalanRHPFLTGLHACFQTEDRLYFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKK 170
Cdd:cd05570    75 MEYVNGGDLMFHIQR-ARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLL-DAEGHIKIADFGMCKEgIWGGNT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRML 250
Cdd:cd05570   153 TSTFCGTPDYIAPEILREQDYG-FSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLL 231
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 251 QRDPKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05570   232 TKDPARRlgcgpKGEADIKAHPFFRNID 259
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
12-269 3.44e-46

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: 165.55  E-value: 3.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDtlATGHLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYL 90
Cdd:cd14183     4 ISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCR--GKEHMIQnEVSILRRVKHPNIVLLIEEMDMPTELYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDYIMKHEEGLNEDlAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSNKFQp 167
Cdd:cd14183    82 VMELVKGGDLFDAITSTNKYTERD-ASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDgskSLKLGDFGLATVVD- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 gKKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQ-EANDSETL---TMIMDCKYTVP--PRVSAG 241
Cdd:cd14183   160 -GPLYTVCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRgSGDDQEVLfdqILMGQVDFPSPywDNVSDS 237
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 242 CRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14183   238 AKELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
16-281 3.84e-46

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: 166.36  E-value: 3.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLatghlfQEVRCM-KLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14175     3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPS------EEIEILlRYGQHPNIITLKDVYDDGKHVYLVTEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSNKFQPGKKL 171
Cdd:cd14175    77 MRGGELLDKILR-QKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGnpeSLRICDFGFAKQLRAENGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 -TTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQ---EANDSETLTMIMDCKYTVP----PRVSAGCR 243
Cdd:cd14175   156 lMTPCYTANFVAPEVLKRQGYDE-GCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSggnwNTVSDAAK 234
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907195986 244 DLITRMLQRDPKRRASLEEIESHPWLQGVDPSPATKYN 281
Cdd:cd14175   235 DLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPQSQLN 272
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
20-273 4.38e-46

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: 167.03  E-value: 4.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTL-ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05574     7 KLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRnKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDF------------------ 159
Cdd:cd05574    87 ELFRLLQKQPGKrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHE-SGHIMLTDFdlskqssvtpppvrkslr 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 160 --GFSNKFQPGKKLTTSCGSLA----------YSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMI 227
Cdd:cd05574   166 kgSRRSSVKSIEKETFVAEPSArsnsfvgteeYIAPEVIKGDGHGS-AVDWWTLGILLYEMLYGTTPFKGSNRDETFSNI 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 228 MDCKYTVP--PRVSAGCRDLITRMLQRDPKRR----ASLEEIESHPWLQGVD 273
Cdd:cd05574   245 LKKELTFPesPPVSSEAKDLIRKLLVKDPSKRlgskRGASEIKRHPFFRGVN 296
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
15-270 4.80e-46

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: 164.69  E-value: 4.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKtLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLAtghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd06614     2 YKNLEK-IGEGASGEVYKATDRATGKEVAIKKMRLRKQNKEL---IINEILIMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK-KLTT 173
Cdd:cd06614    78 MDGGSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILL-SKDGSVKLADFGFAAQLTKEKsKRNS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKytVPP-----RVSAGCRDLITR 248
Cdd:cd06614   157 VVGTPYWMAPEVIKRKDYG-PKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKG--IPPlknpeKWSPEFKDFLNK 233
                         250       260
                  ....*....|....*....|..
gi 1907195986 249 MLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd06614   234 CLVKDPEKRPSAEELLQHPFLK 255
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-273 8.96e-46

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: 166.63  E-value: 8.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVF---TGEKVAVKVIDKTKLDTLA--TGHLFQEVRCMKLV-QHPNIVRLYEVIDTQTKLY 89
Cdd:cd05614     2 FELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAALVQKAktVEHTRTERNVLEHVrQSPFLVTLHYAFQTDAKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK 169
Cdd:cd05614    82 LILDYVSGGELFTHLYQRDH-FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILL-DSEGHVVLTDFGLSKEFLTEE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTS--CGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPF----QEANDSETLTMIMDCKYTVPPRVSAGCR 243
Cdd:cd05614   160 KERTYsfCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVAR 239
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907195986 244 DLITRMLQRDPKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05614   240 DLLQKLLCKDPKKRlgagpQGAQEIKEHPFFKGLD 274
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
14-263 1.40e-45

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: 164.00  E-value: 1.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLD----KTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLY 89
Cdd:cd13996     2 SRYLNDfeeiELLGSGGFGSVYKVRNKVDGVTYAIKKI-RLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMK--HEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGF------ 161
Cdd:cd13996    81 IQMELCEGGTLRDWIDRrnSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVKIGDFGLatsign 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 ------SNKFQPGK---KLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCgqpPFQEAndSETLTMIMDC-K 231
Cdd:cd13996   161 qkrelnNLNNNNNGntsNNSVGIGTPLYASPEQLDGENYNEKA-DIYSLGIILFEMLH---PFKTA--MERSTILTDLrN 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907195986 232 YTVPPRVSAGC---RDLITRMLQRDPKRRASLEEI 263
Cdd:cd13996   235 GILPESFKAKHpkeADLIQSLLSKNPEERPSAEQL 269
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
20-273 1.95e-45

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: 163.42  E-value: 1.95e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTL--ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd05611     2 KPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKnqVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSCGS 177
Cdd:cd05611    82 GDC-ASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLL-IDQTGHLKLTDFGLSRNGLEKRHNKKFVGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGC----RDLITRMLQRD 253
Cdd:cd05611   160 PDYLAPETILGVGDDK-MSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCspeaVDLINRLLCMD 238
                         250       260
                  ....*....|....*....|...
gi 1907195986 254 PKRRAS---LEEIESHPWLQGVD 273
Cdd:cd05611   239 PAKRLGangYQEIKSHPFFKSIN 261
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
19-268 4.46e-45

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: 162.20  E-value: 4.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  19 DKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDgG 98
Cdd:cd14082     8 DEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLH-G 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL--VKLTDFGFSnKFQPGKKLTTS- 174
Cdd:cd14082    87 DMLEMILSSEKGrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFpqVKLCDFGFA-RIIGEKSFRRSv 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEanDSETLTMIMDCKYTVPP----RVSAGCRDLITRML 250
Cdd:cd14082   166 VGTPAYLAPEVLRNKGYNR-SLDMWSVGVIIYVSLSGTFPFNE--DEDINDQIQNAAFMYPPnpwkEISPDAIDLINNLL 242
                         250
                  ....*....|....*...
gi 1907195986 251 QRDPKRRASLEEIESHPW 268
Cdd:cd14082   243 QVKMRKRYSVDKSLSHPW 260
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
16-270 4.53e-45

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: 162.87  E-value: 4.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARH-VFTGEKVAVKVIDKTKLDTlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14201     8 YSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSK-SQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYiMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF----EKQGL----VKLTDFGFSNKFQ 166
Cdd:cd14201    87 CNGGDLADY-LQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrKKSSVsgirIKIADFGFARYLQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQeANDSETLTMIMD----CKYTVPPRVSAGC 242
Cdd:cd14201   166 SNMMAATLCGSPMYMAPEVIMSQHYDAKA-DLWSIGTVIYQCLVGKPPFQ-ANSPQDLRMFYEknknLQPSIPRETSPYL 243
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 243 RDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14201   244 ADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
16-285 7.56e-45

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: 162.88  E-value: 7.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlatghlFQEVRCM-KLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14178     5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDP------SEEIEILlRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSNKFQPGKK- 170
Cdd:cd14178    79 MRGGELLDRILR-QKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGnpeSIRICDFGFAKQLRAENGl 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEAND---SETLTMIMDCKYTVP----PRVSAGCR 243
Cdd:cd14178   158 LMTPCYTANFVAPEVLKRQGYDA-ACDIWSLGILLYTMLAGFTPFANGPDdtpEEILARIGSGKYALSggnwDSISDAAK 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907195986 244 DLITRMLQRDPKRRASLEEIESHPWL---QGVDPSPATKYNIPLV 285
Cdd:cd14178   237 DIVSKMLHVDPHQRLTAPQVLRHPWIvnrEYLSQNQLSRQDVHLV 281
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
16-269 7.89e-45

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: 161.27  E-value: 7.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14002     3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGgDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd14002    83 QG-ELFQ-ILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILI-GKGGVVKLCDFGFARAMSCNTLVLTSI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 -GSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIM--DCKYtvPPRVSAGCRDLITRMLQR 252
Cdd:cd14002   160 kGTPLYMAPELVQEQPYDHTA-DLWSLGCILYELFVGQPPFYTNSIYQLVQMIVkdPVKW--PSNMSPEFKSFLQGLLNK 236
                         250
                  ....*....|....*..
gi 1907195986 253 DPKRRASLEEIESHPWL 269
Cdd:cd14002   237 DPSKRLSWPDLLEHPFV 253
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
15-276 9.81e-45

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: 162.49  E-value: 9.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlatghlFQEVRC-MKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd14177     5 VYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDP------SEEIEIlMRYGQHPNIITLKDVYDDGRYVYLVTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSNKFQPGKK 170
Cdd:cd14177    79 LMKGGELLDRILR-QKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSAnadSIRICDFGFAKQLRGENG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 -LTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEA-NDS--ETLTMIMDCKYTVP----PRVSAGC 242
Cdd:cd14177   158 lLLTPCYTANFVAPEVLMRQGYDA-ACDIWSLGVLLYTMLAGYTPFANGpNDTpeEILLRIGSGKFSLSggnwDTVSDAA 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907195986 243 RDLITRMLQRDPKRRASLEEIESHPWLQGVDPSP 276
Cdd:cd14177   237 KDLLSHMLHVDPHQRYTAEQVLKHSWIACRDQLP 270
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
22-270 2.21e-44

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: 160.56  E-value: 2.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGE-KVAVKVIDKTKLDTLATgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDM 100
Cdd:cd14202    10 IGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQT-LLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYImkHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG--------LVKLTDFGFSNKFQPGKKL 171
Cdd:cd14202    89 ADYL--HTMRtLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGrksnpnniRIKIADFGFARYLQNNMMA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP--PR-VSAGCRDLITR 248
Cdd:cd14202   167 ATLCGSPMYMAPEVIMSQHYDAKA-DLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPniPReTSSHLRQLLLG 245
                         250       260
                  ....*....|....*....|..
gi 1907195986 249 MLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14202   246 LLQRNQKDRMDFDEFFHHPFLD 267
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
16-273 2.29e-44

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: 162.48  E-value: 2.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVR-CMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERdIMAKANSPWITKLQYAFQDSENLYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd05601    83 HPGGDLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENIL-IDRTGHIKLADFGSAAKLSSDKTVTSK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 --CGSLAYSAPEILLGDEYDA-----PAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTV----PPRVSAGCR 243
Cdd:cd05601   162 mpVGTPDYIAPEVLTSMNGGSkgtygVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLkfpeDPKVSESAV 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 244 DLITRMLQrDPKRRASLEEIESHPWLQGVD 273
Cdd:cd05601   242 DLIKGLLT-DAKERLGYEGLCCHPFFSGID 270
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
15-270 2.60e-44

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: 160.01  E-value: 2.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DTLATGHLF-QEVRCMKLV----QHPNIVRLYEVIDTQT 86
Cdd:cd14101     1 QYTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVqqwSKLPGVNPVpNEVALLQSVgggpGHRGVIRLLDWFEIPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 KLYLILELGD-GGDMFDYIMkhEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGfSNK 164
Cdd:cd14101    81 GFLLVLERPQhCQDLFDYIT--ERGaLDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGDIKLIDFG-SGA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 165 FQPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDsetltmIMDCKYTVPPRVSAGCRD 244
Cdd:cd14101   158 TLKDSMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFERDTD------ILKAKPSFNKRVSNDCRS 231
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14101   232 LIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
38-268 3.06e-44

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: 160.15  E-value: 3.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  38 TGEKVAVKVI-DKTKLDtlatghlfQEVRC-MKLVQHPNIVRL---YEVIDTQTKLYLI-LELGDGGDMFDYIMKHEEG- 110
Cdd:cd14089    25 TGEKFALKVLrDNPKAR--------REVELhWRASGCPHIVRIidvYENTYQGRKCLLVvMECMEGGELFSRIQERADSa 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 111 LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKFQPGKKLTTSCGSLAYSAPEILLG 188
Cdd:cd14089    97 FTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGpnAILKLTDFGFAKETTTKKSLQTPCYTPYYVAPEVLGP 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 189 DEYDApAVDIWSLGVILFMLVCGQPPFQEANDSE-TLTM---IMDCKYTVP----PRVSAGCRDLITRMLQRDPKRRASL 260
Cdd:cd14089   177 EKYDK-SCDMWSLGVIMYILLCGYPPFYSNHGLAiSPGMkkrIRNGQYEFPnpewSNVSEEAKDLIRGLLKTDPSERLTI 255

                  ....*...
gi 1907195986 261 EEIESHPW 268
Cdd:cd14089   256 EEVMNHPW 263
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
16-270 3.65e-44

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: 161.17  E-value: 3.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDT---LATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd14094     5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSspgLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDM-FDYIMKHEEGL--NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKFqP 167
Cdd:cd14094    85 EFMDGADLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsAPVKLGGFGVAIQL-G 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTS--CGSLAYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPFQeANDSETLTMIMDCKYTVPPR----VSAG 241
Cdd:cd14094   164 ESGLVAGgrVGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFY-GTKERLFEGIIKGKYKMNPRqwshISES 241
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 242 CRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14094   242 AKDLVRRMLMLDPAERITVYEALNHPWIK 270
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
16-269 5.27e-44

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: 160.01  E-value: 5.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRC-MKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKM-KKKFYSWEECMNLREVKSlRKLNEHPNIVKLKEVFRENDELYFVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGgDMFDYIMKHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd07830    80 MEG-NLYQLMKDRKGKpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV-SGPEVVKIADFGLAREIRSRPPYTD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGD-EYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM-------------------DCKYT 233
Cdd:cd07830   158 YVSTRWYRAPEILLRStSYSSP-VDIWALGCIMAELYTLRPLFPGSSEIDQLYKICsvlgtptkqdwpegyklasKLGFR 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907195986 234 VP-----------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07830   237 FPqfaptslhqliPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
15-268 6.39e-44

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: 159.89  E-value: 6.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDL-DKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKldTLATGHLFQEVRCMKLVQ-HPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd14090     2 LYKLtGELLGEGAYASVQTCINLYTGKEYAVKIIEKHP--GHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENV--VFFEKQGLVKLTDFGF-------SN 163
Cdd:cd14090    80 EKMRGGPLLSHIEKRVH-FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENIlcESMDKVSPVKICDFDLgsgiklsST 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQPGK--KLTTSCGSLAYSAPEI--LLGDE---YDApAVDIWSLGVILFMLVCGQPPFQEANDSET------------- 223
Cdd:cd14090   159 SMTPVTtpELLTPVGSAEYMAPEVvdAFVGEalsYDK-RCDLWSLGVILYIMLCGYPPFYGRCGEDCgwdrgeacqdcqe 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907195986 224 --LTMIMDCKYTVPPR----VSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd14090   238 llFHSIQEGEYEFPEKewshISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
16-273 2.49e-43

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: 158.37  E-value: 2.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTL-ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLkQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYiMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQpgKKLTTS 174
Cdd:cd05612    83 VPGGELFSY-LRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL-DKEGHIKLTDFGFAKKLR--DRTWTL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDP 254
Cdd:cd05612   159 CGTPEYLAPEVIQSKGHNK-AVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDR 237
                         250       260
                  ....*....|....*....|....
gi 1907195986 255 KRRA-----SLEEIESHPWLQGVD 273
Cdd:cd05612   238 TRRLgnmknGADDVKNHRWFKSVD 261
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
22-269 3.52e-43

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: 157.00  E-value: 3.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDK--TKLDTLAtghlFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd14190    12 LGGGKFGKVHTCTEKRTGLKLAAKVINKqnSKDKEMV----LLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG-LVKLTDFGFSNKFQPGKKLTTSCGSL 178
Cdd:cd14190    88 LFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGhQVKIIDFGLARRYNPREKLKVNFGTP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSAGCRDLITRMLQRDP 254
Cdd:cd14190   168 EFLSPEVVNYDQVSFP-TDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEEtfehVSDEAKDFVSNLIIKER 246
                         250
                  ....*....|....*
gi 1907195986 255 KRRASLEEIESHPWL 269
Cdd:cd14190   247 SARMSATQCLKHPWL 261
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
23-269 4.41e-43

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: 156.69  E-value: 4.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  23 GRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFD 102
Cdd:cd06626     9 GEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTLEE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 103 yIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKlTTSCGSL---- 178
Cdd:cd06626    89 -LLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPAN-IFLDSNGLIKLGDFGSAVKLKNNTT-TMAPGEVnslv 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 ---AYSAPEILLGDEYDAP--AVDIWSLG-VILFMlVCGQPPFQEAnDSETLTMI---MDCKYTVPPR--VSAGCRDLIT 247
Cdd:cd06626   166 gtpAYMAPEVITGNKGEGHgrAADIWSLGcVVLEM-ATGKRPWSEL-DNEWAIMYhvgMGHKPPIPDSlqLSPEGKDFLS 243
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06626   244 RCLESDPKKRPTASELLDHPFI 265
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
21-269 5.24e-43

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: 157.48  E-value: 5.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  21 TLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGgDM 100
Cdd:cd07833     8 VVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER-TL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ--PGKKLTTSCGSL 178
Cdd:cd07833    87 LELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENIL-VSESGVLKLCDFGFARALTarPASPLTDYVATR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR---------VSAGCR------ 243
Cdd:cd07833   166 WYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPLPPShqelfssnpRFAGVAfpepsq 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907195986 244 -----------------DLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07833   246 peslerrypgkvsspalDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
16-283 7.76e-43

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: 157.35  E-value: 7.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATGH------LFQEVRCMKLVQHPNIVRLYEVIDTQTKLY 89
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIK---KIKLGERKEAKdginftALREIKLLQELKHPNIIGLLDVFGHKSNIN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGgDMfdyimkheEGLNEDLA--------KKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGF 161
Cdd:cd07841    79 LVFEFMET-DL--------EKVIKDKSivltpadiKSYMLMTLRGLEYLHSNWILHRDLKPNNL-LIASDGVLKLADFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 SNKF-QPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD----------- 229
Cdd:cd07841   149 ARSFgSPNRKMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEalgtpteenwp 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195986 230 --------CKYT-VPPR--------VSAGCRDLITRMLQRDPKRRASLEEIESHPWLQgVDPSPATKYNIP 283
Cdd:cd07841   229 gvtslpdyVEFKpFPPTplkqifpaASDDALDLLQRLLTLNPNKRITARQALEHPYFS-NDPAPTPPSQLP 298
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
16-263 9.06e-43

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: 155.89  E-value: 9.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMmDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGD---MFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFG----FSNKfqp 167
Cdd:cd08224    82 ADAGDlsrLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPAN-VFITANGVVKLGDLGlgrfFSSK--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 gkklTTSCGSLA----YSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPF--QEANDSETLTMIMDCKYtvPP----R 237
Cdd:cd08224   158 ----TTAAHSLVgtpyYMSPERIREQGYDFKS-DIWSLGCLLYEMAALQSPFygEKMNLYSLCKKIEKCEY--PPlpadL 230
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 238 VSAGCRDLITRMLQRDPKRRASLEEI 263
Cdd:cd08224   231 YSQELRDLVAACIQPDPEKRPDISYV 256
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
16-281 1.27e-42

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: 157.87  E-value: 1.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLatghlfQEVRCM-KLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14176    21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEILlRYGQHPNIITLKDVYDDGKYVYVVTEL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSNKFQPGKK- 170
Cdd:cd14176    95 MKGGELLDKILR-QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpeSIRICDFGFAKQLRAENGl 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEAND---SETLTMIMDCKYTVP----PRVSAGCR 243
Cdd:cd14176   174 LMTPCYTANFVAPEVLERQGYDA-ACDIWSLGVLLYTMLTGYTPFANGPDdtpEEILARIGSGKFSLSggywNSVSDTAK 252
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907195986 244 DLITRMLQRDPKRRASLEEIESHPWLQGVDPSPATKYN 281
Cdd:cd14176   253 DLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLN 290
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
20-268 1.54e-42

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: 155.21  E-value: 1.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGH---LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd06625     6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEvkaLECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQP---GKKLTT 173
Cdd:cd06625    86 GGSVKDEIKAYGA-LTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL-RDSNGNVKLGDFGASKRLQTicsSTGMKS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAvDIWSLG-VILFMLVCgQPPFqeaNDSETLTMIM-----DCKYTVPPRVSAGCRDLIT 247
Cdd:cd06625   164 VTGTPYWMSPEVINGEGYGRKA-DIWSVGcTVVEMLTT-KPPW---AEFEPMAAIFkiatqPTNPQLPPHVSEDARDFLS 238
                         250       260
                  ....*....|....*....|.
gi 1907195986 248 RMLQRDPKRRASLEEIESHPW 268
Cdd:cd06625   239 LIFVRNKKQRPSAEELLSHSF 259
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
18-268 2.14e-42

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: 155.72  E-value: 2.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKtLGRGHFAVVKLARHVFTGEKVAVKVIdktKLD----TLATGhlFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd07836     5 LEK-LGEGTYATVYKGRNRTTGEIVALKEI---HLDaeegTPSTA--IREISLMKELKHENIVRLHDVIHTENKLMLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGgDMFDYIMKHEE--GLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQ-PGKK 170
Cdd:cd07836    79 YMDK-DLKKYMDTHGVrgALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLI-NKRGELKLADFGLARAFGiPVNT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC------------------KY 232
Cdd:cd07836   157 FSNEVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRImgtptestwpgisqlpeyKP 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907195986 233 TVP-----------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07836   237 TFPryppqdlqqlfPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
20-273 2.63e-42

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: 156.41  E-value: 2.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVF---TGEKVAVKVIDKTKL---DTLATGhlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITgpdAGTLYAMKVLKKATLkvrDRVRTK---MERDILADVNHPFIVKLHYAFQTEGKLYLILD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNK-FQPGKKLT 172
Cdd:cd05582    78 FLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE-DGHIKLTDFGLSKEsIDHEKKAY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQR 252
Cdd:cd05582   156 SFCGTVEYMAPEVVNRRGHTQSA-DWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKR 234
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 253 DPKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05582   235 NPANRlgagpDGVEEIKRHPFFATID 260
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
22-268 2.86e-42

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: 155.35  E-value: 2.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATG---HLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGg 98
Cdd:cd07860     8 IGEGTYGVVYKARNKLTGEVVALK---KIRLDTETEGvpsTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQ- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYI-MKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ-PGKKLTTSCG 176
Cdd:cd07860    84 DLKKFMdASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLL-INTEGAIKLADFGLARAFGvPVRTYTHEVV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFqeANDSE---------TL-----------TMIMDCKYTVP- 235
Cdd:cd07860   163 TLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALF--PGDSEidqlfrifrTLgtpdevvwpgvTSMPDYKPSFPk 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907195986 236 ----------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07860   241 warqdfskvvPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
16-270 4.75e-42

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: 154.74  E-value: 4.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---------------DTLATG---------HLFQEVRCMKLVQ 71
Cdd:cd14199     4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLmrqagfprrppprgaRAAPEGctqprgpieRVYQEIAILKKLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  72 HPNIVRLYEVID--TQTKLYLILELGDGGDMFDyiMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE 149
Cdd:cd14199    84 HPNVVKLVEVLDdpSEDHLYMVFELVKQGPVME--VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 150 kQGLVKLTDFGFSNKFQPGKK-LTTSCGSLAYSAPEILLGDE--YDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTM 226
Cdd:cd14199   162 -DGHIKIADFGVSNEFEGSDAlLTNTVGTPAFMAPETLSETRkiFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907195986 227 IMDCKYTVP--PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14199   241 IKTQPLEFPdqPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
19-269 7.53e-42

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: 153.15  E-value: 7.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  19 DKTLGRGHFAVVKLARHVFTGEKVAVKVIDktkldtlATGH-----LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd14193     9 EEILGGGRFGQVHKCEEKSSGLKLAAKIIK-------ARSQkekeeVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG-LVKLTDFGFSNKFQPGKKLT 172
Cdd:cd14193    82 YVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAnQVKIIDFGLARRYKPREKLR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSAGCRDLITR 248
Cdd:cd14193   162 VNFGTPEFLAPEVVNYEFVSFPT-DMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEefadISEEAKDFISK 240
                         250       260
                  ....*....|....*....|.
gi 1907195986 249 MLQRDPKRRASLEEIESHPWL 269
Cdd:cd14193   241 LLIKEKSWRMSASEALKHPWL 261
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
16-269 8.80e-42

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: 153.09  E-value: 8.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLA-TGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGmVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKFQ-PGKKLTT 173
Cdd:cd14186    83 CHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN-IKIADFGLATQLKmPHEKHFT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd14186   162 MCGTPNYISPEIATRSAHGLES-DVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKN 240
                         250
                  ....*....|....*.
gi 1907195986 254 PKRRASLEEIESHPWL 269
Cdd:cd14186   241 PADRLSLSSVLDHPFM 256
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
15-268 1.18e-41

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: 152.83  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDldkTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDtlatgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14010     4 LYD---EIGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRP-----EVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ-------- 166
Cdd:cd14010    76 CTGGDLET-LLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNIL-LDGNGTLKLSDFGLARREGeilkelfg 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 ---------PGKKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMdCKYTVPPR 237
Cdd:cd14010   154 qfsdegnvnKVSKKQAKRGTPYYMAPELFQGGVH-SFASDLWALGCVLYEMFTGKPPFVAESFTELVEKIL-NEDPPPPP 231
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907195986 238 VSAGCR------DLITRMLQRDPKRRASLEEIESHP-W 268
Cdd:cd14010   232 PKVSSKpspdfkSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
20-266 1.27e-41

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: 154.74  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDK-TKLDTLATGHLFQEVRCM-KLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKkTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNK-FQPGKKLTTSCG 176
Cdd:cd05603    81 GELF-FHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENIL-LDCQGHVVLTDFGLCKEgMEPEETTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP-RVSAGCrDLITRMLQRDPK 255
Cdd:cd05603   159 TPEYLAPEVLRKEPYDR-TVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGgKTVAAC-DLLQGLLHKDQR 236
                         250
                  ....*....|....*
gi 1907195986 256 RR----ASLEEIESH 266
Cdd:cd05603   237 RRlgakADFLEIKNH 251
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
16-269 1.77e-41

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: 153.18  E-value: 1.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL--------------DTLATG----------HLFQEVRCMKLVQ 71
Cdd:cd14200     2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrppprgSKAAQGeqakplapleRVYQEIAILKKLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  72 HPNIVRLYEVID--TQTKLYLILELGDGGDMFDyiMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE 149
Cdd:cd14200    82 HVNIVKLIEVLDdpAEDNLYMVFDLLRKGPVME--VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 150 kQGLVKLTDFGFSNKFQPGK-KLTTSCGSLAYSAPEILL--GDEYDAPAVDIWSLGVILFMLVCGQPPFQeanDSETLTM 226
Cdd:cd14200   160 -DGHVKIADFGVSNQFEGNDaLLSSTAGTPAFMAPETLSdsGQSFSGKALDVWAMGVTLYCFVYGKCPFI---DEFILAL 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907195986 227 IMDCKYTV-----PPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14200   236 HNKIKNKPvefpeEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
16-269 2.31e-41

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: 152.37  E-value: 2.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLarhVFTGEK--VAVKVIDKTKLDTLATGHLFQEVRCMKLVQH-PNIVRL--YEVIDTQTKLYL 90
Cdd:cd14131     3 YEILKQLGKGGSSKVYK---VLNPKKkiYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIQLydYEVTDEDDYLYM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGgDMFDYIMKHEE-GLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkqGLVKLTDFGFSNKFQPGk 169
Cdd:cd14131    80 VMECGEI-DLATILKKKRPkPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK--GRLKLIDFGIAKAIQND- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 klTTS------CGSLAYSAPEILLGDEYDA---------PAVDIWSLGVILFMLVCGQPPFQE-ANDSETLTMIMDCKYT 233
Cdd:cd14131   156 --TTSivrdsqVGTLNYMSPEAIKDTSASGegkpkskigRPSDVWSLGCILYQMVYGKTPFQHiTNPIAKLQAIIDPNHE 233
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907195986 234 VP-PRVS-AGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14131   234 IEfPDIPnPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
16-266 2.74e-41

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: 154.02  E-value: 2.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQEVRCM-KLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd05602     9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAiLKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLYFVLD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLT 172
Cdd:cd05602    89 YINGGELF-YHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILL-DSQGHIVLTDFGLCKEnIEPNGTTS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQR 252
Cdd:cd05602   167 TFCGTPEYLAPEVLHKQPYDR-TVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQK 245
                         250
                  ....*....|....*...
gi 1907195986 253 DPKRRASLE----EIESH 266
Cdd:cd05602   246 DRTKRLGAKddftEIKNH 263
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
15-269 9.89e-41

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: 150.46  E-value: 9.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLD-KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQ-HPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd14198     8 FYILTsKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKsNPRVVNLHEVYETTSEIILIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF--FEKQGLVKLTDFGFSNKFQPGK 169
Cdd:cd14198    88 EYAAGGEIFNLCVPDLaEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLssIYPLGDIKIVDFGMSRKIGHAC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILlgdEYD--APAVDIWSLGVILFMLVCGQPPFQEANDSETLTMI----MDCKYTVPPRVSAGCR 243
Cdd:cd14198   168 ELREIMGTPEYLAPEIL---NYDpiTTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNIsqvnVDYSEETFSSVSQLAT 244
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 244 DLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14198   245 DFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
20-273 1.25e-40

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: 151.70  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DTLAtgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05595     1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIiakDEVA--HTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYAN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLTTSC 175
Cdd:cd05595    79 GGELF-FHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML-DKDGHIKITDFGLCKEgITDGATMKTFC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd05595   157 GTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPK 235
                         250       260
                  ....*....|....*....|...
gi 1907195986 256 RR-----ASLEEIESHPWLQGVD 273
Cdd:cd05595   236 QRlgggpSDAKEVMEHRFFLSIN 258
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
16-267 1.67e-40

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: 149.50  E-value: 1.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKH-EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd08220    82 PGGTLFEYIQQRkGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVKIGDFGISKILSSKSKAYTV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYT-VPPRVSAGCRDLITRMLQRD 253
Cdd:cd08220   162 VGTPCYISPELCEGKPYNQKS-DIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHLILSMLHLD 240
                         250
                  ....*....|....
gi 1907195986 254 PKRRASLEEIESHP 267
Cdd:cd08220   241 PNKRPTLSEIMAQP 254
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
20-273 2.10e-40

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: 150.97  E-value: 2.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DTLAtgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05571     1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIiakDEVA--HTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLTTSC 175
Cdd:cd05571    79 GGELF-FHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL-DKDGHIKITDFGLCKEeISYGATTKTFC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd05571   157 GTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPK 235
                         250       260
                  ....*....|....*....|...
gi 1907195986 256 RR-----ASLEEIESHPWLQGVD 273
Cdd:cd05571   236 KRlgggpRDAKEIMEHPFFASIN 258
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
16-293 2.97e-40

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: 150.75  E-value: 2.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVI-----DTQTKLYL 90
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILrppspEEFNDVYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGgDMfDYIMKHEEGLNEDlAKKYF-AQIVHAISYCHKLHVVHRDLKPENVvffekqgLV------KLTDFGFSN 163
Cdd:cd07834    82 VTELMET-DL-HKVIKSPQPLTDD-HIQYFlYQILRGLKYLHSAGVIHRDLKPSNI-------LVnsncdlKICDFGLAR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQPGKKLTTSCGSLA---YSAPEILLG-DEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC--------- 230
Cdd:cd07834   152 GVDPDEDKGFLTEYVVtrwYRAPELLLSsKKYT-KAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVlgtpseedl 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 231 ---------KY-------------TVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGV-DPSPATKYNIPLVSY 287
Cdd:cd07834   231 kfissekarNYlkslpkkpkkplsEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLhDPEDEPVAKPPFDFP 310

                  ....*.
gi 1907195986 288 KNLSEE 293
Cdd:cd07834   311 FFDDEE 316
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-273 3.77e-40

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: 149.38  E-value: 3.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVF---TGEKVAVKVIDKTKLDTLA--TGHLFQEVRCMKLV-QHPNIVRLYEVIDTQTKLY 89
Cdd:cd05613     2 FELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKATIVQKAktAEHTRTERQVLEHIrQSPFLVTLHYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKF--QP 167
Cdd:cd05613    82 LILDYINGGELFTHLSQRER-FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENIL-LDSSGHVVLTDFGLSKEFllDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTSCGSLAYSAPEILL-GDEYDAPAVDIWSLGVILFMLVCGQPPF----QEANDSETLTMIMDCKYTVPPRVSAGC 242
Cdd:cd05613   160 NERAYSFCGTIEYMAPEIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALA 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907195986 243 RDLITRMLQRDPKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05613   240 KDIIQRLLMKDPKKRlgcgpNGADEIKKHPFFQKIN 275
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
15-270 1.02e-39

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: 148.25  E-value: 1.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDL-DKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTkldtlaTGH----LFQEVRCMKLVQ-HPNIVRLYEVIDTQTKL 88
Cdd:cd14174     2 LYRLtDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKN------AGHsrsrVFREVETLYQCQgNKNILELIEFFEDDTRF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVV--FFEKQGLVKLTDFGFSNKFQ 166
Cdd:cd14174    76 YLVFEKLRGGSILAHIQKRKH-FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILceSPDKVSPVKICDFDLGSGVK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGK--------KLTTSCGSLAYSAPEIL--LGDE---YDApAVDIWSLGVILFMLVCGQPPFQ---------------EA 218
Cdd:cd14174   155 LNSactpittpELTTPCGSAEYMAPEVVevFTDEatfYDK-RCDLWSLGVILYIMLSGYPPFVghcgtdcgwdrgevcRV 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 219 NDSETLTMIMDCKYTVPPR----VSAGCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14174   234 CQNKLFESIQEGKYEFPDKdwshISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
20-283 1.40e-39

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: 148.96  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDK-TKLDTLATGHLFQEVRCM-KLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd05604     2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKkVILNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVNG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNK-FQPGKKLTTSCG 176
Cdd:cd05604    82 GELFFHLQR-ERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENIL-LDSQGHIVLTDFGLCKEgISNSDTTTTFCG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKR 256
Cdd:cd05604   160 TPEYLAPEVIRKQPYDN-TVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQL 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907195986 257 R----ASLEEIESHPWLQGVDPSPATKYNIP 283
Cdd:cd05604   239 RlgakEDFLEIKNHPFFESINWTDLVQKKIP 269
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
22-269 1.41e-39

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: 147.04  E-value: 1.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHlfqEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd14113    15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTH---ELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEK--QGLVKLTDFGFSNKFQPGKKLTTSCGSLA 179
Cdd:cd14113    92 DYVVRWGN-LTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSlsKPTIKLADFGDAVQLNTTYYIHQLLGSPE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 180 YSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSAGCRDLITRMLQRDPK 255
Cdd:cd14113   171 FAAPEIILGNPVSLTS-DLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDyfkgVSQKAKDFVCFLLQMDPA 249
                         250
                  ....*....|....
gi 1907195986 256 RRASLEEIESHPWL 269
Cdd:cd14113   250 KRPSAALCLQEQWL 263
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
20-267 1.64e-39

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: 146.38  E-value: 1.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVID------KTKLDTLatghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd08530     6 KKLGKGSYGSVYKVKRLSDNQVYALKEVNlgslsqKEREDSV------NEIRLLASVNHPNIIRYKEAFLDGNRLCIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEG---LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSnKFQPGKK 170
Cdd:cd08530    80 YAPFGDLSKLISKRKKKrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSAN-ILLSAGDLVKIGDLGIS-KVLKKNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFqEANDSETLTM-IMDCKYT-VPPRVSAGCRDLITR 248
Cdd:cd08530   158 AKTQIGTPLYAAPEVWKGRPYDYKS-DIWSLGCLLYEMATFRPPF-EARTMQELRYkVCRGKFPpIPPVYSQDLQQIIRS 235
                         250
                  ....*....|....*....
gi 1907195986 249 MLQRDPKRRASLEEIESHP 267
Cdd:cd08530   236 LLQVNPKKRPSCDKLLQSP 254
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
20-269 2.48e-39

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: 146.26  E-value: 2.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKlDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKII-KVK-GAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG-LVKLTDFGFSNKFQPGKKLTTSCGSL 178
Cdd:cd14192    88 LFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGnQIKIIDFGLARRYKPREKLKVNFGTP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP----RVSAGCRDLITRMLQRDP 254
Cdd:cd14192   168 EFLAPEVVNYDFVSFP-TDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAeafeNLSEEAKDFISRLLVKEK 246
                         250
                  ....*....|....*
gi 1907195986 255 KRRASLEEIESHPWL 269
Cdd:cd14192   247 SCRMSATQCLKHEWL 261
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
16-269 2.57e-39

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: 146.19  E-value: 2.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKldTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPH--ESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL-VKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd14114    82 SGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNeVKLIDFGLATHLDPKESVKVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDeydaPA---VDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP----PRVSAGCRDLIT 247
Cdd:cd14114   162 TGTAEFAAPEIVERE----PVgfyTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDdsafSGISEEAKDFIR 237
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14114   238 KLLLADPNKRMTIHQALEHPWL 259
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
22-269 2.88e-39

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: 146.71  E-value: 2.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVK-VIDKTKLDTLATGHLfQEVRCMKLVQ-HPNIVRLYEVIDTQTKLYLILELGDGgD 99
Cdd:cd07832     8 IGEGAHGIVFKAKDRETGETVALKkVALRKLEGGIPNQAL-REIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYMLS-S 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKF--QPGKKLTTSCGS 177
Cdd:cd07832    86 LSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISST-GVLKIADFGLARLFseEDPRLYSHQVAT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLG-DEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC-------------------KYTVP-- 235
Cdd:cd07832   165 RWYRAPELLYGsRKYD-EGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTlgtpnektwpeltslpdynKITFPes 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907195986 236 ---------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07832   244 kgirleeifPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
22-268 3.94e-39

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: 145.10  E-value: 3.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKT--KLDTLAtghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKmkKKEQAA-----HEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNEDLAkKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL--VKLTDFGFSNKFQPGKKLTTSCGS 177
Cdd:cd14115    76 LLDYLMNHDELMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDLEDAVQISGHRHVHHLLGN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSAGCRDLITRMLQRD 253
Cdd:cd14115   155 PEFAAPEVIQGTPVSL-ATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEyfgdVSQAARDFINVILQED 233
                         250
                  ....*....|....*
gi 1907195986 254 PKRRASLEEIESHPW 268
Cdd:cd14115   234 PRRRPTAATCLQHPW 248
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
22-268 5.69e-39

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: 145.16  E-value: 5.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDK--TKLdtlaTGHLFQEVRCMKLVQHPNIVRLYEV-IDTQTKLYLILELGDGG 98
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKpsTKL----KDFLREYNISLELSVHPHIIKTYDVaFETEDYYVFAQEYAPYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ-GLVKLTDFGFSNKfqPGKKLTTSCGS 177
Cdd:cd13987    77 DLFS-IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcRRVKLCDFGLTRR--VGSTVKRVSGT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDA----PAVDIWSLGVILFMLVCGQPPFQEAndsetltMIMDCKY-----------TVPP----RV 238
Cdd:cd13987   154 IPYTAPEVCEAKKNEGfvvdPSIDVWAFGVLLFCCLTGNFPWEKA-------DSDDQFYeefvrwqkrknTAVPsqwrRF 226
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907195986 239 SAGCRDLITRMLQRDPKRRASLEEIES---HPW 268
Cdd:cd13987   227 TPKALRMFKKLLAPEPERRCSIKEVFKylgDRW 259
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
20-269 6.45e-39

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: 145.46  E-value: 6.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQ-HPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd14197    15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDY-IMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd14197    95 EIFNQcVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplGDIKIVDFGLSRILKNSEELREIM 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILlgdEYD--APAVDIWSLGVILFMLVCGQPPFQEANDSETLTMI--MDCKYTVP--PRVSAGCRDLITRM 249
Cdd:cd14197   175 GTPEYVAPEIL---SYEpiSTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNIsqMNVSYSEEefEHLSESAIDFIKTL 251
                         250       260
                  ....*....|....*....|
gi 1907195986 250 LQRDPKRRASLEEIESHPWL 269
Cdd:cd14197   252 LIKKPENRATAEDCLKHPWL 271
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
18-263 7.95e-39

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 144.60  E-value: 7.95e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   18 LDKTLGRGHFAVVKLAR----HVFTGEKVAVKVIDKTKlDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   94 LGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSnKFQPGKKLTT 173
Cdd:smart00219  82 YMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCL-VGENLVVKISDFGLS-RDLYDDDYYR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  174 SCGS---LAYSAPEILLGDEYDaPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKY-TVPPRVSAGCRDLITR 248
Cdd:smart00219 160 KRGGklpIRWMAPESLKEGKFT-SKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEYLKNGYRlPQPPNCPPELYDLMLQ 238
                          250
                   ....*....|....*
gi 1907195986  249 MLQRDPKRRASLEEI 263
Cdd:smart00219 239 CWAEDPEDRPTFSEL 253
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
20-273 1.20e-38

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: 146.31  E-value: 1.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKtkLDTL---ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05598     7 KTIGVGAFGEVSLVRKKDTNALYAMKTLRK--KDVLkrnQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVMDYIP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ--PGKKLTTS 174
Cdd:cd05598    85 GGDLMSLLIK-KGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNIL-IDRDGHIKLTDFGLCTGFRwtHDSKYYLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 C---GSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYT--VPP--RVSAGCRDLIT 247
Cdd:cd05598   163 HslvGTPNYIAPEVLLRTGYTQ-LCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTlkIPHeaNLSPEAKDLIL 241
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 248 RMLQRDPKR--RASLEEIESHPWLQGVD 273
Cdd:cd05598   242 RLCCDAEDRlgRNGADEIKAHPFFAGID 269
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
16-269 1.35e-38

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: 144.73  E-value: 1.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVI------DKTKLDTLatghlfQEVRCMKLVQ---HPNIVRLYEV----- 81
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVrvplseEGIPLSTI------REIALLKQLEsfeHPNVVRLLDVchgpr 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  82 IDTQTKLYLILELGDGgDMFDYIMKH-EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFG 160
Cdd:cd07838    75 TDRELKLTLVFEHVDQ-DLATYLDKCpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILV-TSDGQVKLADFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 FSNKFQPGKKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD----------- 229
Cdd:cd07838   153 LARIYSFEMALTSVVVTLWYRAPEVLLQSSY-ATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDviglpseeewp 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 230 ----------CKYTVP------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07838   232 rnsalprssfPSYTPRpfksfvPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
16-268 2.19e-38

