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Conserved domains on  [gi|1907169597|ref|XP_036021601|]
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dual specificity tyrosine-phosphorylation-regulated kinase 4 isoform X8 [Mus musculus]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

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

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
1-232 9.80e-177

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


The actual alignment was detected with superfamily member cd14225:

Pssm-ID: 451246 [Multi-domain]  Cd Length: 341  Bit Score: 493.45  E-value: 9.80e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKV 80
Cdd:cd14225   110 MKEYFYFRNHLCITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSIKV 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFT 160
Cdd:cd14225   190 IDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGLPPPELI 269
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 161 QTASRRQVFFDSKGLPKNINNNRGGKRYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14225   270 ENAQRRRLFFDSKGNPRCITNSKGKKRRPNSKDLASALKTSDPLFLDFIRRCLEWDPSKRMTPDEALQHEWI 341
 
Name Accession Description Interval E-value
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1-232 9.80e-177

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: 493.45  E-value: 9.80e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKV 80
Cdd:cd14225   110 MKEYFYFRNHLCITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSIKV 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFT 160
Cdd:cd14225   190 IDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGLPPPELI 269
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 161 QTASRRQVFFDSKGLPKNINNNRGGKRYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14225   270 ENAQRRRLFFDSKGNPRCITNSKGKKRRPNSKDLASALKTSDPLFLDFIRRCLEWDPSKRMTPDEALQHEWI 341
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1-232 2.58e-60

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 194.29  E-value: 2.58e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597    1 MKDFFYFRNHLCITFELL-GINLYELMKNNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVK 79
Cdd:smart00220  62 LYDVFEDEDKLYLVMEYCeGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG--HVK 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   80 VIDFGSSCYEH--QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQlacIMEVLGLPPA 157
Cdd:smart00220 138 LADFGLARQLDpgEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLE---LFKKIGKPKP 214
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597  158 HFtqtasrrqvffdskglpkninnnrggkrYPDSKDLtmvvktyDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:smart00220 215 PF----------------------------PPPEWDI-------SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
1-232 3.00e-41

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 144.67  E-value: 3.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvK 79
Cdd:pfam00069  63 LYDAFEDKDNLYLVLEYVeGGSLFDLLSEKG--AFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNL--K 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  80 VIDFGSSCYEH--QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMevlglppa 157
Cdd:pfam00069 139 ITDFGLARQLNsgSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELII-------- 210
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 158 hftqtasRRQVFFDSkgLPKNINnnrggkrypdskdltmvvktydSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:pfam00069 211 -------DQPYAFPE--LPSNLS----------------------EEAKDLLKKLLKKDPSKRLTATEALQHPWF 254
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
1-236 7.88e-38

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 140.17  E-value: 7.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFY---FRNH-----LCITFELLGINLYELMK----NNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENI 68
Cdd:PTZ00036  124 LKDYYYtecFKKNeknifLNVVMEFIPQTVHKYMKhyarNN--HALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  69 VLYQRGQvTVKVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQL 145
Cdd:PTZ00036  202 LIDPNTH-TLKLCDFGSAknLLAGQRSVSYICSRFYRAPELMLGATnYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQL 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 146 ACIMEVLGLPpahftqtaSRRQVffdskglpKNINNNRGGKRYPD--SKDLTMVV-KTYDSSFLDFLRRCLVWEPSLRMT 222
Cdd:PTZ00036  281 VRIIQVLGTP--------TEDQL--------KEMNPNYADIKFPDvkPKDLKKVFpKGTPDDAINFISQFLKYEPLKRLN 344
                         250
                  ....*....|....
gi 1907169597 223 PEQALKHAWIHEPR 236
Cdd:PTZ00036  345 PIEALADPFFDDLR 358
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1-259 2.12e-27

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 110.99  E-value: 2.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNSFHG-FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtV 78
Cdd:COG0515    63 LYDFFQDEGSLYLVMEYVdGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRV-V 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSC---------YEHQKVYTYIQSRFYRSPEVILG---HPYNMAIDMWSLGCIMAELYTGYPLFPGENE---VE 143
Cdd:COG0515   142 KLIDFGLAKllpdpgstsSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNssaTS 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 144 QLACIMEVLGLPPahftqtasrrqvffdskglpkninnnrggKRYPDSKDLTmvvKTYDSSFLDFLRRCLVWEPSLRMTP 223
Cdd:COG0515   222 QTLKIILELPTPS-----------------------------LASPLSPSNP---ELISKAASDLLKKLLAKDPKNRLSS 269
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907169597 224 EQALKHAWIHEPRKFKPRPKPQILRKPGASISSEIS 259
Cdd:COG0515   270 SSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLP 305
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
58-142 6.66e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 57.11  E-value: 6.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  58 IIHCDLKPENIVLYQRGQvtVKVIDFG-------SSCYEHQKVytyIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELY 130
Cdd:NF033483  128 IVHRDIKPQNILITKDGR--VKVTDFGiaralssTTMTQTNSV---LGTVHYLSPEQARGGTVDARSDIYSLGIVLYEML 202
                          90
                  ....*....|..
gi 1907169597 131 TGYPLFPGENEV 142
Cdd:NF033483  203 TGRPPFDGDSPV 214
 
Name Accession Description Interval E-value
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1-232 9.80e-177

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: 493.45  E-value: 9.80e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKV 80
Cdd:cd14225   110 MKEYFYFRNHLCITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSIKV 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFT 160
Cdd:cd14225   190 IDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGLPPPELI 269
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 161 QTASRRQVFFDSKGLPKNINNNRGGKRYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14225   270 ENAQRRRLFFDSKGNPRCITNSKGKKRRPNSKDLASALKTSDPLFLDFIRRCLEWDPSKRMTPDEALQHEWI 341
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1-232 4.08e-154

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: 435.05  E-value: 4.08e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKV 80
Cdd:cd14210    80 YKDSFIFRGHLCIVFELLSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKV 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFT 160
Cdd:cd14210   160 IDFGSSCFEGEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLGVPPKSLI 239
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 161 QTASRRQVFFDSKGLPKNINNNRGGKRYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14210   240 DKASRRKKFFDSNGKPRPTTNSKGKKRRPGSKSLAQVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
1-232 1.61e-121

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: 354.82  E-value: 1.61e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKV 80
Cdd:cd14224   132 MLESFTFRNHICMTFELLSMNLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKV 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFT 160
Cdd:cd14224   212 IDFGSSCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPPQKLL 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 161 QTASRRQVFFDSKGLPK--------------NINNNRGGKRY--PDSKDLTMVVK-TYDSSFLDFLRRCLVWEPSLRMTP 223
Cdd:cd14224   292 ETSKRAKNFISSKGYPRyctvttlpdgsvvlNGGRSRRGKMRgpPGSKDWVTALKgCDDPLFLDFLKRCLEWDPAARMTP 371

                  ....*....
gi 1907169597 224 EQALKHAWI 232
Cdd:cd14224   372 SQALRHPWL 380
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
1-232 1.63e-100

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: 297.26  E-value: 1.63e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKV 80
Cdd:cd14133    66 LKDVFYFKNHLCIVFELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKI 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFt 160
Cdd:cd14133   146 IDFGSSCFLTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHM- 224
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 161 qtasrrqvffdskglpknINNnrGGKRYPDskdltmvvktydssFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14133   225 ------------------LDQ--GKADDEL--------------FVDFLKKLLEIDPKERPTASQALSHPWL 262
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
1-232 1.10e-97

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: 292.62  E-value: 1.10e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKV 80
Cdd:cd14212    67 LLDHFMHHGHLCIVFELLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFT 160
Cdd:cd14212   147 IDFGSACFENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEMLGMPPDWML 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 161 QTASRRQVFFDSKGLPKNIN-------------NNRG---GKRYPDSKDLTMVVKTYD----------------SSFLDF 208
Cdd:cd14212   227 EKGKNTNKFFKKVAKSGGRStyrlktpeefeaeNNCKlepGKRYFKYKTLEDIIMNYPmkkskkeqidkemetrLAFIDF 306
                         250       260
                  ....*....|....*....|....
gi 1907169597 209 LRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14212   307 LKGLLEYDPKKRWTPDQALNHPFI 330
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1-229 7.53e-92

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: 278.05  E-value: 7.53e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVE--KIIHCDLKPENIVLYQRGQVTV 78
Cdd:cd14226    80 LKRHFMFRNHLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLCNPKRSAI 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAH 158
Cdd:cd14226   160 KIIDFGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGMPPVH 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 159 FTQTASRRQVFFDSkgLPKNINN---NRGGKRY--PDSKDLTMV--VKT-----------------YdSSFLDFLRRCLV 214
Cdd:cd14226   240 MLDQAPKARKFFEK--LPDGTYYlkkTKDGKKYkpPGSRKLHEIlgVETggpggrragepghtvedY-LKFKDLILRMLD 316
                         250
                  ....*....|....*
gi 1907169597 215 WEPSLRMTPEQALKH 229
Cdd:cd14226   317 YDPKTRITPAEALQH 331
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
1-231 5.26e-69

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: 218.97  E-value: 5.26e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVL----YQRGQV 76
Cdd:cd14134    79 LRDWFDYRGHMCIVFELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdYVKVYN 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  77 T-------------VKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVE 143
Cdd:cd14134   159 PkkkrqirvpkstdIKLIDFGSATFDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLE 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 144 QLAcIME-VLGLPPAHFTQTASRRQVFFDSKGL----PKNINNNRGGKRYPDSKDLTMV-VKTYDSSFLDFLRRCLVWEP 217
Cdd:cd14134   239 HLA-MMErILGPLPKRMIRRAKKGAKYFYFYHGrldwPEGSSSGRSIKRVCKPLKRLMLlVDPEHRLLFDLIRKMLEYDP 317
                         250
                  ....*....|....
gi 1907169597 218 SLRMTPEQALKHAW 231
Cdd:cd14134   318 SKRITAKEALKHPF 331
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1-232 2.00e-68

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: 214.79  E-value: 2.00e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFR--NHLCITFELLGINLYELMKNNSfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtV 78
Cdd:cd05118    64 LLDVFEHRggNHLCLVFELMGMNLYELIKDYP-RGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQ-L 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQKVYT-YIQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPP 156
Cdd:cd05118   142 KLADFGLARSFTSPPYTpYVATRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGTPE 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 157 ahftqtasrrqvffdskglpkninnnrggkrypdskdltmvvktydssFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd05118   222 ------------------------------------------------ALDLLSKMLKYDPAKRITASQALAHPYF 249
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1-232 2.58e-60

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 194.29  E-value: 2.58e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597    1 MKDFFYFRNHLCITFELL-GINLYELMKNNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVK 79
Cdd:smart00220  62 LYDVFEDEDKLYLVMEYCeGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG--HVK 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   80 VIDFGSSCYEH--QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQlacIMEVLGLPPA 157
Cdd:smart00220 138 LADFGLARQLDpgEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLE---LFKKIGKPKP 214
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597  158 HFtqtasrrqvffdskglpkninnnrggkrYPDSKDLtmvvktyDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:smart00220 215 PF----------------------------PPPEWDI-------SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
3-232 1.72e-57

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: 189.20  E-value: 1.72e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQ--RGQVTVKV 80
Cdd:cd14211    67 ECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDpvRQPYRVKV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKV-YTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHF 159
Cdd:cd14211   147 IDFGSASHVSKAVcSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPAEHL 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 160 TQTASRRQVFFD-------------------------SKGLPKNINNN-------RGGKRYPDSKdlTMVVKTYDSSFLD 207
Cdd:cd14211   227 LNAATKTSRFFNrdpdspyplwrlktpeeheaetgikSKEARKYIFNClddmaqvNGPSDLEGSE--LLAEKADRREFID 304
                         250       260
                  ....*....|....*....|....*
gi 1907169597 208 FLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14211   305 LLKRMLTIDQERRITPGEALNHPFV 329
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
9-232 4.63e-54

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: 180.08  E-value: 4.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVLYQrGQVTVKVIDFGSSC 87
Cdd:cd14136    91 THVCMVFEVLGPNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCI-SKIEVKIADLGNAC 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  88 YEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLF---PGEN---EVEQLACIMEVLGLPPAHFTQ 161
Cdd:cd14136   170 WTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdphSGEDysrDEDHLALIIELLGRIPRSIIL 249
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597 162 TASRRQVFFDSKGLPKNINNNrggKRYPdskdLTMV-VKTYD------SSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14136   250 SGKYSREFFNRKGELRHISKL---KPWP----LEDVlVEKYKwskeeaKEFASFLLPMLEYDPEKRATAAQCLQHPWL 320
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
1-232 1.98e-53

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: 178.57  E-value: 1.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMK---NNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRgQVT 77
Cdd:cd14135    68 LLRHFEHKNHLCLVFESLSMNLREVLKkygKN--VGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEK-KNT 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  78 VKVIDFGSSCYEHQKVYT-YIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPP 156
Cdd:cd14135   145 LKLCDFGSASDIGENEITpYLVSRFYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGKFP 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 157 AHFTQTASRRQVFFDSKG-----------------LPKNINNNR-------GGKRYPDSkDLTMVvktydSSFLDFLRRC 212
Cdd:cd14135   225 KKMLRKGQFKDQHFDENLnfiyrevdkvtkkevrrVMSDIKPTKdlktlliGKQRLPDE-DRKKL-----LQLKDLLDKC 298
                         250       260
                  ....*....|....*....|
gi 1907169597 213 LVWEPSLRMTPEQALKHAWI 232
Cdd:cd14135   299 LMLDPEKRITPNEALQHPFI 318
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
1-229 1.96e-51

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: 172.30  E-value: 1.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFR------NHLCITFELLGINLYELMKNNSFHGFNLSI--VRRFTFSILKCLHMLYVEKIIHCDLKPENIvLYQ 72
Cdd:cd14137    62 LKYFFYSSgekkdeVYLNLVMEYMPETLYRVIRHYSKNKQTIPIiyVKLYSYQLFRGLAYLHSLGICHRDIKPQNL-LVD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  73 RGQVTVKVIDFGSSCY--EHQKVYTYIQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIM 149
Cdd:cd14137   141 PETGVLKLCDFGSAKRlvPGEPNVSYICSRYYRAPELIFGATdYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEII 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 150 EVLGLPpahftqtaSRRQVffdskglpKNINNNRGGKRYPDSK--DLTMVVKTY-DSSFLDFLRRCLVWEPSLRMTPEQA 226
Cdd:cd14137   221 KVLGTP--------TREQI--------KAMNPNYTEFKFPQIKphPWEKVFPKRtPPDAIDLLSKILVYNPSKRLTALEA 284

                  ...
gi 1907169597 227 LKH 229
Cdd:cd14137   285 LAH 287
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
5-232 2.18e-50

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: 170.98  E-value: 2.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQ--RGQVTVKVID 82
Cdd:cd14229    70 FQHRNHTCLVFEMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDpvRQPYRVKVID 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FGSSCYEHQKV-YTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQ 161
Cdd:cd14229   150 FGSASHVSKTVcSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLN 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 162 TASRRQVFF-------------------------DSKGLPKNINNNRGGKRYP------DSKDLtMVVKTYDSSFLDFLR 210
Cdd:cd14229   230 VGTKTSRFFcretdapysswrlktleeheaetgmKSKEARKYIFNSLDDIAHVnmvmdlEGSDL-LAEKADRREFVALLK 308
                         250       260
                  ....*....|....*....|..
gi 1907169597 211 RCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14229   309 KMLLIDADLRITPADTLSHPFV 330
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
1-231 6.31e-49