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: 144.34  E-value: 2.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMK-LVQHPNIVRLYEVI-DTQT-KLYLIL 92
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCM-KKHFKSLEQVNNLREIQALRrLSPHPNILRLIEVLfDRKTgRLALVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfeKQGLVKLTDFGfsnkfqpgkklt 172
Cdd:cd07831    80 ELMDM-NLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI--KDDILKLADFG------------ 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 tSCGSLA-------------YSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD---------- 229
Cdd:cd07831   145 -SCRGIYskppyteyistrwYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDvlgtpdaevl 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 230 --------CKYTVPPR-----------VSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07831   224 kkfrksrhMNYNFPSKkgtglrkllpnASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
16-267 2.33e-38

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: 143.65  E-value: 2.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd06610     3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQT-SMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDyIMKH---EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFS-NKFQPG--- 168
Cdd:cd06610    82 SGGSLLD-IMKSsypRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGE-DGSVKIADFGVSaSLATGGdrt 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 -KKLTTSCGSLAYSAPEILLGDE-YDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDckyTVPPRV-------- 238
Cdd:cd06610   160 rKVRKTFVGTPCWMAPEVMEQVRgYDFKA-DIWSFGITAIELATGAAPYSKYPPMKVLMLTLQ---NDPPSLetgadykk 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 239 -SAGCRDLITRMLQRDPKRRASLEEIESHP 267
Cdd:cd06610   236 ySKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
15-269 2.36e-38

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: 143.22  E-value: 2.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdkTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14191     3 FYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL-VKLTDFGFSNKFQPGKKLTT 173
Cdd:cd14191    81 VSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTkIKLIDFGLARRLENAGSLKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILlgdEYDAP--AVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP----PRVSAGCRDLIT 247
Cdd:cd14191   161 LFGTPEFVAPEVI---NYEPIgyATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFIS 237
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14191   238 NLLKKDMKARLTCTQCLQHPWL 259
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
17-270 2.73e-38

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: 143.25  E-value: 2.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  17 DLD--KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTkLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd06605     2 DLEylGELGEGNGGVVSKVRHRPSGQIMAVKVIRLE-IDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDmFDYIMKHEEGLNEDLAKKYFAQIVHAISYCH-KLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLTt 173
Cdd:cd06605    81 MDGGS-LDKILKEVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILV-NSRGQVKLCDFGVSGQLVDSLAKT- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTV---PPRVSAGC-----RDL 245
Cdd:cd06605   158 FVGTRSYMAPERISGGKYTVKS-DIWSLGLSLVELATGRFPYPPPNAKPSMMIFELLSYIVdepPPLLPSGKfspdfQDF 236
                         250       260
                  ....*....|....*....|....*
gi 1907195986 246 ITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd06605   237 VSQCLQKDPTERPSYKELMEHPFIK 261
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
16-273 4.26e-38

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: 144.80  E-value: 4.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHF---AVVKLARhvfTGEKVAVKVIDKTKLDTLATGHLFQEVRCMkLVQ--HPNIVRLYEVIDTQTKLYL 90
Cdd:cd05597     3 FEILKVIGRGAFgevAVVKLKS---TEKVYAMKILNKWEMLKRAETACFREERDV-LVNgdRRWITKLHYAFQDENYLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKK 170
Cdd:cd05597    79 VMDYYCGGDLLTLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVL-LDRNGHIRLADFGSCLKLREDGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 L--TTSCGSLAYSAPEILLGDE-----YdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK--YTVP---PRV 238
Cdd:cd05597   158 VqsSVAVGTPDYISPEILQAMEdgkgrY-GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKehFSFPddeDDV 236
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907195986 239 SAGCRDLITRMLQRDPKR--RASLEEIESHPWLQGVD 273
Cdd:cd05597   237 SEEAKDLIRRLICSRERRlgQNGIDDFKKHPFFEGID 273
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
22-273 4.34e-38

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: 143.05  E-value: 4.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-----DTLAtghlFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIkkkkgETMA----LNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKH-EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd05577    77 GGDLKYHIYNVgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILL-DDHGHVRISDLGLAVEFKGGKKIKGRV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDE-YDAPaVDIWSLGVILFMLVCGQPPFQ------EANDSETLTMIMDCKYtvPPRVSAGCRDLITR 248
Cdd:cd05577   156 GTHGYMAPEVLQKEVaYDFS-VDWFALGCMLYEMIAGRSPFRqrkekvDKEELKRRTLEMAVEY--PDSFSPEARSLCEG 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 249 MLQRDPKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05577   233 LLQKDPERRlgcrgGSADEVKEHPFFRSLN 262
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
16-273 4.56e-38

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: 143.32  E-value: 4.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLdTL--ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNL-ILrnQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSnkfQPG-KKLT 172
Cdd:cd05609    81 YVEGGDCAT-LLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLL-ITSMGHIKLTDFGLS---KIGlMSLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TS------------------CGSLAYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTV 234
Cdd:cd05609   156 TNlyeghiekdtrefldkqvCGTPEYIAPEVILRQGYGKP-VDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEW 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907195986 235 PPR---VSAGCRDLITRMLQRDPKRR---ASLEEIESHPWLQGVD 273
Cdd:cd05609   235 PEGddaLPDDAQDLITRLLQQNPLERlgtGGAEEVKQHPFFQDLD 279
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
16-268 1.36e-37

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: 142.32  E-value: 1.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATGHLFQEVRCMKLVQ---HPNIVRLYEVI------DTQT 86
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALK---KIRMENEKEGFPITAIREIKLLQkldHPNVVRLKEIVtskgsaKYKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 KLYLIlelgdggdmFDYiMKHeeglneDLA---------------KKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQ 151
Cdd:cd07840    78 SIYMV---------FEY-MDH------DLTglldnpevkftesqiKCYMKQLLEGLQYLHSNGILHRDIKGSNILI-NND 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 152 GLVKLTDFGFSNKFQPGKK--LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD 229
Cdd:cd07840   141 GVLKLADFGLARPYTKENNadYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFE 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 230 -C----------------------KYTVPPRV--------SAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07840   221 lCgspteenwpgvsdlpwfenlkpKKPYKRRLrevfknviDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
20-266 2.19e-37

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: 140.45  E-value: 2.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLdtlATGH----LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14189     7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRV---AKPHqrekIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvvFFEKQGL-VKLTDFGFSNKFQPG-KKLTT 173
Cdd:cd14189    84 SRKSL-AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGN--FFINENMeLKVGDFGLAARLEPPeQRKKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd14189   161 ICGTPNYLAPEVLLRQGH-GPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRN 239
                         250
                  ....*....|...
gi 1907195986 254 PKRRASLEEIESH 266
Cdd:cd14189   240 PGDRLTLDQILEH 252
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
16-268 2.27e-37

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: 141.41  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd07846     3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ-PGKKLTTS 174
Cdd:cd07846    83 DH-TVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENIL-VSQSGVVKLCDFGFARTLAaPGEVYTDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR---------VSAGCR-- 243
Cdd:cd07846   161 VATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNLIPRhqelfqknpLFAGVRlp 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907195986 244 --------------------DLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07846   241 evkeveplerrypklsgvviDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
16-269 2.60e-37

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 140.24  E-value: 2.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYImKHEEG--LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLT- 172
Cdd:cd08529    82 ENGDLHSLI-KSQRGrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMN-IFLDKGDNVKIGDLGVAKILSDTTNFAq 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYT-VPPRVSAGCRDLITRMLQ 251
Cdd:cd08529   160 TIVGTPYYLSPELCEDKPYNEKS-DVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSCLT 238
                         250
                  ....*....|....*...
gi 1907195986 252 RDPKRRASLEEIESHPWL 269
Cdd:cd08529   239 KDYRQRPDTTELLRNPSL 256
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
22-268 2.80e-37

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: 140.97  E-value: 2.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGgDMF 101
Cdd:cd07847     9 IGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDH-TVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTSC-GSLAY 180
Cdd:cd07847    88 NELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPEN-ILITKQGQIKLCDFGFARILTGPGDDYTDYvATRWY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC-------------------KYTVP------ 235
Cdd:cd07847   167 RAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTlgdliprhqqifstnqffkGLSIPepetre 246
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907195986 236 ------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07847   247 pleskfPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
16-269 2.96e-37

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: 140.27  E-value: 2.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLD--KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd06648     7 SDLDnfVKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRREL--LFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDyIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ---PGKK 170
Cdd:cd06648    85 FLEGGALTD-IVTHTR-MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSIL-LTSDGRVKLSDFGFCAQVSkevPRRK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 ltTSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKytvPPR------VSAGCRD 244
Cdd:cd06648   162 --SLVGTPYWMAPEVISRLPYG-TEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNE---PPKlknlhkVSPRLRS 235
                         250       260
                  ....*....|....*....|....*
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06648   236 FLDRMLVRDPAQRATAAELLNHPFL 260
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
18-263 6.07e-37

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: 139.22  E-value: 6.07e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   18 LDKTLGRGHFAVVKLAR----HVFTGEKVAVKVIDKTKlDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:smart00221   3 LGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   94 LGDGGDMFDYIMKHEE-GLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSnKFQPGKKLT 172
Cdd:smart00221  82 YMPGGDLLDYLRKNRPkELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCL-VGENLVVKISDFGLS-RDLYDDDYY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  173 TSCGS---LAYSAPEILLGDEYDaPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKY-TVPPRVSAGCRDLIT 247
Cdd:smart00221 160 KVKGGklpIRWMAPESLKEGKFT-SKSDVWSFGVLLWeIFTLGEEPYPGMSNAEVLEYLKKGYRlPKPPNCPPELYKLML 238
                          250
                   ....*....|....*.
gi 1907195986  248 RMLQRDPKRRASLEEI 263
Cdd:smart00221 239 QCWAEDPEDRPTFSEL 254
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
20-273 1.03e-36

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: 140.81  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLATghlFQEVRCMKLV-QHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVIlqddDVECT---MTEKRILSLArNHPFLTQLYCCFQTPDRLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLTT 173
Cdd:cd05590    78 VNGGDLMFHIQKSRR-FDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLL-DHEGHCKLADFGMCKEgIFNGKTTST 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd05590   156 FCGTPDYIAPEILQEMLY-GPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKN 234
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 254 P-KRRASL-----EEIESHPWLQGVD 273
Cdd:cd05590   235 PtMRLGSLtlggeEAILRHPFFKELD 260
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
16-273 1.73e-36

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: 140.60  E-value: 1.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DTLAtgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd05593    17 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiakDEVA--HTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKL 171
Cdd:cd05593    95 EYVNGGELF-FHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML-DKDGHIKITDFGLCKEgITDAATM 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd05593   173 KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLI 251
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 252 RDPKRRA-----SLEEIESHPWLQGVD 273
Cdd:cd05593   252 KDPNKRLgggpdDAKEIMRHSFFTGVN 278
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
15-269 2.82e-36

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: 138.24  E-value: 2.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDL-DKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKldtlatGH----LFQEVRCMKLVQ-HPNIVRLYEVIDTQTKL 88
Cdd:cd14173     2 VYQLqEEVLGEGAYARVQTCINLITNKEYAVKIIEKRP------GHsrsrVFREVEMLYQCQgHRNVLELIEFFEEEDKF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL--VKLTDFGFSNKFQ 166
Cdd:cd14173    76 YLVFEKMRGGSILSHIHRRRH-FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspVKICDFDLGSGIK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 --------PGKKLTTSCGSLAYSAPEIL--LGDE---YDApAVDIWSLGVILFMLVCGQPPFQ---------------EA 218
Cdd:cd14173   155 lnsdcspiSTPELLTPCGSAEYMAPEVVeaFNEEasiYDK-RCDLWSLGVILYIMLSGYPPFVgrcgsdcgwdrgeacPA 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907195986 219 NDSETLTMIMDCKYTVPPR----VSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14173   234 CQNMLFESIQEGKYEFPEKdwahISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
22-273 3.53e-36

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: 138.86  E-value: 3.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLA-TGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDM 100
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSeVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSN-KFQPGKKLTTSCGSLA 179
Cdd:cd05585    82 FHHLQR-EGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILL-DYTGHIALCDFGLCKlNMKDDDKTNTFCGTPE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 180 YSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKRRAS 259
Cdd:cd05585   160 YLAPELLLGHGY-TKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLG 238
                         250
                  ....*....|....*..
gi 1907195986 260 L---EEIESHPWLQGVD 273
Cdd:cd05585   239 YngaQEIKNHPFFDQID 255
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
16-269 3.76e-36

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: 137.43  E-value: 3.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDK-TLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQhpnIVRLYEVIDTQTK-LYLILE 93
Cdd:cd14172     5 YKLSKqVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRASGGPHIVH---ILDVYENMHHGKRcLLIIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKH-EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF--EKQGLVKLTDFGFSNKFQPGKK 170
Cdd:cd14172    82 CMEGGELFSRIQERgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskEKDAVLKLTDFGFAKETTVQNA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQeANDSETLTMIMDCK-----YTVP----PRVSAG 241
Cdd:cd14172   162 LQTPCYTPYYVAPEVLGPEKYDK-SCDMWSLGVIMYILLCGFPPFY-SNTGQAISPGMKRRirmgqYGFPnpewAEVSEE 239
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 242 CRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14172   240 AKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
16-269 4.00e-36

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: 137.08  E-value: 4.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVI---DKTKLDTLATghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd14088     3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFlkrDGRKVRKAAK----NEINILKMVKHPNILQLVDVFETRKEYFIFL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMkhEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE--KQGLVKLTDFGFSnKFQPGk 169
Cdd:cd14088    79 ELATGREVFDWIL--DQGyYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNrlKNSKIVISDFHLA-KLENG- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPF--------QEANDSETLTMIM--DCKYTVP--PR 237
Cdd:cd14088   155 LIKEPCGTPEYLAPEVVGRQRYGRP-VDCWAIGVIMYILLSGNPPFydeaeeddYENHDKNLFRKILagDYEFDSPywDD 233
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 238 VSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14088   234 ISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
33-269 4.57e-36

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: 136.40  E-value: 4.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  33 ARHVFTGEKVAVKVIDKTKLDTLATGHLfqevrcmKLVQHPNIVRLYEVIDTQTKLYLILElGDGGDMFDYImKHEEGLN 112
Cdd:cd13976    12 CVDIHTGEELVCKVVPVPECHAVLRAYF-------RLPSHPNISGVHEVIAGETKAYVFFE-RDHGDLHSYV-RSRKRLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 113 EDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF-EKQGLVKLTDFGFSNKFQ-PGKKLTTSCGSLAYSAPEIL-LGD 189
Cdd:cd13976    83 EPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFAdEERTKLRLESLEDAVILEgEDDSLSDKHGCPAYVSPEILnSGA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 190 EYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd13976   163 TYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
22-269 4.85e-36

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: 137.55  E-value: 4.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGgDMF 101
Cdd:cd07861     8 IGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFLSM-DLK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYI--MKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ-PGKKLTTSCGSL 178
Cdd:cd07861    87 KYLdsLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLL-IDNKGVIKLADFGLARAFGiPVRVYTHEVVTL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQeaNDSET--------------------LTMIMDCKYTVP--- 235
Cdd:cd07861   166 WYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFH--GDSEIdqlfrifrilgtptediwpgVTSLPDYKNTFPkwk 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907195986 236 --------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07861   244 kgslrtavKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
16-270 5.34e-36

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: 137.30  E-value: 5.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVV-----KLARHVFTGEKVAVKVIDKTKLDtlatghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYL 90
Cdd:cd14104     2 YMIAEELGRGQFGIVhrcveTSSKKTYMAKFVKVKGADQVLVK--------KEISILNIARHRNILRLHESFESHEELVM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQG-LVKLTDFGFSNKFQPGK 169
Cdd:cd14104    74 IFEFISGVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGsYIKIIEFGQSRQLKPGD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEIlLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSAGCRDL 245
Cdd:cd14104   154 KFRLQYTSAEFYAPEV-HQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEafknISIEALDF 232
                         250       260
                  ....*....|....*....|....*
gi 1907195986 246 ITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14104   233 VDRLLVKERKSRMTAQEALNHPWLK 257
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
15-269 1.05e-35

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: 135.79  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14107     3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFI---PLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENV--VFFEKQGLvKLTDFGFSNKFQPGKKLT 172
Cdd:cd14107    80 CSSEELLDRLFL-KGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNIlmVSPTREDI-KICDFGFAQEITPSEHQF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD--CKYTVPPRV--SAGCRDLITR 248
Cdd:cd14107   158 SKYGSPEFVAPEIVHQEPVSA-ATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEgvVSWDTPEIThlSEDAKDFIKR 236
                         250       260
                  ....*....|....*....|.
gi 1907195986 249 MLQRDPKRRASLEEIESHPWL 269
Cdd:cd14107   237 VLQPDPEKRPSASECLSHEWF 257
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
20-269 1.92e-35

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: 134.86  E-value: 1.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd08221     6 RVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTSC-GS 177
Cdd:cd08221    86 LHDKIAQQKnQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLN-IFLTKADLVKLGDFGISKVLDSESSMAESIvGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYT-VPPRVSAGCRDLITRMLQRDPKR 256
Cdd:cd08221   165 PYYMSPELVQGVKYNF-KSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEdIDEQYSEEIIQLVHDCLHQDPED 243
                         250
                  ....*....|...
gi 1907195986 257 RASLEEIESHPWL 269
Cdd:cd08221   244 RPTAEELLERPLL 256
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
38-294 2.86e-35

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: 135.93  E-value: 2.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  38 TGEKVAVKVI-DKTKLDTLATGHlFQEVRCMKLVQhpnIVRLYEVIDTQTK-LYLILELGDGGDMFDYIM-KHEEGLNED 114
Cdd:cd14170    26 TQEKFALKMLqDCPKARREVELH-WRASQCPHIVR---IVDVYENLYAGRKcLLIVMECLDGGELFSRIQdRGDQAFTER 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 115 LAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKFQPGKKLTTSCGSLAYSAPEILLGDEYD 192
Cdd:cd14170   102 EASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRpnAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 193 ApAVDIWSLGVILFMLVCGQPPFQeANDSETLTMIMDCK-----YTVP----PRVSAGCRDLITRMLQRDPKRRASLEEI 263
Cdd:cd14170   182 K-SCDMWSLGVIMYILLCGYPPFY-SNHGLAISPGMKTRirmgqYEFPnpewSEVSEEVKMLIRNLLKTEPTQRMTITEF 259
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907195986 264 ESHPWLQGVDPSPATkyniPLVSYKNLSEEE 294
Cdd:cd14170   260 MNHPWIMQSTKVPQT----PLHTSRVLKEDK 286
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
16-273 4.12e-35

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 136.65  E-value: 4.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTG-EKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:PTZ00426   32 FNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIiKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNeDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQpgKKLTT 173
Cdd:PTZ00426  112 FVIGGEFFTFLRRNKRFPN-DVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLL-LDKDGFIKMTDFGFAKVVD--TRTYT 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:PTZ00426  188 LCGTPEYIAPEILLNVGH-GKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHD 266
                         250       260
                  ....*....|....*....|....*
gi 1907195986 254 -PKRRASL----EEIESHPWLQGVD 273
Cdd:PTZ00426  267 lTKRYGNLkkgaQNVKEHPWFGNID 291
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
22-265 4.23e-35

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 133.72  E-value: 4.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARhvFTGEKVAVKVIDktkldTLATGHLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDM 100
Cdd:cd14058     1 VGRGSFGVVCKAR--WRNQIVAVKIIE-----SESEKKAFEvEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYImkHeeglNEDLAKKYFAQivHAISYCHK-------LH------VVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQp 167
Cdd:cd14058    74 YNVL--H----GKEPKPIYTAA--HAMSWALQcakgvayLHsmkpkaLIHRDLKPPNLLLTNGGTVLKICDFGTACDIS- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 gKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVsAGC----R 243
Cdd:cd14058   145 -THMTNNKGSAAWMAPEVFEGSKYSEKC-DVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERPPLI-KNCpkpiE 221
                         250       260
                  ....*....|....*....|..
gi 1907195986 244 DLITRMLQRDPKRRASLEEIES 265
Cdd:cd14058   222 SLMTRCWSKDPEKRPSMKEIVK 243
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
16-273 4.75e-35

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: 136.74  E-value: 4.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVR-CMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05596    28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERdIMAHANSEWIVQLHYAFQDDKYLYMVMDY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKL--T 172
Cdd:cd05596   108 MPGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNML-LDASGHLKLADFGTCMKMDKDGLVrsD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILL---GDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK----YTVPPRVSAGCRDL 245
Cdd:cd05596   185 TAVGTPDYISPEVLKsqgGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKnslqFPDDVEISKDAKSL 264
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 246 ITRMLQRDPKR--RASLEEIESHPWLQGVD 273
Cdd:cd05596   265 ICAFLTDREVRlgRNGIEEIKAHPFFKNDQ 294
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
20-272 5.67e-35

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: 136.70  E-value: 5.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DTLAtgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05594    31 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvakDEVA--HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYAN 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCH-KLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLTTS 174
Cdd:cd05594   109 GGELF-FHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML-DKDGHIKITDFGLCKEgIKDGATMKTF 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDP 254
Cdd:cd05594   187 CGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDP 265
                         250       260
                  ....*....|....*....|...
gi 1907195986 255 KRR-----ASLEEIESHPWLQGV 272
Cdd:cd05594   266 KQRlgggpDDAKEIMQHKFFAGI 288
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
16-269 6.36e-35

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: 133.55  E-value: 6.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLAtghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd06612     5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVV-PVEEDLQE---IIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDyIMK-HEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNK-FQPGKKLTT 173
Cdd:cd06612    81 GAGSVSD-IMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEE-GQAKLADFGVSGQlTDTMAKRNT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC---KYTVPPRVSAGCRDLITRML 250
Cdd:cd06612   159 VIGTPFWMAPEVIQEIGYNNKA-DIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKpppTLSDPEKWSPEFNDFVKKCL 237
                         250
                  ....*....|....*....
gi 1907195986 251 QRDPKRRASLEEIESHPWL 269
Cdd:cd06612   238 VKDPEERPSAIQLLQHPFI 256
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
22-269 7.85e-35

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: 134.34  E-value: 7.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd06659    29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRREL--LFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYImkHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFS---NKFQPGKKltTSCGSL 178
Cdd:cd06659   107 DIV--SQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILL-TLDGRVKLSDFGFCaqiSKDVPKRK--SLVGTP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDckyTVPP------RVSAGCRDLITRMLQR 252
Cdd:cd06659   182 YWMAPEVISRCPY-GTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRD---SPPPklknshKASPVLRDFLERMLVR 257
                         250
                  ....*....|....*..
gi 1907195986 253 DPKRRASLEEIESHPWL 269
Cdd:cd06659   258 DPQERATAQELLDHPFL 274
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
22-273 8.87e-35

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: 136.70  E-value: 8.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTL-ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDm 100
Cdd:cd05600    19 VGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLnEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGGD- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSN-------------KFQP 167
Cdd:cd05600    98 FRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFL-IDSSGHIKLTDFGLASgtlspkkiesmkiRLEE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTSC-------------------------GSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSE 222
Cdd:cd05600   177 VKNTAFLEltakerrniyramrkedqnyansvvGSPDYMAPEVLRGEGYDL-TVDYWSLGCILFECLVGFPPFSGSTPNE 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195986 223 TLTMIMDCK-------YTVP---PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGVD 273
Cdd:cd05600   256 TWANLYHWKktlqrpvYTDPdleFNLSDEAWDLITKLITDPQDRLQSPEQIKNHPFFKNID 316
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
20-264 9.08e-35

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: 133.61  E-value: 9.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHlfQEVRCMK-LVQHPNIVRLY--EVIDTQT-KLYLILELG 95
Cdd:cd13985     6 KQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAI--KEIEIMKrLCGHPNIVQYYdsAILSSEGrKEVLLLMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYI-MKHEEGLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVFFEkQGLVKLTDFG---FSNKFQPGK 169
Cdd:cd13985    84 CPGSLVDILeKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSN-TGRFKLCDFGsatTEHYPLERA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 -----------KLTTscgsLAYSAPEILlgDEYDAPAV----DIWSLGVILFMLVCGQPPFqeanDSETLTMIMDCKYTV 234
Cdd:cd13985   163 eevniieeeiqKNTT----PMYRAPEMI--DLYSKKPIgekaDIWALGCLLYKLCFFKLPF----DESSKLAIVAGKYSI 232
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 235 P--PRVSAGCRDLITRMLQRDPKRRASLEEIE 264
Cdd:cd13985   233 PeqPRYSPELHDLIRHMLTPDPAERPDIFQVI 264
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
20-273 1.05e-34

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: 136.13  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKT---KLDTLAtgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05629     7 KVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSemfKKDQLA--HVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIMEFLP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKF----------- 165
Cdd:cd05629    85 GGDLMTMLIKYDT-FSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNIL-IDRGGHIKLSDFGLSTGFhkqhdsayyqk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 -------QPGKK-----------LTTSCGS-----------LAYS--------APEILLGDEYdAPAVDIWSLGVILFML 208
Cdd:cd05629   163 llqgksnKNRIDnrnsvavdsinLTMSSKDqiatwkknrrlMAYStvgtpdyiAPEIFLQQGY-GQECDWWSLGAIMFEC 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195986 209 VCGQPPFQEANDSETLTMIMDCKYTV--PP--RVSAGCRDLITRMLQRDPKR--RASLEEIESHPWLQGVD 273
Cdd:cd05629   242 LIGWPPFCSENSHETYRKIINWRETLyfPDdiHLSVEAEDLIRRLITNAENRlgRGGAHEIKSHPFFRGVD 312
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
20-266 1.07e-34

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: 132.83  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLdtlATGH----LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14188     7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRV---SKPHqrekIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvvFFEKQGL-VKLTDFGFSNKFQP-GKKLTT 173
Cdd:cd14188    84 SRRSM-AHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGN--FFINENMeLKVGDFGLAARLEPlEHRRRT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd14188   161 ICGTPNYLSPEVLNKQGHGCES-DIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKN 239
                         250
                  ....*....|...
gi 1907195986 254 PKRRASLEEIESH 266
Cdd:cd14188   240 PEDRPSLDEIIRH 252
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
16-265 1.19e-34

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: 133.01  E-value: 1.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFA-VVKLARHVFTGEKVAVKVIDKTKLDTLAT--------GHLFQEVRCMK-LVQHPNIVRLYEVIDTQ 85
Cdd:cd08528     2 YAVLELLGSGAFGcVYKVRKKSNGQTLLALKEINMTNPAFGRTeqerdksvGDIISEVNIIKeQLRHPNIVRYYKTFLEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  86 TKLYLILELGDG---GDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHK-LHVVHRDLKPENVVFFEKQGlVKLTDFGF 161
Cdd:cd08528    82 DRLYIVMELIEGaplGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDK-VTITDFGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 SNKFQP-GKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP--RV 238
Cdd:cd08528   161 AKQKGPeSSKMTSVVGTILYSCPEIVQNEPYGEKA-DIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEPLPegMY 239
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 239 SAGCRDLITRMLQRDPKRRASLEEIES 265
Cdd:cd08528   240 SDDITFVIRSCLTPDPEARPDIVEVSS 266
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
20-269 1.38e-34

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: 132.63  E-value: 1.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd08218     6 KKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKhEEGLN--EDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTSC-G 176
Cdd:cd08218    86 LYKRINA-QRGVLfpEDQILDWFVQLCLALKHVHDRKILHRDIKSQN-IFLTKDGIIKLGDFGIARVLNSTVELARTCiG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY-TVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd08218   164 TPYYLSPEICENKPYNNKS-DIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLFKRNPR 242
                         250
                  ....*....|....
gi 1907195986 256 RRASLEEIESHPWL 269
Cdd:cd08218   243 DRPSINSILEKPFI 256
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
20-269 1.40e-34

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: 132.53  E-value: 1.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVK---VIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVKevsLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSnKFQPGKKLTTSC- 175
Cdd:cd06632    86 GGSIHK-LLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANIL-VDTNGVVKLADFGMA-KHVEAFSFAKSFk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILL--GDEYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYT--VPPRVSAGCRDLITRMLQ 251
Cdd:cd06632   163 GSPYWMAPEVIMqkNSGYGLA-VDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELppIPDHLSPDAKDFIRLCLQ 241
                         250
                  ....*....|....*...
gi 1907195986 252 RDPKRRASLEEIESHPWL 269
Cdd:cd06632   242 RDPEDRPTASQLLEHPFV 259
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
22-283 1.43e-34

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: 134.62  E-value: 1.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQE---VRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIvAKKEVAHTIGErniLVRTALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLT-TSCG 176
Cdd:cd05586    81 GELF-WHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILL-DANGHIALCDFGLSKADLTDNKTTnTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV-SAGCRDLITRMLQRDPK 255
Cdd:cd05586   159 TTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDVlSDEGRSFVKGLLNRNPK 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 256 RR----ASLEEIESHPWLQGVDPSPATKYNIP 283
Cdd:cd05586   239 HRlgahDDAVELKEHPFFADIDWDLLSKKKIT 270
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
16-267 1.49e-34

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: 133.40  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTlatGHLFQEVRCMKLVQHPNIVRL----YEVIDTQTKLYLI 91
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIK---KVLQDK---RYKNRELQIMRRLKHPNIVKLkyffYSSGEKKDEVYLN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LelgdggdMFDYI-------MKH----EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFG 160
Cdd:cd14137    80 L-------VMEYMpetlyrvIRHysknKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 fSNKF-QPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC--------- 230
Cdd:cd14137   153 -SAKRlVPGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVlgtptreqi 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 231 -----KYTV---------------PPRVSAGCRDLITRMLQRDPKRRASLEEIESHP 267
Cdd:cd14137   232 kamnpNYTEfkfpqikphpwekvfPKRTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
20-273 2.11e-34

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: 134.05  E-value: 2.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLATghlFQEVRCMKLV-QHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05592     1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVleddDVECT---MIERRVLALAsQHPFLTHLFCTFQTESHLFFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYImkHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSN-KFQPGKKLT 172
Cdd:cd05592    78 LNGGDLMFHI--QQSGrFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL-DREGHIKIADFGMCKeNIYGENKAS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQR 252
Cdd:cd05592   155 TFCGTPDYIAPEILKGQKYNQ-SVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLER 233
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 253 DPKRRASLEE-----IESHPWLQGVD 273
Cdd:cd05592   234 NPEKRLGVPEcpagdIRDHPFFKTID 259
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
22-273 2.84e-34

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 132.17  E-value: 2.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd06611    13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELED--FMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGALD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGK-KLTTSCGSLAY 180
Cdd:cd06611    91 SIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNIL-LTLDGDVKLADFGVSAKNKSTLqKRDTFIGTPYW 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGDEY-DAP---AVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC---KYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd06611   170 MAPEVVACETFkDNPydyKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSeppTLDQPSKWSSSFNDFLKSCLVKD 249
                         250       260
                  ....*....|....*....|
gi 1907195986 254 PKRRASLEEIESHPWLQGVD 273
Cdd:cd06611   250 PDDRPTAAELLKHPFVSDQS 269
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
16-276 4.47e-34

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 132.25  E-value: 4.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:PLN00009    4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DggdmFDyIMKH-----EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQ-PGK 169
Cdd:PLN00009   84 D----LD-LKKHmdsspDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALKLADFGLARAFGiPVR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFqeANDSET--------------------LTMIMD 229
Cdd:PLN00009  159 TFTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLF--PGDSEIdelfkifrilgtpneetwpgVTSLPD 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 230 CKYTVP-----------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGVDPSP 276
Cdd:PLN00009  237 YKSAFPkwppkdlatvvPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGDAP 294
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
9-303 4.49e-34

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: 133.45  E-value: 4.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   9 DGKIAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVI-DKTKLDTLA--TghlFQEVrcM---KLVQHPNIVRLYEVI 82
Cdd:cd07852     2 DKHILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfDAFRNATDAqrT---FREI--MflqELNDHPNIIKLLNVI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  83 --DTQTKLYLILELGDGgDMFDYIMKheeGLNEDLAKKY-FAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDF 159
Cdd:cd07852    77 raENDKDIYLVFEYMET-DLHAVIRA---NILEDIHKQYiMYQLLKALKYLHSGGVIHRDLKPSN-ILLNSDCRVKLADF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 160 GFSNKFQPGKK------LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQ----------------- 216
Cdd:cd07852   152 GLARSLSQLEEddenpvLTDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPgtstlnqlekiievigr 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 217 ------EANDSE-TLTMIMDCKYTVP-------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL-QGVDPSPATKYN 281
Cdd:cd07852   232 psaediESIQSPfAATMLESLPPSRPksldelfPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVaQFHNPADEPSLP 311
                         330       340
                  ....*....|....*....|....*.
gi 1907195986 282 ----IPLVSYKNLSEEEHNSIIQRMV 303
Cdd:cd07852   312 gpivIPLDDNKKLTVDEYRNRLYEEI 337
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
16-269 4.58e-34

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: 131.23  E-value: 4.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYI-MKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLV-KLTDFGFSNKFQPGKKLTT 173
Cdd:cd08225    82 DGGDLMKRInRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQN-IFLSKNGMVaKLGDFGIARQLNDSMELAY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SC-GSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFqEANDSETLTMIMDCKYTVP--PRVSAGCRDLITRML 250
Cdd:cd08225   161 TCvGTPYYLSPEICQNRPYNN-KTDIWSLGCVLYELCTLKHPF-EGNNLHQLVLKICQGYFAPisPNFSRDLRSLISQLF 238
                         250
                  ....*....|....*....
gi 1907195986 251 QRDPKRRASLEEIESHPWL 269
Cdd:cd08225   239 KVSPRDRPSITSILKRPFL 257
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
16-273 5.97e-34

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: 133.62  E-value: 5.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVI------DKTKLDTLAT-GHLFQEVRcmklvQHPNIVRLYEVIDTQTKL 88
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVkkelvnDDEDIDWVQTeKHVFEQAS-----NHPFLVGLHSCFQTESRL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNK-FQP 167
Cdd:cd05618    97 FFVIEYVNGGDLM-FHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVL-LDSEGHIKLTDYGMCKEgLRP 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSET---------LTMIMDCKYTVPPRV 238
Cdd:cd05618   175 GDTTSTFCGTPNYIAPEILRGEDY-GFSVDWWALGVLMFEMMAGRSPFDIVGSSDNpdqntedylFQVILEKQIRIPRSL 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907195986 239 SAGCRDLITRMLQRDPKRR------ASLEEIESHPWLQGVD 273
Cdd:cd05618   254 SVKAASVLKSFLNKDPKERlgchpqTGFADIQGHPFFRNVD 294
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
14-273 9.10e-34

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: 133.22  E-value: 9.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVI------DKTKLDTLAT-GHLFQEVRcmklvQHPNIVRLYEVIDTQT 86
Cdd:cd05617    15 QDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVkkelvhDDEDIDWVQTeKHVFEQAS-----SNPFLVGLHSCFQTTS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 KLYLILELGDGGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNK-F 165
Cdd:cd05617    90 RLFLVIEYVNGGDLM-FHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVL-LDADGHIKLTDYGMCKEgL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGKKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLT-------MIMDCKYTVPPRV 238
Cdd:cd05617   168 GPGDTTSTFCGTPNYIAPEILRGEEY-GFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNtedylfqVILEKPIRIPRFL 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907195986 239 SAGCRDLITRMLQRDPKRR------ASLEEIESHPWLQGVD 273
Cdd:cd05617   247 SVKASHVLKGFLNKDPKERlgcqpqTGFSDIKSHTFFRSID 287
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
16-269 1.61e-33

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: 129.47  E-value: 1.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLV---QHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVGELQPDETVDANREAKLLsklDHPAIVKFHDSFVEKESFCIVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYI---MKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvfFEKQGLVKLTDFGFSNKFQPGK 169
Cdd:cd08222    82 EYCEGGDLDDKIseyKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNI--FLKNNVIKVGDFGISRILMGTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KL-TTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY-TVPPRVSAGCRDLIT 247
Cdd:cd08222   160 DLaTTFTGTPYYMSPEVLKHEGYNSKS-DIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYS 238
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd08222   239 RMLNKDPALRPSAAEILKIPFI 260
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
25-268 1.74e-33

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: 130.42  E-value: 1.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  25 GHFAVVKLARHVFTGEKVAVKvidKTKLDTLATGhlF-----QEVRCMKLVQHPNIVRLYEVI--DTQTKLYLILELgdg 97
Cdd:cd07843    16 GTYGVVYRARDKKTGEIVALK---KLKMEKEKEG--FpitslREINILLKLQHPNIVTVKEVVvgSNLDKIYMVMEY--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 gdmfdyiMKHE-EGLNEDLAKKYFA--------QIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQ-P 167
Cdd:cd07843    88 -------VEHDlKSLMETMKQPFLQsevkclmlQLLSGVAHLHDNWILHRDLKTSNLLL-NNRGILKICDFGLAREYGsP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD------------------ 229
Cdd:cd07843   160 LKPYTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKllgtptekiwpgfselpg 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907195986 230 ---CKYTVPPRVSAGCR-----------DLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07843   240 akkKTFTKYPYNQLRKKfpalslsdngfDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
15-269 2.34e-33

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: 128.92  E-value: 2.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDK---TKLDTLATGHLFQEVRCMKLVQHP--NIVRLYEVIDTQTKLY 89
Cdd:cd14102     1 VYQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKervTEWGTLNGVMVPLEIVLLKKVGSGfrGVIKLLDWYERPDGFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGD-GGDMFDYIMkhEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGfSNKFQP 167
Cdd:cd14102    81 IVMERPEpVKDLFDFIT--EKGaLDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTGELKLIDFG-SGALLK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEanDSEtltmIMDCKYTVPPRVSAGCRDLIT 247
Cdd:cd14102   158 DTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQ--DEE----ILRGRLYFRRRVSPECQQLIK 231
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14102   232 WCLSLRPSDRPTLEQIFDHPWM 253
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
22-288 2.59e-33

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: 129.52  E-value: 2.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDktkLDT--LATGHLFQEVRCM---KLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd06917     9 VGRGSYGAVYRGYHVKTGRVVALKVLN---LDTddDDVSDIQKEVALLsqlKLGQPKNIIKYYGSYLKGPSLWIIMDYCE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMfDYIMKHEEglnedLAKKYFAQIVH----AISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK-KL 171
Cdd:cd06917    86 GGSI-RTLMRAGP-----IAERYIAVIMRevlvALKFIHKDGIIHRDIKAANILV-TNTGNVKLCDFGVAASLNQNSsKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILL-GDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKytvPPRV-----SAGCRDL 245
Cdd:cd06917   159 STFVGTPYWMAPEVITeGKYYDTKA-DIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSK---PPRLegngySPLLKEF 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907195986 246 ITRMLQRDPKRRASLEEIESHPWLQGVDPSPATKYNIPLVSYK 288
Cdd:cd06917   235 VAACLDEEPKDRLSADELLKSKWIKQHSKTPTSVLKELISRYN 277
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
15-269 2.70e-33

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: 129.29  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVID----KTKLDTLAtghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYL 90
Cdd:cd06609     2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDleeaEDEIEDIQ-----QEIQFLSQCDSPYITKYYGSFLKGSKLWI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDyIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKF-QPGK 169
Cdd:cd06609    77 IMEYCGGGSVLD-LLK-PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANIL-LSEEGDVKLADFGVSGQLtSTMS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKytvPPRV-----SAGCRD 244
Cdd:cd06609   154 KRNTFVGTPFWMAPEVIKQSGYDEKA-DIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNN---PPSLegnkfSKPFKD 229
                         250       260
                  ....*....|....*....|....*
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06609   230 FVELCLNKDPKERPSAKELLKHKFI 254
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
16-273 3.19e-33

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: 132.83  E-value: 3.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMkLVQHPN--IVRLYEVIDTQTKLYLILE 93
Cdd:cd05624    74 FEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNV-LVNGDCqwITTLHYAFQDENYLYLVMD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd05624   153 YYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVL-LDMNGHIRLADFGSCLKMNDDGTVQS 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 S--CGSLAYSAPEILLGDE-----YdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC--KYTVPPR---VSAG 241
Cdd:cd05624   232 SvaVGTPDYISPEILQAMEdgmgkY-GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHeeRFQFPSHvtdVSEE 310
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907195986 242 CRDLITRMLQRDPKR--RASLEEIESHPWLQGVD 273
Cdd:cd05624   311 AKDLIQRLICSRERRlgQNGIEDFKKHAFFEGLN 344
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
22-273 3.39e-33

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: 130.50  E-value: 3.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDK------TKLDTLAT-GHLFQEVRCMKlvqHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTGELFAIKALKKgdiiarDEVESLMCeKRIFETVNSAR---HPFLVNLFACFQTPEHVCFVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYImkHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNK-FQPGKKLTT 173
Cdd:cd05589    84 AAGGDLMMHI--HEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLL-LDTEGYVKIADFGLCKEgMGFGDRTST 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYdAPAVDIWSLGVILF-MLVcGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQR 252
Cdd:cd05589   161 FCGTPEFLAPEVLTDTSY-TRAVDWWGLGVLIYeMLV-GESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRK 238
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 253 DPKRR--AS---LEEIESHPWLQGVD 273
Cdd:cd05589   239 NPERRlgASerdAEDVKKQPFFRNID 264
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
18-266 3.49e-33

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: 128.38  E-value: 3.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGE----KVAVKVIDK--TKLDTLAtghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:pfam07714   3 LGEKLGEGAFGEVYKGTLKGEGEntkiKVAVKTLKEgaDEEERED---FLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEGLN-EDLAkKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKK 170
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTlKDLL-SMALQIAKGMEYLESKNFVHRDLAARN-CLVSENLVVKISDFGLSRDIYDDDY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSL---AYSAPEILLGDEYDaPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMI-----MDCKYTVPPRVsag 241
Cdd:pfam07714 158 YRKRGGGKlpiKWMAPESLKDGKFT-SKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEFLedgyrLPQPENCPDEL--- 233
                         250       260
                  ....*....|....*....|....*
gi 1907195986 242 cRDLITRMLQRDPKRRASLEEIESH 266
Cdd:pfam07714 234 -YDLMKQCWAYDPEDRPTFSELVED 257
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
20-273 3.65e-33