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: 165.78  E-value: 6.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKV 80
Cdd:cd07830    63 LKEVFRENDELYFVFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV--SGPEVVKI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFG-SSCYEHQKVYT-YIQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLP-- 155
Cdd:cd07830   141 ADFGlAREIRSRPPYTdYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPtk 220
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 156 ---PAHFtQTASRRQVFFdskglPKNInnnrggkrypdSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07830   221 qdwPEGY-KLASKLGFRF-----PQFA-----------PTSLHQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
1-232 8.57e-49

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: 165.35  E-value: 8.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKV 80
Cdd:cd07829    63 LLDVIHTENKLYLVFEYCDQDLKKYLDKRP-GPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDG--VLKL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFG-SSCYEHQ-KVYTY-IQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPp 156
Cdd:cd07829   140 ADFGlARAFGIPlRTYTHeVVTLWYRAPEILLGsKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTP- 218
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 157 ahftqTASrrqvffDSKGLPKNINNNRGGKRYPdSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd07829   219 -----TEE------SWPGVTKLPDYKPTFPKWP-KNDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
1-231 2.00e-47

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: 163.26  E-value: 2.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENI--------VLYQ 72
Cdd:cd14214    81 MSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENIlfvnsefdTLYN 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  73 RGQ---------VTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVE 143
Cdd:cd14214   161 ESKsceeksvknTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENRE 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 144 QLACIMEVLGLPPAHFTQTaSRRQVFFDSKGLPKNINNNRGGKRYPDSKDLtMVVKTYDS----SFLDFLRRCLVWEPSL 219
Cdd:cd14214   241 HLVMMEKILGPIPSHMIHR-TRKQKYFYKGSLVWDENSSDGRYVSENCKPL-MSYMLGDSlehtQLFDLLRRMLEFDPAL 318
                         250
                  ....*....|..
gi 1907169597 220 RMTPEQALKHAW 231
Cdd:cd14214   319 RITLKEALLHPF 330
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
1-231 3.12e-47

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: 161.33  E-value: 3.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKV 80
Cdd:cd07833    65 LKEAFRRKGRLYLVFEYVERTLLELLEASP-GGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESG--VLKL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQK---VYT-YIQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLG-L 154
Cdd:cd07833   142 CDFGFARALTARpasPLTdYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGpL 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 155 PPAHfTQTASRRQVFfdskglpkninnnrGGKRYPDSKDLTMVVKTY----DSSFLDFLRRCLVWEPSLRMTPEQALKHA 230
Cdd:cd07833   222 PPSH-QELFSSNPRF--------------AGVAFPEPSQPESLERRYpgkvSSPALDFLKACLRMDPKERLTCDELLQHP 286

                  .
gi 1907169597 231 W 231
Cdd:cd07833   287 Y 287
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
9-235 4.44e-46

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: 159.61  E-value: 4.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELLGINLYELMKNNSfhgfNLSI--VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFG-- 84
Cdd:cd07834    77 NDVYIVTELMETDLHKVIKSPQ----PLTDdhIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNS--NCDLKICDFGla 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  85 -SSCYEHQKVY-T-YIQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAH-- 158
Cdd:cd07834   151 rGVDPDEDKGFlTeYVVTRWYRAPELLLSsKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEEdl 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 159 --FTQTASRRQVffdsKGLPKNinnnrggkrypDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW---IH 233
Cdd:cd07834   231 kfISSEKARNYL----KSLPKK-----------PKKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYlaqLH 295

                  ..
gi 1907169597 234 EP 235
Cdd:cd07834   296 DP 297
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
10-229 3.24e-44

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: 153.59  E-value: 3.24e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  10 HLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSScye 89
Cdd:cd07838    80 KLTLVFEHVDQDLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQV--KLADFGLA--- 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  90 hqKVYTYiQSRF--------YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHftq 161
Cdd:cd07838   155 --RIYSF-EMALtsvvvtlwYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPSEE--- 228
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597 162 tasrrqvffdskGLPKNINNNRGGKRYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd07838   229 ------------EWPRNSALPRSSFPSYTPRPFKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQH 284
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
1-229 4.16e-44

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: 154.62  E-value: 4.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVT--- 77
Cdd:cd14213    80 MLEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYVVkyn 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  78 --------------VKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVE 143
Cdd:cd14213   160 pkmkrdertlknpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKE 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 144 QLACIMEVLGLPPAHFTQTASRRQVFFDSKgLPKNINNNRG---GKRYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLR 220
Cdd:cd14213   240 HLAMMERILGPLPKHMIQKTRKRKYFHHDQ-LDWDEHSSAGryvRRRCKPLKEFMLSQDVDHEQLFDLIQKMLEYDPAKR 318

                  ....*....
gi 1907169597 221 MTPEQALKH 229
Cdd:cd14213   319 ITLDEALKH 327
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
5-232 2.36e-43

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: 153.32  E-value: 2.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLY--QRGQVTVKVID 82
Cdd:cd14227    85 FQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVdpSRQPYRVKVID 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FGSSCYEHQKV-YTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQ 161
Cdd:cd14227   165 FGSASHVSKAVcSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLS 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 162 TASRRQVFFDSK----------GLPKNINNNRGGKRYPDSK-------DLTMVVKTYD-------------SSFLDFLRR 211
Cdd:cd14227   245 AGTKTTRFFNRDtdspyplwrlKTPEDHEAETGIKSKEARKyifncldDMAQVNMTTDlegsdmlvekadrREFIDLLKK 324
                         250       260
                  ....*....|....*....|.
gi 1907169597 212 CLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14227   325 MLTIDADKRITPIETLNHPFV 345
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
1-229 2.51e-43

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: 150.89  E-value: 2.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCIT--FELLGINLYELMKNNSFHgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRgqvTV 78
Cdd:cd07831    63 LIEVLFDRKTGRLAlvFELMDMNLYELIKGRKRP-LPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD---IL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQKV-YT-YIQSRFYRSPEVIL--GHpYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGL 154
Cdd:cd07831   139 KLADFGSCRGIYSKPpYTeYISTRWYRAPECLLtdGY-YGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGT 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 155 PPA---HFTQTASRRQVFFDSK---GLPKNINNnrggkrypdskdltmvvktYDSSFLDFLRRCLVWEPSLRMTPEQALK 228
Cdd:cd07831   218 PDAevlKKFRKSRHMNYNFPSKkgtGLRKLLPN-------------------ASAEGLDLLKKLLAYDPDERITAKQALR 278

                  .
gi 1907169597 229 H 229
Cdd:cd07831   279 H 279
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
5-232 6.92e-42

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: 149.47  E-value: 6.92e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQ--RGQVTVKVID 82
Cdd:cd14228    85 FQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDpvRQPYRVKVID 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FGSSCYEHQKV-YTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQ 161
Cdd:cd14228   165 FGSASHVSKAVcSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLS 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 162 TASRRQVFFDSKglpKNINNNRGGKRYPDSKDLTMVVKTYDS---------------------------------SFLDF 208
Cdd:cd14228   245 AGTKTSRFFNRD---PNLGYPLWRLKTPEEHELETGIKSKEArkyifnclddmaqvnmstdlegtdmlaekadrrEYIDL 321
                         250       260
                  ....*....|....*....|....
gi 1907169597 209 LRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14228   322 LKKMLTIDADKRITPLKTLNHPFV 345
Pkinase pfam00069
Protein kinase domain;
1-232 3.00e-41

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 144.67  E-value: 3.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvK 79
Cdd:pfam00069  63 LYDAFEDKDNLYLVLEYVeGGSLFDLLSEKG--AFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNL--K 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  80 VIDFGSSCYEH--QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMevlglppa 157
Cdd:pfam00069 139 ITDFGLARQLNsgSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELII-------- 210
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 158 hftqtasRRQVFFDSkgLPKNINnnrggkrypdskdltmvvktydSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:pfam00069 211 -------DQPYAFPE--LPSNLS----------------------EEAKDLLKKLLKKDPSKRLTATEALQHPWF 254
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
13-231 3.15e-41

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: 145.55  E-value: 3.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNnSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG-------- 84
Cdd:cd07832    77 LVFEYMLSSLSEVLRD-EERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVL--KIADFGlarlfsee 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  85 -SSCYEHQkvytyIQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPpahftqt 162
Cdd:cd07832   154 dPRLYSHQ-----VATRWYRAPELLYGSRkYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTP------- 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 163 asRRQVFFDSKGLPkninnnRGGK-RYPDSKDLTMVVKTYDSS--FLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07832   222 --NEKTWPELTSLP------DYNKiTFPESKGIRLEEIFPDCSpeAIDLLKGLLVYNPKKRLSAEEALRHPY 285
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
1-229 7.31e-40

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: 143.23  E-value: 7.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLY--------- 71
Cdd:cd14215    80 MFDWFDYHGHMCISFELLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVnsdyeltyn 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  72 ---QRGQVTVK-----VIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVE 143
Cdd:cd14215   160 lekKRDERSVKstairVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNRE 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 144 QLACIMEVLGLPPAHFTQTASRRQVFFDSKglpKNINNNRGGKRY------PDSKDLTMVVKTYdSSFLDFLRRCLVWEP 217
Cdd:cd14215   240 HLAMMERILGPIPSRMIRKTRKQKYFYHGR---LDWDENTSAGRYvrenckPLRRYLTSEAEEH-HQLFDLIESMLEYEP 315
                         250
                  ....*....|..
gi 1907169597 218 SLRMTPEQALKH 229
Cdd:cd14215   316 SKRLTLAAALKH 327
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
3-231 5.17e-39

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: 139.92  E-value: 5.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELLGINLYELMKNNSFHG-FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVI 81
Cdd:cd07836    65 DVIHTENKLMLVFEYMDKDLKKYMDTHGVRGaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGEL--KLA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  82 DFGSSCYEHQKVYTY---IQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPA 157
Cdd:cd07836   143 DFGLARAFGIPVNTFsneVVTLWYRAPDVLLGsRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTE 222
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169597 158 HFTQTASRrqvffdskgLPKnINNNrgGKRYPdSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07836   223 STWPGISQ---------LPE-YKPT--FPRYP-PQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
46-244 8.93e-39

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: 140.39  E-value: 8.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFG--SSCYEHQKVYT------YIQSRFYRSPEVILG-HPYNMA 116
Cdd:cd07852   116 LLKALKYLHSGGVIHRDLKPSNILLNS--DCRVKLADFGlaRSLSQLEEDDEnpvltdYVATRWYRAPEILLGsTRYTKG 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 117 IDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPA--------HFTQTasrrqvFFDSkgLPkninnnrggkrY 188
Cdd:cd07852   194 VDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIEVIGRPSAediesiqsPFAAT------MLES--LP-----------P 254
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 189 PDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI---HEPRKFKPRPKP 244
Cdd:cd07852   255 SRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVaqfHNPADEPSLPGP 313
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
16-234 9.35e-39

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: 140.51  E-value: 9.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  16 ELLGINLYELMKnnsFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFGSSCYEHQKVYT 95
Cdd:cd07851   100 HLMGADLNNIVK---CQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAV--NEDCELKILDFGLARHTDDEMTG 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  96 YIQSRFYRSPEVIL--GHpYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQ--TASRRQVFFd 171
Cdd:cd07851   175 YVATRWYRAPEIMLnwMH-YNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPDEELLKkiSSESARNYI- 252
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 172 sKGLPKNinnnrggKRypdsKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHE 234
Cdd:cd07851   253 -QSLPQM-------PK----KDFKEVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAE 303
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
1-236 7.88e-38

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 140.17  E-value: 7.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFY---FRNH-----LCITFELLGINLYELMK----NNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENI 68
Cdd:PTZ00036  124 LKDYYYtecFKKNeknifLNVVMEFIPQTVHKYMKhyarNN--HALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  69 VLYQRGQvTVKVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQL 145
Cdd:PTZ00036  202 LIDPNTH-TLKLCDFGSAknLLAGQRSVSYICSRFYRAPELMLGATnYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQL 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 146 ACIMEVLGLPpahftqtaSRRQVffdskglpKNINNNRGGKRYPD--SKDLTMVV-KTYDSSFLDFLRRCLVWEPSLRMT 222
Cdd:PTZ00036  281 VRIIQVLGTP--------TEDQL--------KEMNPNYADIKFPDvkPKDLKKVFpKGTPDDAINFISQFLKYEPLKRLN 344
                         250
                  ....*....|....
gi 1907169597 223 PEQALKHAWIHEPR 236
Cdd:PTZ00036  345 PIEALADPFFDDLR 358
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
1-231 2.14e-37

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: 135.50  E-value: 2.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKV 80
Cdd:cd07835    63 LLDVVHSENKLYLVFEFLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEG--ALKL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSS--------CYEHQKVytyiqSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEV 151
Cdd:cd07835   141 ADFGLArafgvpvrTYTHEVV-----TLWYRAPEILLGsKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRT 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 152 LGLPpahftqtasrrqvffDSKGLPkninnnrGGKRYPD---------SKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMT 222
Cdd:cd07835   216 LGTP---------------DEDVWP-------GVTSLPDykptfpkwaRQDLSKVVPSLDEDGLDLLSQMLVYDPAKRIS 273

                  ....*....
gi 1907169597 223 PEQALKHAW 231
Cdd:cd07835   274 AKAALQHPY 282
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
3-244 6.99e-36

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: 131.93  E-value: 6.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELLGINLYELMKNNSFHgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVID 82
Cdd:cd07841    69 DVFGHKSNINLVFEFMETDLEKVIKDKSIV-LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVL--KLAD 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FGSSC--------YEHQkVYTyiqsRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLG 153
Cdd:cd07841   146 FGLARsfgspnrkMTHQ-VVT----RWYRAPELLFGaRHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALG 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 154 LPpahftqtasrrqvffdskglpkNINNNRGGKRYPDS--------KDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQ 225
Cdd:cd07841   221 TP----------------------TEENWPGVTSLPDYvefkpfppTPLKQIFPAASDDALDLLQRLLTLNPNKRITARQ 278
                         250
                  ....*....|....*....
gi 1907169597 226 ALKHAWiheprkFKPRPKP 244
Cdd:cd07841   279 ALEHPY------FSNDPAP 291
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
1-229 1.52e-35

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: 130.89  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKV 80
Cdd:cd07848    65 LKEAFRRRGKLYLVFEYVEKNMLELLEEMP-NGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHND--VLKL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSS---CYEHQKVYT-YIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLG-LP 155
Cdd:cd07848   142 CDFGFArnlSEGSNANYTeYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGpLP 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 156 PAHFtqtasrrQVFFdskglpkniNNNR-GGKRYPDSKDLTMVVKTY----DSSFLDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd07848   222 AEQM-------KLFY---------SNPRfHGLRFPAVNHPQSLERRYlgilSGVLLDLMKNLLKLNPTDRYLTEQCLNH 284
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
41-231 3.88e-35

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: 129.61  E-value: 3.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  41 RFTFSILKC--------LHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG---SSCYEHQKVYTY-IQSRFYRSPEVI 108
Cdd:cd07840   100 KFTESQIKCymkqllegLQYLHSNGILHRDIKGSNILINNDGVL--KLADFGlarPYTKENNADYTNrVITLWYRPPELL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 109 LGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRRQVF--FDSKGLPKNInnnrgg 185
Cdd:cd07840   178 LGATrYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENWPGVSDLPWFenLKPKKPYKRR------ 251
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907169597 186 krypdskdLTMVVKTY-DSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07840   252 --------LREVFKNViDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
32-229 4.98e-35