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: 130.62  E-value: 3.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVI------DKTKLDTLAT-GHLFQEVRcmklvQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd05588     1 RVIGRGSYAKVLMVELKKTKRIYAMKVIkkelvnDDEDIDWVQTeKHVFETAS-----NHPFLVGLHSCFQTESRLFFVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNK-FQPGKKL 171
Cdd:cd05588    76 EFVNGGDLM-FHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVL-LDSEGHIKLTDYGMCKEgLRPGDTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPF-----QEANDSET----LTMIMDCKYTVPPRVSAGC 242
Cdd:cd05588   154 STFCGTPNYIAPEILRGEDYGF-SVDWWALGVLMFEMLAGRSPFdivgsSDNPDQNTedylFQVILEKPIRIPRSLSVKA 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907195986 243 RDLITRMLQRDPKRR------ASLEEIESHPWLQGVD 273
Cdd:cd05588   233 ASVLKGFLNKNPAERlgchpqTGFADIQSHPFFRTID 269
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
15-269 5.18e-33

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: 127.78  E-value: 5.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLD---TLATG-HLFQEVRCMKLVQH--PNIVRLYEVIDTQTKL 88
Cdd:cd14100     1 QYQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSewgELPNGtRVPMEIVLLKKVGSgfRGVIRLLDWFERPDSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDG-GDMFDYIMkhEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGfSNKFQ 166
Cdd:cd14100    81 VLVLERPEPvQDLFDFIT--ERGaLPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGELKLIDFG-SGALL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEanDSEtltmIMDCKYTVPPRVSAGCRDLI 246
Cdd:cd14100   158 KDTVYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEH--DEE----IIRGQVFFRQRVSSECQHLI 231
                         250       260
                  ....*....|....*....|...
gi 1907195986 247 TRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14100   232 KWCLALRPSDRPSFEDIQNHPWM 254
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
22-285 5.48e-33

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: 128.71  E-value: 5.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-----DTLAtghlFQEVRCMKLVQH----PNIVRLYEVIDTQTKLYLIL 92
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkmkqgETLA----LNERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPgKKLT 172
Cdd:cd05606    78 DLMNGGDLHYHLSQHGV-FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDE-HGHVRISDLGLACDFSK-KKPH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILL-GDEYDAPAvDIWSLGVILFMLVCGQPPFQEAN-------DSETLTMIMDckytVPPRVSAGCRD 244
Cdd:cd05606   155 ASVGTHGYMAPEVLQkGVAYDSSA-DWFSLGCMLYKLLKGHSPFRQHKtkdkheiDRMTLTMNVE----LPDSFSPELKS 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907195986 245 LITRMLQRDPKRR-----ASLEEIESHPWLQGVDPSPA--TKYNIPLV 285
Cdd:cd05606   230 LLEGLLQRDVSKRlgclgRGATEVKEHPFFKGVDWQQVylQKYPPPLI 277
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
12-269 6.75e-33

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: 129.20  E-value: 6.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFA-VVKLARHVfTGEKVAVKVI-DKTKLdtlaTGHLFQEVRCMKLVQH------PNIVRLYEVID 83
Cdd:cd14210    11 IAYRYEVLSVLGKGSFGqVVKCLDHK-TGQLVAIKIIrNKKRF----HQQALVEVKILKHLNDndpddkHNIVRYKDSFI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  84 TQTKLYLILELGdGGDMFDYI-MKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfeKQGL---VKLTDF 159
Cdd:cd14210    86 FRGHLCIVFELL-SINLYELLkSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILL--KQPSkssIKVIDF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 160 GfSNKFQpGKKLTTSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM----------- 228
Cdd:cd14210   163 G-SSCFE-GEKVYTYIQSRFYRAPEVILGLPYD-TAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMevlgvppksli 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 229 ----------DCKYTVPPRVSAGCR---------------------DLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14210   240 dkasrrkkffDSNGKPRPTTNSKGKkrrpgskslaqvlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
18-270 6.91e-33

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: 128.97  E-value: 6.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKtLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd07873     7 LDK-LGEGTYATVYKGRSKLTDNLVALKEI-RLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 gDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSN-KFQPGKKLTTSCG 176
Cdd:cd07873    85 -DLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINER-GELKLADFGLARaKSIPTKTYSNEVV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM---------------------------- 228
Cdd:cd07873   163 TLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFrilgtpteetwpgilsneefksynypky 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907195986 229 --DCKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd07873   243 raDALHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFH 286
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
18-273 6.95e-33

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: 129.66  E-value: 6.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLATghlFQEVRCMKLV-QHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd05619     9 LHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVlmddDVECT---MVEKRVLSLAwEHPFLTHLFCTFQTKENLFFVM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMK-HEEGLNEdlAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK-K 170
Cdd:cd05619    86 EYLNGGDLMFHIQScHKFDLPR--ATFYAAEIICGLQFLHSKGIVYRDLKLDNILL-DKDGHIKIADFGMCKENMLGDaK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRML 250
Cdd:cd05619   163 TSTFCGTPDYIAPEILLGQKYNT-SVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLF 241
                         250       260
                  ....*....|....*....|....
gi 1907195986 251 QRDPKRRASLE-EIESHPWLQGVD 273
Cdd:cd05619   242 VREPERRLGVRgDIRQHPFFREIN 265
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
10-269 9.47e-33

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: 128.20  E-value: 9.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  10 GKIAGLYDLDKtLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLY 89
Cdd:cd07871     2 GKLETYVKLDK-LGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSN-KFQPG 168
Cdd:cd07871    80 LVFEYLDS-DLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEK-GELKLADFGLARaKSVPT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGD-EYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC----------------- 230
Cdd:cd07871   158 KTYSNEVVTLWYRPPDVLLGStEYSTP-IDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLlgtpteetwpgvtsnee 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 231 --KYTVP-----------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07871   237 frSYLFPqyraqplinhaPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
16-268 1.23e-32

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: 127.44  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKV-------IDKTKLDTlaTGHLFQEVRCMKLVQHPNIVRLYEV--IDTQT 86
Cdd:cd13990     2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIhqlnkdwSEEKKQNY--IKHALREYEIHKSLDHPRIVKLYDVfeIDTDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 kLYLILELGDGGDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYC--HKLHVVHRDLKPENVVFFEKQ--GLVKLTDFGFS 162
Cdd:cd13990    80 -FCTVLEYCDGNDL-DFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNvsGEIKITDFGLS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 163 ------NKFQPGKKLTTS-CGSLAYSAPEILLGDEyDAP----AVDIWSLGVILFMLVCGQPPF-----QEAnDSETLTM 226
Cdd:cd13990   158 kimddeSYNSDGMELTSQgAGTYWYLPPECFVVGK-TPPkissKVDVWSVGVIFYQMLYGRKPFghnqsQEA-ILEENTI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907195986 227 IMDCKYTVP--PRVSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd13990   236 LKATEVEFPskPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
22-267 1.58e-32

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: 126.34  E-value: 1.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRC-MKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDM 100
Cdd:cd13997     8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAhAALGQHPNIVRYYSSWEEGGHLYIQMELCENGSL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYIMK--HEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFqpGKKLTTSCGSL 178
Cdd:cd13997    88 QDALEElsPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNI-FISNKGTCKIGDFGLATRL--ETSGDVEEGDS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMimdCKYTVPPRV--SAGCRDLITRMLQRDPKR 256
Cdd:cd13997   165 RYLAPELLNENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQLRQ---GKLPLPPGLvlSQELTRLLKVMLDPDPTR 241
                         250
                  ....*....|.
gi 1907195986 257 RASLEEIESHP 267
Cdd:cd13997   242 RPTADQLLAHD 252
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-269 1.76e-32

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: 127.50  E-value: 1.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKtLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd07844     5 LDK-LGEGSYATVYKGRSKLTGQLVALKEI-RLEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLDT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 gDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSN-KFQPGKKLTTSCG 176
Cdd:cd07844    83 -DLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISER-GELKLADFGLARaKSVPSKTYSNEVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGD-EYDAPaVDIWSLGVILFMLVCGQPPFQEANDS-ETLTMIMD------------------------C 230
Cdd:cd07844   161 TLWYRPPDVLLGStEYSTS-LDMWGVGCIFYEMATGRPLFPGSTDVeDQLHKIFRvlgtpteetwpgvssnpefkpysfP 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907195986 231 KYT------VPPRVS--AGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07844   240 FYPprplinHAPRLDriPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
20-273 2.10e-32

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: 127.31  E-value: 2.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlATGH--LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd05608     7 RVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKK-RKGYegAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDYIMKHEE---GLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd05608    86 GDLRYHIYNVDEenpGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVL-LDDDGNVRISDLGLAVELKDGQTKTKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 -CGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPF----QEANDSETLTMIMDCKYTVPPRVSAGCRDLITRM 249
Cdd:cd05608   165 yAGTPGFMAPELLLGEEYDY-SVDYFTLGVTLYEMIAARGPFrargEKVENKELKQRILNDSVTYSEKFSPASKSICEAL 243
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 250 LQRDPKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05608   244 LAKDPEKRlgfrdGNCDGLRTHPFFRDIN 272
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
15-267 2.34e-32

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: 126.27  E-value: 2.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEI--IQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNK-FQPGKKLTT 173
Cdd:cd06613    79 CGGGSLQD-IYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTE-DGDVKLADFGVSAQlTATIAKRKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILL---GDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYtVPPRV------SAGCRD 244
Cdd:cd06613   157 FIGTPYWMAPEVAAverKGGYDG-KCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNF-DPPKLkdkekwSPDFHD 234
                         250       260
                  ....*....|....*....|...
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHP 267
Cdd:cd06613   235 FIKKCLTKNPKKRPTATKLLQHP 257
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
22-215 2.44e-32

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: 127.18  E-value: 2.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATGHLFQ----EVRCMKLVQHPNIVRLYEV-----IDTQTKL-YLI 91
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIK---KCRQELSPSDKNRErwclEVQIMKKLNHPNVVSARDVppeleKLSPNDLpLLA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEE--GLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLV--KLTDFGFSNKFQP 167
Cdd:cd13989    78 MEYCSGGDLRKVLNQPENccGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRViyKLIDLGYAKELDQ 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907195986 168 GKKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPF 215
Cdd:cd13989   158 GSLCTSFVGTLQYLAPELFESKKYTC-TVDYWSFGTLAFECITGYRPF 204
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
20-273 4.07e-32

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: 128.07  E-value: 4.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05610    10 KPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMiNKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 D------MFDYimkheegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFS---------- 162
Cdd:cd05610    90 DvksllhIYGY-------FDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNML-ISNEGHIKLTDFGLSkvtlnrelnm 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 163 ---------------NKFQPGK--KLTTS---------------------------CGSLAYSAPEILLGDEYDaPAVDI 198
Cdd:cd05610   162 mdilttpsmakpkndYSRTPGQvlSLISSlgfntptpyrtpksvrrgaarvegeriLGTPDYLAPELLLGKPHG-PAVDW 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 199 WSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP---PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGVD 273
Cdd:cd05610   241 WALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAGLKELKQHPLFHGVD 318
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
16-269 4.35e-32

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: 125.46  E-value: 4.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGhlFQEVRCMKLVQ------HPNIVRLYEVIDTQTKLY 89
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKII-KNNKDYLDQS--LDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELgDGGDMFDYI-MKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE-KQGLVKLTDFGFSnkFQP 167
Cdd:cd14133    78 IVFEL-LSQNLYEFLkQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASySRCQIKIIDFGSS--CFL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR--VSAGCR-- 243
Cdd:cd14133   155 TQRLYSYIQSRYYRAPEVILGLPYDE-KIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHmlDQGKADde 233
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 244 ---DLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14133   234 lfvDFLKKLLEIDPKERPTASQALSHPWL 262
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
20-263 5.39e-32

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: 125.34  E-value: 5.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLAR-HVFTGEK--VAVKVI-----DKTKLDtlatghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd00192     1 KKLGEGAFGEVYKGKlKGGDGKTvdVAVKTLkedasESERKD------FLKEARVMKKLGHPNVVRLLGVCTEEEPLYLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEGLNEDLAK--------KYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFS- 162
Cdd:cd00192    75 MEYMEGGDLLDFLRKSRPVFPSPEPStlslkdllSFAIQIAKGMEYLASKKFVHRDLAARN-CLVGEDLVVKISDFGLSr 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 163 --NKFQPGKKLTTSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKYTVPPrvs 239
Cdd:cd00192   154 diYDDDYYRKKTGGKLPIRWMAPESLKDGIFT-SKSDVWSFGVLLWeIFTLGATPYPGLSNEEVLEYLRKGYRLPKP--- 229
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 240 AGCRDLITRMLQR----DPKRRASLEEI 263
Cdd:cd00192   230 ENCPDELYELMLScwqlDPEDRPTFSEL 257
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
16-265 6.18e-32

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: 125.09  E-value: 6.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKlDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPK-SSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYImKHEEG--LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKF-QPGKKLT 172
Cdd:cd08219    81 DGGDLMQKI-KLQRGklFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKN-IFLTQNGKVKLGDFGSARLLtSPGAYAC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQeANDSETLTMIM--DCKYTVPPRVSAGCRDLITRML 250
Cdd:cd08219   159 TYVGTPYYVPPEIWENMPYNNKS-DIWSLGCILYELCTLKHPFQ-ANSWKNLILKVcqGSYKPLPSHYSYELRSLIKQMF 236
                         250
                  ....*....|....*
gi 1907195986 251 QRDPKRRASLEEIES 265
Cdd:cd08219   237 KRNPRSRPSATTILS 251
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
67-269 8.24e-32

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: 124.00  E-value: 8.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  67 MKLVQHPNIVRLYEVIDTQTKLYLILElGDGGDMFDYImKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVV 146
Cdd:cd14023    39 IQLPSHRNITGIVEVILGDTKAYVFFE-KDFGDMHSYV-RSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 147 F------------FEKQGLVKLTDFGFSNKFqpgkklttscGSLAYSAPEIL-LGDEYDAPAVDIWSLGVILFMLVCGQP 213
Cdd:cd14023   117 FsdeertqlrlesLEDTHIMKGEDDALSDKH----------GCPAYVSPEILnTTGTYSGKSADVWSLGVMLYTLLVGRY 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 214 PFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14023   187 PFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERLTAPEILLHPWF 242
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
16-273 8.31e-32

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: 128.59  E-value: 8.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMkLVQHPN--IVRLYEVIDTQTKLYLILE 93
Cdd:cd05623    74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDV-LVNGDSqwITTLHYAFQDDNNLYLVMD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd05623   153 YYVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNIL-MDMNGHIRLADFGSCLKLMEDGTVQS 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 S--CGSLAYSAPEILL----GDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK--YTVPPR---VSAGC 242
Cdd:cd05623   232 SvaVGTPDYISPEILQamedGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKerFQFPTQvtdVSENA 311
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907195986 243 RDLITRMLQRDPKR--RASLEEIESHPWLQGVD 273
Cdd:cd05623   312 KDLIRRLICSREHRlgQNGIEDFKNHPFFVGID 344
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
20-273 8.37e-32

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: 126.35  E-value: 8.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLATghlFQEVRCMKLVQHPN-IVRLYEVIDTQTKLYLILEL 94
Cdd:cd05587     2 MVLGKGSFGKVMLAERKGTDELYAIKILKKDVIiqddDVECT---MVEKRVLALSGKPPfLTQLHSCFQTMDRLYFVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLTT 173
Cdd:cd05587    79 VNGGDLM-YHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-DAEGHIKIADFGMCKEgIFGGKTTRT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd05587   157 FCGTPDYIAPEIIAYQPYGK-SVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKH 235
                         250       260
                  ....*....|....*....|....*
gi 1907195986 254 PKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05587   236 PAKRlgcgpTGERDIKEHPFFRRID 260
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
33-269 9.06e-32

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: 123.99  E-value: 9.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  33 ARHVFTGEKVAVKVIDKTKL-DTLATghlfqevrCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGgDMFDYIMKHEEgL 111
Cdd:cd14022    12 AVHLHSGEELVCKVFDIGCYqESLAP--------CFCLPAHSNINQITEIILGETKAYVFFERSYG-DMHSFVRTCKK-L 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 112 NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF-EKQGLVKL-----------TDFGFSNKFqpgkklttscGSLA 179
Cdd:cd14022    82 REEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKdEERTRVKLesledayilrgHDDSLSDKH----------GCPA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 180 YSAPEIL-LGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKRRA 258
Cdd:cd14022   152 YVSPEILnTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL 231
                         250
                  ....*....|.
gi 1907195986 259 SLEEIESHPWL 269
Cdd:cd14022   232 TSQEILDHPWF 242
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
22-263 1.30e-31

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: 124.28  E-value: 1.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTkldTLATGH----LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVPKS---LLLKPHqkekMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFQ-PGKKLTTSCG 176
Cdd:cd14187    92 RSLLE-LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNL-FLNDDMEVKIGDFGLATKVEyDGERKKTLCG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILlGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKR 256
Cdd:cd14187   170 TPNYIAPEVL-SKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTA 248

                  ....*..
gi 1907195986 257 RASLEEI 263
Cdd:cd14187   249 RPTINEL 255
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
22-270 1.51e-31

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: 123.88  E-value: 1.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVID-----KTKLdtlatghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd06647    15 IGQGASGTVYTAIDVATGQEVAIKQMNlqqqpKKEL-------IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMkhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK-KLTTSC 175
Cdd:cd06647    88 GGSLTDVVT--ETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL-GMDGSVKLTDFGFCAQITPEQsKRSTMV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM---DCKYTVPPRVSAGCRDLITRMLQR 252
Cdd:cd06647   165 GTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPEKLSAIFRDFLNRCLEM 243
                         250
                  ....*....|....*...
gi 1907195986 253 DPKRRASLEEIESHPWLQ 270
Cdd:cd06647   244 DVEKRGSAKELLQHPFLK 261
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
16-270 2.23e-31

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: 126.65  E-value: 2.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVR-CMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05621    54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFCAFQDDKYLYMVMEY 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKF-QPGK-KLT 172
Cdd:cd05621   134 MPGGDLVNLMSNYD--VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNML-LDKYGHLKLADFGTCMKMdETGMvHCD 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILL---GDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTV----PPRVSAGCRDL 245
Cdd:cd05621   211 TAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLnfpdDVEISKHAKNL 290
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 246 ITRMLQRDPKR--RASLEEIESHPWLQ 270
Cdd:cd05621   291 ICAFLTDREVRlgRNGVEEIKQHPFFR 317
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
22-270 2.76e-31

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: 124.40  E-value: 2.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVI--DKTKlDTLATGHLfQEVRCMKLVQHPNIVRLYEVI--DTQTKLYLILELGDG 97
Cdd:cd07845    15 IGEGTYGIVYRARDTTSGEIVALKKVrmDNER-DGIPISSL-REITLLLNLRHPNIVELKEVVvgKHLDSIFLVMEYCEQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 gDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKFQ-PGKKLTTSCG 176
Cdd:cd07845    93 -DLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK-GCLKIADFGLARTYGlPAKPMTPKVV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC-------------------KYTVP-- 235
Cdd:cd07845   171 TLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLlgtpnesiwpgfsdlplvgKFTLPkq 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1907195986 236 ---------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd07845   251 pynnlkhkfPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFK 294
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
16-274 3.96e-31

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: 123.68  E-value: 3.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd06655    21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKEL--IINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMkhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK-KLTTS 174
Cdd:cd06655    99 AGGSLTDVVT--ETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLL-GMDGSVKLTDFGFCAQITPEQsKRSTM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC---KYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd06655   176 VGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPEKLSPIFRDFLNRCLE 254
                         250       260
                  ....*....|....*....|...
gi 1907195986 252 RDPKRRASLEEIESHPWLQGVDP 274
Cdd:cd06655   255 MDVEKRGSAKELLQHPFLKLAKP 277
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
20-273 4.43e-31

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: 124.14  E-value: 4.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLATghlFQEVRCMKLV-QHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVIlqddDVDCT---MTEKRILALAaKHPFLTALHSCFQTKDRLFFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLTT 173
Cdd:cd05591    78 VNGGDLMFQIQRARK-FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILL-DAEGHCKLADFGMCKEgILNGKTTTT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd05591   156 FCGTPDYIAPEILQELEYG-PSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKN 234
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 254 PKRR-------ASLEEIESHPWLQGVD 273
Cdd:cd05591   235 PAKRlgcvasqGGEDAIRQHPFFREID 261
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
13-269 4.80e-31

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: 122.80  E-value: 4.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  13 AGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRcmKLVQHPNIVRLYEV------IDTQT 86
Cdd:cd06608     5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILR--KFSNHPNIATFYGAfikkdpPGGDD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 KLYLILELGDGG---DMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSN 163
Cdd:cd06608    83 QLWLVMEYCGGGsvtDLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNIL-LTEEAEVKLVDFGVSA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQP--GKKlTTSCGSLAYSAPEILLGDE-----YDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDckyTVPP 236
Cdd:cd06608   162 QLDStlGRR-NTFIGTPYWMAPEVIACDQqpdasYDARC-DVWSLGITAIELADGKPPLCDMHPMRALFKIPR---NPPP 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907195986 237 RV------SAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06608   237 TLkspekwSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
20-273 5.16e-31

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: 125.17  E-value: 5.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05627     8 KVIGRGAFGEVRLVQKKDTGHIYAMKILRKADmLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFG------------------ 160
Cdd:cd05627    88 DMMTLLMK-KDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLL-DAKGHVKLSDFGlctglkkahrtefyrnlt 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 --------FSNKFQPGKKLT----------TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSE 222
Cdd:cd05627   166 hnppsdfsFQNMNSKRKAETwkknrrqlaySTVGTPDYIAPEVFMQTGYNK-LCDWWSLGVIMYEMLIGYPPFCSETPQE 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 223 TLTMIMDCKYTV--PPRV--SAGCRDLITRMLQRDPKR--RASLEEIESHPWLQGVD 273
Cdd:cd05627   245 TYRKVMNWKETLvfPPEVpiSEKAKDLILRFCTDAENRigSNGVEEIKSHPFFEGVD 301
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
20-273 5.19e-31

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: 123.90  E-value: 5.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLATghlFQEVRCMKLV-QHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVliddDVECT---MVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYImkHEEGlNEDL--AKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK-KL 171
Cdd:cd05620    78 LNGGDLMFHI--QDKG-RFDLyrATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML-DRDGHIKIADFGMCKENVFGDnRA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMI-MDCKYtVPPRVSAGCRDLITRML 250
Cdd:cd05620   154 STFCGTPDYIAPEILQGLKYTF-SVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIrVDTPH-YPRWITKESKDILEKLF 231
                         250       260
                  ....*....|....*....|....
gi 1907195986 251 QRDPKRRASLE-EIESHPWLQGVD 273
Cdd:cd05620   232 ERDPTRRLGVVgNIRGHPFFKTIN 255
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
20-274 7.47e-31

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: 122.91  E-value: 7.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd06656    25 EKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMkhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK-KLTTSCGSL 178
Cdd:cd06656   103 LTDVVT--ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL-GMDGSVKLTDFGFCAQITPEQsKRSTMVGTP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC---KYTVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd06656   180 YWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMDVD 258
                         250
                  ....*....|....*....
gi 1907195986 256 RRASLEEIESHPWLQGVDP 274
Cdd:cd06656   259 RRGSAKELLQHPFLKLAKP 277
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
22-236 8.27e-31

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: 122.41  E-value: 8.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGgDMF 101
Cdd:cd07848     9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEK-NML 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGK--KLTTSCGSLA 179
Cdd:cd07848    88 ELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLL-ISHNDVLKLCDFGFARNLSEGSnaNYTEYVATRW 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 180 YSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP 236
Cdd:cd07848   167 YRSPELLLGAPY-GKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPA 222
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
16-269 9.26e-31

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: 122.99  E-value: 9.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATGHLFQEVRCMKLV---QHPNIVRLYE-VIDTQTKLYLI 91
Cdd:cd07864     9 FDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFPITAIREIKILrqlNHRSVVNLKEiVTDKQDALDFK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYiMKH------EEGL---NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFS 162
Cdd:cd07864    86 KDKGAFYLVFEY-MDHdlmgllESGLvhfSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNK-GQIKLADFGLA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 163 NKFQPGKK--LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMI------------- 227
Cdd:cd07864   164 RLYNSEESrpYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELIsrlcgspcpavwp 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195986 228 ----------MDCKYTVPPR-------VSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07864   244 dviklpyfntMKPKKQYRRRlreefsfIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
22-275 1.77e-30

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 123.40  E-value: 1.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:PLN00034   82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRR-QICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLnEDLAKkyfaQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKF-QPGKKLTTSCGSLAY 180
Cdd:PLN00034  161 GTHIADEQFL-ADVAR----QILSGIAYLHRRHIVHRDIKPSNLLINSAKN-VKIADFGVSRILaQTMDPCNSSVGTIAY 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGD----EYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----VSAGCRDLITRMLQR 252
Cdd:PLN00034  235 MSPERINTDlnhgAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQPPEapatASREFRHFISCCLQR 314
                         250       260
                  ....*....|....*....|...
gi 1907195986 253 DPKRRASLEEIESHPWLQGVDPS 275
Cdd:PLN00034  315 EPAKRWSAMQLLQHPFILRAQPG 337
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
18-284 4.57e-30

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 121.79  E-value: 4.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGH------------LFQEVRCMKLVQHPNIVRLYEVIDTQ 85
Cdd:PTZ00024   13 KGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDrqlvgmcgihftTLRELKIMNEIKHENIMGLVDVYVEG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  86 TKLYLILEL--GDGGDMFDYIMKheegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSN 163
Cdd:PTZ00024   93 DFINLVMDImaSDLKKVVDRKIR----LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANI-FINSKGICKIADFGLAR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KF---------------QPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM 228
Cdd:PTZ00024  168 RYgyppysdtlskdetmQRREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIF 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 229 D-------------------CKYT---------VPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQgVDPSPATKY 280
Cdd:PTZ00024  248 EllgtpnednwpqakklplyTEFTprkpkdlktIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFK-SDPLPCDPS 326

                  ....
gi 1907195986 281 NIPL 284
Cdd:PTZ00024  327 QLPF 330
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
16-268 8.27e-30

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: 118.97  E-value: 8.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVI--DKTKLDTLATGHLFQ-EVRCMKLVQHPNIVRLYEVI--DTQTKLYL 90
Cdd:cd06653     4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfDPDSQETSKEVNALEcEIQLLKNLRHDRIVQYYGCLrdPEEKKLSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDYiMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ---- 166
Cdd:cd06653    84 FVEYMPGGSVKDQ-LKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL-RDSAGNVKLGDFGASKRIQticm 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMI--MDCKYTVPPRVSAGCRD 244
Cdd:cd06653   162 SGTGIKSVTGTPYWMSPEVISGEGYGRKA-DVWSVACTVVEMLTEKPPWAEYEAMAAIFKIatQPTKPQLPDGVSDACRD 240
                         250       260
                  ....*....|....*....|....
gi 1907195986 245 LITRMLQRDpKRRASLEEIESHPW 268
Cdd:cd06653   241 FLRQIFVEE-KRRPTAEFLLRHPF 263
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
10-274 8.52e-30

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: 120.10  E-value: 8.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  10 GKIAGLYDLDKtLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLY 89
Cdd:cd07872     3 GKMETYIKLEK-LGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSN-KFQPG 168
Cdd:cd07872    81 LVFEYLDK-DLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINER-GELKLADFGLARaKSVPT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC------------------ 230
Cdd:cd07872   159 KTYSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLlgtpteetwpgissndef 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 231 -KYTVP-----------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGVDP 274
Cdd:cd07872   239 kNYNFPkykpqplinhaPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRSLGT 294
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
20-273 1.06e-29

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: 121.68  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05628     7 KVIGRGAFGEVRLVQKKDTGHVYAMKILRKADmLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFG------------------ 160
Cdd:cd05628    87 DMMTLLMK-KDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLL-DSKGHVKLSDFGlctglkkahrtefyrnln 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 --------FSNKFQPGKKLT----------TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSE 222
Cdd:cd05628   165 hslpsdftFQNMNSKRKAETwkrnrrqlafSTVGTPDYIAPEVFMQTGYNK-LCDWWSLGVIMYEMLIGYPPFCSETPQE 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 223 TLTMIMDCKYTV--PPRV--SAGCRDLITRMLQRDPKRRAS--LEEIESHPWLQGVD 273
Cdd:cd05628   244 TYKKVMNWKETLifPPEVpiSEKAKDLILRFCCEWEHRIGApgVEEIKTNPFFEGVD 300
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
20-275 1.06e-29

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: 121.66  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTK-LDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05626     7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDvLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKF------------- 165
Cdd:cd05626    87 DMMSLLIRMEV-FPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNIL-IDLDGHIKLTDFGLCTGFrwthnskyyqkgs 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 -----------------------------QPGKKLTTSC------GSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVC 210
Cdd:cd05626   165 hirqdsmepsdlwddvsncrcgdrlktleQRATKQHQRClahslvGTPNYIAPEVLLRKGY-TQLCDWWSVGVILFEMLV 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195986 211 GQPPFQEANDSETLTMIMDCKYT--VPPRV--SAGCRDLITRMLQRDPKR--RASLEEIESHPWLQGVDPS 275
Cdd:cd05626   244 GQPPFLAPTPTETQLKVINWENTlhIPPQVklSPEAVDLITKLCCSAEERlgRNGADDIKAHPFFSEVDFS 314
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
68-269 1.30e-29

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 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 TRB3 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: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 117.67  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  68 KLVQHPNIVRLYEVIDTQTKLYLILElGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF 147
Cdd:cd14024    40 RLGPHEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRR-LSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 148 FEKQ----GLVKLTDFGFSNkfQPGKKLTTSCGSLAYSAPEIL-LGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSE 222
Cdd:cd14024   118 TDELrtklVLVNLEDSCPLN--GDDDSLTDKHGCPAYVGPEILsSRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAA 195
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907195986 223 TLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14024   196 LFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
60-269 1.33e-29

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: 118.00  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  60 LFQEVRCMKLVQHPNIVRLYEVIDTQTK-LYLILELGDGGDMF-DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVH 137
Cdd:cd14109    43 LMREVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLASTIELVrDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 138 RDLKPENVVFfeKQGLVKLTDFGFSNKFQPGKKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQE 217
Cdd:cd14109   123 LDLRPEDILL--QDDKLKLADFGQSRRLLRGKLTTLIYGSPEFVSPEIVNSYPVTL-ATDMWSVGVLTYVLLGGISPFLG 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 218 ANDSETLTMIMDCKY----TVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14109   200 DNDRETLTNVRSGKWsfdsSPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
16-267 1.33e-29

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: 119.57  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLAtghlfQEVRCMKLVQ-HPNIVRLYEVI-DTQTKLY-LIL 92
Cdd:cd14132    20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKIK-----REIKILQNLRgGPNIVKLLDVVkDPQSKTPsLIF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDmFDYIMkheEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKLT 172
Cdd:cd14132    95 EYVNNTD-FKTLY---PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRKLRLIDWGLAEFYHPGQEYN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEAND-------------SETLTMIMDcKY--TVPPR 237
Cdd:cd14132   171 VRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDnydqlvkiakvlgTDDLYAYLD-KYgiELPPR 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907195986 238 VSAGCR------------------------DLITRMLQRDPKRRASLEEIESHP 267
Cdd:cd14132   250 LNDILGrhskkpwerfvnsenqhlvtpealDLLDKLLRYDHQERITAKEAMQHP 303
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
23-269 2.08e-29

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: 117.62  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  23 GRGHFAVVKLARHVFTGEKVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG---- 98
Cdd:cd14111    12 ARGRFGVIRRCRENATGKNFPAKIV---PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKellh 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 ---DMFDYimkheeglNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNKFQPG--KKLTT 173
Cdd:cd14111    89 sliDRFRY--------SEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAI-KIVDFGSAQSFNPLslRQLGR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY---TVPPRVSAGCRDLITRML 250
Cdd:cd14111   160 RTGTLEYMAPEMVKGEPVGPPA-DIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFdafKLYPNVSQSASLFLKKVL 238
                         250
                  ....*....|....*....
gi 1907195986 251 QRDPKRRASLEEIESHPWL 269
Cdd:cd14111   239 SSYPWSRPTTKDCFAHAWL 257
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
16-260 2.50e-29

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: 117.82  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMmDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGD---MFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFG----FSNKFQP 167
Cdd:cd08228    84 ADAGDlsqMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPAN-VFITATGVVKLGDLGlgrfFSSKTTA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKLTtscGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPF--QEANDSETLTMIMDCKYtvPP----RVSAG 241
Cdd:cd08228   163 AHSLV---GTPYYMSPERIHENGYNFKS-DIWSLGCLLYEMAALQSPFygDKMNLFSLCQKIEQCDY--PPlpteHYSEK 236
                         250
                  ....*....|....*....
gi 1907195986 242 CRDLITRMLQRDPKRRASL 260
Cdd:cd08228   237 LRELVSMCIYPDPDQRPDI 255
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
22-274 2.54e-29

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: 118.59  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DyIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFS---NKFQPGKKltTSCGSL 178
Cdd:cd06657   106 D-IVTHTR-MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILL-THDGRVKLSDFGFCaqvSKEVPRRK--SLVGTP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDckyTVPPR------VSAGCRDLITRMLQR 252
Cdd:cd06657   181 YWMAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD---NLPPKlknlhkVSPSLKGFLDRLLVR 256
                         250       260
                  ....*....|....*....|..
gi 1907195986 253 DPKRRASLEEIESHPWLQGVDP 274
Cdd:cd06657   257 DPAQRATAAELLKHPFLAKAGP 278
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
16-269 3.41e-29

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: 117.51  E-value: 3.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKT-----LGRGHFAVVKLARHVFTGEKVAVKVIDKTklDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYL 90
Cdd:cd06624     5 YEYDESgervvLGKGTFGVVYAARDLSTQVRIAIKEIPER--DSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDyIMKHEEG---LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSnkfqp 167
Cdd:cd06624    83 FMEQVPGGSLSA-LLRSKWGplkDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVVKISDFGTS----- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 gKKL-------TTSCGSLAYSAPEILlgDE----YDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYT--- 233
Cdd:cd06624   157 -KRLaginpctETFTGTLQYMAPEVI--DKgqrgYGPPA-DIWSLGCTIIEMATGKPPFIELGEPQAAMFKVGMFKIhpe 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907195986 234 VPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06624   233 IPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
16-268 6.35e-29

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: 117.15  E-value: 6.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATG---HLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALK---RVRLDDDDEGvpsSALREICLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ-PGKKL 171
Cdd:cd07839    79 EYCDQ-DLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLL-INKNGELKLADFGLARAFGiPVRCY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSE-------------------TLTMIMDCKY 232
Cdd:cd07839   157 SAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDdqlkrifrllgtpteeswpGVSKLPDYKP 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907195986 233 TVP-----------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07839   237 YPMypattslvnvvPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
20-275 9.02e-29

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: 117.86  E-value: 9.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKT---KLDTLATghlFQEVRCMKLVQHPNIVRLYEVI-----DTQTKLYLI 91
Cdd:cd07858    11 KPIGRGAYGIVCSAKNSETNEKVAIKKIANAfdnRIDAKRT---LREIKLLRHLDHENVIAIKDIMppphrEAFNDVYIV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGgDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSN-KFQPGKK 170
Cdd:cd07858    88 YELMDT-DLHQ-IIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDL-KICDFGLARtTSEKGDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLG-DEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC------------------K 231
Cdd:cd07858   165 MTEYVVTRWYRAPELLLNcSEYTT-AIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELlgspseedlgfirnekarR 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 232 Y--TVP-----------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGV-DPS 275
Cdd:cd07858   244 YirSLPytprqsfarlfPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLhDPS 301
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
22-274 1.16e-28

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: 116.68  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRREL--LFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DyIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFS---NKFQPGKKLTTscGSL 178
Cdd:cd06658   108 D-IVTHTR-MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILL-TSDGRIKLSDFGFCaqvSKEVPKRKSLV--GTP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDckyTVPPR------VSAGCRDLITRMLQR 252
Cdd:cd06658   183 YWMAPEVISRLPY-GTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRD---NLPPRvkdshkVSSVLRGFLDLMLVR 258
                         250       260
                  ....*....|....*....|..
gi 1907195986 253 DPKRRASLEEIESHPWLQGVDP 274
Cdd:cd06658   259 EPSQRATAQELLQHPFLKLAGP 280
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
20-274 1.62e-28

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: 116.36  E-value: 1.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd06654    26 EKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMkhEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGK-KLTTSCGSL 178
Cdd:cd06654   104 LTDVVT--ETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL-GMDGSVKLTDFGFCAQITPEQsKRSTMVGTP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC---KYTVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd06654   181 YWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMDVE 259
                         250
                  ....*....|....*....
gi 1907195986 256 RRASLEEIESHPWLQGVDP 274
Cdd:cd06654   260 KRGSAKELLQHQFLKIAKP 278
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
20-267 1.63e-28

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: 115.77  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHL-FQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05607     8 RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMaLLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMK-HEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSCGS 177
Cdd:cd05607    88 DLKYHIYNvGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVL-LDDNGNCRLSDLGLAVEVKEGKPITQRAGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPF---QEANDSETL---TMIMDCKYTvPPRVSAGCRDLITRMLQ 251
Cdd:cd05607   167 NGYMAPEILKEESYSYP-VDWFAMGCSIYEMVAGRTPFrdhKEKVSKEELkrrTLEDEVKFE-HQNFTEEAKDICRLFLA 244
                         250
                  ....*....|....*.
gi 1907195986 252 RDPKRRASLEEIESHP 267
Cdd:cd05607   245 KKPENRLGSRTNDDDP 260
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
20-276 1.63e-28

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: 116.00  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVI---DKTKLDTlatgHLFQEVRCMKLVQHPNIVRLY-EVIDTQTKLYLILELG 95
Cdd:cd06620    11 KDLGAGNGGSVSKVLHIPTGTIMAKKVIhidAKSSVRK----QILRELQILHECHSPYIVSFYgAFLNENNNIIICMEYM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDmFDYIMKHEEGLNEDLAKKYFAQIVHAISYCH-KLHVVHRDLKPENVVFfEKQGLVKLTDFGFSnkfqpgKKLTTS 174
Cdd:cd06620    87 DCGS-LDKILKKKGPFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILV-NSKGQIKLCDFGVS------GELINS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 -----CGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEAND---SETLTM-IMDCKYTV----PPRVSAG 241
Cdd:cd06620   159 iadtfVGTSTYMSPERIQGGKYSVKS-DVWSLGLSIIELALGEFPFAGSNDdddGYNGPMgILDLLQRIvnepPPRLPKD 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907195986 242 ------CRDLITRMLQRDPKRRASLEEIESH-PWLQGVDPSP 276
Cdd:cd06620   238 rifpkdLRDFVDRCLLKDPRERPSPQLLLDHdPFIQAVRASD 279
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
15-263 1.84e-28

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 119.74  E-value: 1.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLA-RHVFTGEKVAVKVIDKTklDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:PTZ00267   68 MYVLTTLVGRNPTTAAFVAtRGSDPKEKVVAKFVMLN--DERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIME 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYI---MKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFQPGKK 170
Cdd:PTZ00267  146 YGSGGDLNKQIkqrLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANI-FLMPTGIIKLGDFGFSKQYSDSVS 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 L---TTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY-TVPPRVSAGCRDLI 246
Cdd:PTZ00267  225 LdvaSSFCGTPYYLAPELWERKRYSKKA-DMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYdPFPCPVSSGMKALL 303
                         250
                  ....*....|....*..
gi 1907195986 247 TRMLQRDPKRRASLEEI 263
Cdd:PTZ00267  304 DPLLSKNPALRPTTQQL 320
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
16-270 2.02e-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: 118.57  E-value: 2.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVR-CMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05622    75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFYAFQDDRYLYMVMEY 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGK--KLT 172
Cdd:cd05622   155 MPGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGHLKLADFGTCMKMNKEGmvRCD 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILL---GDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK--YTVP--PRVSAGCRDL 245
Cdd:cd05622   232 TAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPddNDISKEAKNL 311
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 246 ITRMLQRDPKR--RASLEEIESHPWLQ 270
Cdd:cd05622   312 ICAFLTDREVRlgRNGVEEIKRHLFFK 338
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
67-269 2.23e-28

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 114.95  E-value: 2.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  67 MKlvQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVV 146
Cdd:PHA03390   65 MK--DNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFD-LLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 147 FFEKQGLVKLTDFGFSnkfqpgkKL--TTSC--GSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSE 222
Cdd:PHA03390  142 YDRAKDRIYLCDYGLC-------KIigTPSCydGTLDYFSPEKIKGHNYD-VSFDWWAVGVLTYELLTGKHPFKEDEDEE 213
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 223 -TLTMIMDCKY---TVPPRVSAGCRDLITRMLQRDPKRRA-SLEEIESHPWL 269
Cdd:PHA03390  214 lDLESLLKRQQkklPFIKNVSKNANDFVQSMLKYNINYRLtNYNEIIKHPFL 265
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
22-259 3.01e-28

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: 114.40  E-value: 3.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLArhVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLvQHPNIVRLYEVIDTQTKLYL---ILELGDGG 98
Cdd:cd13979    11 LGSGGFGSVYKA--TYKGETVAVKIVRRRRKNRASRQSFWAELNAARL-RHENIVRVLAAETGTDFASLgliIMEYCGNG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNK-FQPGKKLTTSC-- 175
Cdd:cd13979    88 TLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANIL-ISEQGVCKLCDFGCSVKlGEGNEVGTPRShi 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 -GSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSetlTMIMDCKYTVPPRVSAG--------CRDLI 246
Cdd:cd13979   167 gGTYTYRAPELLKGERV-TPKADIYSFGITLWQMLTRELPYAGLRQH---VLYAVVAKDLRPDLSGLedsefgqrLRSLI 242
                         250
                  ....*....|...
gi 1907195986 247 TRMLQRDPKRRAS 259
Cdd:cd13979   243 SRCWSAQPAERPN 255
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
21-270 3.54e-28

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: 114.83  E-value: 3.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  21 TLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVR-CMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG- 98
Cdd:cd06617     8 ELGRGAYGVVDKMRHVPTGTIMAVKRI-RATVNSQEQKRLLMDLDiSMRSVDCPYTVTFYGALFREGDVWICMEVMDTSl 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 -DMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCH-KLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSCG 176
Cdd:cd06617    87 dKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHsKLSVIHRDVKPSNVL-INRNGQVKLCDFGISGYLVDSVAKTIDAG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGD----EYDAPAvDIWSLGVILFMLVCGQPPFQEANdsetlTMIMDCKYTV---PPRV-----SAGCRD 244
Cdd:cd06617   166 CKPYMAPERINPElnqkGYDVKS-DVWSLGITMIELATGRFPYDSWK-----TPFQQLKQVVeepSPQLpaekfSPEFQD 239
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd06617   240 FVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
22-272 4.69e-28