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: 129.46  E-value: 4.98e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  32 HGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG--SSCYEHQKVYT-YIQSRFYRSPEVI 108
Cdd:cd07846    95 NGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSG--VVKLCDFGfaRTLAAPGEVYTdYVATRWYRAPELL 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 109 LGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLG-LPPAHftQTASRRQVFFDSKGLP--KNINNNRg 184
Cdd:cd07846   173 VGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGnLIPRH--QELFQKNPLFAGVRLPevKEVEPLE- 249
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907169597 185 gKRYPdskdltmvvkTYDSSFLDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd07846   250 -RRYP----------KLSGVVIDLAKKCLHIDPDKRPSCSELLHH 283
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
16-235 1.23e-34

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: 129.23  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  16 ELLGINLYELMKNNSFHGfnlSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSCYEHQKVYT 95
Cdd:cd07856    90 ELLGTDLHRLLTSRPLEK---QFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNE--NCDLKICDFGLARIQDPQMTG 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  96 YIQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRRQVFFDSKG 174
Cdd:cd07856   165 YVSTRYYRAPEIMLTwQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVINTICSENTLRFVQS 244
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169597 175 LPKNinnnrggKRYPdskdLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI---HEP 235
Cdd:cd07856   245 LPKR-------ERVP----FSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLapyHDP 297
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
17-245 2.97e-34

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: 128.53  E-value: 2.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  17 LLGINLYELMKNNSFhgfNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSCYEHQKVYTY 96
Cdd:cd07880   101 FMGTDLGKLMKHEKL---SEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNE--DCELKILDFGLARQTDSEMTGY 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  97 IQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRRQVFFDSKGL 175
Cdd:cd07880   176 VVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKLQSEDAKNYVKKL 255
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 176 PKninnnrggkryPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEPRKFKPRPKPQ 245
Cdd:cd07880   256 PR-----------FRKKDFRSLLPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPEDETEAP 314
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
18-232 2.28e-33

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: 125.94  E-value: 2.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  18 LGINLY---ELMKNNSFH------GFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG---- 84
Cdd:cd07855    81 DFKDVYvvlDLMESDLHHiihsdqPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENC--ELKIGDFGmarg 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  85 --SSCYEHQKVYT-YIQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFT 160
Cdd:cd07855   159 lcTSPEEHKYFMTeYVATRWYRAPELMLSlPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPSQAVI 238
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169597 161 QT--ASRRQVFFDSkgLPKNinnnrggkrypDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd07855   239 NAigADRVRRYIQN--LPNK-----------QPVPWETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFL 299
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
22-231 2.34e-33

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: 124.79  E-value: 2.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  22 LYELMKNNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG------SSCYEhqkvYT 95
Cdd:cd07847    87 LNELEKNP--RGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQI--KLCDFGfariltGPGDD----YT 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  96 -YIQSRFYRSPEVILGH-PYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLG-LPPAHfTQTASRRQvFFDS 172
Cdd:cd07847   159 dYVATRWYRAPELLVGDtQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGdLIPRH-QQIFSTNQ-FFKG 236
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 173 KGLPKNinnnrggkryPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07847   237 LSIPEP----------ETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
41-232 7.94e-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: 123.49  E-value: 7.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  41 RFTFSILKCL--------HMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSS--CYEHQKVYTYIQ-SRFYRSPEVIL 109
Cdd:cd07843   102 PFLQSEVKCLmlqllsgvAHLHDNWILHRDLKTSNLLLNNRGIL--KICDFGLAreYGSPLKPYTQLVvTLWYRAPELLL 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 110 GHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLP-----PAHFTQTASRRQVFfdskglpKNINNNR 183
Cdd:cd07843   180 GAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPtekiwPGFSELPGAKKKTF-------TKYPYNQ 252
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907169597 184 GGKRYPdSKDLTmvvktyDSSFlDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd07843   253 LRKKFP-ALSLS------DNGF-DLLNRLLTYDPAKRISAEDALKHPYF 293
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
3-244 1.04e-32

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 124.49  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELLGINLYELMKNNSFhgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVID 82
Cdd:PTZ00024   87 DVYVEGDFINLVMDIMASDLKKVVDRKIR--LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGIC--KIAD 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FG-SSCYEHQKVY------TYIQSR----------FYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQ 144
Cdd:PTZ00024  163 FGlARRYGYPPYSdtlskdETMQRReemtskvvtlWYRAPELLMGaEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQ 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 145 LACIMEVLGLPPAHFTQTASRRQVFFD-SKGLPkninnnrggkrypdsKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTP 223
Cdd:PTZ00024  243 LGRIFELLGTPNEDNWPQAKKLPLYTEfTPRKP---------------KDLKTIFPNASDDAIDLLQSLLKLNPLERISA 307
                         250       260
                  ....*....|....*....|.
gi 1907169597 224 EQALKHAWiheprkFKPRPKP 244
Cdd:PTZ00024  308 KEALKHEY------FKSDPLP 322
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
10-232 4.22e-32

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: 122.83  E-value: 4.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  10 HLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVL----------------YQ 72
Cdd:cd14216    92 HICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLsvneqyirrlaaeateWQ 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  73 RG------------QVTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLF---P 137
Cdd:cd14216   172 RNflvnplepknaeKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFephS 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 138 GEN---EVEQLACIMEVLGLPPAHFTQTASRRQVFFDSKGLPKNINnnrggKRYPDSKdLTMVVKTYD------SSFLDF 208
Cdd:cd14216   252 GEDysrDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHIT-----KLKPWGL-FEVLVEKYEwsqeeaAGFTDF 325
                         250       260
                  ....*....|....*....|....
gi 1907169597 209 LRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14216   326 LLPMLELIPEKRATAAECLRHPWL 349
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
42-235 6.21e-32

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: 122.13  E-value: 6.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSC-------YEHQKVYTYIQSRFYRSPEVILGH-PY 113
Cdd:cd07857   110 FIYQILCGLKYIHSANVLHRDLKPGNLLVNADCEL--KICDFGLARgfsenpgENAGFMTEYVATRWYRAPEIMLSFqSY 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 114 NMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRRQVFFDSKGLPkNINNNRGGKRYPDSkd 193
Cdd:cd07857   188 TKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPDEETLSRIGSPKAQNYIRSLP-NIPKKPFESIFPNA-- 264
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907169597 194 ltmvvktyDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI---HEP 235
Cdd:cd07857   265 --------NPLALDLLEKLLAFDPTKRISVEEALEHPYLaiwHDP 301
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
58-233 1.48e-31

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: 121.37  E-value: 1.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  58 IIHCDLKPENIVLyqRGQVTVKVIDFG--SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPL 135
Cdd:cd07850   123 IIHRDLKPSNIVV--KSDCTLKILDFGlaRTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVL 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 136 FPGENEVEQLACIMEVLGLPPAHFT---QTASRRQVffdskglpKNINNNRG---GKRYPDS---KDLTMVVKTYDSSFL 206
Cdd:cd07850   201 FPGTDHIDQWNKIIEQLGTPSDEFMsrlQPTVRNYV--------ENRPKYAGysfEELFPDVlfpPDSEEHNKLKASQAR 272
                         170       180
                  ....*....|....*....|....*..
gi 1907169597 207 DFLRRCLVWEPSLRMTPEQALKHAWIH 233
Cdd:cd07850   273 DLLSKMLVIDPEKRISVDDALQHPYIN 299
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
37-231 1.53e-31

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: 120.85  E-value: 1.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRG--QVTVKVIDFG---------SSCYEHQKVYTYIqsrFYRSP 105
Cdd:cd07842   108 SMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGpeRGVVKIGDLGlarlfnaplKPLADLDPVVVTI---WYRAP 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 106 EVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENE---------VEQLACIMEVLGLPPAhftqtasrrQVFFDSKGL 175
Cdd:cd07842   185 ELLLGaRHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfqRDQLERIFEVLGTPTE---------KDWPDIKKM 255
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 176 P--KNINNNRGGKRYPDSKDLTMV--VKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07842   256 PeyDTLKSDTKASTYPNSLLAKWMhkHKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPY 315
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
1-231 1.77e-31

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: 119.12  E-value: 1.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNSFhgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLY-QRGQVTV 78
Cdd:cd05117    64 LYEVFEDDKNLYLVMELCtGGELFDRIVKKGS--FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAsKDPDSPI 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCY--EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEvlglpp 156
Cdd:cd05117   142 KIIDFGLAKIfeEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILK------ 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 157 AHFTqtasrrqvfFDSKglpkninnnrggkrypdskdltmVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd05117   216 GKYS---------FDSP-----------------------EWKNVSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
9-232 2.14e-31

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: 121.04  E-value: 2.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELLGINLYELMKNNSF---HgfnlsiVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRgQVTVKVIDFG- 84
Cdd:cd07854    89 NSVYIVQEYMETDLANVLEQGPLseeH------ARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTE-DLVLKIGDFGl 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  85 ----SSCYEHQKVYTY-IQSRFYRSPEVILgHP--YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLppa 157
Cdd:cd07854   162 arivDPHYSHKGYLSEgLVTKWYRSPRLLL-SPnnYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVPV--- 237
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 158 hfTQTASRRQVFfdsKGLPKNINNNRGGKRYPdskdLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd07854   238 --VREEDRNELL---NVIPSFVRNDGGEPRRP----LRDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYM 303
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-234 2.65e-31

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 119.54  E-value: 2.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIvLYQRGQVTVKV 80
Cdd:PLN00009   66 LQDVVHSEKRLYLVFEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNL-LIDRRTNALKL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTY---IQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPP 156
Cdd:PLN00009  145 ADFGLARAFGIPVRTFtheVVTLWYRAPEILLGsRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPN 224
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597 157 AHFTQTASRRQVFFDSkgLPKninnnrggkrYPdSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHE 234
Cdd:PLN00009  225 EETWPGVTSLPDYKSA--FPK----------WP-PKDLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKD 289
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
39-244 2.93e-31

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: 120.53  E-value: 2.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILG--HpYNMA 116
Cdd:cd07877   122 VQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNE--DCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNwmH-YNQT 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 117 IDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRRQVFFDSKGLPkninnnrggkrYPDSKDLTM 196
Cdd:cd07877   199 VDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLT-----------QMPKMNFAN 267
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907169597 197 VVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI---HEPRKfKPRPKP 244
Cdd:cd07877   268 VFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFaqyHDPDD-EPVADP 317
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
9-244 4.32e-31

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: 120.15  E-value: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELLGINLYELMKnnsFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSCY 88
Cdd:cd07878    93 NEVYLVTNLMGADLNNIVK---CQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNE--DCELRILDFGLARQ 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  89 EHQKVYTYIQSRFYRSPEVILG--HpYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRR 166
Cdd:cd07878   168 ADDEMTGYVATRWYRAPEIMLNwmH-YNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKISSE 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 167 --QVFFDSkgLPkninnnrggkrYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI---HEPRKfKPR 241
Cdd:cd07878   247 haRKYIQS--LP-----------HMPQQDLKKIFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFsqyHDPED-EPE 312

                  ...
gi 1907169597 242 PKP 244
Cdd:cd07878   313 AEP 315
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
13-244 6.88e-31

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: 119.40  E-value: 6.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNNSfhgfNLSI--VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFG---SSC 87
Cdd:cd07858    86 IVYELMDTDLHQIIRSSQ----TLSDdhCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLL--NANCDLKICDFGlarTTS 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  88 YEHQKVYTYIQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPA---HFTQTA 163
Cdd:cd07858   160 EKGDFMTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEedlGFIRNE 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 164 SRRQVFfdsKGLPKNINNNRgGKRYPDSKDLTmvvktydssfLDFLRRCLVWEPSLRMTPEQALKHAW---IHEPRKFKP 240
Cdd:cd07858   240 KARRYI---RSLPYTPRQSF-ARLFPHANPLA----------IDLLEKMLVFDPSKRITVEEALAHPYlasLHDPSDEPV 305

                  ....
gi 1907169597 241 RPKP 244
Cdd:cd07858   306 CQTP 309
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
37-231 2.51e-30

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: 116.76  E-value: 2.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSS--------CYEHQKVytyiqSRFYRSPEVI 108
Cdd:cd07839    99 EIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGE--LKLADFGLArafgipvrCYSAEVV-----TLWYRPPDVL 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 109 LGHP-YNMAIDMWSLGCIMAELYT-GYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRrqvFFDSKGLPKninnnrggk 186
Cdd:cd07839   172 FGAKlYSTSIDMWSAGCIFAELANaGRPLFPGNDVDDQLKRIFRLLGTPTEESWPGVSK---LPDYKPYPM--------- 239
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907169597 187 rYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07839   240 -YPATTSLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
32-245 2.67e-30

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: 118.08  E-value: 2.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  32 HGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILG- 110
Cdd:cd07879   112 HPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCEL--KILDFGLARHADAEMTGYVVTRWYRAPEVILNw 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 111 -HpYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRRQVFFDSKGLPKninnnrggkrYP 189
Cdd:cd07879   190 mH-YNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGPEFVQKLEDKAAKSYIKSLPK----------YP 258
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 190 dSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEPRKFKPRPKPQ 245
Cdd:cd07879   259 -RKDFSTLFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDADEETEQQ 313
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
16-235 7.21e-30

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: 116.63  E-value: 7.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  16 ELLGINLYELMKNNsfhgfNLSI--VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFG-----SSCY 88
Cdd:cd07849    88 ELMETDLYKLIKTQ-----HLSNdhIQYFLYQILRGLKYIHSANVLHRDLKPSNLLL--NTNCDLKICDFGlariaDPEH 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  89 EHQKVYT-YIQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAH-FTQTASR 165
Cdd:cd07849   161 DHTGFLTeYVATRWYRAPEIMLNSKgYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQEdLNCIISL 240
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 166 RQVFFdSKGLPkninnnrggkrYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI---HEP 235
Cdd:cd07849   241 KARNY-IKSLP-----------FKPKVPWNKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLeqyHDP 301
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
10-232 1.81e-29

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: 116.27  E-value: 1.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  10 HLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVL-----YQR---------- 73
Cdd:cd14218    92 HVCMVLEVLGHQLLKWIIKSNYQGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILMcvdegYVRrlaaeatiwq 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  74 -----------------------------GQVTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGC 124
Cdd:cd14218   172 qagapppsgssvsfgasdflvnplepqnaDKIRVKIADLGNACWVHKHFTEDIQTRQYRALEVLIGAEYGTPADIWSTAC 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 125 IMAELYTGYPLF---PGEN---EVEQLACIMEVLGLPPAHFTQTASRRQVFFDSKGLPKNINNNRGGKRYpdskdlTMVV 198
Cdd:cd14218   252 MAFELATGDYLFephSGEDytrDEDHIAHIVELLGDIPPHFALSGRYSREYFNRRGELRHIKNLKHWGLY------EVLV 325
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907169597 199 KTYD------SSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14218   326 EKYEwpleqaAQFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
3-229 3.24e-29

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: 113.75  E-value: 3.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVID 82
Cdd:cd07860    66 DVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAI--KLAD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FGSS--------CYEHQKVytyiqSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLG 153
Cdd:cd07860   144 FGLArafgvpvrTYTHEVV-----TLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLG 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 154 LPpahftqtasrrqvffDSKGLPkninnnrGGKRYPDSK---------DLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPE 224
Cdd:cd07860   219 TP---------------DEVVWP-------GVTSMPDYKpsfpkwarqDFSKVVPPLDEDGRDLLSQMLHYDPNKRISAK 276

                  ....*
gi 1907169597 225 QALKH 229
Cdd:cd07860   277 AALAH 281
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
1-229 3.43e-29