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: 114.74  E-value: 4.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd06644    20 LGDGAFGKVYKAKNKETGALAAAKVIETKSEEELED--YMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAVD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNK-FQPGKKLTTSCGSLAY 180
Cdd:cd06644    98 AIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVL-LTLDGDIKLADFGVSAKnVKTLQRRDSFIGTPYW 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGDEY-DAP---AVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK---YTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd06644   177 MAPEVVMCETMkDTPydyKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFLKTALDKH 256
                         250
                  ....*....|....*....
gi 1907195986 254 PKRRASLEEIESHPWLQGV 272
Cdd:cd06644   257 PETRPSAAQLLEHPFVSSV 275
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
22-267 9.00e-28

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: 113.29  E-value: 9.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVID---KTKLDTLAT-GHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd06630     8 LGTGAFSSCYQARDVKTGTLMAVKQVSfcrNSSSEQEEVvEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQpgKKLTTS--- 174
Cdd:cd06630    88 GSV-ASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQRLRIADFGAAARLA--SKGTGAgef 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 ----CGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMI--MDCKYTVPP---RVSAGCRDL 245
Cdd:cd06630   165 qgqlLGTIAFMAPEVLRGEQY-GRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIfkIASATTPPPipeHLSPGLRDV 243
                         250       260
                  ....*....|....*....|..
gi 1907195986 246 ITRMLQRDPKRRASLEEIESHP 267
Cdd:cd06630   244 TLRCLELQPEDRPPARELLKHP 265
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
16-268 9.46e-28

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: 113.78  E-value: 9.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATG---HLFQEVRCMKLVQH-PNIVRLYEVIDTQTK---- 87
Cdd:cd07837     3 YEKLEKIGEGTYGKVYKARDKNTGKLVALK---KTRLEMEEEGvpsTALREVSLLQMLSQsIYIVRLLDVEHVEENgkpl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGgDMFDYIMKHEEG----LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSN 163
Cdd:cd07837    80 LYLVFEYLDT-DLKKFIDSYGRGphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLLKIADLGLGR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQ-PGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM-------------- 228
Cdd:cd07837   159 AFTiPIKSYTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFrllgtpneevwpgv 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907195986 229 ---------------DCKYTVPPRVSAGCrDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07837   239 sklrdwheypqwkpqDLSRAVPDLEPEGV-DLLTKMLAYDPAKRISAKAALQHPY 292
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
16-266 1.00e-27

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: 112.83  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVI--DKTKLDTLATGHLFQ-EVRCMKLVQHPNIVRLYEVI-DTQTK-LYL 90
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfDPESPETSKEVNALEcEIQLLKNLLHERIVQYYGCLrDPQERtLSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDYiMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ---- 166
Cdd:cd06652    84 FMEYMPGGSIKDQ-LKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL-RDSVGNVKLGDFGASKRLQticl 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMI--MDCKYTVPPRVSAGCRD 244
Cdd:cd06652   162 SGTGMKSVTGTPYWMSPEVISGEGYGRKA-DIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIatQPTNPQLPAHVSDHCRD 240
                         250       260
                  ....*....|....*....|..
gi 1907195986 245 LITRMLQrDPKRRASLEEIESH 266
Cdd:cd06652   241 FLKRIFV-EAKLRPSADELLRH 261
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
22-215 2.61e-27

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: 112.36  E-value: 2.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------YLILELG 95
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQC-RQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEE--GLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF--FEKQGLVKLTDFGFSNKFQPGKKL 171
Cdd:cd14038    81 QGGDLRKYLNQFENccGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLqqGEQRLIHKIIDLGYAKELDQGSLC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPF 215
Cdd:cd14038   161 TSFVGTLQYLAPELLEQQKYTV-TVDYWSFGTLAFECITGFRPF 203
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
22-215 3.07e-27

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: 112.32  E-value: 3.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL-----YLILELGD 96
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSC-RLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYCS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEE--GLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLV--KLTDFGFSNKFQPGKKLT 172
Cdd:cd14039    80 GGDLRKLLNKPENccGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIvhKIIDLGYAKDLDQGSLCT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPF 215
Cdd:cd14039   160 SFVGTLQYLAPELFENKSYTV-TVDYWSFGTMVFECIAGFRPF 201
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
20-273 3.87e-27

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: 112.04  E-value: 3.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHL-FQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05630     6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DM-FDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSCGS 177
Cdd:cd05630    86 DLkFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENIL-LDDHGHIRISDLGLAVHVPEGQTIKGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYD-APavDIWSLGVILFMLVCGQPPFQEAND----SETLTMIMDCKYTVPPRVSAGCRDLITRMLQR 252
Cdd:cd05630   165 VGYMAPEVVKNERYTfSP--DWWALGCLLYEMIAGQSPFQQRKKkikrEEVERLVKEVPEEYSEKFSPQARSLCSMLLCK 242
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 253 DPKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05630   243 DPAERlgcrgGGAREVKEHPLFKKLN 268
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
20-269 4.81e-27

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: 111.59  E-value: 4.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVID-KTKLDTLATGhlFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGg 98
Cdd:cd07870     6 EKLGEGSYATVYKGISRINGQLVALKVISmKTEEGVPFTA--IREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSN-KFQPGKKLTTSCGS 177
Cdd:cd07870    83 DLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLL-ISYLGELKLADFGLARaKSIPSQTYSSEVVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDS-ETLTMIMDC-----------------------KYT 233
Cdd:cd07870   162 LWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVfEQLEKIWTVlgvptedtwpgvsklpnykpewfLPC 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907195986 234 VPPRVSAGCR---------DLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07870   242 KPQQLRVVWKrlsrppkaeDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
16-274 5.08e-27

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: 112.84  E-value: 5.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTkLDTLATG-HLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------ 88
Cdd:cd07855     7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNA-FDVVTTAkRTLRELKILRHFKHDNIIAIRDILRPKVPYadfkdv 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGdmFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSN---KF 165
Cdd:cd07855    86 YVVLDLMESD--LHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCEL-KIGDFGMARglcTS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGKK--LTTSCGSLAYSAPEILLG-DEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV--SA 240
Cdd:cd07855   163 PEEHKyfMTEYVATRWYRAPELMLSlPEY-TQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPSQAVinAI 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195986 241 GCR-----------------------------DLITRMLQRDPKRRASLEEIESHPWLQG-VDP 274
Cdd:cd07855   242 GADrvrryiqnlpnkqpvpwetlypkadqqalDLLSQMLRFDPSERITVAEALQHPFLAKyHDP 305
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
16-269 7.34e-27

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: 110.39  E-value: 7.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLAtghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQL---VLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQPGKKLTT-S 174
Cdd:cd14110    82 SGPELL-YNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKN-LLKIVDLGNAQPFNQGKVLMTdK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGS-LAYSAPEILLGdEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP---PRVSAGCRDLITRML 250
Cdd:cd14110   160 KGDyVETMAPELLEG-QGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSrcyAGLSGGAVNFLKSTL 238
                         250
                  ....*....|....*....
gi 1907195986 251 QRDPKRRASLEEIESHPWL 269
Cdd:cd14110   239 CAKPWGRPTASECLQNPWL 257
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
22-273 8.72e-27

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 110.89  E-value: 8.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd06643    13 LGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELED--YMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNK-FQPGKKLTTSCGSLAY 180
Cdd:cd06643    91 AVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNIL-FTLDGDIKLADFGVSAKnTRTLQRRDSFIGTPYW 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGDE-----YDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK---YTVPPRVSAGCRDLITRMLQR 252
Cdd:cd06643   170 MAPEVVMCETskdrpYDYKA-DVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPEFKDFLRKCLEK 248
                         250       260
                  ....*....|....*....|.
gi 1907195986 253 DPKRRASLEEIESHPWLQGVD 273
Cdd:cd06643   249 NVDARWTTSQLLQHPFVSVLV 269
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
22-269 8.89e-27

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: 110.32  E-value: 8.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVID------------KTKLDTLAtghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLY 89
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVElpsvsaenkdrkKSMLDALQ-----REIALLRELQHENIVQYLGSSSDANHLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGK 169
Cdd:cd06628    83 IFLEYVPGGSVATLLNNYGA-FEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANIL-VDNKGGIKISDFGISKKLEANS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSC-------GSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD-CKYTVPPRVSAG 241
Cdd:cd06628   161 LSTKNNgarpslqGSVFWMAPEVVKQTSY-TRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGEnASPTIPSNISSE 239
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 242 CRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06628   240 ARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
19-267 1.06e-26

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: 110.05  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  19 DKTLGRG-HFAVVklARHVFTGEKVAVKVIDKTKLDtLAtghlFQEVrcmKLVQ----HPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd13982     6 PKVLGYGsEGTIV--FRGTFDGRPVAVKRLLPEFFD-FA----DREV---QLLResdeHPNVIRYFCTEKDRQFLYIALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGgDMFDYIMKHEEGL----NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF----FEKQGLVKLTDFGFSNKF 165
Cdd:cd13982    76 LCAA-SLQDLVESPRESKlflrPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstpnAHGNVRAMISDFGLCKKL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGK----KLTTSCGSLAYSAPEILLGDEYDAP--AVDIWSLG-VILFMLVCGQPPF-----QEANdsetltmIMDCKYT 233
Cdd:cd13982   155 DVGRssfsRRSGVAGTSGWIAPEMLSGSTKRRQtrAVDIFSLGcVFYYVLSGGSHPFgdkleREAN-------ILKGKYS 227
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907195986 234 VPPRVSAG-----CRDLITRMLQRDPKRRASLEEIESHP 267
Cdd:cd13982   228 LDKLLSLGehgpeAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
16-269 1.27e-26

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: 109.61  E-value: 1.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVID-KTKLDTLATghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPvRAKKKTSAR----RELALLAELDHKSIVRFHDAFEKRRVVIIVTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GdGGDMFDYIMKHEEGLNEDLaKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE-KQGLVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd14108    80 C-HEELLERITKRPTVCESEV-RSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADqKTDQVRICDFGNAQELTPNEPQYC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEIlLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAG-CRD---LITRM 249
Cdd:cd14108   158 KYGTPEFVAPEI-VNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDlCREakgFIIKV 236
                         250       260
                  ....*....|....*....|
gi 1907195986 250 LQRDpKRRASLEEIESHPWL 269
Cdd:cd14108   237 LVSD-RLRPDAEETLEHPWF 255
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
16-268 1.34e-26

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: 110.92  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVI----DKTKLDTLAtghlFQEVRCMKLVQHPNIVRLYEVIDTQTK---- 87
Cdd:cd07865    14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVlmenEKEGFPITA----LREIKILQLLKHENVVNLIEICRTKATpynr 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 ----LYLILELGDGgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSN 163
Cdd:cd07865    90 ykgsIYLVFEFCEH-DLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI-TKDGVLKLADFGLAR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQPGK-----KLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV 238
Cdd:cd07865   168 AFSLAKnsqpnRYTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEV 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 239 SAGCR--------------------------------DLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07865   248 WPGVDklelfkkmelpqgqkrkvkerlkpyvkdpyalDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
20-275 1.52e-26

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: 111.12  E-value: 1.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEV-IDTQTKLYLILELgDGG 98
Cdd:cd07856    16 QPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISPLEDIYFVTEL-LGT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNKFQPgkKLTTSCGSL 178
Cdd:cd07856    95 DLHRLLTSRP--LEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDL-KICDFGLARIQDP--QMTGYVSTR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLG-DEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP---------------------- 235
Cdd:cd07856   170 YYRAPEIMLTwQKYDV-EVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPddvinticsentlrfvqslpkr 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907195986 236 ---------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGV-DPS 275
Cdd:cd07856   249 ervpfsekfKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYhDPT 298
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
16-275 1.59e-26

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: 111.34  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFT--GEKVAVKVIDKTKLDTLATGHLFQEVRCMK-LVQHPNIVRLYEV----IDTQTKL 88
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETseEETVAIKKITNVFSKKILAKRALRELKLLRhFRGHKNITCLYDMdivfPGNFNEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGgDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPG 168
Cdd:cd07857    82 YLYEELMEA-DL-HQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLV-NADCELKICDFGLARGFSEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KK-----LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEAN---------------DSETLTMIM 228
Cdd:cd07857   159 PGenagfMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDyvdqlnqilqvlgtpDEETLSRIG 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195986 229 DCK-------YTVPPRVSAG---------CRDLITRMLQRDPKRRASLEEIESHPWLQGV-DPS 275
Cdd:cd07857   239 SPKaqnyirsLPNIPKKPFEsifpnanplALDLLEKLLAFDPTKRISVEEALEHPYLAIWhDPD 302
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
16-257 1.61e-26

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: 110.12  E-value: 1.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGD---MFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKL 171
Cdd:cd08229   106 ADAGDlsrMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPAN-VFITATGVVKLGDLGLGRFFSSKTTA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTS-CGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPF--QEANDSETLTMIMDCKYTVPP--RVSAGCRDLI 246
Cdd:cd08229   185 AHSlVGTPYYMSPERIHENGYNFKS-DIWSLGCLLYEMAALQSPFygDKMNLYSLCKKIEQCDYPPLPsdHYSEELRQLV 263
                         250
                  ....*....|.
gi 1907195986 247 TRMLQRDPKRR 257
Cdd:cd08229   264 NMCINPDPEKR 274
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
16-275 1.66e-26

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: 111.24  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLfQEVRCMKLVQHPNIVRLYEVI-----DTQTKLYL 90
Cdd:cd07849     7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTL-REIKILLRFKHENIIGILDIQrpptfESFKDVYI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGgDMFDYImkHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFS----NKFQ 166
Cdd:cd07849    86 VQELMET-DLYKLI--KTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDL-KICDFGLAriadPEHD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD----------------- 229
Cdd:cd07849   162 HTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGilgtpsqedlnciislk 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195986 230 ---------CKYTVP-----PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL-QGVDPS 275
Cdd:cd07849   242 arnyikslpFKPKVPwnklfPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLeQYHDPS 302
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
16-285 1.88e-26

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: 110.91  E-value: 1.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCM-KLVQH---PNIVRLYEVIDTQTKLYLI 91
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMlSLVSTgdcPFIVCMSYAFHTPDKLSFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEEGLNEDLaKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPgKKL 171
Cdd:cd14223    82 LDLMNGGDLHYHLSQHGVFSEAEM-RFYAAEIILGLEHMHSRFVVYRDLKPANIL-LDEFGHVRISDLGLACDFSK-KKP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILL-GDEYDAPAvDIWSLGVILFMLVCGQPPFQEAN-------DSETLTMIMDckytVPPRVSAGCR 243
Cdd:cd14223   159 HASVGTHGYMAPEVLQkGVAYDSSA-DWFSLGCMLFKLLRGHSPFRQHKtkdkheiDRMTLTMAVE----LPDSFSPELR 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907195986 244 DLITRMLQRDPKRRASL-----EEIESHPWLQGVDPSPA--TKYNIPLV 285
Cdd:cd14223   234 SLLEGLLQRDVNRRLGCmgrgaQEVKEEPFFRGLDWQMVflQKYPPPLI 282
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
16-269 1.97e-26

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: 109.16  E-value: 1.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVK--LARHVFTGEKVAVKVIDKTKLDTLATghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd14112     5 FSFGSEIFRGRFSVIVkaVDSTTETDAHCAVKIFEVSDEASEAV----REFESLRTLQHENVQRLIAAFKPSNFAYLVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGgDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL-VKLTDFGFSNKFQPGKKlT 172
Cdd:cd14112    81 KLQE-DVFTRFSSNDY-YSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWqVKLVDFGRAQKVSKLGK-V 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEAND--SETLTMIMDCKYT---VPPRVSAGCRDLIT 247
Cdd:cd14112   158 PVDGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDdeEETKENVIFVKCRpnlIFVEATQEALRFAT 237
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14112   238 WALKKSPTRRMRTDEALEHRWL 259
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
12-216 2.40e-26

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 114.12  E-value: 2.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdktKLDtLATGHLFQ-----EVRCM-KLVqHPNIVRLYEVIDTQ 85
Cdd:NF033483    5 LGGRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL---RPD-LARDPEFVarfrrEAQSAaSLS-HPNIVSVYDVGEDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  86 TKLYLILELGDGGDMFDYImkHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFG---- 160
Cdd:NF033483   80 GIPYIVMEYVDGRTLKDYI--REHGpLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL-ITKDGRVKVTDFGiara 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 161 FSNkfqpgkklTTSC------GSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQ 216
Cdd:NF033483  157 LSS--------TTMTqtnsvlGTVHYLSPEQARGGTVDARS-DIYSLGIVLYEMLTGRPPFD 209
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
16-273 2.69e-26

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: 110.47  E-value: 2.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLATghlFQEVRCMKLV-QHPNIVRLYEVIDTQTKLYL 90
Cdd:cd05616     2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVViqddDVECT---MVEKRVLALSgKPPFLTQLHSCFQTMDRLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGK 169
Cdd:cd05616    79 VMEYVNGGDLM-YHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVML-DSEGHIKIADFGMCKEnIWDGV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVS----AGCRDL 245
Cdd:cd05616   157 TTKTFCGTPDYIAPEIIAYQPY-GKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSkeavAICKGL 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907195986 246 ITrmlqRDPKRRASL-----EEIESHPWLQGVD 273
Cdd:cd05616   236 MT----KHPGKRLGCgpegeRDIKEHAFFRYID 264
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
22-269 2.96e-26

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: 109.28  E-value: 2.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIdktKLDTLATGHLFQEVRCMKLVQ------HPNIVRLYEV-----IDTQTKLYL 90
Cdd:cd07863     8 IGVGAYGTVYKARDPHSGHFVALKSV---RVQTNEDGLPLSTVREVALLKrleafdHPNIVRLMDVcatsrTDRETKVTL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGgDMFDYIMK-HEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGK 169
Cdd:cd07863    85 VFEHVDQ-DLRTYLDKvPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENIL-VTSGGQVKLADFGLARIYSCQM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC----------------KYT 233
Cdd:cd07863   163 ALTPVVVTLWYRAPEVLLQSTYATP-VDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLiglppeddwprdvtlpRGA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907195986 234 VPPR-----------VSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07863   242 FSPRgprpvqsvvpeIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
16-259 4.74e-26

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 112.66  E-value: 4.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVI---DTQTK----- 87
Cdd:PTZ00283   34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSIVKCHEDFakkDPRNPenvlm 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGGDMFDYI----------MKHEEGLnedlakkYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLT 157
Cdd:PTZ00283  114 IALVLDYANAGDLRQEIksraktnrtfREHEAGL-------LFIQVLLAVHHVHSKHMIHRDIKSANILLCS-NGLVKLG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 158 DFGFSNKFQP------GKkltTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCK 231
Cdd:PTZ00283  186 DFGFSKMYAAtvsddvGR---TFCGTPYYVAPEIWRRKPYSKKA-DMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGR 261
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 232 YT-VPPRVSAGCRDLITRMLQRDPKRRAS 259
Cdd:PTZ00283  262 YDpLPPSISPEMQEIVTALLSSDPKRRPS 290
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
16-285 5.08e-26

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: 110.15  E-value: 5.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-----DTLAtghlFQEVRCMKLVQH---PNIVRLYEVIDTQTK 87
Cdd:cd05633     7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkmkqgETLA----LNERIMLSLVSTgdcPFIVCMTYAFHTPDK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQP 167
Cdd:cd05633    83 LCFILDLMNGGDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL-DEHGHVRISDLGLACDFSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 gKKLTTSCGSLAYSAPEILL-GDEYDAPAvDIWSLGVILFMLVCGQPPFQE---ANDSETLTMIMDCKYTVPPRVSAGCR 243
Cdd:cd05633   161 -KKPHASVGTHGYMAPEVLQkGTAYDSSA-DWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELPDSFSPELK 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907195986 244 DLITRMLQRDPKRR-----ASLEEIESHPWLQGVDPSPA--TKYNIPLV 285
Cdd:cd05633   239 SLLEGLLQRDVSKRlgchgRGAQEVKEHSFFKGIDWQQVylQKYPPPLI 287
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
22-273 5.35e-26

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: 108.60  E-value: 5.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTG-----EKVAVKVIDKTKLDTLAtghlFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05605     8 LGKGGFGEVCACQVRATGkmyacKKLEKKRIKKRKGEAMA----LNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMK-HEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd05605    84 GGDLKFHIYNmGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENIL-LDDHGHVRISDLGLAVEIPEGETIRGRV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEAND----SETLTMIMDCKYTVPPRVSAGCRDLITRMLQ 251
Cdd:cd05605   163 GTVGYMAPEVVKNERY-TFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVDRRVKEDQEEYSEKFSEEAKSICSQLLQ 241
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 252 RDPK-----RRASLEEIESHPWLQGVD 273
Cdd:cd05605   242 KDPKtrlgcRGEGAEDVKSHPFFKSIN 268
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
18-257 5.70e-26

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: 108.14  E-value: 5.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEKVAVK---VIDKTKLDTLAtghlfQEVRCMK-LVQHPNIVRLY-----EVIDTQTKL 88
Cdd:cd14037     7 IEKYLAEGGFAHVYLVKTSNGGNRAALKrvyVNDEHDLNVCK-----REIEIMKrLSGHKNIVGYIdssanRSGNGVYEV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFDYIMKH-EEGLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVFFEKqGLVKLTDFG-FSNK 164
Cdd:cd14037    82 LLLMEYCKGGGVIDLMNQRlQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDS-GNYKLCDFGsATTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 165 FQPG-------------KKLTTscgsLAYSAPEILlgDEYDAPAV----DIWSLGVILFMLVCGQPPFQEandSETLTmI 227
Cdd:cd14037   161 ILPPqtkqgvtyveediKKYTT----LQYRAPEMI--DLYRGKPIteksDIWALGCLLYKLCFYTTPFEE---SGQLA-I 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 228 MDCKYTVP--PRVSAGCRDLITRMLQRDPKRR 257
Cdd:cd14037   231 LNGNFTFPdnSRYSKRLHKLIRYMLEEDPEKR 262
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
18-269 6.62e-26

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: 107.31  E-value: 6.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL--ELG 95
Cdd:cd13983     5 FNEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKklTT 173
Cdd:cd13983    85 TSGTLKQYLKRFKR-LKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTGEVKIGDLGLATLLRQSF--AK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SC-GSLAYSAPEiLLGDEYDaPAVDIWSLGVILFMLVCGQPPFQE-ANDSETLTMIMDckyTVPP----RVSAGC-RDLI 246
Cdd:cd13983   162 SViGTPEFMAPE-MYEEHYD-EKVDIYAFGMCLLEMATGEYPYSEcTNAAQIYKKVTS---GIKPeslsKVKDPElKDFI 236
                         250       260
                  ....*....|....*....|...
gi 1907195986 247 TRMLqRDPKRRASLEEIESHPWL 269
Cdd:cd13983   237 EKCL-KPPDERPSARELLEHPFF 258
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
20-263 6.76e-26

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: 107.84  E-value: 6.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd14046    12 QVLGKGAFGQVVKVRNKLDGRYYAIKKI-KLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCEKST 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYImkhEEGLNEDLAK--KYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGF---------------- 161
Cdd:cd14046    91 LRDLI---DSGLFQDTDRlwRLFRQILEGLAYIHSQGIIHRDLKPVN-IFLDSNGNVKIGDFGLatsnklnvelatqdin 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 ---SNKFQPGKKLTTSCGSLAYSAPEILLGDE--YDApAVDIWSLGVILFMLVcgQPPFQEANDSETLTMIMDCKYTVPP 236
Cdd:cd14046   167 kstSAALGSSGDLTGNVGTALYVAPEVQSGTKstYNE-KVDMYSLGIIFFEMC--YPFSTGMERVQILTALRSVSIEFPP 243
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907195986 237 rvsAGCRD-------LITRMLQRDPKRRASLEEI 263
Cdd:cd14046   244 ---DFDDNkhskqakLIRWLLNHDPAKRPSAQEL 274
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
16-268 7.86e-26

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: 108.56  E-value: 7.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVK-VIDKTKLDTLATGHLfQEVRCMKLVQHPNIVRLYEVI----DTQTKLYL 90
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHNEKDGFPITAL-REIKILKKLKHPNVVPLIDMAverpDKSKRKRG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELgdggdMFDYiMKHE-EGL--NEDL------AKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGF 161
Cdd:cd07866    89 SVYM-----VTPY-MDHDlSGLleNPSVkltesqIKCYMLQLLEGINYLHENHILHRDIKAANIL-IDNQGILKIADFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 SNKFQ-PGKKLTTSCGSLA-----------YSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD 229
Cdd:cd07866   162 ARPYDgPPPNPKGGGGGGTrkytnlvvtrwYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFK 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195986 230 -C-------------------KYTVPP----------RVSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07866   242 lCgtpteetwpgwrslpgcegVHSFTNyprtleerfgKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
20-275 8.35e-26

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: 110.14  E-value: 8.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTklDTL---ATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05625     7 KTLGIGAFGEVCLARKVDTKALYATKTLRKK--DVLlrnQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGF---------SNKFQP 167
Cdd:cd05625    85 GGDMMSLLIRMGV-FPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDGHIKLTDFGLctgfrwthdSKYYQS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 168 GKKL-------------TTSC--------------------------GSLAYSAPEILLGDEYdAPAVDIWSLGVILFML 208
Cdd:cd05625   163 GDHLrqdsmdfsnewgdPENCrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGY-TQLCDWWSVGVILFEM 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195986 209 VCGQPPFQEANDSETLTMIMDCKYT--VPP--RVSAGCRDLITRmLQRDPKRRA---SLEEIESHPWLQGVDPS 275
Cdd:cd05625   242 LVGQPPFLAQTPLETQMKVINWQTSlhIPPqaKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTIDFS 314
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
15-269 9.43e-26

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: 106.92  E-value: 9.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLARHVFT-------GEKVAVKVIDKTKLDTlatgHLFQEVRCMKLVQ-HPNIVRLYEVIDTQT 86
Cdd:cd14019     2 KYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPS----RILNELECLERLGgSNNVSGLITAFRNED 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 KLYLILELGDGGDMFDYIMKheeGLNEDLaKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQ 166
Cdd:cd14019    78 QVVAVLPYIEHDDFRDFYRK---MSLTDI-RIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGVLVDFGLAQREE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKKLTTSC-GSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQ-PPFQEANDSETLTMIMDCkytvppRVSAGCRD 244
Cdd:cd14019   154 DRPEQRAPRaGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATI------FGSDEAYD 227
                         250       260
                  ....*....|....*....|....*
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14019   228 LLDKLLELDPSKRITAEEALKHPFF 252
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
16-269 1.26e-25

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: 106.75  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTK-LYLILEL 94
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGfLYIVMGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYiMKHEEG--LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKL- 171
Cdd:cd08223    82 CEGGDLYTR-LKEQKGvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQN-IFLTKSNIIKVGDLGIARVLESSSDMa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQeANDSETLTM-IMDCKY-TVPPRVSAGCRDLITRM 249
Cdd:cd08223   160 TTLIGTPYYMSPELFSNKPYNHKS-DVWALGCCVYEMATLKHAFN-AKDMNSLVYkILEGKLpPMPKQYSPELGELIKAM 237
                         250       260
                  ....*....|....*....|
gi 1907195986 250 LQRDPKRRASLEEIESHPWL 269
Cdd:cd08223   238 LHQDPEKRPSVKRILRQPYI 257
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
15-268 1.89e-25

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: 107.76  E-value: 1.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVKLAR--HVFTGEKVAVKVIDKTKLDTlaTGHLFQEVRCMKL---VQHPNIVRLYEVIDTQT--K 87
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKrkNGKDGKEYAIKKFKGDKEQY--TGISQSACREIALlreLKHENVVSLVEVFLEHAdkS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGgDMFDYIMKHEEG----LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVV---FFEKQGLVKLTDFG 160
Cdd:cd07842    79 VYLLFDYAEH-DLWQIIKFHRQAkrvsIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILvmgEGPERGVVKIGDLG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 FSNKFQ-PGKKLTTSCG---SLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEAND---------SETLTMI 227
Cdd:cd07842   158 LARLFNaPLKPLADLDPvvvTIWYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfqRDQLERI 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 228 MDCK-------------------------------------YTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd07842   238 FEVLgtptekdwpdikkmpeydtlksdtkastypnsllakwMHKHKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPY 315
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
22-269 2.47e-25

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: 107.76  E-value: 2.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------YLILELG 95
Cdd:cd07851    23 VGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLedfqdvYLVTHLM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 dGGDMfDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNkfQPGKKLTTSC 175
Cdd:cd07851   103 -GADL-NNIVKCQK-LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCEL-KILDFGLAR--HTDDEMTGYV 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC----------------------KYT 233
Cdd:cd07851   177 ATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLvgtpdeellkkissesarnyiqSLP 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907195986 234 VPPR---------VSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd07851   257 QMPKkdfkevfsgANPLAIDLLEKMLVLDPDKRITAAEALAHPYL 301
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
22-264 3.56e-25

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: 105.82  E-value: 3.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARhVFTGEKVAVKvidktKLDTLATGHLFQ----EVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVK-----RLNEMNCAASKKefltELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDYIMKHEEGLNEDLAKKY-FAQ-IVHAISYCH---KLHVVHRDLKPENVvfFEKQGLV-KLTDFGFSNKFQP---G 168
Cdd:cd14066    75 GSLEDRLHCHKGSPPLPWPQRLkIAKgIARGLEYLHeecPPPIIHGDIKSSNI--LLDEDFEpKLTDFGLARLIPPsesV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDckyTVPPRVSAGCRDLITR 248
Cdd:cd14066   153 SKTSAVKGTIGYLAPEYIRTGRV-STKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVE---WVESKGKEELEDILDK 228
                         250
                  ....*....|....*.
gi 1907195986 249 MLQRDPKRRasLEEIE 264
Cdd:cd14066   229 RLVDDDGVE--EEEVE 242
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
22-269 3.86e-25

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: 105.54  E-value: 3.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVI----------DKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd06629     9 IGKGTYGRVYLAMNATTGEMLAVKQVelpktssdraDSRQKTVVDA--LKSEIDTLKDLDHPNIVQYLGFEETEDYFSIF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKHEeGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQP--GK 169
Cdd:cd06629    87 LEYVPGGSIGSCLRKYG-KFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADN-ILVDLEGICKISDFGISKKSDDiyGN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSC-GSLAYSAPEIL--LGDEYDApAVDIWSLGVILFMLVCGQPPFqeaNDSETLTMIMDC--KYTVPP-----RVS 239
Cdd:cd06629   165 NGATSMqGSVFWMAPEVIhsQGQGYSA-KVDIWSLGCVVLEMLAGRRPW---SDDEAIAAMFKLgnKRSAPPvpedvNLS 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 240 AGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06629   241 PEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
22-275 5.35e-25

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: 105.92  E-value: 5.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTK-----------LDTLATGHlfqevRCmklvqhPNIVRLYEVIDTQTKLYL 90
Cdd:cd06618    23 IGSGTCGQVYKMRHKKTGHVMAVKQMRRSGnkeenkrilmdLDVVLKSH-----DC------PYIVKCYGYFITDSDVFI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGdgGDMFDYIMKHEEG-LNEDLAKKYFAQIVHAISYCHKLH-VVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPG 168
Cdd:cd06618    92 CMELM--STCLDKLLKRIQGpIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILL-DESGNVKLCDFGISGRLVDS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLAYSAPEIL---LGDEYDAPAvDIWSLGVILFMLVCGQPPFQEAN-DSETLTMIMDCKYTVPP---RVSAG 241
Cdd:cd06618   169 KAKTRSAGCAAYMAPERIdppDNPKYDIRA-DVWSLGISLVELATGQFPYRNCKtEFEVLTKILNEEPPSLPpneGFSPD 247
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907195986 242 CRDLITRMLQRDPKRRASLEEIESHPWLQGVDPS 275
Cdd:cd06618   248 FCSFVDLCLTKDHRYRPKYRELLQHPFIRRYETA 281
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
20-294 5.43e-25

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: 106.96  E-value: 5.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEV------IDTQTKLYLILE 93
Cdd:cd07880    21 KQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVftpdlsLDRFHDFYLVMP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGdGGDMfDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNkfQPGKKLTT 173
Cdd:cd07880   101 FM-GTDL-GKLMKHEK-LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCEL-KILDFGLAR--QTDSEMTG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP------------------ 235
Cdd:cd07880   175 YVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSkefvqklqsedaknyvkk 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 236 -------------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGV----DPSPATKY-------NIPLVSYKNLS 291
Cdd:cd07880   255 lprfrkkdfrsllPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFhdpeDETEAPPYddsfdevDQSLEEWKRLT 334

                  ...
gi 1907195986 292 EEE 294
Cdd:cd07880   335 FTE 337
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
22-269 7.03e-25

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: 105.32  E-value: 7.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMf 101
Cdd:cd06622     9 LGKGNYGSVYKVLHRPTGVTMAMKEI-RLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGSL- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIM---KHEEGLNEDLAKKYFAQIVHAISYCHKLH-VVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQpgKKLT-TSCG 176
Cdd:cd06622    87 DKLYaggVATEGIPEDVLRRITYAVVKGLKFLKEEHnIIHRDVKPTNVLV-NGNGQVKLCDFGVSGNLV--ASLAkTNIG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPE-ILLGDEYDAPAV----DIWSLGVILFMLVCGQ---PPFQEANDSETLTMIMDCKY-TVPPRVSAGCRDLIT 247
Cdd:cd06622   164 CQSYMAPErIKSGGPNQNPTYtvqsDVWSLGLSILEMALGRypyPPETYANIFAQLSAIVDGDPpTLPSGYSDDAQDFVA 243
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06622   244 KCLNKIPNRRPTYAQLLEHPWL 265
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
13-274 8.60e-25

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: 105.55  E-value: 8.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  13 AGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd07869     4 ADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVI-RLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSN-KFQPGKKL 171
Cdd:cd07869    83 EYVHT-DLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLL-ISDTGELKLADFGLARaKSVPSHTY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEAND----------------SETLTMIMDCKYTVP 235
Cdd:cd07869   161 SNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDiqdqleriflvlgtpnEDTWPGVHSLPHFKP 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 236 PRVSA-----------------GCRDLITRMLQRDPKRRASLEEIESHPWLQGVDP 274
Cdd:cd07869   241 ERFTLyspknlrqawnklsyvnHAEDLASKLLQCFPKNRLSAQAALSHEYFSDLPP 296
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
20-270 8.67e-25

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: 106.40  E-value: 8.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTklDTLATGHLFQEVRCMKLVQHPNIVRLYEV-----------IDTQTKL 88
Cdd:cd07854    11 RPLGCGSNGLVFSAVDSDCDKRVAVKKIVLT--DPQSVKHALREIKIIRRLDHDNIVKVYEVlgpsgsdltedVGSLTEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 ---YLILELGDGgDMFDYImkhEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNK 164
Cdd:cd07854    89 nsvYIVQEYMET-DLANVL---EQGpLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVLKIGDFGLARI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 165 FQPGKK----LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD----------- 229
Cdd:cd07854   165 VDPHYShkgyLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILEsvpvvreedrn 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 230 -CKYTVP------------------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd07854   245 eLLNVIPsfvrndggeprrplrdllPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
11-268 1.04e-24

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: 105.86  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  11 KIAGLYDLDKTLGRGHFA-VVKLARHVfTGEKVAVKVIdKTKLDTLATGHLfqEVRCMKLV-QHP-----NIVRLYEVID 83
Cdd:cd14226    10 KWMDRYEIDSLIGKGSFGqVVKAYDHV-EQEWVAIKII-KNKKAFLNQAQI--EVRLLELMnKHDtenkyYIVRLKRHFM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  84 TQTKLYLILELGDGgDMFDYIMK-HEEGLNEDLAKKYFAQIVHAISYCHK--LHVVHRDLKPENVVF-FEKQGLVKLTDF 159
Cdd:cd14226    86 FRNHLCLVFELLSY-NLYDLLRNtNFRGVSLNLTRKFAQQLCTALLFLSTpeLSIIHCDLKPENILLcNPKRSAIKIIDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 160 GFSNkfQPGKKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCkYTVPPRvs 239
Cdd:cd14226   165 GSSC--QLGQRIYQYIQSRFYRSPEVLLGLPYDL-AIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV-LGMPPV-- 238
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 240 agcrdlitRMLQRDPKRRASLEEIESHPW 268
Cdd:cd14226   239 --------HMLDQAPKARKFFEKLPDGTY 259
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
16-304 1.09e-24

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: 106.02  E-value: 1.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTkLDTLATGH-LFQEVRCMKLVQHPNIVRLYEVIDTQTK-----LY 89
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDV-FEHVSDATrILREIKLLRLLRHPDIVEIKHIMLPPSRrefkdIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGgDMFDYImkheeGLNEDLAKKYFA----QIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFS--- 162
Cdd:cd07859    81 VVFELMES-DLHQVI-----KANDDLTPEHHQfflyQLLRALKYIHTANVFHRDLKPKNILANADCKL-KICDFGLArva 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 163 -NKFQPGKKLTTSCGSLAYSAPEiLLGDEYD--APAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVS 239
Cdd:cd07859   154 fNDTPTAIFWTDYVATRWYRAPE-LCGSFFSkyTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 240 AGCR-------------------------------DLITRMLQRDPKRRASLEEIESHPWLQGV-----DPS--PATKYN 281
Cdd:cd07859   233 SRVRnekarrylssmrkkqpvpfsqkfpnadplalRLLERLLAFDPKDRPTAEEALADPYFKGLakverEPSaqPITKLE 312
                         330       340
                  ....*....|....*....|...
gi 1907195986 282 IPLVSYKnLSEEEHNSIIQRMVL 304
Cdd:cd07859   313 FEFERRR-LTKEDVRELIYREIL 334
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
18-271 1.13e-24

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: 106.75  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEV-----IDTQTKLYLIL 92
Cdd:cd07853     4 PDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDIlqpphIDPFEEIYVVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGgDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQP--GKK 170
Cdd:cd07853    84 ELMQS-DLHKIIVSPQP-LSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLV-NSNCVLKICDFGLARVEEPdeSKH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD-------------CK------ 231
Cdd:cd07853   161 MTQEVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDllgtpsleamrsaCEgarahi 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907195986 232 -------------YTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQG 271
Cdd:cd07853   241 lrgphkppslpvlYTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDE 293
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
70-267 1.76e-24

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: 103.21  E-value: 1.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  70 VQHPNIVRLYEV-----IDTQT-KLYLILELGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPE 143
Cdd:cd14012    55 LRHPNLVSYLAFsierrGRSDGwKVYLLTEYAPGGSLSELLDSVGS-VPLDTARRWTLQLLEALEYLHRNGVVHKSLHAG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 144 NVVFFEKQ--GLVKLTDFGFSNKFQ----PGKKLTTScgSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQE 217
Cdd:cd14012   134 NVLLDRDAgtGIVKLTDYSLGKTLLdmcsRGSLDEFK--QTYWLPPELAQGSKSPTRKTDVWDLGLLFLQMLFGLDVLEK 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907195986 218 andSETLTMIMdckytVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHP 267
Cdd:cd14012   212 ---YTSPNPVL-----VSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
22-273 2.23e-24

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: 105.08  E-value: 2.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKL----DTLATghlFQEVRCMKLVQHPN-IVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKKDVViqddDVECT---MVEKRVLALQDKPPfLTQLHSCFQTVDRLYFVMEYVN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFdYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGKKLTTSC 175
Cdd:cd05615    95 GGDLM-YHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVML-DSEGHIKIADFGMCKEhMVEGVTTRTFC 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPK 255
Cdd:cd05615   173 GTPDYIAPEIIAYQPY-GRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPA 251
                         250       260
                  ....*....|....*....|...
gi 1907195986 256 RRASL-----EEIESHPWLQGVD 273
Cdd:cd05615   252 KRLGCgpegeRDIREHAFFRRID 274
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
16-270 6.27e-24

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: 101.76  E-value: 6.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLdKTLGRGHFAVVKLARHVFTGEKVAVKVIDKT-KLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE- 93
Cdd:cd06607     4 EDL-REIGHGSFGAVYYARNKRTSEVVAIKKMSYSgKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEy 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 -LGDGGDMFDYimkHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPGkklT 172
Cdd:cd06607    83 cLGSASDIVEV---HKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTE-PGTVKLADFGSASLVCPA---N 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGSLAYSAPEILLG-DE--YDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKytvPPRVSAG-----CRD 244
Cdd:cd06607   156 SFVGTPYWMAPEVILAmDEgqYDG-KVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQND---SPTLSSGewsddFRN 231
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd06607   232 FVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
16-269 8.10e-24

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: 102.01  E-value: 8.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKT-KLDTlatgHLFQEVRCMK-LVQHPNIVRLYEV-----IDTQTKL 88
Cdd:cd06638    20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIhDIDE----EIEAEYNILKaLSDHPNVVKFYGMyykkdVKNGDQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFDYI---MKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKF 165
Cdd:cd06638    96 WLVLELCNGGSVTDLVkgfLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNIL-LTTEGGVKLVDFGVSAQL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGK-KLTTSCGSLAYSAPEIL-----LGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMImdcKYTVPPRV- 238
Cdd:cd06638   175 TSTRlRRNTSVGTPFWMAPEVIaceqqLDSTYDA-RCDVWSLGITAIELGDGDPPLADLHPMRALFKI---PRNPPPTLh 250
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907195986 239 -----SAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06638   251 qpelwSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
16-229 1.26e-23

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: 101.65  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEK-VAVKvidKTKLDT------LATGHLFQEVRCMKLVQHPNIVRLYEV-----ID 83
Cdd:cd07862     3 YECVAEIGEGAYGKVFKARDLKNGGRfVALK---RVRVQTgeegmpLSTIREVAVLRHLETFEHPNVVRLFDVctvsrTD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  84 TQTKLYLILELGDGgDMFDYIMK-HEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFS 162
Cdd:cd07862    80 RETKLTLVFEHVDQ-DLTTYLDKvPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNIL-VTSSGQIKLADFGLA 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 163 NKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD 229
Cdd:cd07862   158 RIYSFQMALTSVVVTLWYRAPEVLLQSSYATP-VDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILD 223
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
16-269 1.31e-23