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: 113.67  E-value: 3.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKN-NSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVK 79
Cdd:cd07861    64 LEDVLMQENRLYLVFEFLSMDLKKYLDSlPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKG--VIK 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  80 VIDFG--SSCYEHQKVYTY-IQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLP 155
Cdd:cd07861   142 LADFGlaRAFGIPVRVYTHeVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTP 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 156 pahftqtasRRQVFFDSKGLPKNINNnrggkrYPDSKD--LTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd07861   222 ---------TEDIWPGVTSLPDYKNT------FPKWKKgsLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVH 282
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1-234 4.44e-29

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: 113.56  E-value: 4.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKN--NSFHGFNlsiVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtv 78
Cdd:cd07873    65 LHDIIHTEKSLTLVFEYLDKDLKQYLDDcgNSINMHN---VKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGEL-- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQKVYTY---IQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGL 154
Cdd:cd07873   140 KLADFGLARAKSIPTKTYsneVVTLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGT 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 155 PPAHfTQTASRRQVFFDSKGLPkninnnrggKRYPDSkdLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHE 234
Cdd:cd07873   220 PTEE-TWPGILSNEEFKSYNYP---------KYRADA--LHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHS 287
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
8-232 4.62e-29

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: 112.61  E-value: 4.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCITFELL-GINLYELMKNnsFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSS 86
Cdd:cd06606    71 ENTLNIFLEYVpGGSLASLLKK--FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG--VVKLADFGCA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  87 cYEHQKVYTYIQSR------FYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLA-CIMEVLGLPPahf 159
Cdd:cd06606   147 -KRLAEIATGEGTKslrgtpYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAALfKIGSSGEPPP--- 222
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 160 tqtasrrqvffdskgLPKNInnnrggkrypdSKDLtmvvktydssfLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06606   223 ---------------IPEHL-----------SEEA-----------KDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
33-232 5.57e-29

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: 113.13  E-value: 5.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  33 GFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG-SSCYEHQKVYT-YIQSRFYRSPEVILG 110
Cdd:cd07863   104 GLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQV--KLADFGlARIYSCQMALTpVVVTLWYRAPEVLLQ 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 111 HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPahftqtasrrqvffdSKGLPKNINNNRGGKRYPD 190
Cdd:cd07863   182 STYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPP---------------EDDWPRDVTLPRGAFSPRG 246
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907169597 191 SKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd07863   247 PRPVQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
39-236 4.45e-28

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: 112.53  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFG--------SSCYEHQKVYTyiqsRFYRSPEVILG 110
Cdd:cd07853   105 VKVFLYQILRGLKYLHSAGILHRDIKPGNLLV--NSNCVLKICDFGlarveepdESKHMTQEVVT----QYYRAPEILMG 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 111 HP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPP--AHFTQ-TASRRQVFfdskglpkninnnRGGK 186
Cdd:cd07853   179 SRhYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSleAMRSAcEGARAHIL-------------RGPH 245
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907169597 187 RYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEPR 236
Cdd:cd07853   246 KPPSLPVLYTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEGR 295
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1-231 9.70e-28

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: 109.71  E-value: 9.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKN--NSFHGFNLSIvrrFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtv 78
Cdd:cd07871    68 LHDIIHTERCLTLVFEYLDSDLKQYLDNcgNLMSMHNVKI---FMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGEL-- 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQKVYTY---IQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGL 154
Cdd:cd07871   143 KLADFGLARAKSVPTKTYsneVVTLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGT 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 155 P-----PAHFTQTASRRQVFfdSKGLPKNINNNrggkrypdskdltmvVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd07871   223 PteetwPGVTSNEEFRSYLF--PQYRAQPLINH---------------APRLDTDGIDLLSSLLLYETKSRISAEAALRH 285

                  ..
gi 1907169597 230 AW 231
Cdd:cd07871   286 SY 287
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
13-249 1.11e-27

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: 110.64  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNN-----SFHGFnlsivrrFTFSILKCLHMLYVEKIIHCDLKPENIVlyQRGQVTVKVIDFGSSC 87
Cdd:cd07859    81 VVFELMESDLHQVIKANddltpEHHQF-------FLYQLLRALKYIHTANVFHRDLKPKNIL--ANADCKLKICDFGLAR 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  88 YEHQKVYT------YIQSRFYRSPEVI--LGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHF 159
Cdd:cd07859   152 VAFNDTPTaifwtdYVATRWYRAPELCgsFFSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPET 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 160 TQ----TASRRQVFFDSKGLPKNInnnrgGKRYPDSkdltmvvktyDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEP 235
Cdd:cd07859   232 ISrvrnEKARRYLSSMRKKQPVPF-----SQKFPNA----------DPLALRLLERLLAFDPKDRPTAEEALADPYFKGL 296
                         250
                  ....*....|....
gi 1907169597 236 RKFKPRPKPQILRK 249
Cdd:cd07859   297 AKVEREPSAQPITK 310
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
34-244 1.94e-27

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: 109.38  E-value: 1.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG-SSCYEH-QKVYT-YIQSRFYRSPEVILG 110
Cdd:cd07845   105 FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKG--CLKIADFGlARTYGLpAKPMTpKVVTLWYRAPELLLG 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 111 -HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAH----FTQTASRRQVFfdskgLPKNINNNrgg 185
Cdd:cd07845   183 cTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNESiwpgFSDLPLVGKFT-----LPKQPYNN--- 254
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 186 krypdskdLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEprkfKPRPKP 244
Cdd:cd07845   255 --------LKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKE----KPLPCE 301
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
11-231 2.03e-27

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: 109.15  E-value: 2.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELLGINLYELMKNN---SFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVL-YQRGQVTVKVIDFGSS 86
Cdd:cd07837    80 LYLVFEYLDTDLKKFIDSYgrgPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVdKQKGLLKIADLGLGRA 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  87 CYEHQKVYTY-IQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPpahftqtas 164
Cdd:cd07837   160 FTIPIKSYTHeIVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTP--------- 230
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 165 RRQVFfdskglpKNINNNRGGKRYPDSK--DLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07837   231 NEEVW-------PGVSKLRDWHEYPQWKpqDLSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1-259 2.12e-27

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 110.99  E-value: 2.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNSFHG-FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtV 78
Cdd:COG0515    63 LYDFFQDEGSLYLVMEYVdGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRV-V 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSC---------YEHQKVYTYIQSRFYRSPEVILG---HPYNMAIDMWSLGCIMAELYTGYPLFPGENE---VE 143
Cdd:COG0515   142 KLIDFGLAKllpdpgstsSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNssaTS 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 144 QLACIMEVLGLPPahftqtasrrqvffdskglpkninnnrggKRYPDSKDLTmvvKTYDSSFLDFLRRCLVWEPSLRMTP 223
Cdd:COG0515   222 QTLKIILELPTPS-----------------------------LASPLSPSNP---ELISKAASDLLKKLLAKDPKNRLSS 269
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907169597 224 EQALKHAWIHEPRKFKPRPKPQILRKPGASISSEIS 259
Cdd:COG0515   270 SSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLP 305
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
25-231 3.57e-27

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: 108.94  E-value: 3.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  25 LMKNNSFHgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG-------------SSCYEHQ 91
Cdd:cd07866   104 LLENPSVK-LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGIL--KIADFGlarpydgpppnpkGGGGGGT 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  92 KVYT-YIQSRFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRrqvf 169
Cdd:cd07866   181 RKYTnLVVTRWYRPPELLLGeRRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCGTPTEETWPGWRS---- 256
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 170 fdskgLPkNINNNRGGKRYPDSkdLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07866   257 -----LP-GCEGVHSFTNYPRT--LEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
11-231 1.47e-26