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 102.06  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKV--IDKTKLDTLATG---HLFQEVRCMKLVQHPNIVRLYEVIDTQTKLY- 89
Cdd:cd14040     8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENyhkHACREYRIHKELDHPRIVKLYDYFSLDTDTFc 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKF 165
Cdd:cd14040    88 TVLEYCEGNDL-DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacGEIKITDFGLSKIM 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QP------GKKLTTS-CGSLAYSAPE-ILLGDEYD--APAVDIWSLGVILFMLVCGQPPF------QEANDSETLTMIMD 229
Cdd:cd14040   167 DDdsygvdGMDLTSQgAGTYWYLPPEcFVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPFghnqsqQDILQENTILKATE 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907195986 230 CKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14040   247 VQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
16-402 3.15e-23

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 105.97  E-value: 3.15e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYE--VIDTQTKLYLILE 93
Cdd:PTZ00266    15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDrfLNKANQKLYILME 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   94 LGDGGDM-------FDYIMKHEEGLNEDLAKkyfaQIVHAISYCHKL-------HVVHRDLKPENVVF------------ 147
Cdd:PTZ00266    95 FCDAGDLsrniqkcYKMFGKIEEHAIVDITR----QLLHALAYCHNLkdgpngeRVLHRDLKPQNIFLstgirhigkita 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  148 ----FEKQGLVKLTDFGFSNKFQPGKKLTTSCGSLAYSAPEILLGD--EYDAPAvDIWSLGVILFMLVCGQPPFQEANDS 221
Cdd:PTZ00266   171 qannLNGRPIAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLHEtkSYDDKS-DMWALGCIIYELCSGKTPFHKANNF 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  222 ETLTMIMDCKYTVPPR-VSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGVDPsPATKYNI---------PLVSYKNLS 291
Cdd:PTZ00266   250 SQLISELKRGPDLPIKgKSKELNILIKNLLNLSAKERPSALQCLGYQIIKNVGP-PVGAAGGgagvaaapgAVVARRNPS 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  292 eEEHNSIiqrmvlgdiadRDAIVEaletNRYNHITATYFLLAERILREKQEKEIQTRSASPSNikaqfRQSWPTKIDVPQ 371
Cdd:PTZ00266   329 -KEHPGL-----------QLAAME----KAKHAEAANYGISPNTLINQRNEEQHGRRSSSCAS-----RQSANNVTNITS 387
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1907195986  372 DLEDDLTATPLSHATVPQS-----PARAGDN--VLNGH 402
Cdd:PTZ00266   388 ITSVTSVASVASVASVPSKddrkyPQDGATHchAVNGH 425
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
20-273 3.52e-23

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: 100.45  E-value: 3.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHL-FQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05631     6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DM-FDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSCGS 177
Cdd:cd05631    86 DLkFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENIL-LDDRGHIRISDLGLAVQIPEGETVRGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEAND----SETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd05631   165 VGYMAPEVINNEKY-TFSPDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKN 243
                         250       260
                  ....*....|....*....|....*
gi 1907195986 254 PKRR-----ASLEEIESHPWLQGVD 273
Cdd:cd05631   244 PKERlgcrgNGAAGVKQHPIFKNIN 268
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
13-269 4.49e-23

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: 100.08  E-value: 4.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  13 AGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDtlaTGHLFQEVRCM-KLVQHPNIVRLYEVIDTQT----- 86
Cdd:cd06636    15 AGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE---EEEIKLEINMLkKYSHHRNIATYYGAFIKKSppghd 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 -KLYLILELGDGGDMFDyIMKHEEG--LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSN 163
Cdd:cd06636    92 dQLWLVMEFCGAGSVTD-LVKNTKGnaLKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE-NAEVKLVDFGVSA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQP--GKKlTTSCGSLAYSAPEILLGDE-----YDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMImdcKYTVPP 236
Cdd:cd06636   170 QLDRtvGRR-NTFIGTPYWMAPEVIACDEnpdatYDYRS-DIWSLGITAIEMAEGAPPLCDMHPMRALFLI---PRNPPP 244
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907195986 237 RV-----SAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06636   245 KLkskkwSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
20-279 4.70e-23

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 99.06  E-value: 4.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARhvFTGE-KVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05059    10 KELGSGQFGVVHLGK--WRGKiDVAIKMI---KEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSnKFQPGKKLTTSCGS- 177
Cdd:cd05059    85 CLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGE-QNVVKVSDFGLA-RYVLDDEYTSSVGTk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 --LAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTmimdckytvppRVSAGCRdlitrmLQRDP 254
Cdd:cd05059   163 fpVKWSPPEVFMYSKFSSKS-DVWSFGVLMWeVFSEGKMPYERFSNSEVVE-----------HISQGYR------LYRPH 224
                         250       260
                  ....*....|....*....|....*
gi 1907195986 255 KRRASLEEIESHPWLQGVDPSPATK 279
Cdd:cd05059   225 LAPTEVYTIMYSCWHEKPEERPTFK 249
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
16-267 5.88e-23

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: 98.53  E-value: 5.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEV-RCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVeRHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDgGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd14050    83 CD-TSLQQYCEETHS-LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPAN-IFLSKDGVCKLGDFGLVVELDKEDIHDAQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEydAPAVDIWSLGVILFMLVC------GQPPFQEANDSEtltmimdckytVPPRVSAGC----RD 244
Cdd:cd14050   160 EGDPRYMAPELLQGSF--TKAADIFSLGITILELACnlelpsGGDGWHQLRQGY-----------LPEEFTAGLspelRS 226
                         250       260
                  ....*....|....*....|...
gi 1907195986 245 LITRMLQRDPKRRASLEEIESHP 267
Cdd:cd14050   227 IIKLMMDPDPERRPTAEDLLALP 249
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
20-270 7.98e-23

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: 99.00  E-value: 7.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVID---KTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVI--DTQTKLYLILEL 94
Cdd:cd06651    13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQfdpESPETSKEVSALECEIQLLKNLQHERIVQYYGCLrdRAEKTLTIFMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYiMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ----PGKK 170
Cdd:cd06651    93 MPGGSVKDQ-LKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGNVKLGDFGASKRLQticmSGTG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMI--MDCKYTVPPRVSAGCRDLITR 248
Cdd:cd06651   171 IRSVTGTPYWMSPEVISGEGYGRKA-DVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatQPTNPQLPSHISEHARDFLGC 249
                         250       260
                  ....*....|....*....|..
gi 1907195986 249 MLQrDPKRRASLEEIESHPWLQ 270
Cdd:cd06651   250 IFV-EARHRPSAEELLRHPFAQ 270
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
22-266 9.68e-23

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: 98.33  E-value: 9.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEkvaVKVIDKTKLDTlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGK---VMVMKELKRFD-EQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDlAKKYFAQ-IVHAISYCHKLHVVHRDLKPENVVFFEKQG--LVKLTDFGFSNKF------QPGKKLT 172
Cdd:cd14065    77 ELLKSMDEQLPWS-QRVSLAKdIASGMAYLHSKNIIHRDLNSKNCLVREANRgrNAVVADFGLAREMpdektkKPDRKKR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 -TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPfqeanDSETLTMIMDCKYTVPP---RVSAGCR----D 244
Cdd:cd14065   156 lTVVGSPYWMAPEMLRGESYDE-KVDVFSFGIVLCEIIGRVPA-----DPDYLPRTMDFGLDVRAfrtLYVPDCPpsflP 229
                         250       260
                  ....*....|....*....|..
gi 1907195986 245 LITRMLQRDPKRRASLEEIESH 266
Cdd:cd14065   230 LAIRCCQLDPEKRPSFVELEHH 251
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
18-263 1.12e-22

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: 98.57  E-value: 1.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVV--KLARHVFTGE---KVAVKVIDKTKLDTLATgHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd05032    10 LIRELGQGSFGMVyeGLAKGVVKGEpetRVAIKTVNENASMRERI-EFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHEEglNEDLAKKY-----------FAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGF 161
Cdd:cd05032    89 ELMAKGDLKSYLRSRRP--EAENNPGLgpptlqkfiqmAAEIADGMAYLAAKKFVHRDLAARNCMVAE-DLTVKIGDFGM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 ------SNKFQPGKKlttscGSLA--YSAPEILLgDEYDAPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKY 232
Cdd:cd05032   166 trdiyeTDYYRKGGK-----GLLPvrWMAPESLK-DGVFTTKSDVWSFGVVLWeMATLAEQPYQGLSNEEVLKFVIDGGH 239
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907195986 233 TVPPRvsaGC----RDLITRMLQRDPKRRASLEEI 263
Cdd:cd05032   240 LDLPE---NCpdklLELMRMCWQYNPKMRPTFLEI 271
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
20-263 1.15e-22

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: 98.74  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIdkTKLDTLATGHLFQEVRCMK-LVQHPNIVRLY-------EVIDTQTKLYLI 91
Cdd:cd14036     6 RVIAEGGFAFVYEAQDVGTGKEYALKRL--LSNEEEKNKAIIQEINFMKkLSGHPNIVQFCsaasigkEESDQGQAEYLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 L-ELGDGGdMFDYIMKHEEG--LNEDLAKKYFAQIVHAISYCHK--LHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-- 164
Cdd:cd14036    84 LtELCKGQ-LVDFVKKVEAPgpFSPDTVLKIFYQTCRAVQHMHKqsPPIIHRDLKIENLLI-GNQGQIKLCDFGSATTea 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 165 FQPGKKLTTSCGSLA-----------YSAPEILlgDEYD----APAVDIWSLGVILFMLVCGQPPFQeanDSETLTmIMD 229
Cdd:cd14036   162 HYPDYSWSAQKRSLVedeitrnttpmYRTPEMI--DLYSnypiGEKQDIWALGCILYLLCFRKHPFE---DGAKLR-IIN 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907195986 230 CKYTVPP--RVSAGCRDLITRMLQRDPKRRASLEEI 263
Cdd:cd14036   236 AKYTIPPndTQYTVFHDLIRSTLKVNPEERLSITEI 271
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
20-273 1.30e-22

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: 99.28  E-value: 1.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHL-FQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05632     8 RVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMaLNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DM-FDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSCGS 177
Cdd:cd05632    88 DLkFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENIL-LDDYGHIRISDLGLAVKIPEGESIRGRVGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPF----QEANDSETLTMIMDCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd05632   167 VGYMAPEVLNNQRYTL-SPDYWGLGCLIYEMIEGQSPFrgrkEKVKREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKD 245
                         250       260
                  ....*....|....*....|....*
gi 1907195986 254 PKRRASLE-----EIESHPWLQGVD 273
Cdd:cd05632   246 PKQRLGCQeegagEVKRHPFFRNMN 270
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
22-271 1.63e-22

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: 98.26  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATgHLFQEVRCMKLVQHPNIVRLYE--VIDTQTKLYLILELGDGGD 99
Cdd:cd06621     9 LGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQK-QILRELEINKSCASPYIVKYYGafLDEQDSSIGIAMEYCEGGS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MfDYIMKHEEGLNEDLAKKYFAQIVHAI----SYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFqpGKKLT-TS 174
Cdd:cd06621    88 L-DSIYKKVKKKGGRIGEKVLGKIAESVlkglSYLHSRKIIHRDIKPSNIL-LTRKGQVKLCDFGVSGEL--VNSLAgTF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPF-----QEANDSETLTMIMDCKYTVPP-------RVSAGC 242
Cdd:cd06621   164 TGTSYYMAPERIQGGPYSITS-DVWSLGLTLLEVAQNRFPFppegePPLGPIELLSYIVNMPNPELKdepengiKWSESF 242
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 243 RDLITRMLQRDPKRRASLEEIESHPWLQG 271
Cdd:cd06621   243 KDFIEKCLEKDGTRRPGPWQMLAHPWIKA 271
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
22-269 1.64e-22

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: 98.21  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd06642    12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSAL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPGK-KLTTSCGSLAY 180
Cdd:cd06642    91 DLLKPGP--LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSE-QGDVKLADFGVAGQLTDTQiKRNTFVGTPFW 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMI-MDCKYTVPPRVSAGCRDLITRMLQRDPKRRAS 259
Cdd:cd06642   168 MAPEVIKQSAYDFKA-DIWSLGITAIELAKGEPPNSDLHPMRVLFLIpKNSPPTLEGQHSKPFKEFVEACLNKDPRFRPT 246
                         250
                  ....*....|
gi 1907195986 260 LEEIESHPWL 269
Cdd:cd06642   247 AKELLKHKFI 256
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
22-263 1.69e-22

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: 97.80  E-value: 1.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAvvKLARHVFTGEKVAVKVI--DKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd14146     2 IGVGGFG--KVYRATWKGQEVAVKAArqDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNEDLAKK--------YFAQIVHAISYCHK---LHVVHRDLKPENVVFFEK-------QGLVKLTDFGF 161
Cdd:cd14146    80 LNRALAAANAAPGPRRARRipphilvnWAVQIARGMLYLHEeavVPILHRDLKSSNILLLEKiehddicNKTLKITDFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 SNKFQPGKKLTTScGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPprVSAG 241
Cdd:cd14146   160 AREWHRTTKMSAA-GTYAWMAPEVIKSSLF-SKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTLP--IPST 235
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 242 CRDLITRML----QRDPKRRASLEEI 263
Cdd:cd14146   236 CPEPFAKLMkecwEQDPHIRPSFALI 261
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
22-269 2.02e-22

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: 97.51  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARhVFTGEKVAVKVIDKTKLDTLATGHLFQ----EVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDG 97
Cdd:cd06631     9 LGKGAYGTVYCGL-TSTGQLIAVKQVELDTSDKEKAEKEYEklqeEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFeKQGLVKLTDFGFSNKF-------QPGKK 170
Cdd:cd06631    88 GSIAS-ILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLM-PNGVIKLIDFGCAKRLcinlssgSQSQL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP---RVSAGCRDLIT 247
Cdd:cd06631   166 LKSMRGTPYWMAPEVINETGHGRKS-DIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRlpdKFSPEARDFVH 244
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06631   245 ACLTRDQDERPSAEQLLKHPFI 266
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
16-266 2.90e-22

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: 97.18  E-value: 2.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDktkldtLATGHLFQEVRCMKLVQHPNIVRLY-------EVIDTQTK- 87
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK------LNNEKAEREVKALAKLDHPNIVRYNgcwdgfdYDPETSSSn 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 --------LYLILELGDGGDMFDYIMKHEEGLNEDL-AKKYFAQIVHAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTD 158
Cdd:cd14047    82 ssrsktkcLFIQMEFCEKGTLESWIEKRNGEKLDKVlALEIFEQITKGVEYIHSKKLIHRDLKPSNI-FLVDTGKVKIGD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 159 FGFSNKFQPGKKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSET------LTMIMDCKY 232
Cdd:cd14047   161 FGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGK-EVDIYALGLILFELLHVCDSAFEKSKFWTdlrngiLPDIFDKRY 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907195986 233 TVPprvsagcRDLITRMLQRDPKRRASLEEIESH 266
Cdd:cd14047   240 KIE-------KTIIKKMLSKKPEDRPNASEILRT 266
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
22-266 3.03e-22

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: 96.41  E-value: 3.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARhvFTGEKVAVKVIDKTKlDTlatghlfqEVRCMKLVQHPNIVRLYEVIdTQTKLYLIL-ELGDGGDM 100
Cdd:cd14059     1 LGSGAQGAVFLGK--FRGEEVAVKKVRDEK-ET--------DIKHLRKLNHPNIIKFKGVC-TQAPCYCILmEYCPYGQL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDyIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLTTSCGSLAY 180
Cdd:cd14059    69 YE-VLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLV-TYNDVLKISDFGTSKELSEKSTKMSFAGTVAW 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLgDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMI--MDCKYTVPPRVSAGCRDLITRMLQRDPKRRA 258
Cdd:cd14059   147 MAPEVIR-NEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVgsNSLQLPVPSTCPDGFKLLMKQCWNSKPRNRP 225

                  ....*...
gi 1907195986 259 SLEEIESH 266
Cdd:cd14059   226 SFRQILMH 233
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
20-223 3.24e-22

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 96.87  E-value: 3.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARhvFTGE-KVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd05113    10 KELGTGQFGVVKYGK--WRGQyDVAIKMI---KEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSnKFQPGKKLTTSCGS- 177
Cdd:cd05113    85 CLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCL-VNDQGVVKVSDFGLS-RYVLDDEYTSSVGSk 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907195986 178 --LAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSET 223
Cdd:cd05113   163 fpVRWSPPEVLMYSKFSSKS-DVWAFGVLMWeVYSLGKMPYERFTNSET 210
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
20-269 4.07e-22

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: 97.07  E-value: 4.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd06641    10 EKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYImkhEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPGK-KLTTSCGS 177
Cdd:cd06641    89 ALDLL---EPGpLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSE-HGEVKLADFGVAGQLTDTQiKRN*FVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMImdcKYTVPPRV----SAGCRDLITRMLQRD 253
Cdd:cd06641   165 PFWMAPEVIKQSAYDSKA-DIWSLGITAIELARGEPPHSELHPMKVLFLI---PKNNPPTLegnySKPLKEFVEACLNKE 240
                         250
                  ....*....|....*.
gi 1907195986 254 PKRRASLEEIESHPWL 269
Cdd:cd06641   241 PSFRPTAKELLKHKFI 256
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
22-263 4.33e-22

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: 96.59  E-value: 4.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAvvKLARHVFTGEKVAVKVI--DKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGd 99
Cdd:cd14148     2 IGVGGFG--KVYKGLWRGEEVAVKAArqDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGG- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 mfdyimkheeGLNEDLAKK---------YFAQIVHAISYCHK---LHVVHRDLKPENVVFFEK-------QGLVKLTDFG 160
Cdd:cd14148    79 ----------ALNRALAGKkvpphvlvnWAVQIARGMNYLHNeaiVPIIHRDLKSSNILILEPienddlsGKTLKITDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 FSNKFQPGKKLTTScGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPprVSA 240
Cdd:cd14148   149 LAREWHKTTKMSAA-GTYAWMAPEVIRLSLF-SKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLP--IPS 224
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 241 GCRDLITRMLQR----DPKRRASLEEI 263
Cdd:cd14148   225 TCPEPFARLLEEcwdpDPHGRPDFGSI 251
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
20-266 4.33e-22

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: 96.87  E-value: 4.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDtLATGHLFQEVRCMKLVQHPNIVRLY------------EVIDtQTK 87
Cdd:cd14048    12 QCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNE-LAREKVLREVRALAKLDHPGIVRYFnawlerppegwqEKMD-EVY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGGDMFDYIMKHEEGLNEDLA--KKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKF 165
Cdd:cd14048    90 LYIQMQLCRKENLKDWMNRRCTMESRELFvcLNIFKQIASAVEYLHSKGLIHRDLKPSN-VFFSLDDVVKVGDFGLVTAM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGK-------------KLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCgqpPFQEAndSETLTMIMDC-K 231
Cdd:cd14048   169 DQGEpeqtvltpmpayaKHTGQVGTRLYMSPEQIHGNQY-SEKVDIFALGLILFELIY---SFSTQ--MERIRTLTDVrK 242
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907195986 232 YTVPPRVSAGC---RDLITRMLQRDPKRRASLEEIESH 266
Cdd:cd14048   243 LKFPALFTNKYpeeRDMVQQMLSPSPSERPEAHEVIEH 280
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
20-208 5.63e-22

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: 96.68  E-value: 5.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVF----TGEKVAVKVIDKTKLDTLATGhLFQEVRCMKLVQHPNIVRLYEVIDTQTK--LYLILE 93
Cdd:cd05038    10 KQLGEGHFGSVELCRYDPlgdnTGEQVAVKSLQPSGEEQHMSD-FKREIEILRTLDHEYIVKYKGVCESPGRrsLRLIME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSnKFQPGKKLTT 173
Cdd:cd05038    89 YLPSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNIL-VESEDLVKISDFGLA-KVLPEDKEYY 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYS-----APEILLGDEYDApAVDIWSLGVILFML 208
Cdd:cd05038   167 YVKEPGESpifwyAPECLRESRFSS-ASDVWSFGVTLYEL 205
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
16-267 7.06e-22

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: 96.34  E-value: 7.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFA-VVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEV---RCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14052     2 FANVELIGSGEFSqVYKVSERVPTGKVYAVKKLKPNYAGAKDRLRRLEEVsilRELTLDGHDNIVQLIDSWEYHGHLYIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDM--FDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFqPGK 169
Cdd:cd14052    82 TELCENGSLdvFLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPAN-VLITFEGTLKIGDFGMATVW-PLI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-------GQPPFQEAND--------SETLTMIMDCKYTV 234
Cdd:cd14052   160 RGIEREGDREYIAPEILSEHMYDKPA-DIFSLGLILLEAAAnvvlpdnGDAWQKLRSGdlsdaprlSSTDLHSASSPSSN 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907195986 235 PPRV---SAGCRDLITRMLQR----DPKRRASLEEIESHP 267
Cdd:cd14052   239 PPPDppnMPILSGSLDRVVRWmlspEPDRRPTADDVLATP 278
UBA_SNRK cd14339
UBA domain of SNF-related serine/threonine-protein kinase (SNRK) and similar proteins mainly ...
288-335 9.39e-22

UBA domain of SNF-related serine/threonine-protein kinase (SNRK) and similar proteins mainly found in metazoa; SNRK, also called Sucrose nonfermenting 1 (Snf1)-related kinase, is a serine/threonine kinase highly expressed in the testis. It is a distant member of the largely adenosine monophosphate (AMP)-activated protein kinase (AMPK) family. SNRK can be phosphorylated and activated by LKB1 and may mediate cellular effects regulated by LKB1. It is also involved in the regulation of colon cancer cell proliferation and beta-catenin signaling. It inhibits colon cancer cell proliferation through calcyclin-binding protein (CacyBP)-dependent reduction of beta-catenin. In addition to an N-terminal protein kinase domain, it harbors an ubiquitin-associated (UBA) domain, previously called SNF1 homology (SNH) domain which is conserved in other Snf1-related kinases, but not in any other protein kinase.


Pssm-ID: 270524  Cd Length: 48  Bit Score: 88.81  E-value: 9.39e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907195986 288 KNLSEEEHNSIIQRMVLGDIADRDAIVEALETNRYNHITATYFLLAER 335
Cdd:cd14339     1 ENLPEEEHELILQKMESGGIASREAILESLEKDAYDHITATYYLLAER 48
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
21-269 9.74e-22

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: 96.10  E-value: 9.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  21 TLGRGHFAVVKLARHVFTGEKVAVKVIdktKLDTLA--TGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd06619     8 ILGHGNGGTVYKAYHLLTRRILAVKVI---PLDITVelQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 --DMFDYIMKHEEGlnedlakKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQpGKKLTTSCG 176
Cdd:cd06619    85 slDVYRKIPEHVLG-------RIAVAVVKGLTYLWSLKILHRDVKPSNML-VNTRGQVKLCDFGVSTQLV-NSIAKTYVG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTM---IMDC-KYTVPPRVSAG-----CRDLIT 247
Cdd:cd06619   156 TNAYMAPERISGEQYGIHS-DVWSLGISFMELALGRFPYPQIQKNQGSLMplqLLQCiVDEDPPVLPVGqfsekFVHFIT 234
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 RMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06619   235 QCMRKQPKERPAPENLMDHPFI 256
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
20-265 1.12e-21

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: 95.49  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHvFTGEKVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd05072    13 KKLGAGQFGEVWMGYY-NNSTKVAVKTL---KPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYiMKHEEGLNEDLAK--KYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQpGKKLTTSCGS 177
Cdd:cd05072    89 LLDF-LKSDEGGKVLLPKliDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESL-MCKIADFGLARVIE-DNEYTAREGA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 ---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMIMDcKYTVP--PRVSAGCRDLITRMLQ 251
Cdd:cd05072   166 kfpIKWTAPEAINFGSFTIKS-DVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQR-GYRMPrmENCPDELYDIMKTCWK 243
                         250
                  ....*....|....
gi 1907195986 252 RDPKRRASLEEIES 265
Cdd:cd05072   244 EKAEERPTFDYLQS 257
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
16-266 1.16e-21

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: 95.83  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGhlFQEVRCMKLVQHPNIVRLY-----EVIDTQTKLYL 90
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEA--MREIENYRLFNHPNILRLLdsqivKEAGGKKEVYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGG---DMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVV---HRDLKPENVVFFEkQGLVKLTDFGFSNK 164
Cdd:cd13986    80 LLPYYKRGslqDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSE-DDEPILMDLGSMNP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 165 ----------FQPGKKLTTSCGSLAYSAPEiLLGDEYDA---PAVDIWSLGVILFMLVCGQPPFQ---EANDSETLTmIM 228
Cdd:cd13986   159 arieiegrreALALQDWAAEHCTMPYRAPE-LFDVKSHCtidEKTDIWSLGCTLYALMYGESPFErifQKGDSLALA-VL 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907195986 229 DCKYTVP--PRVSAGCRDLITRMLQRDPKRRASLEEIESH 266
Cdd:cd13986   237 SGNYSFPdnSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
18-263 1.63e-21

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: 95.11  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAvvKLARHVFTGEKVAVKVI----DKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd14145    10 LEEIIGIGGFG--KVYRAIWIGDEVAVKAArhdpDEDISQTIEN--VRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEegLNEDLAKKYFAQIVHAISYCHK---LHVVHRDLKPENVVFFEK-------QGLVKLTDFGFSN 163
Cdd:cd14145    86 FARGGPLNRVLSGKR--IPPDILVNWAVQIARGMNYLHCeaiVPVIHRDLKSSNILILEKvengdlsNKILKITDFGLAR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQPGKKLTTScGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPprVSAGCR 243
Cdd:cd14145   164 EWHRTTKMSAA-GTYAWMAPEVIRSSMF-SKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSLP--IPSTCP 239
                         250       260
                  ....*....|....*....|....
gi 1907195986 244 DLITRMLQR----DPKRRASLEEI 263
Cdd:cd14145   240 EPFARLMEDcwnpDPHSRPPFTNI 263
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
16-295 1.71e-21

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: 97.02  E-value: 1.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------Y 89
Cdd:cd07876    23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLeefqdvY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGgDMFDYImkHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGK 169
Cdd:cd07876   103 LVMELMDA-NLCQVI--HME-LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIV-VKSDCTLKILDFGLARTACTNF 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQ------------EANDSETLTMIMDCKYTVPPR 237
Cdd:cd07876   178 MMTPYVVTRYYRAPEVILGMGYKE-NVDIWSVGCIMGELVKGSVIFQgtdhidqwnkviEQLGTPSAEFMNRLQPTVRNY 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 238 V------------------------------SAGCRDLITRMLQRDPKRRASLEEIESHPWLQ-GVDPSPAtKYNIPLVS 286
Cdd:cd07876   257 VenrpqypgisfeelfpdwifpseserdklkTSQARDLLSKMLVIDPDKRISVDEALRHPYITvWYDPAEA-EAPPPQIY 335

                  ....*....
gi 1907195986 287 YKNLSEEEH 295
Cdd:cd07876   336 DAQLEEREH 344
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
20-263 2.04e-21

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 94.23  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAKFL-QEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQPGkkLTTSCGSL- 178
Cdd:cd05084    81 FLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKN-VLKISDFGMSREEEDG--VYAATGGMk 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 ----AYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKYTVPPRvsaGCRDLITRMLQR- 252
Cdd:cd05084   158 qipvKWTAPEALNYGRYSSES-DVWSFGILLWeTFSLGAVPYANLSNQQTREAVEQGVRLPCPE---NCPDEVYRLMEQc 233
                         250
                  ....*....|....
gi 1907195986 253 ---DPKRRASLEEI 263
Cdd:cd05084   234 weyDPRKRPSFSTV 247
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
22-263 2.49e-21

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 94.05  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKFL-QEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKfQPGKKLTTSCG----S 177
Cdd:cd05041    82 TFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGEN-NVLKISDFGMSRE-EEDGEYTVSDGlkqiP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 LAYSAPEILLGDEYDApAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMImDCKYTVPPrvSAGCRDLITRMLQR---- 252
Cdd:cd05041   160 IKWTAPEALNYGRYTS-ESDVWSFGILLWeIFSLGATPYPGMSNQQTREQI-ESGYRMPA--PELCPEAVYRLMLQcway 235
                         250
                  ....*....|.
gi 1907195986 253 DPKRRASLEEI 263
Cdd:cd05041   236 DPENRPSFSEI 246
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
107-257 2.66e-21

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: 94.78  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 107 HEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFsnkfqpGKKL-------TTSCGSLA 179
Cdd:cd13974   125 REKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRKITITNFCL------GKHLvseddllKDQRGSPA 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 180 YSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPP--RVSAGCRDLITRMLQRDPKRR 257
Cdd:cd13974   199 YISPDVLSGKPYLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKR 278
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
13-270 2.96e-21

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: 94.67  E-value: 2.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  13 AGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDK-TKLDTlatgHLFQEVRCMK-LVQHPNIVRLYEVIDTQTK--- 87
Cdd:cd06639    21 SDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPiSDVDE----EIEAEYNILRsLPNHPNVVKFYGMFYKADQyvg 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 --LYLILELGDGG---DMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFS 162
Cdd:cd06639    97 gqLWLVLELCNGGsvtELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILL-TTEGGVKLVDFGVS 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 163 NKFQPGK-KLTTSCGSLAYSAPEILLGDE-----YDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMImdcKYTVPP 236
Cdd:cd06639   176 AQLTSARlRRNTSVGTPFWMAPEVIACEQqydysYDA-RCDVWSLGITAIELADGDPPLFDMHPVKALFKI---PRNPPP 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907195986 237 RV---SAGCRD---LITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd06639   252 TLlnpEKWCRGfshFISQCLIKDFEKRPSVTHLLEHPFIK 291
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
16-302 3.31e-21

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 97.03  E-value: 3.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVK-VIDKTKLDTlatghlfQEVRCMKLVQHPNIVRLYEVIDTQT------KL 88
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKkVLQDPQYKN-------RELLIMKNLNHINIIFLKDYYYTECfkknekNI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILelgdggdMFDYI-------MKHEEGLNEDL----AKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLT 157
Cdd:PTZ00036  141 FLNV-------VMEFIpqtvhkyMKHYARNNHALplflVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLKLC 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 158 DFGFSNKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM--------- 228
Cdd:PTZ00036  214 DFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIqvlgtpted 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 229 --------------------DCKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQGV-DPS-PATKYNIPLVS 286
Cdd:PTZ00036  294 qlkemnpnyadikfpdvkpkDLKKVFPKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLrDPCiKLPKYIDKLPD 373
                         330
                  ....*....|....*.
gi 1907195986 287 YKNLSEEEhnsiIQRM 302
Cdd:PTZ00036  374 LFNFCDAE----IKEM 385
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
16-269 3.89e-21

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: 94.74  E-value: 3.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKV--IDKTKLDTLATG---HLFQEVRCMKLVQHPNIVRLYEVIDTQTKLY- 89
Cdd:cd14041     8 YLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNWRDEKKENyhkHACREYRIHKELDHPRIVKLYDYFSLDTDSFc 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKF 165
Cdd:cd14041    88 TVLEYCEGNDL-DFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTacGEIKITDFGLSKIM 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QP-------GKKLTTS-CGSLAYSAPE-ILLGDEYD--APAVDIWSLGVILFMLVCGQPPF------QEANDSETLTMIM 228
Cdd:cd14041   167 DDdsynsvdGMELTSQgAGTYWYLPPEcFVVGKEPPkiSNKVDVWSVGVIFYQCLYGRKPFghnqsqQDILQENTILKAT 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907195986 229 DCKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14041   247 EVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
20-265 3.98e-21

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 93.44  E-value: 3.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLArhVFTGE-KVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIdTQTKLYLILELGDGG 98
Cdd:cd14203     1 VKLGQGCFGEVWMG--TWNGTtKVAIKTL---KPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVV-SEEPIYIVTEFMSKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYiMKHEEGLNEDLAK--KYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkqGLV-KLTDFGFS-----NKFQP--G 168
Cdd:cd14203    75 SLLDF-LKDGEGKYLKLPQlvDMAAQIASGMAYIERMNYIHRDLRAANILVGD--NLVcKIADFGLArliedNEYTArqG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLttscgSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMI-----MDCkytvPPRVSAGC 242
Cdd:cd14203   152 AKF-----PIKWTAPEAALYGRFTIKS-DVWSFGILLTELVTkGRVPYPGMNNREVLEQVergyrMPC----PPGCPESL 221
                         250       260
                  ....*....|....*....|...
gi 1907195986 243 RDLITRMLQRDPKRRASLEEIES 265
Cdd:cd14203   222 HELMCQCWRKDPEERPTFEYLQS 244
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
20-296 4.11e-21

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: 95.17  E-value: 4.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------YLILE 93
Cdd:cd07850     6 KPIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLeefqdvYLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGG--DMFDYIMKHEEglnedlaKKYFA-QIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNKFQPGKK 170
Cdd:cd07850    86 LMDANlcQVIQMDLDHER-------MSYLLyQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTL-KILDFGLARTAGTSFM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD------------CKYTV---- 234
Cdd:cd07850   158 MTPYVVTRYYRAPEVILGMGYKE-NVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEqlgtpsdefmsrLQPTVrnyv 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 235 --------------------PP-------RVSAGCRDLITRMLQRDPKRRASLEEIESHPWL-QGVDPS----PAtkyni 282
Cdd:cd07850   237 enrpkyagysfeelfpdvlfPPdseehnkLKASQARDLLSKMLVIDPEKRISVDDALQHPYInVWYDPSeveaPP----- 311
                         330
                  ....*....|....
gi 1907195986 283 PLVSYKNLSEEEHN 296
Cdd:cd07850   312 PAPYDHSIDEREHT 325
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
22-274 4.63e-21

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 94.72  E-value: 4.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKT-KLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE--LGDGG 98
Cdd:cd06633    29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSgKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEycLGSAS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDYimkHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKFQPGKKLTtscGSL 178
Cdd:cd06633   109 DLLEV---HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP-GQVKLADFGSASIASPANSFV---GTP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLG-DE--YDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIM--DCKYTVPPRVSAGCRDLITRMLQRD 253
Cdd:cd06633   182 YWMAPEVILAmDEgqYDG-KVDIWSLGITCIELAERKPPLFNMNAMSALYHIAqnDSPTLQSNEWTDSFRGFVDYCLQKI 260
                         250       260
                  ....*....|....*....|.
gi 1907195986 254 PKRRASLEEIESHPWLQGVDP 274
Cdd:cd06633   261 PQERPSSAELLRHDFVRRERP 281
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
20-265 4.73e-21

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 93.18  E-value: 4.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEK---VAVKVIDKTKLDTLaTGHLFQEVRCMKLVQHPNIVRLYEVIDTQTkLYLILELGD 96
Cdd:cd05060     1 KELGHGNFGSVRKGVYLMKSGKeveVAVKTLKQEHEKAG-KKEFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEEGLNEDLaKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKL--TTS 174
Cdd:cd05060    79 LGPLLKYLKKRREIPVSDL-KELAHQVAMGMAYLESKHFVHRDLAARNVL-LVNRHQAKISDFGMSRALGAGSDYyrATT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGS--LAYSAPEILLGDEYDApAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMI-----MDCkytvPPRVSAGCRDLI 246
Cdd:cd05060   157 AGRwpLKWYAPECINYGKFSS-KSDVWSYGVTLWeAFSYGAKPYGEMKGPEVIAMLesgerLPR----PEECPQEIYSIM 231
                         250
                  ....*....|....*....
gi 1907195986 247 TRMLQRDPKRRASLEEIES 265
Cdd:cd05060   232 LSCWKYRPEDRPTFSELES 250
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
22-274 4.85e-21

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: 95.11  E-value: 4.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------YLILELG 95
Cdd:cd07877    25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLeefndvYLVTHLM 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 dGGDMfDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNkfQPGKKLTTSC 175
Cdd:cd07877   105 -GADL-NNIVKCQK-LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCEL-KILDFGLAR--HTDDEMTGYV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV-----SAGCR------- 243
Cdd:cd07877   179 ATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELlkkisSESARnyiqslt 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907195986 244 -------------------DLITRMLQRDPKRRASLEEIESHPWL-QGVDP 274
Cdd:cd07877   259 qmpkmnfanvfiganplavDLLEKMLVLDSDKRITAAQALAHAYFaQYHDP 309
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
13-270 6.24e-21

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: 94.02  E-value: 6.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  13 AGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDtlaTGHLFQEVRCM-KLVQHPNIVRLYEVIDTQT----- 86
Cdd:cd06637     5 AGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDE---EEEIKQEINMLkKYSHHRNIATYYGAFIKKNppgmd 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 -KLYLILELGDGGDMFDYImKHEEG--LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSN 163
Cdd:cd06637    82 dQLWLVMEFCGAGSVTDLI-KNTKGntLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTE-NAEVKLVDFGVSA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 164 KFQP--GKKlTTSCGSLAYSAPEILLGDE-----YDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMImdcKYTVPP 236
Cdd:cd06637   160 QLDRtvGRR-NTFIGTPYWMAPEVIACDEnpdatYDFKS-DLWSLGITAIEMAEGAPPLCDMHPMRALFLI---PRNPAP 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907195986 237 RV-----SAGCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd06637   235 RLkskkwSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIR 273
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
22-274 9.14e-21

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: 94.35  E-value: 9.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------YLILELG 95
Cdd:cd07878    23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSIenfnevYLVTNLM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 dGGDMfDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNkfQPGKKLTTSC 175
Cdd:cd07878   103 -GADL-NNIVKCQK-LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCEL-RILDFGLAR--QADDEMTGYV 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV-----SAGCR------- 243
Cdd:cd07878   177 ATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVlkkisSEHARkyiqslp 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907195986 244 -------------------DLITRMLQRDPKRRASLEEIESHPWL-QGVDP 274
Cdd:cd07878   257 hmpqqdlkkifrganplaiDLLEKMLVLDSDKRISASEALAHPYFsQYHDP 307
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
22-263 9.35e-21

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: 92.46  E-value: 9.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAvvKLARHVFTGEKVAVKVIDKTKLD--TLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGd 99
Cdd:cd14061     2 IGVGGFG--KVYRGIWRGEEVAVKAARQDPDEdiSVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGG- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 mfdyimkheeGLNEDLAKK---------YFAQIVHAISYCHK---LHVVHRDLKPENVVFFEK-------QGLVKLTDFG 160
Cdd:cd14061    79 ----------ALNRVLAGRkipphvlvdWAIQIARGMNYLHNeapVPIIHRDLKSSNILILEAienedleNKTLKITDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 FSNKFQPGKKLTTScGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQE----------ANDSETLTMIMDC 230
Cdd:cd14061   149 LAREWHKTTRMSAA-GTYAWMAPEVIKSSTF-SKASDVWSYGVLLWELLTGEVPYKGidglavaygvAVNKLTLPIPSTC 226
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907195986 231 kytvpPRVSAgcrDLITRMLQRDPKRRASLEEI 263
Cdd:cd14061   227 -----PEPFA---QLMKDCWQPDPHDRPSFADI 251
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
20-263 1.22e-20

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: 92.02  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKlaRHVFTGE-----KVAVKVIDKTKLDTLAT-GHLFQEVRCMKLVQHPNIVRLYEVIDTQtKLYLILE 93
Cdd:cd05040     1 EKLGDGSFGVVR--RGEWTTPsgkviQVAVKCLKSDVLSQPNAmDDFLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMVTE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSN---------K 164
Cdd:cd05040    78 LAPLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKD-KVKIGDFGLMRalpqnedhyV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 165 FQPGKKLttscgSLAYSAPEILLGDEYdAPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMImDCKYTVPPRVSAGCR 243
Cdd:cd05040   157 MQEHRKV-----PFAWCAPESLKTRKF-SHASDVWMFGVTLWeMFTYGEEPWLGLNGSQILEKI-DKEGERLERPDDCPQ 229
                         250       260
                  ....*....|....*....|...
gi 1907195986 244 DLITRMLQ---RDPKRRASLEEI 263
Cdd:cd05040   230 DIYNVMLQcwaHKPADRPTFVAL 252
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
17-278 1.26e-20

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: 93.51  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  17 DLDKTLGRG--HFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd08216     1 ELLYEIGKCfkGGGVVHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKH-EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKF-QPGKKLT 172
Cdd:cd08216    81 MAYGSCRDLLKTHfPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGD-GKVVLSGLRYAYSMvKHGKRQR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 T-------SCGSLAYSAPEIL----LGdeYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLT--------MIMDCKyT 233
Cdd:cd08216   160 VvhdfpksSEKNLPWLSPEVLqqnlLG--YNEKS-DIYSVGITACELANGVVPFSDMPATQMLLekvrgttpQLLDCS-T 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195986 234 VPP---------------RVSAGCRDLI-TRM------------LQRDPKRRASLEEIESHPWLQGVDPSPAT 278
Cdd:cd08216   236 YPLeedsmsqsedsstehPNNRDTRDIPyQRTfseafhqfvelcLQRDPELRPSASQLLAHSFFKQCRRSNTS 308
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
20-265 1.53e-20

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


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 91.58  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAvvklarHVFTGE-----KVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05034     1 KKLGAGQFG------EVWMGVwngttKVAVKTL---KPGTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTEL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYiMKHEEGLNEDLAK--KYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQPGkKLT 172
Cdd:cd05034    72 MSKGSLLDY-LRTGEGRALRLPQliDMAAQIASGMAYLESRNYIHRDLAARNILVGENN-VCKVADFGLARLIEDD-EYT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGS---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMImDCKYTVP-PrvsAGCRDLIT 247
Cdd:cd05034   149 AREGAkfpIKWTAPEAALYGRFTIKS-DVWSFGILLYEIVTyGRVPYPGMTNREVLEQV-ERGYRMPkP---PGCPDELY 223
                         250       260
                  ....*....|....*....|..
gi 1907195986 248 R-MLQ---RDPKRRASLEEIES 265
Cdd:cd05034   224 DiMLQcwkKEPEERPTFEYLQS 245
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
22-270 1.56e-20

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: 92.81  E-value: 1.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTkLDTLATGHLFQEVRC-MKLVQHPNIVRLYEVIDTQTKLYLILELGDGG-D 99
Cdd:cd06616    14 IGRGAFGTVNKMLHKPSGTIMAVKRIRST-VDEKEQKRLLMDLDVvMRSSDCPYIVKFYGALFREGDCWICMELMDISlD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFdYIMKHEEG---LNEDLAKKYFAQIVHAISYCHK-LHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd06616    93 KF-YKYVYEVLdsvIPEEILGKIAVATVKALNYLKEeLKIIHRDVKPSNILL-DRNGNIKLCDFGISGQLVDSIAKTRDA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILL----GDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDS-ETLTMIMdckYTVPPR--------VSAGC 242
Cdd:cd06616   171 GCRPYMAPERIDpsasRDGYDVRS-DVWSLGITLYEVATGKFPYPKWNSVfDQLTQVV---KGDPPIlsnseereFSPSF 246
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 243 RDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd06616   247 VNFVNLCLIKDESKRPKYKELLKHPFIK 274
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
20-269 1.58e-20

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: 93.40  E-value: 1.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVI-------DKTKLdtlatghlfqEVRCMKLVQH------PNIVRLYEVIDTQT 86
Cdd:cd14134    18 RLLGEGTFGKVLECWDRKRKRYVAVKIIrnvekyrEAAKI----------EIDVLETLAEkdpngkSHCVQLRDWFDYRG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  87 KLYLILELGdGGDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVF----FEKQGL-------- 153
Cdd:cd14134    88 HMCIVFELL-GPSLYDFLKKNNyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdYVKVYNpkkkrqir 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 154 ------VKLTDFG---FSNKFQpgkklTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETL 224
Cdd:cd14134   167 vpkstdIKLIDFGsatFDDEYH-----SSIVSTRHYRAPEVILGLGWSYPC-DVWSIGCILVELYTGELLFQTHDNLEHL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 225 TMI----------M------DCKY---------------------TVPPRVSAGCR----------DLITRMLQRDPKRR 257
Cdd:cd14134   241 AMMerilgplpkrMirrakkGAKYfyfyhgrldwpegsssgrsikRVCKPLKRLMLlvdpehrllfDLIRKMLEYDPSKR 320
                         330
                  ....*....|..
gi 1907195986 258 ASLEEIESHPWL 269
Cdd:cd14134   321 ITAKEALKHPFF 332
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
18-265 2.44e-20

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: 91.71  E-value: 2.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFA-VVKLARHVFTGEKVAVKVIDKTKLDTLATGHLF-QEVRCMKLVQHPNIVRLYEVIdTQTKLYLILELG 95
Cdd:cd05056    10 LGRCIGEGQFGdVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFlQEAYIMRQFDHPHIVKLIGVI-TENPVWIVMELA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd05056    89 PLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPD-CVKLGDFGLSRYMEDESYYKASK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSL--AYSAPEILLGDEYDApAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMI-----MDCKYTVPPRVSAgcrdLIT 247
Cdd:cd05056   168 GKLpiKWMAPESINFRRFTS-ASDVWMFGVCMWeILMLGVKPFQGVKNNDVIGRIengerLPMPPNCPPTLYS----LMT 242
                         250
                  ....*....|....*...
gi 1907195986 248 RMLQRDPKRRASLEEIES 265
Cdd:cd05056   243 KCWAYDPSKRPRFTELKA 260
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
16-209 3.20e-20

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: 92.23  E-value: 3.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATGHL-FQEVRCMKLV--QHPNIVRLYE------------ 80
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVK---KIRCNAPENVELaLREFWALSSIqrQHPNVIQLEEcvlqrdglaqrm 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  81 ------------VIDTQTK------------LYLILELGDGGDMFDYIMKHEEglNEDLAKKYFAQIVHAISYCHKLHVV 136
Cdd:cd13977    79 shgssksdlyllLVETSLKgercfdprsacyLWFVMEFCDGGDMNEYLLSRRP--DRQTNTSFMLQLSSALAFLHRNQIV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 137 HRDLKPENVVFFEKQG--LVKLTDFGFS--------NKFQPGK----KLTTSCGSLAYSAPEILLGdEYDAPAvDIWSLG 202
Cdd:cd13977   157 HRDLKPDNILISHKRGepILKVADFGLSkvcsgsglNPEEPANvnkhFLSSACGSDFYMAPEVWEG-HYTAKA-DIFALG 234

                  ....*..
gi 1907195986 203 VILFMLV 209
Cdd:cd13977   235 IIIWAMV 241
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
18-265 4.08e-20

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 90.86  E-value: 4.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLA---RHVftgeKVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIdTQTKLYLILEL 94
Cdd:cd05073    15 LEKKLGAGQFGEVWMAtynKHT----KVAVKTM---KPGSMSVEAFLAEANVMKTLQHDKLVKLHAVV-TKEPIYIITEF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYiMKHEEGLNEDLAK--KYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLT 172
Cdd:cd05073    87 MAKGSLLDF-LKSDEGSKQPLPKliDFSAQIAEGMAFIEQRNYIHRDLRAANIL-VSASLVCKIADFGLARVIEDNEYTA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 TSCGS--LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMiMDCKYTVPPRVSA--GCRDLIT 247
Cdd:cd05073   165 REGAKfpIKWTAPEAINFGSFTIKS-DVWSFGILLMEIVTyGRIPYPGMSNPEVIRA-LERGYRMPRPENCpeELYNIMM 242
                         250
                  ....*....|....*...
gi 1907195986 248 RMLQRDPKRRASLEEIES 265
Cdd:cd05073   243 RCWKNRPEERPTFEYIQS 260
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
16-269 4.19e-20

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 91.87  E-value: 4.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVID------KTKLDTLatgHLFQEVRCMKLVQHP--NIVRLYEVIDTQ-- 85
Cdd:cd14136    12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKsaqhytEAALDEI---KLLKCVREADPKDPGreHVVQLLDDFKHTgp 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  86 --TKLYLILELGdGGDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCH-KLHVVHRDLKPENVVFFEKQGLVKLTDFGF 161
Cdd:cd14136    89 ngTHVCMVFEVL-GPNLLKLIKRYNyRGIPLPLVKKIARQVLQGLDYLHtKCGIIHTDIKPENVLLCISKIEVKIADLGN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 SNKFQpgKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPF--QEAN----DSETLTMIMDC----- 230
Cdd:cd14136   168 ACWTD--KHFTEDIQTRQYRSPEVILGAGYGTPA-DIWSTACMAFELATGDYLFdpHSGEdysrDEDHLALIIELlgrip 244
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 231 -------------------------------------KYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14136   245 rsiilsgkysreffnrkgelrhisklkpwpledvlveKYKWSKEEAKEFASFLLPMLEYDPEKRATAAQCLQHPWL 320
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
12-269 5.32e-20

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: 92.07  E-value: 5.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFA-VVKLARHVfTGEKVAVKVI-DKTKLDTLAtghlFQEVRCMKLVQHP------NIVRLYEVID 83
Cdd:cd14225    41 IAYRYEILEVIGKGSFGqVVKALDHK-TNEHVAIKIIrNKKRFHHQA----LVEVKILDALRRKdrdnshNVIHMKEYFY 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  84 TQTKLYLILELGdGGDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEK-QGLVKLTDFGF 161
Cdd:cd14225   116 FRNHLCITFELL-GMNLYELIKKNNfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRgQSSIKVIDFGS 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 SNKFQpgKKLTTSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV--- 238
Cdd:cd14225   195 SCYEH--QRVYTYIQSRFYRSPEVILGLPYS-MAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGLPPPELien 271
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 239 -------------------SAGCR--------------------DLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14225   272 aqrrrlffdskgnprcitnSKGKKrrpnskdlasalktsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
20-263 5.95e-20

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: 90.31  E-value: 5.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVfTGEKVAVKVIDKtklDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd05114    10 KELGSGLFGVVRLGKWR-AQYKVAIKAIRE---GAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSnKFQPGKKLTTSCGS-- 177
Cdd:cd05114    86 LLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVND-TGVVKVSDFGMT-RYVLDDQYTSSSGAkf 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 178 -LAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKYTVPPRV-SAGCRDLITRMLQRDP 254
Cdd:cd05114   164 pVKWSPPEVFNYSKFSSKS-DVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSRGHRLYRPKLaSKSVYEVMYSCWHEKP 242

                  ....*....
gi 1907195986 255 KRRASLEEI 263
Cdd:cd05114   243 EGRPTFADL 251
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
20-270 6.26e-20

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: 91.89  E-value: 6.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------YLILE 93
Cdd:cd07879    21 KQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGdefqdfYLVMP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LgdggdMF---DYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNkfQPGKK 170
Cdd:cd07879   101 Y-----MQtdlQKIMGHP--LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCEL-KILDFGLAR--HADAE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 171 LTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMdcKYT-VP-------------- 235
Cdd:cd07879   171 MTGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQIL--KVTgVPgpefvqkledkaak 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907195986 236 ------------------PRVSAGCRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd07879   249 syikslpkyprkdfstlfPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFD 301
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
17-265 7.81e-20

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 89.72  E-value: 7.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  17 DLDKTLGRGHFAVVKLArhVFTGEKVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05039     9 KLGELIGKGEFGDVMLG--DYRGQKVAVKCL---KDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEEGLNEDLAKKYFA-QIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGF---SNKFQPGKKLt 172
Cdd:cd05039    84 KGSLVDYLRSRGRAVITRKDQLGFAlDVCEGMEYLESKKFVHRDLAARNVLVSE-DNVAKVSDFGLakeASSNQDGGKL- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 tscgSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMI-----MDCKYTVPPRVsagcRDLI 246
Cdd:cd05039   162 ----PIKWTAPEALREKKFSTKS-DVWSFGILLWEIYSfGRVPYPRIPLKDVVPHVekgyrMEAPEGCPPEV----YKVM 232
                         250
                  ....*....|....*....
gi 1907195986 247 TRMLQRDPKRRASLEEIES 265
Cdd:cd05039   233 KNCWELDPAKRPTFKQLRE 251
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
22-160 1.77e-19

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: 85.19  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVID-KTKLDTLATGHlfqEVRCMKLVQ--HPNIVRLYEVIDTQTKLYLILELGDGG 98
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDdVNNEEGEDLES---EMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195986  99 DMFDYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFG 160
Cdd:cd13968    78 TLIAYTQEEE--LDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDN-ILLSEDGNVKLIDFG 136
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
20-274 1.99e-19

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: 90.11  E-value: 1.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKT-KLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE--LGD 96
Cdd:cd06635    31 REIGHGSFGAVYFARDVRTSEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEycLGS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYimkHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKFQPGKKLTtscG 176
Cdd:cd06635   111 ASDLLEV---HKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP-GQVKLADFGSASIASPANSFV---G 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLG-DE--YDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKytvPPRVSAG-----CRDLITR 248
Cdd:cd06635   184 TPYWMAPEVILAmDEgqYDG-KVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNE---SPTLQSNewsdyFRNFVDS 259
                         250       260
                  ....*....|....*....|....*.
gi 1907195986 249 MLQRDPKRRASLEEIESHPWLQGVDP 274
Cdd:cd06635   260 CLQKIPQDRPTSEELLKHMFVLRERP 285
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
18-263 2.14e-19

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: 88.93  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAvvKLARHVFTGEKVAVKVI--DKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd14147     7 LEEVIGIGGFG--KVYRGSWRGELVAVKAArqDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEegLNEDLAKKYFAQIVHAISYCHK---LHVVHRDLKPENVVFFE-------KQGLVKLTDFGFSNKF 165
Cdd:cd14147    85 AGGPLSRALAGRR--VPPHVLVNWAVQIARGMHYLHCealVPVIHRDLKSNNILLLQpienddmEHKTLKITDFGLAREW 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGKKLTTScGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPprVSAGCRDL 245
Cdd:cd14147   163 HKTTQMSAA-GTYAWMAPEVIKASTFSKGS-DVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLP--IPSTCPEP 238
                         250       260
                  ....*....|....*....|..
gi 1907195986 246 ITRML----QRDPKRRASLEEI 263
Cdd:cd14147   239 FAQLMadcwAQDPHRRPDFASI 260
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
22-257 2.50e-19

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: 88.83  E-value: 2.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARhvFTGEKVAVKVIDK------------TKLDTLATGH-------LFQEVRCMKLVQHPNIVRLYEVi 82
Cdd:cd14000     2 LGDGGFGSVYRAS--YKGEPVAVKIFNKhtssnfanvpadTMLRHLRATDamknfrlLRQELTVLSHLHHPSIVYLLGI- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  83 dTQTKLYLILELGDGGDMfDYIMKHEEG----LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE----KQGLV 154
Cdd:cd14000    79 -GIHPLMLVLELAPLGSL-DHLLQQDSRsfasLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTlypnSAIII 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 155 KLTDFGFSNK-FQPGKKltTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPP------FQEAND-SETLTM 226
Cdd:cd14000   157 KIADYGISRQcCRMGAK--GSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPmvghlkFPNEFDiHGGLRP 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907195986 227 IMDCKYTVPPRVsagCRDLITRMLQRDPKRR 257
Cdd:cd14000   235 PLKQYECAPWPE---VEVLMKKCWKENPQQR 262
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
22-285 2.53e-19

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: 88.96  E-value: 2.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd06640    12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSAL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPGK-KLTTSCGSLAY 180
Cdd:cd06640    91 DLLRAGP--FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSE-QGDVKLADFGVAGQLTDTQiKRNTFVGTPFW 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMdcKYTVPPRV---SAGCRDLITRMLQRDPKRR 257
Cdd:cd06640   168 MAPEVIQQSAYDSKA-DIWSLGITAIELAKGEPPNSDMHPMRVLFLIP--KNNPPTLVgdfSKPFKEFIDACLNKDPSFR 244
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 258 ASLEEIESHPWLqgVDPSPATKYNIPLV 285
Cdd:cd06640   245 PTAKELLKHKFI--VKNAKKTSYLTELI 270
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
22-277 3.78e-19

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 87.70  E-value: 3.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLArHVFTGEKVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd05112    12 IGSGQFGLVHLG-YWLNKDKVAIKTI---REGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSnKFQPGKKLTTSCGS---L 178
Cdd:cd05112    88 DYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQ-VVKVSDFGMT-RFVLDDQYTSSTGTkfpV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSEtltmimdckytVPPRVSAGCRDLITRMLQRdpkrr 257
Cdd:cd05112   166 KWSSPEVFSFSRYSSKS-DVWSFGVLMWEVFSeGKIPYENRSNSE-----------VVEDINAGFRLYKPRLAST----- 228
                         250       260
                  ....*....|....*....|
gi 1907195986 258 aSLEEIESHPWLQGVDPSPA 277
Cdd:cd05112   229 -HVYEIMNHCWKERPEDRPS 247
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
22-264 4.48e-19

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: 87.37  E-value: 4.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAvvklarHVFTGE-----KVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd05085     4 LGKGNFG------EVYKGTlkdktPVAVKTC-KEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNKFQPGkkLTTSCG 176
Cdd:cd05085    77 GGDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNAL-KISDFGMSRQEDDG--VYSSSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 ----SLAYSAPEILLGDEYDAPAvDIWSLGVIL---FML-VCGQPPF--QEANDSETLTMIMDCKYTVPPRVSagcrDLI 246
Cdd:cd05085   154 lkqiPIKWTAPEALNYGRYSSES-DVWSFGILLwetFSLgVCPYPGMtnQQAREQVEKGYRMSAPQRCPEDIY----KIM 228
                         250
                  ....*....|....*...
gi 1907195986 247 TRMLQRDPKRRASLEEIE 264
Cdd:cd05085   229 QRCWDYNPENRPKFSELQ 246
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
22-218 4.92e-19

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: 87.51  E-value: 4.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVfFEKQGLVKLTDFGFS-----NKFQPGKKLTTS 174
Cdd:cd13978    81 SLLEREIQDVPWSLRFRIIHEIALGMNFLHNMDppLLHHDLKPENIL-LDNHFHVKISDFGLSklgmkSISANRRRGTEN 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907195986 175 -CGSLAYSAPEiLLGDEYDAP--AVDIWSLGVILFMLVCGQPPFQEA 218
Cdd:cd13978   160 lGGTPIYMAPE-AFDDFNKKPtsKSDVYSFAIVIWAVLTRKEPFENA 205
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
38-270 5.28e-19

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: 88.15  E-value: 5.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  38 TGEKVAVKVIDKTKLDTL---ATGHLFQ----EVRCMKLVQHPNIVRLYEVIDTQTK-LYLILE---------LGDGGDM 100
Cdd:cd14011    20 TKQEVSVFVFEKKQLEEYskrDREQILEllkrGVKQLTRLRHPRILTVQHPLEESREsLAFATEpvfaslanvLGERDNM 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYIMKHEEGLNEDLAKKY-FAQIVHAISYCH-KLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKF-QPGKKLTTSCG- 176
Cdd:cd14011   100 PSPPPELQDYKLYDVEIKYgLLQISEALSFLHnDVKLVHGNICPESV-VINSNGEWKLAGFDFCISSeQATDQFPYFREy 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 ----------SLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVC-GQPPFQEAND--------SETLTMIMDCKYTVPPR 237
Cdd:cd14011   179 dpnlpplaqpNLNYLAPEYILSKTCD-PASDMFSLGVLIYAIYNkGKPLFDCVNNllsykknsNQLRQLSLSLLEKVPEE 257
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907195986 238 VsagcRDLITRMLQRDPKRRASLEEIESHPWLQ 270
Cdd:cd14011   258 L----RDHVKTLLNVTPEVRPDAEQLSKIPFFD 286
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
16-266 6.00e-19

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: 87.39  E-value: 6.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSL--IQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDyiMKHEEGLNEDLAKKYFA-QIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPG-KKLTT 173
Cdd:cd06646    89 GGGSLQD--IYHVTGPLSELQIAYVCrETLQGLAYLHSKGKMHRDIKGANILLTD-NGDVKLADFGVAAKITATiAKRKS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDE---YDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTvPPRV------SAGCRD 244
Cdd:cd06646   166 FIGTPYWMAPEVAAVEKnggYNQ-LCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQ-PPKLkdktkwSSTFHN 243
                         250       260
                  ....*....|....*....|..
gi 1907195986 245 LITRMLQRDPKRRASLEEIESH 266
Cdd:cd06646   244 FVKISLTKNPKKRPTAERLLTH 265
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
20-274 6.91e-19

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: 88.16  E-value: 6.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKT-KLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE--LGD 96
Cdd:cd06634    21 REIGHGSFGAVYFARDVRNNEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEycLGS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYimkHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKFQPGKKLTtscG 176
Cdd:cd06634   101 ASDLLEV---HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEP-GLVKLGDFGSASIMAPANSFV---G 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLG-DE--YDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTV--PPRVSAGCRDLITRMLQ 251
Cdd:cd06634   174 TPYWMAPEVILAmDEgqYDG-KVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPAlqSGHWSEYFRNFVDSCLQ 252
                         250       260
                  ....*....|....*....|...
gi 1907195986 252 RDPKRRASLEEIESHPWLQGVDP 274
Cdd:cd06634   253 KIPQDRPTSDVLLKHRFLLRERP 275
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
20-263 7.77e-19

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: 87.38  E-value: 7.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHV----FTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDT--QTKLYLILE 93
Cdd:cd14205    10 QQLGKGNFGSVEMCRYDplqdNTGEVVAVKKLQHSTEEHLRD--FEREIEILKSLQHDNIVKYKGVCYSagRRNLRLIME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd14205    88 YLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNIL-VENENRVKIGDFGLTKVLPQDKEYYK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 ----SCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLV-----CGQPP--FQE--ANDSET------LTMIMDCKYTV 234
Cdd:cd14205   167 vkepGESPIFWYAPESLTESKFSV-ASDVWSFGVVLYELFtyiekSKSPPaeFMRmiGNDKQGqmivfhLIELLKNNGRL 245
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907195986 235 PPrvSAGCRDLITRMLQR----DPKRRASLEEI 263
Cdd:cd14205   246 PR--PDGCPDEIYMIMTEcwnnNVNQRPSFRDL 276
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
73-268 8.84e-19

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: 86.83  E-value: 8.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  73 PNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKHEEG---------------------LNEDLAKKYFAQIVHAISYCH 131
Cdd:cd05576    51 PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKFLNDkeihqlfadlderlaaasrfyIPEECIQRWAAEMVVALDALH 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 132 KLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPgkklttSCGSLA----YSAPEIlLGDEYDAPAVDIWSLGVILFM 207
Cdd:cd05576   131 REGIVCRDLNPNNIL-LNDRGHIQLTYFSRWSEVED------SCDSDAienmYCAPEV-GGISEETEACDWWSLGALLFE 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 208 LVCGQPPFQ----EANDSETLTMimdckytvPPRVSAGCRDLITRMLQRDPKRR-----ASLEEIESHPW 268
Cdd:cd05576   203 LLTGKALVEchpaGINTHTTLNI--------PEWVSEEARSLLQQLLQFNPTERlgagvAGVEDIKSHPF 264
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
42-263 9.29e-19

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 86.71  E-value: 9.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  42 VAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKHEEGLNEDLAKKYFA 121
Cdd:cd05052    34 VAVKTL---KEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDYLRECNREELNAVVLLYMA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 122 -QIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSnKFQPGKKLTTSCGS---LAYSAPEILLGDEYDAPAvD 197
Cdd:cd05052   111 tQIASAMEYLEKKNFIHRDLAARNCLVGE-NHLVKVADFGLS-RLMTGDTYTAHAGAkfpIKWTAPESLAYNKFSIKS-D 187
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 198 IWSLGVILFMLVC-GQPPFQEANDSETLTMI-----MDCKYTVPPRVsagcRDLITRMLQRDPKRRASLEEI 263
Cdd:cd05052   188 VWAFGVLLWEIATyGMSPYPGIDLSQVYELLekgyrMERPEGCPPKV----YELMRACWQWNPSDRPSFAEI 255
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
18-261 1.08e-18

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 86.69  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAvvklarHVFTG-----EKVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd05068    12 LLRKLGSGQFG------EVWEGlwnntTPVAVKTL---KPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIIT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHEEGLNE----DLAkkyfAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPG 168
Cdd:cd05068    83 ELMKHGSLLEYLQGKGRSLQLpqliDMA----AQVASGMAYLESQNYIHRDLAARNVLVGE-NNICKVADFGLARVIKVE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGS---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMI-----MDCKYTVPPrvs 239
Cdd:cd05068   158 DEYEAREGAkfpIKWTAPEAANYNRFSIKS-DVWSFGILLTEIVTyGRIPYPGMTNAEVLQQVergyrMPCPPNCPP--- 233
                         250       260
                  ....*....|....*....|....*
gi 1907195986 240 agcrDLITRMLQ---RDPKRRASLE 261
Cdd:cd05068   234 ----QLYDIMLEcwkADPMERPTFE 254
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
18-272 1.09e-18

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 86.57  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHvfTGEKVAVKVIdktKLDtlATGHLF-QEVRCMKLVQHPNIVRLYEVI-DTQTKLYLILELG 95
Cdd:cd05082    10 LLQTIGKGEFGDVMLGDY--RGNKVAVKCI---KND--ATAQAFlAEASVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPGKKltTS 174
Cdd:cd05082    83 AKGSLVDYLRSRGRSvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSE-DNVAKVSDFGLTKEASSTQD--TG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMI-----MDCKYTVPPRVsagcRDLITR 248
Cdd:cd05082   160 KLPVKWTAPEALREKKFSTKS-DVWSFGILLWEIYSfGRVPYPRIPLKDVVPRVekgykMDAPDGCPPAV----YDVMKN 234
                         250       260
                  ....*....|....*....|....
gi 1907195986 249 MLQRDPKRRASLEEIEShpWLQGV 272
Cdd:cd05082   235 CWHLDAAMRPSFLQLRE--QLEHI 256
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
16-269 1.63e-18

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: 86.25  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd06645    13 FELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAV--VQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDyiMKHEEGLNEDLAKKYFA-QIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPG-KKLTT 173
Cdd:cd06645    91 GGGSLQD--IYHVTGPLSESQIAYVSrETLQGLYYLHSKGKMHRDIKGANILLTD-NGHVKLADFGVSAQITATiAKRKS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDA--PAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTvPPRV------SAGCRDL 245
Cdd:cd06645   168 FIGTPYWMAPEVAAVERKGGynQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQ-PPKLkdkmkwSNSFHHF 246
                         250       260
                  ....*....|....*....|....
gi 1907195986 246 ITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd06645   247 VKMALTKNPKKRPTAEKLLQHPFV 270
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
22-270 1.97e-18

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: 86.02  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIdkTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKEL--IRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVkLTDFGFSN-----KFQPG-------- 168
Cdd:cd14154    79 DVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVV-VADFGLARliveeRLPSGnmspsetl 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 --------KKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFML---VCGQPPFQEANDSETLTM-IMDCKY--TV 234
Cdd:cd14154   158 rhlkspdrKKRYTVVGNPYWMAPEMLNGRSYDE-KVDIFSFGIVLCEIigrVEADPDYLPRTKDFGLNVdSFREKFcaGC 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907195986 235 PP---RVSAGCRDLitrmlqrDPKRRASLEEIEShpWLQ 270
Cdd:cd14154   237 PPpffKLAFLCCDL-------DPEKRPPFETLEE--WLE 266
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
22-212 2.02e-18

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: 85.39  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVklARHVFTGEKVAVKVIDKTKLDTLatghLFQEVRCMKLVQHPNIVRLYEViDTQTKLyLILELGDGGDMf 101
Cdd:cd14068     2 LGDGGFGSV--YRAVYRGEDVAVKIFNKHTSFRL----LRQELVVLSHLHHPSLVALLAA-GTAPRM-LVMELAPKGSL- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEG-LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF----EKQGLVKLTDFGFSnKFQPGKKLTTSCG 176
Cdd:cd14068    73 DALLQQDNAsLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFtlypNCAIIAKIADYGIA-QYCCRMGIKTSEG 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907195986 177 SLAYSAPEILLGDEYDAPAVDIWSLGVILF-MLVCGQ 212
Cdd:cd14068   152 TPGFRAPEVARGNVIYNQQADVYSFGLLLYdILTCGE 188
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
17-217 2.44e-18

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: 85.86  E-value: 2.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  17 DLDKTLGRGHFAVVKLARhvFTGEkVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd14063     3 EIKEVIGKGRFGRVHRGR--WHGD-VAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKqGLVKLTDFGFSNK---FQPGKKLTT 173
Cdd:cd14063    80 GRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKN-IFLEN-GRVVITDFGLFSLsglLQPGRREDT 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 174 ---SCGSLAYSAPEIL--LGDEYDAP-------AVDIWSLGVILFMLVCGQPPFQE 217
Cdd:cd14063   158 lviPNGWLCYLAPEIIraLSPDLDFEeslpftkASDVYAFGTVWYELLAGRWPFKE 213
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
22-263 3.68e-18

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: 85.26  E-value: 3.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKvidKTKLDTLATghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVK---KVRLEVFRA----EELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYImKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQP---GKKLTTS---C 175
Cdd:cd13991    87 QLI-KEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAFLCDFGHAECLDPdglGKSLFTGdyiP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDApAVDIW-SLGVILFMLVCGQPPFQEANDSETLTMIMDCK--YTVPPRVSAGCRDLITRMLQR 252
Cdd:cd13991   166 GTETHMAPEVVLGKPCDA-KVDVWsSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPplREIPPSCAPLTAQAIQAGLRK 244
                         250
                  ....*....|.
gi 1907195986 253 DPKRRASLEEI 263
Cdd:cd13991   245 EPVHRASAAEL 255
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
18-265 4.22e-18

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 85.12  E-value: 4.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAvvKLARHVFTGE-KVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIdTQTKLYLILELGD 96
Cdd:cd05070    13 LIKRLGNGQFG--EVWMGTWNGNtKVAIKTL---KPGTMSPESFLEEAQIMKKLKHDKLVQLYAVV-SEEPIYIVTEYMS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYiMKHEEGLNEDLAK--KYFAQIVHAISYCHKLHVVHRDLKPENVVFfeKQGLV-KLTDFGFSNKFQpGKKLTT 173
Cdd:cd05070    87 KGSLLDF-LKDGEGRALKLPNlvDMAAQVAAGMAYIERMNYIHRDLRSANILV--GNGLIcKIADFGLARLIE-DNEYTA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGS---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMI-----MDCKYTVPPRVsagcRD 244
Cdd:cd05070   163 RQGAkfpIKWTAPEAALYGRFTIKS-DVWSFGILLTELVTkGRVPYPGMNNREVLEQVergyrMPCPQDCPISL----HE 237
                         250       260
                  ....*....|....*....|.
gi 1907195986 245 LITRMLQRDPKRRASLEEIES 265
Cdd:cd05070   238 LMIHCWKKDPEERPTFEYLQG 258
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
20-227 4.88e-18

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: 85.16  E-value: 4.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEK----VAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTkLYLILELG 95
Cdd:cd05057    13 KVLGSGAFGTVYKGVWIPEGEKvkipVAIKVL-REETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQ-VQLITQLM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd05057    91 PLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPN-HVKITDFGLAKLLDVDEKEYHAE 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 176 GS---LAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMI 227
Cdd:cd05057   170 GGkvpIKWMALESIQYRIYTHKS-DVWSYGVTVWeLMTFGAKPYEGIPAVEIPDLL 224
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
19-263 5.42e-18

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: 85.00  E-value: 5.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  19 DKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRcMKLVQHPNIVRLYEVIDTQTKLYLILElgdgg 98
Cdd:cd13980     5 DKSLGSTRFLKVARARHDEGLVVVKVFVKPDPALPLRSYKQRLEEIR-DRLLELPNVLPFQKVIETDKAAYLIRQ----- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 dmfdYImKHeeglN-----------EDLAKKYFA-QIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFG------ 160
Cdd:cd13980    79 ----YV-KY----NlydristrpflNLIEKKWIAfQLLHALNQCHKRGVCHGDIKTENVL-VTSWNWVYLTDFAsfkpty 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 --------FSNKFQPGKKLTTscgslaYSAPEILL-GDEYDA----------PAVDIWSLG-VILFMLVCGQPPFQ---- 216
Cdd:cd13980   149 lpednpadFSYFFDTSRRRTC------YIAPERFVdALTLDAeserrdgeltPAMDIFSLGcVIAELFTEGRPLFDlsql 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907195986 217 ------EANDSETLTMImdckytVPPRVsagcRDLITRMLQRDPKRRASLEEI 263
Cdd:cd13980   223 layrkgEFSPEQVLEKI------EDPNI----RELILHMIQRDPSKRLSAEDY 265
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
21-215 5.65e-18

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: 85.76  E-value: 5.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  21 TLGRGHFA-VVKLARHVfTGEKVAVKVIdKTKLDTLATGHLfqEVRCMKLVQ-------HPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd14212     6 LLGQGTFGqVVKCQDLK-TNKLVAVKVL-KNKPAYFRQAML--EIAILTLLNtkydpedKHHIVRLLDHFMHHGHLCIVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELgDGGDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQ-GLVKLTDFG---FSNkfqp 167
Cdd:cd14212    82 EL-LGVNLYELLKQNQfRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDsPEIKLIDFGsacFEN---- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907195986 168 gKKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPF 215
Cdd:cd14212   157 -YTLYTYIQSRFYRSPEVLLGLPYST-AIDMWSLGCIAAELFLGLPLF 202
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
20-209 6.38e-18

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: 84.98  E-value: 6.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHV----FTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRlYEVI---DTQTKLYLIL 92
Cdd:cd05079    10 RDLGEGHFGKVELCRYDpegdNTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVK-YKGIcteDGGNGIKLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLT 172
Cdd:cd05079    88 EFLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVL-VESEHQVKIGDFGLTKAIETDKEYY 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907195986 173 TSCGSLA----YSAPEILLGDEYdAPAVDIWSLGVILFMLV 209
Cdd:cd05079   167 TVKDDLDspvfWYAPECLIQSKF-YIASDVWSFGVTLYELL 206
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
60-289 6.60e-18

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 87.37  E-value: 6.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  60 LF-QE-VRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKheEGL-NEDLAKKYFAQIVHAISYCHKLHVV 136
Cdd:COG5752    83 LFrQEaVRLDELGKHPQIPELLAYFEQDQRLYLVQEFIEGQTLAQELEK--KGVfSESQIWQLLKDLLPVLQFIHSRNVI 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 137 HRDLKPENVVFFEKQGLVKLTDFGFSnkfqpgKKLT--------TSCGSLAYSAPEILLGDEYdaPAVDIWSLGVILFML 208
Cdd:COG5752   161 HRDIKPANIIRRRSDGKLVLIDFGVA------KLLTitallqtgTIIGTPEYMAPEQLRGKVF--PASDLYSLGVTCIYL 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 209 VCGQPPFQEANDSEtltmimDC----KYtVPP--RVSAGCRDLITRMLQRDPKRR-ASLEEIE------------SHPWL 269
Cdd:COG5752   233 LTGVSPFDLFDVSE------DRwvwrDF-LPPgtKVSDRLGQILDKLLQNALKQRyQSATEVLqalkrqppvsysPIPVA 305
                         250       260
                  ....*....|....*....|
gi 1907195986 270 QGVDPSPATKYNIPLVSYKN 289
Cdd:COG5752   306 PTKLPIQAQPPDITLKSAKG 325
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
16-236 6.63e-18

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: 84.43  E-value: 6.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlatgHLFQEVRCMKLVQ-HPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHP----QLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 gdggdmfdyimkheEGLN-EDLAKKY-----------FA-QIVHAISYCHKLHVVHRDLKPENVVFF--EKQGLVKLTDF 159
Cdd:cd14016    78 --------------LGPSlEDLFNKCgrkfslktvlmLAdQMISRLEYLHSKGYIHRDIKPENFLMGlgKNSNKVYLIDF 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 160 GFSNK-----------FQPGKKLTtscGSLAYSAPEILLGDEY---DapavDIWSLGVILFMLVCGQPPFQE---ANDSE 222
Cdd:cd14016   144 GLAKKyrdprtgkhipYREGKSLT---GTARYASINAHLGIEQsrrD----DLESLGYVLIYFLKGSLPWQGlkaQSKKE 216
                         250
                  ....*....|....
gi 1907195986 223 TLTMIMDCKYTVPP 236
Cdd:cd14016   217 KYEKIGEKKMNTSP 230
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
22-270 8.11e-18

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 84.24  E-value: 8.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRT--FLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVkLTDFGFS-----NKFQPG-------- 168
Cdd:cd14221    79 GIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVV-VADFGLArlmvdEKTQPEglrslkkp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 --KKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCgqppfQEANDSETLTMIMD------------CKYTV 234
Cdd:cd14221   158 drKKRYTVVGNPYWMAPEMINGRSYDE-KVDVFSFGIVLCEIIG-----RVNADPDYLPRTMDfglnvrgfldryCPPNC 231
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907195986 235 PPR---VSAGCRDLitrmlqrDPKRRASLEEIEShpWLQ 270
Cdd:cd14221   232 PPSffpIAVLCCDL-------DPEKRPSFSKLEH--WLE 261
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
16-228 1.33e-17

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: 83.25  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVfTGEKVAVKVIDKTklDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd05148     8 FTLERKLGSGYFGEVWEGLWK-NRVRVAIKILKSD--DLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYiMKHEEGLNEDLAKK-YFA-QIVHAISYCHKLHVVHRDLKPENVVFFEkqGLV-KLTDFGFSNKFQPGKKLT 172
Cdd:cd05148    85 EKGSLLAF-LRSPEGQVLPVASLiDMAcQVAEGMAYLEEQNSIHRDLAARNILVGE--DLVcKVADFGLARLIKEDVYLS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 173 TSCG-SLAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMIM 228
Cdd:cd05148   162 SDKKiPYKWTAPEAASHGTFSTKS-DVWSFGILLYeMFTYGQVPYPGMNNHEVYDQIT 218
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
20-264 1.66e-17

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 83.09  E-value: 1.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKlaRHVFTGEK----VAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTkLYLILELG 95
Cdd:cd05116     1 GELGSGNFGTVK--KGYYQMKKvvktVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAES-WMLVMEMA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKheeglNEDLAKKYFAQIVHAIS----YCHKLHVVHRDLKPENVVFFeKQGLVKLTDFGFSNKFQPG--- 168
Cdd:cd05116    78 ELGPLNKFLQK-----NRHVTEKNITELVHQVSmgmkYLEESNFVHRDLAARNVLLV-TQHYAKISDFGLSKALRADeny 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 -KKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMI-----MDCkytvPPRVSAG 241
Cdd:cd05116   152 yKAQTHGKWPVKWYAPECMNYYKFSSKS-DVWSFGVLMWeAFSYGQKPYKGMKGNEVTQMIekgerMEC----PAGCPPE 226
                         250       260
                  ....*....|....*....|...
gi 1907195986 242 CRDLITRMLQRDPKRRASLEEIE 264
Cdd:cd05116   227 MYDLMKLCWTYDVDERPGFAAVE 249
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
23-263 2.12e-17

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: 82.31  E-value: 2.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  23 GRGHFAVVKLARHVFTGEKVAVKVIDKTKldtlatghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFD 102
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIE----------KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 103 YI-MKHEEGLNEDLAKKYFAQIVHAISYCHK---LHVVHRDLKPENVVfFEKQGLVKLTDFGFSnKFQPGKKLTTSCGSL 178
Cdd:cd14060    72 YLnSNESEEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVV-IAADGVLKICDFGAS-RFHSHTTHMSLVGTF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC--KYTVPPRVSAGCRDLITRMLQRDPKR 256
Cdd:cd14060   150 PWMAPEVIQSLPV-SETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKneRPTIPSSCPRSFAELMRRCWEADVKE 228

                  ....*..
gi 1907195986 257 RASLEEI 263
Cdd:cd14060   229 RPSFKQI 235
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
22-216 3.80e-17

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 82.92  E-value: 3.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLfQEVRCMKLVQHPNIVRLY---EVIDTQTKLyLILELGDGG 98
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQM-REFEVLKKLNHKNIVKLFaieEELTTRHKV-LVMELCPCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  99 DMFDyIMKHEE---GLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF---EKQGLVKLTDFGFSNKFQPGKKLT 172
Cdd:cd13988    79 SLYT-VLEEPSnayGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVigeDGQSVYKLTDFGAARELEDDEQFV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 173 TSCGSLAYSAPEIL--------LGDEYDApAVDIWSLGVILFMLVCGQPPFQ 216
Cdd:cd13988   158 SLYGTEEYLHPDMYeravlrkdHQKKYGA-TVDLWSIGVTFYHAATGSLPFR 208
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
20-263 4.83e-17

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: 82.13  E-value: 4.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEK-----VAVKVIDKTKlDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05046    11 TTLGRGEFGEVFLAKAKGIEEEggetlVLVKALQKTK-DENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIM----KHEEGLNEDLAKKYF----AQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKF- 165
Cdd:cd05046    90 TDLGDLKQFLRatksKDEKLKPPPLSTKQKvalcTQIALGMDHLSNARFVHRDLAARNCLVSS-QREVKVSLLSLSKDVy 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 -QPGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMIMDCKYTVPPrvSAGCR 243
Cdd:cd05046   169 nSEYYKLRNALIPLRWLAPEAVQEDDFSTKS-DVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELPV--PEGCP 245
                         250       260
                  ....*....|....*....|....
gi 1907195986 244 DLITRMLQR----DPKRRASLEEI 263
Cdd:cd05046   246 SRLYKLMTRcwavNPKDRPSFSEL 269
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
20-295 4.88e-17

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: 83.56  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------YLILE 93
Cdd:cd07875    30 KPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLeefqdvYIVME 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGdmFDYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd07875   110 LMDAN--LCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIV-VKSDCTLKILDFGLARTAGTSFMMTP 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQ-----------------------PPFQEANDSETLTMIMD- 229
Cdd:cd07875   185 YVVTRYYRAPEVILGMGYKE-NVDIWSVGCIMGEMIKGGvlfpgtdhidqwnkvieqlgtpcPEFMKKLQPTVRTYVENr 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 230 CKYT------VPPRV------------SAGCRDLITRMLQRDPKRRASLEEIESHPWLQ-GVDPSPAtKYNIPLVSYKNL 290
Cdd:cd07875   264 PKYAgysfekLFPDVlfpadsehnklkASQARDLLSKMLVIDASKRISVDEALQHPYINvWYDPSEA-EAPPPKIPDKQL 342

                  ....*
gi 1907195986 291 SEEEH 295
Cdd:cd07875   343 DEREH 347
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
22-259 5.57e-17

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: 82.17  E-value: 5.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYE--VIDTQTKLYLILELGDGgD 99
Cdd:cd14049    14 LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTawMEHVQLMLYIQMQLCEL-S 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNE-------------DLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNK-- 164
Cdd:cd14049    93 LWDWIVERNKRPCEeefksapytpvdvDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIHVRIGDFGLACPdi 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 165 FQPGKKL-----------TTSCGSLAYSAPEILLGDEYDaPAVDIWSLGVILFMLVcgQPPFQEANDSETLTMIMdcKYT 233
Cdd:cd14049   173 LQDGNDSttmsrlnglthTSGVGTCLYAAPEQLEGSHYD-FKSDMYSIGVILLELF--QPFGTEMERAEVLTQLR--NGQ 247
                         250       260
                  ....*....|....*....|....*....
gi 1907195986 234 VPPRVSAGCR---DLITRMLQRDPKRRAS 259
Cdd:cd14049   248 IPKSLCKRWPvqaKYIKLLTSTEPSERPS 276
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
18-263 7.21e-17

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


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 81.07  E-value: 7.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARhvFTGEKVAVKVIdktKLDTLATGHLfQEVRCMKLVQHPNIVRLYEVIdTQTKLYLILELGDG 97
Cdd:cd05083    10 LGEIIGEGEFGAVLQGE--YMGQKVAVKNI---KCDVTAQAFL-EETAVMTKLQHKNLVRLLGVI-LHNGLYIVMELMSK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDYIMKHEEGLNEDLAKKYFA-QIVHAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSnKFQPgKKLTTSCG 176
Cdd:cd05083    83 GNLVNFLRSRGRALVPVIQLLQFSlDVAEGMEYLESKKLVHRDLAARNILVSED-GVAKISDFGLA-KVGS-MGVDNSRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMI-----MDCKYTVPPRVSAgcrdLITRML 250
Cdd:cd05083   160 PVKWTAPEALKNKKFSSKS-DVWSYGVLLWEVFSyGRAPYPKMSVKEVKEAVekgyrMEPPEGCPPDVYS----IMTSCW 234
                         250
                  ....*....|...
gi 1907195986 251 QRDPKRRASLEEI 263
Cdd:cd05083   235 EAEPGKRPSFKKL 247
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
18-265 7.37e-17

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: 81.26  E-value: 7.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEK---VAVKVI-----DKTKLDTLAtghlfqEVRCMKLVQHPNIVRLYEVIDTQTKLY 89
Cdd:cd05033     8 IEKVIGGGEFGEVCSGSLKLPGKKeidVAIKTLksgysDKQRLDFLT------EASIMGQFDHPNVIRLEGVVTKSRPVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGK 169
Cdd:cd05033    82 IVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNIL-VNSDLVCKVSDFGLSRRLEDSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTSCG---SLAYSAPEILLGDEYdAPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDcKYTVPPRVSagCRDL 245
Cdd:cd05033   161 ATYTTKGgkiPIRWTAPEAIAYRKF-TSASDVWSFGIVMWeVMSYGERPYWDMSNQDVIKAVED-GYRLPPPMD--CPSA 236
                         250       260
                  ....*....|....*....|....
gi 1907195986 246 ITR-ML---QRDPKRRASLEEIES 265
Cdd:cd05033   237 LYQlMLdcwQKDRNERPTFSQIVS 260
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
22-273 7.80e-17

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: 82.10  E-value: 7.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMf 101
Cdd:cd06615     9 LGAGNGGVVTKVLHRPSGLIMARKLI-HLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSL- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLH-VVHRDLKPENVVfFEKQGLVKLTDFGFS--------NKFqpgkklt 172
Cdd:cd06615    87 DQVLKKAGRIPENILGKISIAVLRGLTYLREKHkIMHRDVKPSNIL-VNSRGEIKLCDFGVSgqlidsmaNSF------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 173 tsCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFqEANDSETLTMIMDCK--------------------- 231
Cdd:cd06615   159 --VGTRSYMSPERLQGTHYTVQS-DIWSLGLSLVEMAIGRYPI-PPPDAKELEAMFGRPvsegeakeshrpvsghppdsp 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 232 ----------YTV---PPRVSAGC-----RDLITRMLQRDPKRRASLEEIESHPWLQGVD 273
Cdd:cd06615   235 rpmaifelldYIVnepPPKLPSGAfsdefQDFVDKCLKKNPKERADLKELTKHPFIKRAE 294
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
22-216 9.14e-17

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: 82.04  E-value: 9.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFA-VVKLARHVFTGEK-VAVKVIDKTKLDTLATghlfQEVRCMKLVQHPNIVRLYEVIDTQT--KLYLILELGDG 97
Cdd:cd07867    10 VGRGTYGhVYKAKRKDGKDEKeYALKQIEGTGISMSAC----REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 gDMFDYIMKHEEG--------LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF---EKQGLVKLTDFGFSNKF- 165
Cdd:cd07867    86 -DLWHIIKFHRASkankkpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegPERGRVKIADMGFARLFn 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907195986 166 ---QPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQ 216
Cdd:cd07867   165 splKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFH 218
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
18-265 1.19e-16

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 80.89  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTgEKVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIdTQTKLYLILELGDG 97
Cdd:cd05069    16 LDVKLGQGCFGEVWMGTWNGT-TKVAIKTL---KPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVV-SEEPIYIVTEFMGK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDYiMKHEEGLNEDLAK--KYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQpGKKLTTSC 175
Cdd:cd05069    91 GSLLDF-LKEGDGKYLKLPQlvDMAAQIADGMAYIERMNYIHRDLRAANILVGDNL-VCKIADFGLARLIE-DNEYTARQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GS---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMImDCKYTVPprVSAGCRDLITRML- 250
Cdd:cd05069   168 GAkfpIKWTAPEAALYGRFTIKS-DVWSFGILLTELVTkGRVPYPGMVNREVLEQV-ERGYRMP--CPQGCPESLHELMk 243
                         250
                  ....*....|....*...
gi 1907195986 251 ---QRDPKRRASLEEIES 265
Cdd:cd05069   244 lcwKKDPDERPTFEYIQS 261
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
20-295 1.30e-16

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: 82.06  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKL------YLILE 93
Cdd:cd07874    23 KPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLeefqdvYLVME 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGdmFDYIMKHEegLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTT 173
Cdd:cd07874   103 LMDAN--LCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIV-VKSDCTLKILDFGLARTAGTSFMMTP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV--------------- 238
Cdd:cd07874   178 YVVTRYYRAPEVILGMGYKE-NVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFmkklqptvrnyvenr 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 239 ---------------------------SAGCRDLITRMLQRDPKRRASLEEIESHPWLQ-GVDPSpATKYNIPLVSYKNL 290
Cdd:cd07874   257 pkyagltfpklfpdslfpadsehnklkASQARDLLSKMLVIDPAKRISVDEALQHPYINvWYDPA-EVEAPPPQIYDKQL 335

                  ....*
gi 1907195986 291 SEEEH 295
Cdd:cd07874   336 DEREH 340
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
15-265 2.33e-16

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: 80.35  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  15 LYDLDKTLGRGHFAVVK---LARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEV-IDTQTKLYL 90
Cdd:cd05074    10 QFTLGRMLGKGEFGSVReaqLKSEDGSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVsLRSRAKGRL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 -----ILELGDGGDMFDYIMKHEEG-----LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFG 160
Cdd:cd05074    90 pipmvILPFMKHGDLHTFLLMSRIGeepftLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMT-VCVADFG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 FSNKFQPGKKLTTSCGS---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLT-MIMDCKYTVP 235
Cdd:cd05074   169 LSKKIYSGDYYRQGCASklpVKWLALESLADNVYTTHS-DVWAFGVTMWEIMTrGQTPYAGVENSEIYNyLIKGNRLKQP 247
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 236 PRVSAGCRDLITRMLQRDPKRRASLEEIES 265
Cdd:cd05074   248 PDCLEDVYELMCQCWSPEPKCRPSFQHLRD 277
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
24-269 2.33e-16

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 79.67  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  24 RGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlatghlfQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFdy 103
Cdd:cd13995    14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKP-------SDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVL-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 104 imkheEGLNEDLAKKYF------AQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLvkLTDFGFSNKFQPGKKLTTSC-G 176
Cdd:cd13995    85 -----EKLESCGPMREFeiiwvtKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV--LVDFGLSVQMTEDVYVPKDLrG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 177 SLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPF-QEANDSETLTMIMDCKYTVPP------RVSAGCRDLITRM 249
Cdd:cd13995   158 TEIYMSPEVILCRGHNTKA-DIYSLGATIIHMQTGSPPWvRRYPRSAYPSYLYIIHKQAPPlediaqDCSPAMRELLEAA 236
                         250       260
                  ....*....|....*....|
gi 1907195986 250 LQRDPKRRASLEEIESHPWL 269
Cdd:cd13995   237 LERNPNHRSSAAELLKHEAL 256
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
18-265 2.36e-16

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 80.12  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAvvKLARHVFTGE-KVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIdTQTKLYLILELGD 96
Cdd:cd05071    13 LEVKLGQGCFG--EVWMGTWNGTtRVAIKTL---KPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVV-SEEPIYIVTEYMS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYiMKHEEGLNEDLAK--KYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQpGKKLTTS 174
Cdd:cd05071    87 KGSLLDF-LKGEMGKYLRLPQlvDMAAQIASGMAYVERMNYVHRDLRAANILVGENL-VCKVADFGLARLIE-DNEYTAR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGS---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMI-----MDCkytvPPRVSAGCRDL 245
Cdd:cd05071   164 QGAkfpIKWTAPEAALYGRFTIKS-DVWSFGILLTELTTkGRVPYPGMVNREVLDQVergyrMPC----PPECPESLHDL 238
                         250       260
                  ....*....|....*....|
gi 1907195986 246 ITRMLQRDPKRRASLEEIES 265
Cdd:cd05071   239 MCQCWRKEPEERPTFEYLQA 258
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
16-238 2.40e-16

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: 80.73  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEK-VAVKVI------DKTKLdtlatghlfQEVRCMKLVQH--PN----IVRLYEVI 82
Cdd:cd14135     2 YRVYGYLGKGVFSNVVRARDLARGNQeVAIKIIrnnelmHKAGL---------KELEILKKLNDadPDdkkhCIRLLRHF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  83 DTQTKLYLILELGDGgDMFDYIMKH--EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFG 160
Cdd:cd14135    73 EHKNHLCLVFESLSM-NLREVLKKYgkNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTLKLCDFG 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 161 fSNKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRV 238
Cdd:cd14135   152 -SASDIGENEITPYLVSRFYRAPEIILGLPYDYP-IDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGKFPKKM 227
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
18-265 2.75e-16

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 79.55  E-value: 2.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTgEKVAVKVIdktKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIdTQTKLYLILELGDG 97
Cdd:cd05067    11 LVERLGAGQFGEVWMGYYNGH-TKVAIKSL---KQGSMSPDAFLAEANLMKQLQHQRLVRLYAVV-TQEPIYIITEYMEN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDYiMKHEEGLNEDLAK--KYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFS-----NKF--QPG 168
Cdd:cd05067    86 GSLVDF-LKTPSGIKLTINKllDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLS-CKIADFGLArliedNEYtaREG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLttscgSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMI-----MDCkytvPPRVSAGC 242
Cdd:cd05067   164 AKF-----PIKWTAPEAINYGTFTIKS-DVWSFGILLTEIVThGRIPYPGMTNPEVIQNLergyrMPR----PDNCPEEL 233
                         250       260
                  ....*....|....*....|...
gi 1907195986 243 RDLITRMLQRDPKRRASLEEIES 265
Cdd:cd05067   234 YQLMRLCWKERPEDRPTFEYLRS 256
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
20-263 7.15e-16

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 78.23  E-value: 7.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVV--KLARHVF---TGE-KVAVKVIDKTKLDTlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd05044     1 KFLGSGAFGEVfeGTAKDILgdgSGEtKVAVKTLRKGATDQ-EKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYI--MKHEEGLNEDLAKKYFAQI-VHAISYCH---KLHVVHRDLKPENVVFFEKQG---LVKLTDFG---- 160
Cdd:cd05044    80 LMEGGDLLSYLraARPTAFTPPLLTLKDLLSIcVDVAKGCVyleDMHFVHRDLAARNCLVSSKDYrerVVKIGDFGlard 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 -FSNKF--QPGKKLTtscgSLAYSAPEILLgDEYDAPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMD-CKYTVP 235
Cdd:cd05044   160 iYKNDYyrKEGEGLL----PVRWMAPESLV-DGVFTTQSDVWAFGVLMWeILTLGQQPYPARNNLEVLHFVRAgGRLDQP 234
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 236 PRVSAGCRDLITRMLQRDPKRRASLEEI 263
Cdd:cd05044   235 DNCPDDLYELMLRCWSTDPEERPSFARI 262
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
22-216 7.86e-16

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: 79.33  E-value: 7.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFA-VVKLARHVFTGEK-VAVKVIDKTKLDTLATghlfQEVRCMKLVQHPNIVRLYEVIDTQT--KLYLILELGDG 97
Cdd:cd07868    25 VGRGTYGhVYKAKRKDGKDDKdYALKQIEGTGISMSAC----REIALLRELKHPNVISLQKVFLSHAdrKVWLLFDYAEH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 gDMFDYIMKHEEG--------LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF---EKQGLVKLTDFGFSNKF- 165
Cdd:cd07868   101 -DLWHIIKFHRASkankkpvqLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegPERGRVKIADMGFARLFn 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907195986 166 ---QPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQ 216
Cdd:cd07868   180 splKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFH 233
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
17-273 7.96e-16

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: 79.33  E-value: 7.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  17 DLDKT--LGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd06650     6 DFEKIseLGAGNGGVVFKVSHKPSGLVMARKLI-HLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLH-VVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKlTT 173
Cdd:cd06650    85 MDGGSL-DQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNIL-VNSRGEIKLCDFGVSGQLIDSMA-NS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEAnDSETLTMIMDCK---------------------- 231
Cdd:cd06650   162 FVGTRSYMSPERLQGTHYSVQS-DIWSMGLSLVEMAVGRYPIPPP-DAKELELMFGCQvegdaaetpprprtpgrplssy 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907195986 232 ---------------YTV---PPRVSAGC-----RDLITRMLQRDPKRRASLEEIESHPWLQGVD 273
Cdd:cd06650   240 gmdsrppmaifelldYIVnepPPKLPSGVfslefQDFVNKCLIKNPAERADLKQLMVHAFIKRSD 304
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
20-216 1.15e-15

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 78.02  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHV----FTGEKVAVKVIDKTKLDTLATGHLfQEVRCMKLVQHPNIVRLYEVIDTQTK--LYLILE 93
Cdd:cd05080    10 RDLGEGHFGKVSLYCYDptndGTGEMVAVKALKADCGPQHRSGWK-QEIDILKTLYHENIVKYKGCCSEQGGksLQLIME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNEDLakkYFAQ-IVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKL- 171
Cdd:cd05080    89 YVPLGSLRDYLPKHSIGLAQLL---LFAQqICEGMAYLHSQHYIHRDLAARNVL-LDNDRLVKIGDFGLAKAVPEGHEYy 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907195986 172 ---TTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQ 216
Cdd:cd05080   165 rvrEDGDSPVFWYAPECLKEYKF-YYASDVWSFGVTLYELLTHCDSSQ 211
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
19-311 2.12e-15

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: 77.76  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  19 DKTLGRGHFAVVKLARHVFTGEK----VAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTkLYLILEL 94
Cdd:cd05108    12 IKVLGSGAFGTVYKGLWIPEGEKvkipVAIKEL-REATSPKANKEILDEAYVMASVDNPHVCRLLGICLTST-VQLITQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKFQPGKKLTTS 174
Cdd:cd05108    90 MPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQH-VKITDFGLAKLLGAEEKEYHA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 175 CGS---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMIMDC-KYTVPPRVSAGCRDLITRM 249
Cdd:cd05108   169 EGGkvpIKWMALESILHRIYTHQS-DVWSYGVTVWELMTfGSKPYDGIPASEISSILEKGeRLPQPPICTIDVYMIMVKC 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195986 250 LQRDPKRRASLEEIESHPWLQGVDPSP--ATKYNIPLVSYKNLSEEEHNSIIQRMVLGDIADRD 311
Cdd:cd05108   248 WMIDADSRPKFRELIIEFSKMARDPQRylVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDAD 311
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
22-264 2.38e-15

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: 76.77  E-value: 2.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVavkvidktkLDTLATGH--------LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd14027     1 LDSGGFGKVSLCFHRTQGLVV---------LKTVYTGPnciehneaLLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVME 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNedLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFS--------NKF 165
Cdd:cd14027    72 YMEKGNLMHVLKKVSVPLS--VKGRIILEIIEGMAYLHGKGVIHKDLKPENIL-VDNDFHIKIADLGLAsfkmwsklTKE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPG--KKLTTSC----GSLAYSAPEiLLGDEYDAPA--VDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY----- 232
Cdd:cd14027   149 EHNeqREVDGTAkknaGTLYYMAPE-HLNDVNAKPTekSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNrpdvd 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 233 TVPPRVSAGCRDLITRMLQRDPKRRASLEEIE 264
Cdd:cd14027   228 DITEYCPREIIDLMKLCWEANPEARPTFPGIE 259
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
22-240 2.40e-15

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: 76.91  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKlaRHVFTGEK----VAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTkLYLILELGDG 97
Cdd:cd05115    12 LGSGNFGCVK--KGVYKMRKkqidVAIKVL-KQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEMASG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQPG----KKLTT 173
Cdd:cd05115    88 GPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQH-YAKISDFGLSKALGADdsyyKARSA 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195986 174 SCGSLAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMI-----MDCKYTVPPRVSA 240
Cdd:cd05115   167 GKWPLKWYAPECINFRKFSSRS-DVWSYGVTMWeAFSYGQKPYKKMKGPEVMSFIeqgkrMDCPAECPPEMYA 238
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
22-229 2.62e-15

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 77.15  E-value: 2.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARhvFTGEKVAVK-VIDKTKLDTLATGHLF-QEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd14158    23 LGEGGFGVVFKGY--INDKNVAVKkLAAMVDISTEDLTKQFeQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYI--MKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkqGLV-KLTDFGFSNKFQPG-KKLTTS- 174
Cdd:cd14158   101 LLDRLacLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDE--TFVpKISDFGLARASEKFsQTIMTEr 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 175 -CGSLAYSAPEILLGDEydAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMD 229
Cdd:cd14158   179 iVGTTAYMAPEALRGEI--TPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDIKE 232
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
22-205 2.76e-15

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 76.91  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKT--FLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDlaKKYFAQ-IVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFS-----NKFQPG------- 168
Cdd:cd14222    79 DFLRADDPFPWQQ--KVSFAKgIASGMAYLHSMSIIHRDLNSHNCL-IKLDKTVVVADFGLSrliveEKKKPPpdkpttk 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907195986 169 ---------KKLTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVIL 205
Cdd:cd14222   156 krtlrkndrKKRYTVVGNPYWMAPEMLNGKSYDE-KVDIFSFGIVL 200
pknD PRK13184
serine/threonine-protein kinase PknD;
16-271 2.92e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 80.20  E-value: 2.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDT-LATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENpLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGgdmfdYIMKH-------EEGLNEDLAKK--------YFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDF 159
Cdd:PRK13184   84 IEG-----YTLKSllksvwqKESLSKELAEKtsvgaflsIFHKICATIEYVHSKGVLHRDLKPDNIL-LGLFGEVVILDW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 160 G-----------------------FSNKFQPGKKLttscGSLAYSAPEILLGdeydAPA---VDIWSLGVILFMLVCGQP 213
Cdd:PRK13184  158 GaaifkkleeedlldidvdernicYSSMTIPGKIV----GTPDYMAPERLLG----VPAsesTDIYALGVILYQMLTLSF 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 214 PFQEandsETLTMIMDCKYTVPPRVSAGCRDL-------ITRMLQRDPKRRAS-----LEEIESHpwLQG 271
Cdd:PRK13184  230 PYRR----KKGRKISYRDVILSPIEVAPYREIppflsqiAMKALAVDPAERYSsvqelKQDLEPH--LQG 293
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
22-205 4.71e-15

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: 75.63  E-value: 4.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGeKVAVKVIDKTKLDTLAtghLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMF 101
Cdd:cd14156     1 IGSGFFSKVYKVTHGATG-KVMVVKIYKNDVDQHK---IVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVK--LTDFGFSNKF------QPGKKLTT 173
Cdd:cd14156    77 ELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREavVTDFGLAREVgempanDPERKLSL 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907195986 174 sCGSLAYSAPEILLGDEYDApAVDIWSLGVIL 205
Cdd:cd14156   157 -VGSAFWMAPEMLRGEPYDR-KVDVFSFGIVL 186
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
12-243 4.82e-15

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: 77.48  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  12 IAGLYDLDKTLGRGHFA-VVKLARHVfTGEKVAVKVI-DKTKLDTLATghlfQEVRCMKLVQHP------NIVRLYEVID 83
Cdd:cd14224    63 IAYRYEVLKVIGKGSFGqVVKAYDHK-THQHVALKMVrNEKRFHRQAA----EEIRILEHLKKQdkdntmNVIHMLESFT 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  84 TQTKLYLILELGDGgDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfEKQGL--VKLTDFG 160
Cdd:cd14224   138 FRNHICMTFELLSM-NLYELIKKNKfQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILL-KQQGRsgIKVIDFG 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 fSNKFQpGKKLTTSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSA 240
Cdd:cd14224   216 -SSCYE-HQRIYTYIQSRFYRAPEVILGARYGMP-IDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPPQKLLE 292

                  ...
gi 1907195986 241 GCR 243
Cdd:cd14224   293 TSK 295
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
16-280 5.11e-15

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 76.72  E-value: 5.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFA-VVKLARHVfTGEKVAVKVIdKTKLDTLATGHLfqEVRCM-KLVQHP----NIVRLYEVIDTQTKLY 89
Cdd:cd14211     1 YEVLEFLGRGTFGqVVKCWKRG-TNEIVAIKIL-KNHPSYARQGQI--EVSILsRLSQENadefNFVRAYECFQHKNHTC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGgDMFDYiMKHEEglNEDLAKKYF----AQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL---VKLTDFGFS 162
Cdd:cd14211    77 LVFEMLEQ-NLYDF-LKQNK--FSPLPLKYIrpilQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQpyrVKVIDFGSA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 163 NKFQPGKKlTTSCGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR-VSAG 241
Cdd:cd14211   153 SHVSKAVC-STYLQSRYYRAPEIILGLPFCE-AIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPAEHlLNAA 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907195986 242 CRdlITRMLQRDPKRRAS---LEEIESHPWLQGVDPSPATKY 280
Cdd:cd14211   231 TK--TSRFFNRDPDSPYPlwrLKTPEEHEAETGIKSKEARKY 270
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
18-221 6.75e-15

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 75.42  E-value: 6.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYE----VIDTQTKLYLILE 93
Cdd:cd14033     5 FNIEIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDswksTVRGHKCIILVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEgLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVFFEKQGLVKLTDFGFSNkFQPGKKL 171
Cdd:cd14033    85 LMTSGTLKTYLKRFRE-MKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGPTGSVKIGDLGLAT-LKRASFA 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEiLLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDS 221
Cdd:cd14033   163 KSVIGTPEFMAPE-MYEEKYDE-AVDVYAFGMCILEMATSEYPYSECQNA 210
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
14-269 6.95e-15

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 76.61  E-value: 6.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATghlFQEVRCMKLVQH-----PNIVRLYEVID----- 83
Cdd:cd14216    10 GRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETA---LDEIKLLKSVRNsdpndPNREMVVQLLDdfkis 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  84 --TQTKLYLILELgDGGDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCH-KLHVVHRDLKPENVVF------------ 147
Cdd:cd14216    87 gvNGTHICMVFEV-LGHHLLKWIIKSNyQGLPLPCVKKIIRQVLQGLDYLHtKCRIIHTDIKPENILLsvneqyirrlaa 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 148 ----FEKQGL-------------VKLTDFGfsNKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC 210
Cdd:cd14216   166 eateWQRNFLvnplepknaeklkVKIADLG--NACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPA-DIWSTACMAFELAT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 211 GQPPFQE------ANDSETLTMIMDC------------------------------------------KYTVPPRVSAGC 242
Cdd:cd14216   243 GDYLFEPhsgedySRDEDHIALIIELlgkvprklivagkyskefftkkgdlkhitklkpwglfevlveKYEWSQEEAAGF 322
                         330       340
                  ....*....|....*....|....*..
gi 1907195986 243 RDLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14216   323 TDFLLPMLELIPEKRATAAECLRHPWL 349
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
18-265 9.13e-15

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 75.38  E-value: 9.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFA-VVKLARHVFTG----EKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd05045     4 LGKTLGEGEFGkVVKATAFRLKGragyTTVAVKML-KENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 E---------------------LGDGGDMFDYIMKH--EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE 149
Cdd:cd05045    83 EyakygslrsflresrkvgpsyLGSDGNRNSSYLDNpdERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 150 KQgLVKLTDFGFS-NKFQPGKKLTTSCGSL--AYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFqEANDSETLT 225
Cdd:cd05045   163 GR-KMKISDFGLSrDVYEEDSYVKRSKGRIpvKWMAIESLFDHIYTTQS-DVWSFGVLLWEIVTlGGNPY-PGIAPERLF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907195986 226 MIMDCKYTV--PPRVSAGCRDLITRMLQRDPKRRASLEEIES 265
Cdd:cd05045   240 NLLKTGYRMerPENCSEEMYNLMLTCWKQEPDKRPTFADISK 281
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
18-230 1.27e-14

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 74.73  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTK----LYLILE 93
Cdd:cd14032     5 FDIELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYiMKHEEGLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVFFEKQGLVKLTDFGFSNkFQPGKKL 171
Cdd:cd14032    85 LMTSGTLKTY-LKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTGSVKIGDLGLAT-LKRASFA 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195986 172 TTSCGSLAYSAPEILlgDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC 230
Cdd:cd14032   163 KSVIGTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTC 219
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
68-261 1.70e-14

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: 74.59  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  68 KLVQHPNIVRLYEVIDTQTKL-----YLILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKP 142
Cdd:cd14020    59 QLQGHRNIVTLYGVFTNHYSAnvpsrCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKP 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 143 ENVVFFEKQGLVKLTDFGFSnkFQPGKKLTTSCGSLAYSAPEILL-------GDEYDA---PAVDIWSLGVILFMLVCG- 211
Cdd:cd14020   139 RNILWSAEDECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAELqnclaqaGLQSETectSAVDLWSLGIVLLEMFSGm 216
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 212 ------QPPFQEANDSETLTMIMDCKYTVPPRVSA-GCRDLITRMLQRDPKRRASLE 261
Cdd:cd14020   217 klkhtvRSQEWKDNSSAIIDHIFASNAVVNPAIPAyHLRDLIKSMLHNDPGKRATAE 273
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
16-269 1.74e-14

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. 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 CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 75.27  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFA-VVKLARHVFTGEKVAVKVI---DKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd14213    14 YEIVDTLGEGAFGkVVECIDHKMGGMHVAVKIVknvDRYREAARSEIQVLEHLNTTDPNSTFRCVQMLEWFDHHGHVCIV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELgDGGDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE------------------KQG 152
Cdd:cd14213    94 FEL-LGLSTYDFIKENSfLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQsdyvvkynpkmkrdertlKNP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 153 LVKLTDFGfsNKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKY 232
Cdd:cd14213   173 DIKVVDFG--SATYDDEHHSTLVSTRHYRAPEVILALGWSQPC-DVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILG 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 233 TVPPRV---------------------SAG------CR-----------------DLITRMLQRDPKRRASLEEIESHPW 268
Cdd:cd14213   250 PLPKHMiqktrkrkyfhhdqldwdehsSAGryvrrrCKplkefmlsqdvdheqlfDLIQKMLEYDPAKRITLDEALKHPF 329

                  .
gi 1907195986 269 L 269
Cdd:cd14213   330 F 330
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
16-318 2.32e-14

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: 75.07  E-value: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFA-VVKLARHvFTGEKVAVKVIdKTKLDTLATGHLfqEVRCMKLVQHPN-----IVRLYEVIDTQTKLY 89
Cdd:cd14229     2 YEVLDFLGRGTFGqVVKCWKR-GTNEIVAVKIL-KNHPSYARQGQI--EVGILARLSNENadefnFVRAYECFQHRNHTC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGgDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE--KQGL-VKLTDFGfSNKF 165
Cdd:cd14229    78 LVFEMLEQ-NLYDFLKQNKfSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDpvRQPYrVKVIDFG-SASH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGKKLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKyTVPPR--VSAGCR 243
Cdd:cd14229   156 VSKTVCSTYLQSRYYRAPEIILGLPF-CEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQ-GLPGEqlLNVGTK 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 244 dlITRMLQRDPKRRAS---LEEIESHPWLQGVDPSPATKYniplvSYKNLSEEEHNSIIQRM----VLGDIADRDAIVEA 316
Cdd:cd14229   234 --TSRFFCRETDAPYSswrLKTLEEHEAETGMKSKEARKY-----IFNSLDDIAHVNMVMDLegsdLLAEKADRREFVAL 306

                  ..
gi 1907195986 317 LE 318
Cdd:cd14229   307 LK 308
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
20-217 2.38e-14

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: 74.23  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARhvFTGEKVAVKVIDKTKLDT-LATGHLFQEVrcmkLVQHPNIVRLYEV----IDTQTKLYLILEL 94
Cdd:cd14056     1 KTIGKGRYGEVWLGK--YRGEKVAVKIFSSRDEDSwFRETEIYQTV----MLRHENILGFIAAdiksTGSWTQLWLITEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEegLNEDLAKKYFAQIVHAISYCH--------KLHVVHRDLKPENVvffekqgLVK------LTDFG 160
Cdd:cd14056    75 HEHGSLYDYLQRNT--LDTEEALRLAYSAASGLAHLHteivgtqgKPAIAHRDLKSKNI-------LVKrdgtccIADLG 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 161 FSNKFQPGKKLT-----TSCGSLAYSAPEILLG----DEYDA-PAVDIWSLGVILFML----VCG------QPPFQE 217
Cdd:cd14056   146 LAVRYDSDTNTIdippnPRVGTKRYMAPEVLDDsinpKSFESfKMADIYSFGLVLWEIarrcEIGgiaeeyQLPYFG 222
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
22-263 2.47e-14

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: 74.26  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLAR----HVFTGEK------------VAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQ 85
Cdd:cd05095    13 LGEGQFGEVHLCEaegmEKFMDKDfalevsenqpvlVAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  86 TKLYLILELGDGGDMFDYIMKHE-EGLNEDLAK---------KYFA-QIVHAISYCHKLHVVHRDLKPENVVfFEKQGLV 154
Cdd:cd05095    92 DPLCMITEYMENGDLNQFLSRQQpEGQLALPSNaltvsysdlRFMAaQIASGMKYLSSLNFVHRDLATRNCL-VGKNYTI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 155 KLTDFGFSNKFQPGKKLTTSCGSLA----YSAPEILLGDEydAPAVDIWSLGVILF--MLVCGQPPFQEANDSE----TL 224
Cdd:cd05095   171 KIADFGMSRNLYSGDYYRIQGRAVLpirwMSWESILLGKF--TTASDVWAFGVTLWetLTFCREQPYSQLSDEQvienTG 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907195986 225 TMIMDCKYTVPPRVSAGCRDLITRML----QRDPKRRASLEEI 263
Cdd:cd05095   249 EFFRDQGRQTYLPQPALCPDSVYKLMlscwRRDTKDRPSFQEI 291
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
16-331 2.61e-14

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: 75.13  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLfqEVRCMKLVQHPN-----IVRLYEVIDTQTKLYL 90
Cdd:cd14228    17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKIL-KNHPSYARQGQI--EVSILSRLSSENadeynFVRSYECFQHKNHTCL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGgDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE---KQGLVKLTDFGFSNKFQ 166
Cdd:cd14228    94 VFEMLEQ-NLYDFLKQNKfSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDpvrQPYRVKVIDFGSASHVS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKkLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKyTVPPR--VSAGCRd 244
Cdd:cd14228   173 KAV-CSTYLQSRYYRAPEIILGLPF-CEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ-GLPAEylLSAGTK- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 245 lITRMLQRDPKRRASLEEI---ESHPWLQGVDPSPATKY-------------NIPLVSYKNLSEE----EHNSIIQRMVl 304
Cdd:cd14228   249 -TSRFFNRDPNLGYPLWRLktpEEHELETGIKSKEARKYifnclddmaqvnmSTDLEGTDMLAEKadrrEYIDLLKKML- 326
                         330       340
                  ....*....|....*....|....*..
gi 1907195986 305 gdIADRDAIVEALETNRYNHITATYFL 331
Cdd:cd14228   327 --TIDADKRITPLKTLNHPFVTMTHLL 351
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
22-265 3.20e-14

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 73.85  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLAR-HVFTGEK----VAVKVIdktKLDTLATGHLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd05092    13 LGEGAFGKVFLAEcHNLLPEQdkmlVAVKAL---KEATESARQDFQrEAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKH-------EEGLNEDLAKKYFAQIVHAIS-------YCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGF 161
Cdd:cd05092    90 RHGDLNRFLRSHgpdakilDGGEGQAPGQLTLGQMLQIASqiasgmvYLASLHFVHRDLATRNCLVGQGL-VVKIGDFGM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 S------NKFQPGKKLTTscgSLAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMI-----MD 229
Cdd:cd05092   169 SrdiystDYYRVGGRTML---PIRWMPPESILYRKFTTES-DIWSFGVVLWeIFTYGKQPWYQLSNTEAIECItqgreLE 244
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907195986 230 CKYTVPPRVSagcrDLITRMLQRDPKRRASLEEIES 265
Cdd:cd05092   245 RPRTCPPEVY----AIMQGCWQREPQQRHSIKDIHS 276
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
22-222 3.22e-14

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: 74.70  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMf 101
Cdd:cd06649    13 LGAGNGGVVTKVQHKPSGLIMARKLI-HLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSL- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 DYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLH-VVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKlTTSCGSLAY 180
Cdd:cd06649    91 DQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNIL-VNSRGEIKLCDFGVSGQLIDSMA-NSFVGTRSY 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907195986 181 SAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSE 222
Cdd:cd06649   169 MSPERLQGTHYSVQS-DIWSMGLSLVELAIGRYPIPPPDAKE 209
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
18-263 5.67e-14

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 73.12  E-value: 5.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGE--KVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVI--DTQTKLY---- 89
Cdd:cd05075     4 LGKTLGEGEFGSVMEGQLNQDDSvlKVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVClqNTESEGYpspv 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEG-----LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNK 164
Cdd:cd05075    84 VILPFMKHGDLHSFLLYSRLGdcpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMN-VCVADFGLSKK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 165 FQPG---KKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMIMDC-KYTVPPRVS 239
Cdd:cd05075   163 IYNGdyyRQGRISKMPVKWIAIESLADRVYTTKS-DVWSFGVTMWEIATrGQTPYPGVENSEIYDYLRQGnRLKQPPDCL 241
                         250       260
                  ....*....|....*....|....
gi 1907195986 240 AGCRDLITRMLQRDPKRRASLEEI 263
Cdd:cd05075   242 DGLYELMSSCWLLNPKDRPSFETL 265
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
20-264 9.38e-14

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: 71.97  E-value: 9.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARhvFTGEkVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVrLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd14150     6 KRIGTGSFGTVFRGK--WHGD-VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGSS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNE----DLAKkyfaQIVHAISYCHKLHVVHRDLKPENVvfFEKQGL-VKLTDFGFS---NKFQPGKKL 171
Cdd:cd14150    82 LYRHLHVTETRFDTmqliDVAR----QTAQGMDYLHAKNIIHRDLKSNNI--FLHEGLtVKIGDFGLAtvkTRWSGSQQV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILLGDEYDAPAV--DIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP--PRVSAGCRDLIT 247
Cdd:cd14150   156 EQPSGSILWMAPEVIRMQDTNPYSFqsDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSPdlSKLSSNCPKAMK 235
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 248 RML------QRD-----PKRRASLEEIE 264
Cdd:cd14150   236 RLLidclkfKREerplfPQILVSIELLQ 263
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
18-263 1.02e-13

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 72.11  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLA--RHVFTGEK---VAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLIL 92
Cdd:cd05049     9 LKRELGEGAFGKVFLGecYNLEPEQDkmlVAVKTL-KDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  93 ELGDGGDMFDYIMKHEEGL----NEDLAKKYF---------AQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDF 159
Cdd:cd05049    88 EYMEHGDLNKFLRSHGPDAaflaSEDSAPGELtlsqllhiaVQIASGMVYLASQHFVHRDLATRNCLVGTNL-VVKIGDF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 160 GFS------NKFQPGKkltTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKY 232
Cdd:cd05049   167 GMSrdiystDYYRVGG---HTMLPIRWMPPESILYRKFTTES-DVWSFGVVLWeIFTYGKQPWFQLSNTEVIECITQGRL 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 233 TVPPRV-SAGCRDLITRMLQRDPKRRASLEEI 263
Cdd:cd05049   243 LQRPRTcPSEVYAVMLGCWKREPQQRLNIKDI 274
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
69-267 1.12e-13

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: 72.05  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  69 LVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKHE---EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENV 145
Cdd:cd14051    56 LGKHPHVVRYYSAWAEDDHMIIQNEYCNGGSLADAISENEkagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 146 VFFEKQGLVKL----TDFGFSNKFQPGKKLTTSCGSLA----------------YSAPEILLGDEYDAPAVDIWSLGVIL 205
Cdd:cd14051   136 FISRTPNPVSSeeeeEDFEGEEDNPESNEVTYKIGDLGhvtsisnpqveegdcrFLANEILQENYSHLPKADIFALALTV 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195986 206 FMLVCGQP-PfqeANDSEtLTMIMDCKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEIESHP 267
Cdd:cd14051   216 YEAAGGGPlP---KNGDE-WHEIRQGNLPPLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
18-221 2.85e-13

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 70.91  E-value: 2.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYE----VIDTQTKLYLILE 93
Cdd:cd14031    14 FDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDswesVLKGKKCIVLVTE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYiMKHEEGLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKl 171
Cdd:cd14031    94 LMTSGTLKTY-LKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTGSVKIGDLGLATLMRTSFA- 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEILlgDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDS 221
Cdd:cd14031   172 KSVIGTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNA 219
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
38-258 3.67e-13

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 73.34  E-value: 3.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   38 TGEKVAVKVIdktKLDTLATGHLFQEVR-----CMKLvQHPNIVRLYEVIDTQ-TKLYLILELGDGGDMFDyIMKHEEGL 111
Cdd:TIGR03903    2 TGHEVAIKLL---RTDAPEEEHQRARFRretalCARL-YHPNIVALLDSGEAPpGLLFAVFEYVPGRTLRE-VLAADGAL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  112 NEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGL--VKLTDFGFSNkFQPG------KKLTTS---CGSLAY 180
Cdd:TIGR03903   77 PAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRphAKVLDFGIGT-LLPGvrdadvATLTRTtevLGTPTY 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  181 SAPEILLGdEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPRVSAGCR--DLITRMLQRDPKRRA 258
Cdd:TIGR03903  156 CAPEQLRG-EPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVSLPPWIAGHPlgQVLRKALNKDPRQRA 234
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
22-205 4.16e-13

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 69.81  E-value: 4.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKvidktkLDTLAT--GHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALK------MNTLSSnrANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MfDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENV-VFFEKQGLVKLT-DFGFSNK---FQPGKKLTTS 174
Cdd:cd14155    75 L-EQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNClIKRDENGYTAVVgDFGLAEKipdYSDGKEKLAV 153
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907195986 175 CGSLAYSAPEILLGDEYDAPAvDIWSLGVIL 205
Cdd:cd14155   154 VGSPYWMAPEVLRGEPYNEKA-DVFSYGIIL 183
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
122-269 4.25e-13

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: 71.19  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 122 QIVHAISYCHKLHVVHRDLKPENVVF----FE--------------KQGLVKLTDFG---FSNKFQpgkklTTSCGSLAY 180
Cdd:cd14214   125 QLCHALKFLHENQLTHTDLKPENILFvnseFDtlynesksceeksvKNTSIRVADFGsatFDHEHH-----TTIVATRHY 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 181 SAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPPR----------------------- 237
Cdd:cd14214   200 RPPEVILELGWAQPC-DVWSLGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHmihrtrkqkyfykgslvwdenss 278
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907195986 238 ----VSAGCR-----------------DLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14214   279 dgryVSENCKplmsymlgdslehtqlfDLLRRMLEFDPALRITLKEALLHPFF 331
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
16-280 4.47e-13

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: 71.27  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGHLfqEVRCMKLVQHP-----NIVRLYEVIDTQTKLYL 90
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL-KNHPSYARQGQI--EVSILARLSTEsaddyNFVRAYECFQHKNHTCL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGgDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFE---KQGLVKLTDFGFSNKFQ 166
Cdd:cd14227    94 VFEMLEQ-NLYDFLKQNKfSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDpsrQPYRVKVIDFGSASHVS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKkLTTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKyTVPPR--VSAGCRd 244
Cdd:cd14227   173 KAV-CSTYLQSRYYRAPEIILGLPF-CEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ-GLPAEylLSAGTK- 248
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907195986 245 lITRMLQRD---PKRRASLEEIESHPWLQGVDPSPATKY 280
Cdd:cd14227   249 -TTRFFNRDtdsPYPLWRLKTPEDHEAETGIKSKEARKY 286
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
22-270 5.92e-13

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: 70.06  E-value: 5.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLAR----HVFTGEK------------VAVKV----IDKTKLDTLatghlFQEVRCMKLVQHPNIVRLYEV 81
Cdd:cd05051    13 LGEGQFGEVHLCEanglSDLTSDDfigndnkdepvlVAVKMlrpdASKNAREDF-----LKEVKIMSQLKDPNIVRLLGV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  82 IDTQTKLYLILELGDGGDMFDYIMKHEEGLNEDLAKK----------YFA-QIVHAISYCHKLHVVHRDLKPENVVfFEK 150
Cdd:cd05051    88 CTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNsktlsygtllYMAtQIASGMKYLESLNFVHRDLATRNCL-VGP 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 151 QGLVKLTDFGFSNKfqpgkklttscgslAYS-----------------APEILLGDEYDApAVDIWSLGVIL---FMLvC 210
Cdd:cd05051   167 NYTIKIADFGMSRN--------------LYSgdyyriegravlpirwmAWESILLGKFTT-KSDVWAFGVTLweiLTL-C 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907195986 211 GQPPFQEANDSEtltMIMDC--KYTV---------PPRVSAGCRDLITRMLQRDPKRRASLEEIesHPWLQ 270
Cdd:cd05051   231 KEQPYEHLTDEQ---VIENAgeFFRDdgmevylsrPPNCPKEIYELMLECWRRDEEDRPTFREI--HLFLQ 296
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
20-272 6.14e-13

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


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 70.00  E-value: 6.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVV--KLARHVFTGE---KVAVKVIDKTKlDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05061    12 RELGQGSFGMVyeGNARDIIKGEaetRVAVKTVNESA-SLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYI------MKHEEGLNEDLAKKYF---AQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKF 165
Cdd:cd05061    91 MAHGDLKSYLrslrpeAENNPGRPPPTLQEMIqmaAEIADGMAYLNAKKFVHRDLAARNCMVAHDFT-VKIGDFGMTRDI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 -------QPGKKLTtscgSLAYSAPEIlLGDEYDAPAVDIWSLGVILFMLVC-GQPPFQEANDSETLTMIMDCKY----- 232
Cdd:cd05061   170 yetdyyrKGGKGLL----PVRWMAPES-LKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVMDGGYldqpd 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907195986 233 TVPPRVSagcrDLITRMLQRDPKRRASLEEI------ESHPWLQGV 272
Cdd:cd05061   245 NCPERVT----DLMRMCWQFNPKMRPTFLEIvnllkdDLHPSFPEV 286
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
18-265 6.29e-13

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: 69.51  E-value: 6.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEK---VAVKVI-----DKTKLDTLAtghlfqEVRCMKLVQHPNIVRLYEVIDTQTKLY 89
Cdd:cd05066     8 IEKVIGAGEFGEVCSGRLKLPGKReipVAIKTLkagytEKQRRDFLS------EASIMGQFDHPNIIHLEGVVTRSKPVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfeKQGLV-KLTDFGFSNKFQ-- 166
Cdd:cd05066    82 IVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILV--NSNLVcKVSDFGLSRVLEdd 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 167 PGKKLTTSCGSLA--YSAPEILLGDEYDApAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMImDCKYTVPPRVS--AG 241
Cdd:cd05066   160 PEAAYTTRGGKIPirWTAPEAIAYRKFTS-ASDVWSYGIVMWeVMSYGERPYWEMSNQDVIKAI-EEGYRLPAPMDcpAA 237
                         250       260
                  ....*....|....*....|....
gi 1907195986 242 CRDLITRMLQRDPKRRASLEEIES 265
Cdd:cd05066   238 LHQLMLDCWQKDRNERPKFEQIVS 261
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
22-208 6.32e-13

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: 69.92  E-value: 6.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHV----FTGEKVAVKVIDKTKLDTLATghlFQ-EVRCMKLVQHPNIVRLYEVIDTQTK--LYLILEL 94
Cdd:cd05081    12 LGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDQQRD---FQrEIQILKALHSDFIVKYRGVSYGPGRrsLRLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSnKFQPGKK---L 171
Cdd:cd05081    89 LPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNIL-VESEAHVKIADFGLA-KLLPLDKdyyV 166
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907195986 172 TTSCGS--LAYSAPEIlLGDEYDAPAVDIWSLGVILFML 208
Cdd:cd05081   167 VREPGQspIFWYAPES-LSDNIFSRQSDVWSFGVVLYEL 204
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
19-265 8.58e-13

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: 69.23  E-value: 8.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  19 DKTLGRGHFAVVKLARHVFTGEK---VAVKVI-----DKTKLDTLAtghlfqEVRCMKLVQHPNIVRLYEVIDTQTKLYL 90
Cdd:cd05063    10 QKVIGAGEFGEVFRGILKMPGRKevaVAIKTLkpgytEKQRQDFLS------EASIMGQFSHHNIIRLEGVVTKFKPAMI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQ--PG 168
Cdd:cd05063    84 ITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNIL-VNSNLECKVSDFGLSRVLEddPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLA--YSAPEILLGDEYdAPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDC-KYTVPPRVSAGCRD 244
Cdd:cd05063   163 GTYTTSGGKIPirWTAPEAIAYRKF-TSASDVWSFGIVMWeVMSFGERPYWDMSNHEVMKAINDGfRLPAPMDCPSAVYQ 241
                         250       260
                  ....*....|....*....|.
gi 1907195986 245 LITRMLQRDPKRRASLEEIES 265
Cdd:cd05063   242 LMLQCWQQDRARRPRFVDIVN 262
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
36-265 9.83e-13

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: 68.96  E-value: 9.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  36 VFTGEKVAVKVIDKTKLdtlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKHEEGLNEDL 115
Cdd:cd13992    22 VYGGRTVAIKHITFSRT---EKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 116 AKKYFAQIVHAISYCHKLH-VVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGKKL----TTSCGSLAYSAPEILLGDE 190
Cdd:cd13992    99 KSSFIKDIVKGMNYLHSSSiGYHGRLKSSNCLV-DSRWVVKLTDFGLRNLLEEQTNHqldeDAQHKKLLWTAPELLRGSL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 191 YD---APAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKyTVPPR---------VSAGCRDLITRMLQRDPKRRA 258
Cdd:cd13992   178 LEvrgTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGG-NKPFRpelavlldeFPPRLVLLVKQCWAENPEKRP 256

                  ....*..
gi 1907195986 259 SLEEIES 265
Cdd:cd13992   257 SFKQIKK 263
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
9-263 1.09e-12

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 68.93  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986   9 DGKIAglydLDKTLGRGHFAVVKLARhvFTGEkVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVrLYEVIDTQTKL 88
Cdd:cd14151     7 DGQIT----VGQRIGSGSFGTVYKGK--WHGD-VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFS---NKF 165
Cdd:cd14151    79 AIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNN-IFLHEDLTVKIGDFGLAtvkSRW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 166 QPGKKLTTSCGSLAYSAPEILLGDEYDAPAV--DIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP--PRVSAG 241
Cdd:cd14151   158 SGSHQFEQLSGSILWMAPEVIRMQDKNPYSFqsDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPdlSKVRSN 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907195986 242 CRDLITRML------QRD-----PKRRASLEEI 263
Cdd:cd14151   238 CPKAMKRLMaeclkkKRDerplfPQILASIELL 270
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
42-265 1.18e-12

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: 69.58  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  42 VAVKVI--DKTKLdtlATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKH------EEGLNE 113
Cdd:cd05096    49 VAVKILrpDANKN---ARNDFLKEVKILSRLKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHhlddkeENGNDA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 114 D------LAKKY------FAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQPGKKLTTSCGS---L 178
Cdd:cd05096   126 VppahclPAISYssllhvALQIASGMKYLSSLNFVHRDLATRNCLVGENL-TIKIADFGMSRNLYAGDYYRIQGRAvlpI 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 179 AYSAPEILLGDEYDApAVDIWSLGVILF--MLVCGQPPFQEANDSETL----TMIMDCKYTV----PPRVSAGCRDLITR 248
Cdd:cd05096   205 RWMAWECILMGKFTT-ASDVWAFGVTLWeiLMLCKEQPYGELTDEQVIenagEFFRDQGRQVylfrPPPCPQGLYELMLQ 283
                         250
                  ....*....|....*..
gi 1907195986 249 MLQRDPKRRASLEEIES 265
Cdd:cd05096   284 CWSRDCRERPSFSDIHA 300
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
17-224 1.73e-12

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: 69.13  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  17 DLDKTLGRG--HFAVVKLARHVFTGEKVAVKVidkTKLDTLATGHLF---QEVRCMKLVQHPNIVRLYEVIDTQTKLYLI 91
Cdd:cd08226     1 ELQVELGKGfcNLTSVYLARHTPTGTLVTVKI---TNLDNCSEEHLKalqNEVVLSHFFRHPNIMTHWTVFTEGSWLWVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  92 LELGDGGDMFDYIMKH-EEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTdfGFSNKF---QP 167
Cdd:cd08226    78 SPFMAYGSARGLLKTYfPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISG-DGLVSLS--GLSHLYsmvTN 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 168 GKKLTT-------SCGSLAYSAPEILLGD--EYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETL 224
Cdd:cd08226   155 GQRSKVvydfpqfSTSVLPWLSPELLRQDlhGYNVKS-DIYSVGITACELARGQVPFQDMRRTQML 219
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
20-266 1.79e-12

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: 68.56  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFA-VVKLARHVFTGEKVAVKVIDKTkLDTLATGHL----FQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05048    11 EELGEGAFGkVYKGELLGPSSEESAISVAIKT-LKENASPKTqqdfRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKH-----------EEGLNEDLAKKYF----AQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDF 159
Cdd:cd05048    90 MAHGDLHEFLVRHsphsdvgvssdDDGTASSLDQSDFlhiaIQIAAGMEYLSSHHYVHRDLAARNCLVGDGL-TVKISDF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 160 GFSNKF-------QPGKKLTtscgSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVC-GQPPFQEANDSETLTMI---- 227
Cdd:cd05048   169 GLSRDIyssdyyrVQSKSLL----PVRWMPPEAILYGKF-TTESDVWSFGVVLWEIFSyGLQPYYGYSNQEVIEMIrsrq 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907195986 228 -MDCKYTVPPRVSAgcrdLITRMLQRDPKRRASLEEIESH 266
Cdd:cd05048   244 lLPCPEDCPARVYS----LMVECWHEIPSRRPRFKEIHTR 279
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
23-217 1.82e-12

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 68.62  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  23 GRGHFAVVKLARhvFTGEKVAVKVIDktkldtlatghlFQEVRCMK---------LVQHPNIVRL----YEVIDTQTKLY 89
Cdd:cd13998     4 GKGRFGEVWKAS--LKNEPVAVKIFS------------SRDKQSWFrekeiyrtpMLKHENILQFiaadERDTALRTELW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEGLNE--DLAKKYFAQIVH---AISYC--HKLHVVHRDLKPENVVfFEKQGLVKLTDFGFS 162
Cdd:cd13998    70 LVTAFHPNGSL*DYLSLHTIDWVSlcRLALSVARGLAHlhsEIPGCtqGKPAIAHRDLKSKNIL-VKNDGTCCIADFGLA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 163 NKFQPG-----KKLTTSCGSLAYSAPEILLG-----DEYDAPAVDIWSLGVILFMLV--CG---------QPPFQE 217
Cdd:cd13998   149 VRLSPStgeedNANNGQVGTKRYMAPEVLEGainlrDFESFKRVDIYAMGLVLWEMAsrCTdlfgiveeyKPPFYS 224
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
16-317 3.58e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 68.36  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFAVVKLARHVFTGEKVAVKVidKTKLDTLATGHLFQEVrcmklvQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:PHA03209   68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKI--GQKGTTLIEAMLLQNV------NHPSVIRMKDTLVSGAITCMVLPHY 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:PHA03209  140 SS-DLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTEN-IFINDVDQVCIGDLGAAQFPVVAPAFLGLA 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVpprvsagcRDLITRM------ 249
Cdd:PHA03209  218 GTVETNAPEVLARDKYNS-KADIWSAGIVLFEMLAYPSTIFEDPPSTPEEYVKSCHSHL--------LKIISTLkvhpee 288
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 250 LQRDPKRRASLEEIEshpwLQGVDPSPATKYniPLVSYKNLsEEEHNSIIQRMVLGDIADRDAIVEAL 317
Cdd:PHA03209  289 FPRDPGSRLVRGFIE----YASLERQPYTRY--PCFQRVNL-PIDGEFLVHKMLTFDAAMRPSAEEIL 349
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
63-212 4.50e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 68.48  E-value: 4.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  63 EVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGgDMFDYIM-KHEEGLNEDLAKKyfAQIVHAISYCHKLHVVHRDLK 141
Cdd:PHA03212  133 EAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAaKRNIAICDILAIE--RSVLRAIQYLHENRIIHRDIK 209
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195986 142 PENVvFFEKQGLVKLTDFGFS--------NKFQpgkkltTSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILFMLVCGQ 212
Cdd:PHA03212  210 AENI-FINHPGDVCLGDFGAAcfpvdinaNKYY------GWAGTIATNAPELLARDPY-GPAVDIWSAGIVLFEMATCH 280
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
45-209 4.82e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 68.95  E-value: 4.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  45 KVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGgDMFDYIMkheeglNEDL--------- 115
Cdd:PHA03210  195 LIAKRVKAGSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMITQKYDF-DLYSFMY------DEAFdwkdrpllk 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 116 -AKKYFAQIVHAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGKKLTTS--CGSLAYSAPEILLGDEYd 192
Cdd:PHA03210  268 qTRAIMKQLLCAVEYIHDKKLIHRDIKLEN-IFLNCDGKIVLGDFGTAMPFEKEREAFDYgwVGTVATNSPEILAGDGY- 345
                         170
                  ....*....|....*..
gi 1907195986 193 APAVDIWSLGVILFMLV 209
Cdd:PHA03210  346 CEITDIWSCGLILLDML 362
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
16-269 6.05e-12

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. 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 CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 67.73  E-value: 6.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  16 YDLDKTLGRGHFA-VVKLARHVFTGEKVAVKVI---DKTKLDTLATGHLFQEVRcMKLVQHPNI-VRLYEVIDTQTKLYL 90
Cdd:cd14215    14 YEIVSTLGEGTFGrVVQCIDHRRGGARVALKIIknvEKYKEAARLEINVLEKIN-EKDPENKNLcVQMFDWFDYHGHMCI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  91 ILELgDGGDMFDYiMKHEEGLNEDLAK-KYFA-QIVHAISYCHKLHVVHRDLKPENVVFFE------------------K 150
Cdd:cd14215    93 SFEL-LGLSTFDF-LKENNYLPYPIHQvRHMAfQVCQAVKFLHDNKLTHTDLKPENILFVNsdyeltynlekkrdersvK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 151 QGLVKLTDFGfSNKFQpGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDC 230
Cdd:cd14215   171 STAIRVVDFG-SATFD-HEHHSTIVSTRHYRAPEVILELGWSQPC-DVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 231 KYTVPPRV---------------------SAG------CR-----------------DLITRMLQRDPKRRASLEEIESH 266
Cdd:cd14215   248 LGPIPSRMirktrkqkyfyhgrldwdentSAGryvrenCKplrryltseaeehhqlfDLIESMLEYEPSKRLTLAAALKH 327

                  ...
gi 1907195986 267 PWL 269
Cdd:cd14215   328 PFF 330
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
22-265 6.40e-12

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 66.75  E-value: 6.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLylilelgdggdmf 101
Cdd:cd14025     4 VGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEPVGL------------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 102 dyIMKHEE--GLNEDLA------KKYFaQIVHAIS------YCHKLHVVHRDLKPENVVfFEKQGLVKLTDFG------F 161
Cdd:cd14025    71 --VMEYMEtgSLEKLLAseplpwELRF-RIIHETAvgmnflHCMKPPLLHLDLKPANIL-LDAHYHVKISDFGlakwngL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 162 SNKFQpgKKLTTSCGSLAYSAPE-ILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDsetLTMIMdckytvpPRVSA 240
Cdd:cd14025   147 SHSHD--LSRDGLRGTIAYLPPErFKEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENN---ILHIM-------VKVVK 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907195986 241 GCR------------------DLITRMLQRDPKRRASLEEIES 265
Cdd:cd14025   215 GHRpslspiprqrpsecqqmiCLMKRCWDQDPRKRPTFQDITS 257
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
62-263 7.44e-12

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: 66.57  E-value: 7.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  62 QEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDY-IMK--HEE---GLNEDLAKK---------YFA-QIVH 125
Cdd:cd05090    56 QEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFlIMRspHSDvgcSSDEDGTVKssldhgdflHIAiQIAA 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 126 AISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPGKKLTTSCGSL---AYSAPEILLGDEYDAPAvDIWSLG 202
Cdd:cd05090   136 GMEYLSSHFFVHKDLAARNILVGE-QLHVKISDLGLSREIYSSDYYRVQNKSLlpiRWMPPEAIMYGKFSSDS-DIWSFG 213
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 203 VILF-MLVCGQPPFQEANDSETLTMI-----MDCKYTVPPRVSAgcrdLITRMLQRDPKRRASLEEI 263
Cdd:cd05090   214 VVLWeIFSFGLQPYYGFSNQEVIEMVrkrqlLPCSEDCPPRMYS----LMTECWQEIPSRRPRFKDI 276
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
14-269 8.86e-12

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 67.35  E-value: 8.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  14 GLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDTLATGhlFQEVRCMKLVQH-----PNIVRLYEVID----- 83
Cdd:cd14218    10 GRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVV-KSAVHYTETA--VDEIKLLKCVRDsdpsdPKRETIVQLIDdfkis 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  84 --TQTKLYLILELgDGGDMFDYIMKHE-EGLNEDLAKKYFAQIVHAISYCH-KLHVVHRDLKPENVVFFEKQGLVK---- 155
Cdd:cd14218    87 gvNGVHVCMVLEV-LGHQLLKWIIKSNyQGLPLPCVKSILRQVLQGLDYLHtKCKIIHTDIKPENILMCVDEGYVRrlaa 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 156 ----------------LTDFGFS----NKFQPG-------------------KKLTTSCGSLAYSAPEILLGDEYDAPAv 196
Cdd:cd14218   166 eatiwqqagapppsgsSVSFGASdflvNPLEPQnadkirvkiadlgnacwvhKHFTEDIQTRQYRALEVLIGAEYGTPA- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 197 DIWSLGVILFMLVCGQPPFQE------ANDSETLTMIMDCKYTVPPRVSAGCR--------------------------- 243
Cdd:cd14218   245 DIWSTACMAFELATGDYLFEPhsgedyTRDEDHIAHIVELLGDIPPHFALSGRysreyfnrrgelrhiknlkhwglyevl 324
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1907195986 244 ---------------DLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14218   325 vekyewpleqaaqftDFLLPMMEFLPEKRATAAQCLQHPWL 365
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
20-213 9.12e-12

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: 66.63  E-value: 9.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKV----AVKVIDKTKlDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTkLYLILELG 95
Cdd:cd05110    13 KVLGSGAFGTVYKGIWVPEGETVkipvAIKILNETT-GPKANVEFMDEALIMASMDHPHLVRLLGVCLSPT-IQLVTQLM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd05110    91 PHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVL-VKSPNHVKITDFGLARLLEGDEKEYNAD 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907195986 176 GS---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC--GQP 213
Cdd:cd05110   170 GGkmpIKWMALECIHYRKFTHQS-DVWSYGVTIWELMTfgGKP 211
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-235 1.58e-11

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 65.82  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARhvFTGEkVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVrLYEVIDTQTKLYLILELGDG 97
Cdd:cd14149    16 LSTRIGSGSFGTVYKGK--WHGD-VAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  98 GDMFDYIMKHEEGLNE----DLAKkyfaQIVHAISYCHKLHVVHRDLKPENVvfFEKQGL-VKLTDFGFSN---KFQPGK 169
Cdd:cd14149    92 SSLYKHLHVQETKFQMfqliDIAR----QTAQGMDYLHAKNIIHRDMKSNNI--FLHEGLtVKIGDFGLATvksRWSGSQ 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195986 170 KLTTSCGSLAYSAPEILLGDEYDAPAV--DIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVP 235
Cdd:cd14149   166 QVEQPTGSILWMAPEVIRMQDNNPFSFqsDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASP 233
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
18-265 1.99e-11

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 65.28  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEK---VAVKVI-----DKTKLDTLAtghlfqEVRCMKLVQHPNIVRLYEVIDTQTKLY 89
Cdd:cd05065     8 IEEVIGAGEFGEVCRGRLKLPGKReifVAIKTLksgytEKQRRDFLS------EASIMGQFDHPNIIHLEGVVTKSRPVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  90 LILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFfeKQGLV-KLTDFGFSNKFQPG 168
Cdd:cd05065    82 IITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILV--NSNLVcKVSDFGLSRFLEDD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 169 KKLTTSCGSLA------YSAPEILLGDEYDApAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMI-MDCKYTVPPRVSA 240
Cdd:cd05065   160 TSDPTYTSSLGgkipirWTAPEAIAYRKFTS-ASDVWSYGIVMWeVMSYGERPYWDMSNQDVINAIeQDYRLPPPMDCPT 238
                         250       260
                  ....*....|....*....|....*
gi 1907195986 241 GCRDLITRMLQRDPKRRASLEEIES 265
Cdd:cd05065   239 ALHQLMLDCWQKDRNLRPKFGQIVN 263
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
18-235 2.38e-11

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 65.42  E-value: 2.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGE-------KVAVKVI--DKTKLDTlatGHLFQEVRCMKLV-QHPNIVRLYEVIDTQTK 87
Cdd:cd05098    17 LGKPLGEGCFGQVVLAEAIGLDKdkpnrvtKVAVKMLksDATEKDL---SDLISEMEMMKMIgKHKNIINLLGACTQDGP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGGDMFDYI-MKHEEGL----------NEDLAKKYFA----QIVHAISYCHKLHVVHRDLKPENVVFFEKQg 152
Cdd:cd05098    94 LYVIVEYASKGNLREYLqARRPPGMeycynpshnpEEQLSSKDLVscayQVARGMEYLASKKCIHRDLAARNVLVTEDN- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 153 LVKLTDFGFSNKFQP---GKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC--GQP----PFQE------ 217
Cdd:cd05098   173 VMKIADFGLARDIHHidyYKKTTNGRLPVKWMAPEALFDRIYTHQS-DVWSFGVLLWEIFTlgGSPypgvPVEElfkllk 251
                         250       260
                  ....*....|....*....|....*..
gi 1907195986 218 --------ANDSETLTMIM-DCKYTVP 235
Cdd:cd05098   252 eghrmdkpSNCTNELYMMMrDCWHAVP 278
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
18-263 2.49e-11

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 64.86  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVV---KLARHVFTGEKVAVKVIdktKLDTLATGHL---FQEVRCMKLVQHPNIVRLYEVIDTQTKL--- 88
Cdd:cd05035     3 LGKILGEGEFGSVmeaQLKQDDGSQLKVAVKTM---KVDIHTYSEIeefLSEAACMKDFDHPNVMRLIGVCFTASDLnkp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 ---YLILELGDGGDMFDYIMKHE-EGLNEDLAK----KYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVkLTDFG 160
Cdd:cd05035    80 pspMVILPFMKHGDLHSYLLYSRlGGLPEKLPLqtllKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVC-VADFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 FSNKFQPGKKLTTSCGS---LAYSAPEIlLGDEYDAPAVDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMD-CKYTVP 235
Cdd:cd05035   159 LSRKIYSGDYYRQGRISkmpVKWIALES-LADNVYTSKSDVWSFGVTMWeIATRGQTPYPGVENHEIYDYLRNgNRLKQP 237
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 236 PRVSAGCRDLITRMLQRDPKRRASLEEI 263
Cdd:cd05035   238 EDCLDEVYFLMYFCWTVDPKDRPTFTKL 265
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
18-235 2.83e-11

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 65.42  E-value: 2.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEK-------VAVKVI--DKTKLDTlatGHLFQEVRCMKLV-QHPNIVRLYEVIDTQTK 87
Cdd:cd05101    28 LGKPLGEGCFGQVVMAEAVGIDKDkpkeavtVAVKMLkdDATEKDL---SDLVSEMEMMKMIgKHKNIINLLGACTQDGP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGGDMFDYI-------MKHEEGLN---------EDLAKKYFaQIVHAISYCHKLHVVHRDLKPENVVFFEKQ 151
Cdd:cd05101   105 LYVIVEYASKGNLREYLrarrppgMEYSYDINrvpeeqmtfKDLVSCTY-QLARGMEYLASQKCIHRDLAARNVLVTENN 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 152 gLVKLTDFGFS---NKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC--GQP----PFQE----- 217
Cdd:cd05101   184 -VMKIADFGLArdiNNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQS-DVWSFGVLMWEIFTlgGSPypgiPVEElfkll 261
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 218 ---------ANDSETLTMIM-DCKYTVP 235
Cdd:cd05101   262 keghrmdkpANCTNELYMMMrDCWHAVP 289
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
18-272 2.95e-11

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 65.06  E-value: 2.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLAR-HVFTGEKVAVKVIDKTKLDTLATGH--LFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05093     9 LKRELGEGAFGKVFLAEcYNLCPEQDKILVAVKTLKDASDNARkdFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKH-------EEG-----LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFS 162
Cdd:cd05093    89 MKHGDLNKFLRAHgpdavlmAEGnrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL-LVKIGDFGMS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 163 NKFQPGKKLTTSCGSL---AYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKYTVPPRV 238
Cdd:cd05093   168 RDVYSTDYYRVGGHTMlpiRWMPPESIMYRKFTTES-DVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQGRVLQRPRT 246
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907195986 239 SAG-CRDLITRMLQRDPKRRASLEEIesHPWLQGV 272
Cdd:cd05093   247 CPKeVYDLMLGCWQREPHMRLNIKEI--HSLLQNL 279
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
20-215 2.97e-11

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 64.98  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTlATGHLFQEVR----CMKLVQHPNIVRLYEvIDTQTKLYLILELG 95
Cdd:cd05111    13 KVLGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQDR-SGRQSFQAVTdhmlAIGSLDHAYIVRLLG-ICPGASLQLVTQLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKK---LT 172
Cdd:cd05111    91 PLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVL-LKSPSQVQVADFGVADLLYPDDKkyfYS 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907195986 173 TSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPF 215
Cdd:cd05111   170 EAKTPIKWMALESIHFGKYTHQS-DVWSYGVTVWeMMTFGAEPY 212
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
22-218 3.08e-11

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


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 64.44  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARhVFTGEKVAVKVIdkTKLDTLATGHLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDM 100
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKRL--KGEGTQGGDHGFQaEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 101 FDYIM-KHEEGLNEDLAKKY--FAQIVHAISYCHK---LHVVHRDLKPENVVF---FEkqglVKLTDFGFSNKFQPGKK- 170
Cdd:cd14664    78 GELLHsRPESQPPLDWETRQriALGSARGLAYLHHdcsPLIIHRDVKSNNILLdeeFE----AHVADFGLAKLMDDKDSh 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907195986 171 -LTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVCGQPPFQEA 218
Cdd:cd14664   154 vMSSVAGSYGYIAPEYAYTGKVSEKS-DVYSYGVVLLELITGKRPFDEA 201
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
18-221 3.90e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 64.69  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTK----LYLILE 93
Cdd:cd14030    29 FDIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYiMKHEEGLNEDLAKKYFAQIVHAISYCHKLH--VVHRDLKPENVVFFEKQGLVKLTDFGFSNkFQPGKKL 171
Cdd:cd14030   109 LMTSGTLKTY-LKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTGSVKIGDLGLAT-LKRASFA 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907195986 172 TTSCGSLAYSAPEiLLGDEYDApAVDIWSLGVILFMLVCGQPPFQEANDS 221
Cdd:cd14030   187 KSVIGTPEFMAPE-MYEEKYDE-SVDVYAFGMCMLEMATSEYPYSECQNA 234
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
18-264 4.54e-11

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 64.26  E-value: 4.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLAR-HVFTGEKVAVKVIDKTKLD-TLATGHLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd05094     9 LKRELGEGAFGKVFLAEcYNLSPTKDKMLVAVKTLKDpTLAARKDFQrEAELLTNLQHDHIVKFYGVCGDGDPLIMVFEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKH-----------------EEGLNEDLakKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQgLVKLT 157
Cdd:cd05094    89 MKHGDLNKFLRAHgpdamilvdgqprqakgELGLSQML--HIATQIASGMVYLASQHFVHRDLATRNCLVGANL-LVKIG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 158 DFGFSNKFQPGKKLTTSCGSL---AYSAPEILLGDEYDAPAvDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKYT 233
Cdd:cd05094   166 DFGMSRDVYSTDYYRVGGHTMlpiRWMPPESIMYRKFTTES-DVWSFGVILWeIFTYGKQPWFQLSNTEVIECITQGRVL 244
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 234 VPPRVSAG-CRDLITRMLQRDPKRRASLEEIE 264
Cdd:cd05094   245 ERPRVCPKeVYDIMLGCWQREPQQRLNIKEIY 276
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
117-269 4.99e-11

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: 64.77  E-value: 4.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 117 KKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKLTTSCGSL--AYSAPE--ILLGDEYD 192
Cdd:cd14013   123 KSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQFKIIDLGAAADLRIGINYIPKEFLLdpRYAPPEqyIMSTQTPS 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 193 APAV-------------------DIWSLGVILFMLVCGqppfQEANDSETL---TMIMDCKY-------TVPPRVSAGCR 243
Cdd:cd14013   203 APPApvaaalspvlwqmnlpdrfDMYSAGVILLQMAFP----NLRSDSNLIafnRQLKQCDYdlnawrmLVEPRASADLR 278
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907195986 244 --------------DLITRMLQRDPKRRASLEEIESHPWL 269
Cdd:cd14013   279 egfeildlddgagwDLVTKLIRYKPRGRLSASAALAHPYF 318
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
22-214 5.24e-11

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 64.22  E-value: 5.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVkLARHVFTGEKVAVKVIDKTKLDTLATG-------HL------------FQEVRCMKLVQHPNIVRLYEVi 82
Cdd:cd14067     1 LGQGGSGTV-IYRARYQGQPVAVKRFHIKKCKKRTDGsadtmlkHLraadamknfsefRQEASMLHSLQHPCIVYLIGI- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  83 dTQTKLYLILELGDGGDMFDYIMKHEEG-----LNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFF---EKQGL- 153
Cdd:cd14067    79 -SIHPLCFALELAPLGSLNTVLEENHKGssfmpLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVWsldVQEHIn 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 154 VKLTDFGFSNK-FQPGKKLTTscGSLAYSAPEILLGDEYDApAVDIWSLGVILFMLVCGQPP 214
Cdd:cd14067   158 IKLSDYGISRQsFHEGALGVE--GTPGYQAPEIRPRIVYDE-KVDMFSYGMVLYELLSGQRP 216
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
20-261 5.80e-11

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: 63.89  E-value: 5.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARHVFTGEK----VAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTkLYLILELG 95
Cdd:cd05109    13 KVLGSGAFGTVYKGIWIPDGENvkipVAIKVL-RENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTST-VQLVTQLM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQPGKKLTTSC 175
Cdd:cd05109    91 PYGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVL-VKSPNHVKITDFGLARLLDIDETEYHAD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 176 GS---LAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPF-------------------QEANDSETLTMIMDCKY 232
Cdd:cd05109   170 GGkvpIKWMALESILHRRFTHQS-DVWSYGVTVWELMTfGAKPYdgipareipdllekgerlpQPPICTIDVYMIMVKCW 248
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907195986 233 TVPPRVSAGCRDLI---TRMlQRDPKRRASLE 261
Cdd:cd05109   249 MIDSECRPRFRELVdefSRM-ARDPSRFVVIQ 279
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
17-235 5.87e-11

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


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 64.58  E-value: 5.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  17 DLDKTLGRG--HFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILEL 94
Cdd:cd08227     1 ELLTVIGRGfeDLMTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  95 GDGGDMFDYIMKH-EEGLNEdLAKKYFAQ-IVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTdfGFSNKF---QPGK 169
Cdd:cd08227    81 MAYGSAKDLICTHfMDGMSE-LAIAYILQgVLKALDYIHHMGYVHRSVKASHIL-ISVDGKVYLS--GLRSNLsmiNHGQ 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907195986 170 KLTT-------SCGSLAYSAPEILLGD--EYDAPAvDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCkyTVP 235
Cdd:cd08227   157 RLRVvhdfpkySVKVLPWLSPEVLQQNlqGYDAKS-DIYSVGITACELANGHVPFKDMPATQMLLEKLNG--TVP 228
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
24-217 6.19e-11

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 63.89  E-value: 6.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  24 RGHFAVVKLARhvFTGEKVAVKVIDKTKLDTLATGhlfQEVRCMKLVQHPNIVRLYEV----IDTQTKLYLILELGDGGD 99
Cdd:cd14053     5 RGRFGAVWKAQ--YLNRLVAVKIFPLQEKQSWLTE---REIYSLPGMKHENILQFIGAekhgESLEAEYWLITEFHERGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYIMKHEEGLNEDLakKYFAQIVHAISYCH----------KLHVVHRDLKPENVvffekqgLVK--LT----DFGFSN 163
Cdd:cd14053    80 LCDYLKGNVISWNELC--KIAESMARGLAYLHedipatngghKPSIAHRDFKSKNV-------LLKsdLTaciaDFGLAL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 164 KFQPGKKLTTSCGSLA---YSAPEILLGD---EYDA-PAVDIWSLGVILFMLV--CG---------QPPFQE 217
Cdd:cd14053   151 KFEPGKSCGDTHGQVGtrrYMAPEVLEGAinfTRDAfLRIDMYAMGLVLWELLsrCSvhdgpvdeyQLPFEE 222
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
17-216 6.73e-11

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: 63.49  E-value: 6.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  17 DLDKTLGRGHFAVVKLARhvFTGEkVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGD 96
Cdd:cd14153     3 EIGELIGKGRFGQVYHGR--WHGE-VAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  97 GGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvfFEKQGLVKLTDFGF---SNKFQPGK---K 170
Cdd:cd14153    80 GRTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV--FYDNGKVVITDFGLftiSGVLQAGRredK 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907195986 171 LTTSCGSLAYSAPEIL--LGDEYDAPAV------DIWSLGVILFMLVCGQPPFQ 216
Cdd:cd14153   158 LRIQSGWLCHLAPEIIrqLSPETEEDKLpfskhsDVFAFGTIWYELHAREWPFK 211
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
18-235 8.05e-11

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: 63.59  E-value: 8.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARHVFTGEK------VAVKVI--DKTKLDTLatgHLFQEVRCMKLV-QHPNIVRLYEVIDTQTKL 88
Cdd:cd05053    16 LGKPLGEGAFGQVVKAEAVGLDNKpnevvtVAVKMLkdDATEKDLS---DLVSEMEMMKMIgKHKNIINLLGACTQDGPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  89 YLILELGDGGDMFDYIMKH---EEGLNEDLAKKYFAQI--VHAISYCHKL----------HVVHRDLKPENVVFFEKQgL 153
Cdd:cd05053    93 YVVVEYASKGNLREFLRARrppGEEASPDDPRVPEEQLtqKDLVSFAYQVargmeylaskKCIHRDLAARNVLVTEDN-V 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 154 VKLTDFGFSNKFQPG---KKltTSCGSLAYS--APEILLGDEYDApAVDIWSLGVILF--MLVCGQP----PFQE----- 217
Cdd:cd05053   172 MKIADFGLARDIHHIdyyRK--TTNGRLPVKwmAPEALFDRVYTH-QSDVWSFGVLLWeiFTLGGSPypgiPVEElfkll 248
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 218 ---------ANDSETLTMIM-DCKYTVP 235
Cdd:cd05053   249 keghrmekpQNCTQELYMLMrDCWHEVP 276
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
18-235 9.63e-11

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 63.83  E-value: 9.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLARhVFTGEK--------VAVKVIDKTKLDT-LATghLFQEVRCMKLV-QHPNIVRLYEVIDTQTK 87
Cdd:cd05099    16 LGKPLGEGCFGQVVRAE-AYGIDKsrpdqtvtVAVKMLKDNATDKdLAD--LISEMELMKLIgKHKNIINLLGVCTQEGP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  88 LYLILELGDGGDM---------------FDYIMKHEEGLN-EDLAKKYFaQIVHAISYCHKLHVVHRDLKPENVVFFEkQ 151
Cdd:cd05099    93 LYVIVEYAAKGNLreflrarrppgpdytFDITKVPEEQLSfKDLVSCAY-QVARGMEYLESRRCIHRDLAARNVLVTE-D 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 152 GLVKLTDFGFS---NKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFML--VCGQP----PFQE----- 217
Cdd:cd05099   171 NVMKIADFGLArgvHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQS-DVWSFGILMWEIftLGGSPypgiPVEElfkll 249
                         250       260
                  ....*....|....*....|....*...
gi 1907195986 218 ---------ANDSETLTMIM-DCKYTVP 235
Cdd:cd05099   250 reghrmdkpSNCTHELYMLMrECWHAVP 277
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
42-265 1.61e-10

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


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 62.25  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  42 VAVKVI-----DKTKLDTLAtghlfqEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKHEEGLNEDLA 116
Cdd:cd05064    36 VAIHTLragcsDKQRRGFLA------EALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNGALDSFLRKHEGQLVAGQL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 117 KKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKFQPGKKLTTSCG-SLA-YSAPEILLGDEYdAP 194
Cdd:cd05064   110 MGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLV-CKISGFRRLQEDKSEAIYTTMSGkSPVlWAAPEAIQYHHF-SS 187
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195986 195 AVDIWSLGVILF-MLVCGQPPFQEANDSETLTMIMDCKYTVPPRvsaGCRDLITRML----QRDPKRRASLEEIES 265
Cdd:cd05064   188 ASDVWSFGIVMWeVMSYGERPYWDMSGQDVIKAVEDGFRLPAPR---NCPNLLHQLMldcwQKERGERPRFSQIHS 260
UBA_AMPK-RKs cd14272
UBA domain of AMPK related kinases; The AMPK-RK family comprises AMP-activated protein kinases ...
295-333 1.62e-10

UBA domain of AMPK related kinases; The AMPK-RK family comprises AMP-activated protein kinases (AMPKs), MAP/microtubule affinity-regulating kinases (MARKs), Brain-specific kinases (BRSKs), Salt inducible kinases (SIKs), maternal embryonic leucine zipper kinase (MELK), and SNF-related serine/threonine-protein kinase (SNRK). It is the only kinase family in the human genome containing an ubiquitin-associated (UBA) or UBA-like domain which is located immediately C-terminal to their N-terminal protein kinase catalytic domain. In addition, most of family members contain a C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK), but some are lack of this region. AMPK-RKs play central roles in metabolic control, energy homeostasis and stress responses in eukaryotes. They require phosphorylation by liver kinase B1 (LKB1) for full activity. Normally, AMPK-RKs appear to exist as heterotrimeric complexes consisting of a catalytic alpha-subunit and regulatory beta- and gamma-subunits. This model corresponds to the catalytic subunit. The UBA domain, previously called SNF1 homology (SNH) domain, regulates the conformation, LKB1-mediated phosphorylation and activation, and localization of the AMPK-RKs, but does not interact with ubiquitin-like molecules. In AMPKalpha subunits, the UBA-like autoinhibitory domain (AID) is responsible for AMPKalpha subunit autoinhibition. Due to the lack of UBA domain, NUAK1 kinase, also called ARK5 (AMPK-related kinase 5), and NUAK2 kinase, also called SNARK (SNF1/AMPK-related kinase), are not included in this family.


Pssm-ID: 270458  Cd Length: 38  Bit Score: 56.47  E-value: 1.62e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907195986 295 HNSIIQRMVLGDIaDRDAIVEALETNRYNHITATYFLLA 333
Cdd:cd14272     1 DDEILQEMVELGY-DREEIVESLRNNRYNDLAATYYLLL 38
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
18-263 1.80e-10

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: 62.69  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  18 LDKTLGRGHFAVVKLAR----HVFTGEK----------VAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVID 83
Cdd:cd05097     9 LKEKLGEGQFGEVHLCEaeglAEFLGEGapefdgqpvlVAVKML-RADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  84 TQTKLYLILELGDGGDMFDYIMKHEegLNEDLAKK------------YFA-QIVHAISYCHKLHVVHRDLKPENVVfFEK 150
Cdd:cd05097    88 SDDPLCMITEYMENGDLNQFLSQRE--IESTFTHAnnipsvsianllYMAvQIASGMKYLASLNFVHRDLATRNCL-VGN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 151 QGLVKLTDFGFSNKFQPGK------KLTTSCGSLAYSApeILLGDEydAPAVDIWSLGVILFML--VCGQPPFQEANDSE 222
Cdd:cd05097   165 HYTIKIADFGMSRNLYSGDyyriqgRAVLPIRWMAWES--ILLGKF--TTASDVWAFGVTLWEMftLCKEQPYSLLSDEQ 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907195986 223 TLTMIMD--------CKYTVPPRVSAGCRDLITRMLQRDPKRRASLEEI 263
Cdd:cd05097   241 VIENTGEffrnqgrqIYLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKI 289
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
22-265 1.92e-10

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 62.34  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLArHVF---TGEK---VAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELG 95
Cdd:cd05091    14 LGEDRFGKVYKG-HLFgtaPGEQtqaVAIKTL-KDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  96 DGGDMFDY-IMK--HEE-GLNED-------LAKKYF----AQIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFG 160
Cdd:cd05091    92 SHGDLHEFlVMRspHSDvGSTDDdktvkstLEPADFlhivTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLN-VKISDLG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 161 FSNKFQPG---KKLTTSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILFMLVC-GQPPFQEANDSETLTMIMDCK-YTVP 235
Cdd:cd05091   171 LFREVYAAdyyKLMGNSLLPIRWMSPEAIMYGKFSIDS-DIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMIRNRQvLPCP 249
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 236 PRVSAGCRDLITRMLQRDPKRRASLEEIES 265
Cdd:cd05091   250 DDCPAWVYTLMLECWNEFPSRRPRFKDIHS 279
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
17-216 3.51e-10

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 61.52  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  17 DLDKTLGRGHFAvvKLARHVFTGEkVAVKV--IDKTKLDTLAtghLFQ-EVRCMKLVQHPNIVRLYEVIDTQTKLYLILE 93
Cdd:cd14152     3 ELGELIGQGRWG--KVHRGRWHGE-VAIRLleIDGNNQDHLK---LFKkEVMNYRQTRHENVVLFMGACMHPPHLAIITS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVvfFEKQGLVKLTDFGF---SNKFQPGKK 170
Cdd:cd14152    77 FCKGRTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV--FYDNGKVVITDFGLfgiSGVVQEGRR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195986 171 ---LTTSCGSLAYSAPEILL----GDEYD----APAVDIWSLGVILFMLVCGQPPFQ 216
Cdd:cd14152   155 eneLKLPHDWLCYLAPEIVRemtpGKDEDclpfSKAADVYAFGTIWYELQARDWPLK 211
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
22-263 7.31e-10

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 60.74  E-value: 7.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  22 LGRGHFAVVKLARHV--FTGEKVAVKVIdKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGD 99
Cdd:cd14206     5 IGNGWFGKVILGEIFsdYTPAQVVVKEL-RVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 100 MFDYI--MKHEEGLNEDLA-------KKYFAQIVHAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFS-NKFQPGK 169
Cdd:cd14206    84 LKRYLraQRKADGMTPDLPtrdlrtlQRMAYEITLGLLHLHKNNYIHSDLALRNCL-LTSDLTVRIGDYGLShNNYKEDY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 170 KLTTS--CGSLAYSAPEILlgDEYDAPAV--------DIWSLGVILFMLV-CGQPPFQEANDSETLTMIMDCKYT--VPP 236
Cdd:cd14206   163 YLTPDrlWIPLRWVAPELL--DELHGNLIvvdqskesNVWSLGVTIWELFeFGAQPYRHLSDEEVLTFVVREQQMklAKP 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907195986 237 RVSAGCRDLITRMLQ---RDPKRRASLEEI 263
Cdd:cd14206   241 RLKLPYADYWYEIMQscwLPPSQRPSVEEL 270
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
122-263 9.35e-10

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: 60.16  E-value: 9.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986 122 QIVHAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKFQPGKklTTSCGS-----LAYSAPEILLGDEYDApAV 196
Cdd:cd05043   124 QIACGMSYLHRRGVIHKDIAARNCVIDDELQ-VKITDNALSRDLFPMD--YHCLGDnenrpIKWMSLESLVNKEYSS-AS 199
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195986 197 DIWSLGVILFMLVC-GQPPFQEANDSETLTMIMDCKYTVPPrvsAGCRD-LITRML---QRDPKRRASLEEI 263
Cdd:cd05043   200 DVWSFGVLLWELMTlGQTPYVEIDPFEMAAYLKDGYRLAQP---INCPDeLFAVMAccwALDPEERPSFQQL 268
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
62-206 9.63e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 61.45  E-value: 9.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  62 QEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGgDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLK 141
Cdd:PHA03211  209 HEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRS-DLYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIK 287
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195986 142 PENvVFFEKQGLVKLTDFGfSNKFQPGKKLTTS----CGSLAYSAPEILLGDEYdAPAVDIWSLGVILF 206
Cdd:PHA03211  288 TEN-VLVNGPEDICLGDFG-AACFARGSWSTPFhygiAGTVDTNAPEVLAGDPY-TPSVDIWSAGLVIF 353
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
20-206 1.09e-09

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 60.05  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  20 KTLGRGHFAVVKLARhvFTGEKVAVKVidktkLDTLATGHLFQEVRCMK--LVQHPNIVRLYEV----IDTQTKLYLILE 93
Cdd:cd14220     1 RQIGKGRYGEVWMGK--WRGEKVAVKV-----FFTTEEASWFRETEIYQtvLMRHENILGFIAAdikgTGSWTQLYLITD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195986  94 LGDGGDMFDYiMKHEEGLNEDLAKKYFAQivhAISYCH----------KLHVVHRDLKPENVVfFEKQGLVKLTDFGFSN 163
Cdd:cd14220    74 YHENGSLYDF-LKCTTLDTRALLKLAYSA---ACGLCHlhteiygtqgKPAIAHRDLKSKNIL-IKKNGTCCIADLGLAV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907195986 164 KFQPGKK-----LTTSCGSLAYSAPEIL---LGDEYDAPAV--DIWSLGVILF 206
Cdd:cd14220   149 KFNSDTNevdvpLNTRVGTKRYMAPEVLdesLNKNHFQAYImaDIYSFGLIIW 201
 
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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