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: 106.70  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELLGINLYELMKNNSfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG------ 84
Cdd:cd07844    73 LTLVFEYLDTDLKQYMDDCG-GGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGEL--KLADFGlaraks 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  85 --SSCYEHQKVytyiqSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEV-EQLACIMEVLGLPpahft 160
Cdd:cd07844   150 vpSKTYSNEVV-----TLWYRPPDVLLGSTeYSTSLDMWGVGCIFYEMATGRPLFPGSTDVeDQLHKIFRVLGTP----- 219
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 161 qtasRRQVFfdsKGLPKNINNNRGGKRYPDSKDLTMVVKTYD--SSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07844   220 ----TEETW---PGVSSNPEFKPYSFPFYPPRPLINHAPRLDriPHGEELALKFLQYEPKKRISAAEAMKHPY 285
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
3-129 1.63e-26

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: 104.66  E-value: 1.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVI 81
Cdd:cd00180    58 DVFETENFLYLVMEYCeGGSLKDLLKENK-GPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT--VKLA 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907169597  82 DFGSSCYEHQKVYTYIQSRF-----YRSPEVILGHPYNMAIDMWSLGCIMAEL 129
Cdd:cd00180   135 DFGLAKDLDSDDSLLKTTGGttppyYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
39-229 6.06e-26

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: 105.32  E-value: 6.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIvLYQRGQVTVKVIDFG-SSCYEHQKVY-TYIQSRFYRSPEVILGHP-YNM 115
Cdd:cd14132   114 IRYYMYELLKALDYCHSKGIMHRDVKPHNI-MIDHEKRKLRLIDWGlAEFYHPGQEYnVRVASRYYKGPELLVDYQyYDY 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 116 AIDMWSLGCIMAEL-YTGYPLFPGENEVEQLACIMEVLG--------------LPPahftqtaSRRQVFFDSKGLPKN-- 178
Cdd:cd14132   193 SLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVKIAKVLGtddlyayldkygieLPP-------RLNDILGRHSKKPWErf 265
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907169597 179 INNNRGGKRYPDSkdltmvvktydssfLDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd14132   266 VNSENQHLVTPEA--------------LDLLDKLLRYDHQERITAKEAMQH 302
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
44-246 5.11e-25

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: 103.95  E-value: 5.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  44 FSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFG---SSCYEHQkVYTYIQSRFYRSPEVILGHPYNMAIDMW 120
Cdd:cd07876   130 YQMLCGIKHLHSAGIIHRDLKPSNIVV--KSDCTLKILDFGlarTACTNFM-MTPYVVTRYYRAPEVILGMGYKENVDIW 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 121 SLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRRQvffdskglpKNINNNRGG-------KRYPD--- 190
Cdd:cd07876   207 SVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSAEFMNRLQPTV---------RNYVENRPQypgisfeELFPDwif 277
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 191 -SKDLTMVVKTydSSFLDFLRRCLVWEPSLRMTPEQALKHAWIH---EPRKFKPrPKPQI 246
Cdd:cd07876   278 pSESERDKLKT--SQARDLLSKMLVIDPDKRISVDEALRHPYITvwyDPAEAEA-PPPQI 334
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
11-229 7.59e-25

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: 102.03  E-value: 7.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG-SSCYE 89
Cdd:cd07862    84 LTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQI--KLADFGlARIYS 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  90 HQKVYT-YIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLP-PAHFTQTAsrrq 167
Cdd:cd07862   162 FQMALTsVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPgEEDWPRDV---- 237
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 168 vffdskGLPKNINNNRggkrypDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd07862   238 ------ALPRQAFHSK------SAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSH 287
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
21-232 1.07e-24

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: 100.63  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  21 NLY-ELMKNNSFhgfNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY-EHQKVYTYIQ 98
Cdd:cd14007    86 ELYkELKKQKRF---DEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGEL--KLADFGWSVHaPSNRRKTFCG 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  99 SRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglppahftqtasrrQVFFdskglPKN 178
Cdd:cd14007   161 TLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNV---------------DIKF-----PSS 220
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907169597 179 INnnrggkryPDSKdltmvvktydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14007   221 VS--------PEAK--------------DLISKLLQKDPSKRLSLEQVLNHPWI 252
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
28-231 1.52e-24

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: 101.68  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  28 NNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG------------SSCYEHqKVYT 95
Cdd:cd07865   110 SNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDG--VLKLADFGlarafslaknsqPNRYTN-RVVT 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  96 YiqsrFYRSPEVILG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLG-LPPAHFTQTAsrRQVFFDSK 173
Cdd:cd07865   187 L----WYRPPELLLGeRDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGsITPEVWPGVD--KLELFKKM 260
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597 174 GLPKninnnrGGKRYPDSKdLTMVVKtyDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07865   261 ELPQ------GQKRKVKER-LKPYVK--DPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
10-232 3.83e-24

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. 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: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 101.65  E-value: 3.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  10 HLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVL----------------YQ 72
Cdd:cd14217    94 HVCMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcvddayvrrmaaeateWQ 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  73 RG---------------------------QVTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd14217   174 KAgapppsgsavstapdllvnpldprnadKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACM 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 126 MAELYTGYPLF---PGEN---EVEQLACIMEVLGLPPAHFTQTASRRQVFFDSKGLPKNINNNRGGKRYpdskdlTMVVK 199
Cdd:cd14217   254 AFELATGDYLFephSGEDysrDEDHIAHIIELLGCIPRHFALSGKYSREFFNRRGELRHITKLKPWSLF------DVLVE 327
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907169597 200 TYD------SSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14217   328 KYGwphedaAQFTDFLIPMLEMVPEKRASAGECLRHPWL 366
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
5-232 4.25e-24

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: 99.20  E-value: 4.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELL-GINLYELMKNNSfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDF 83
Cdd:cd05122    66 YLKKDELWIVMEFCsGGSLKDLLKNTN-KTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEV--KLIDF 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  84 GSSCY--EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENeveqlacIMEVLGLPPAHftq 161
Cdd:cd05122   143 GLSAQlsDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELP-------PMKALFLIATN--- 212
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907169597 162 tasrrqvffDSKGLPKNinnnrggkrypdskdltmvvKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd05122   213 ---------GPPGLRNP--------------------KKWSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1-231 1.18e-23

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: 99.30  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMkNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKV 80
Cdd:cd07872    69 LHDIVHTDKSLTLVFEYLDKDLKQYM-DDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGEL--KL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTY---IQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPP 156
Cdd:cd07872   146 ADFGLARAKSVPTKTYsneVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPT 225
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597 157 AHFTQTASRRQVFfdskglpKNINnnrggkrYPDSKDLTMV--VKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07872   226 EETWPGISSNDEF-------KNYN-------FPKYKPQPLInhAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAY 288
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
4-143 1.82e-23

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: 97.67  E-value: 1.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   4 FFY-F--RNHLCITFELL-GINLYELMKNnsFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvK 79
Cdd:cd05579    58 LYYsFqgKKNLYLVMEYLpGGDLYSLLEN--VGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHL--K 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  80 VIDFGSSCY--EHQKVYTYIQSRF----------------YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENE 141
Cdd:cd05579   134 LTDFGLSKVglVRRQIKLSIQKKSngapekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETP 213

                  ..
gi 1907169597 142 VE 143
Cdd:cd05579   214 EE 215
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
3-157 1.84e-23

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: 97.27  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVI 81
Cdd:cd14014    67 DVGEDDGRPYIVMEYVeGGSLADLLRER--GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRV--KLT 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  82 DFGSSCYEHQKVYTYIQSR----FYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPA 157
Cdd:cd14014   143 DFGIARALGDSGLTQTGSVlgtpAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPS 222
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-143 2.59e-23

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: 96.82  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   4 FFYF--RNHLCITFELL-GINLYELMKNnsFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKV 80
Cdd:cd05123    59 HYAFqtEEKLYLVLDYVpGGELFSHLSK--EGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHI--KL 134
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597  81 IDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVE 143
Cdd:cd05123   135 TDFGLAKElssDGDRTYTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKE 200
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
2-232 3.52e-23

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: 96.53  E-value: 3.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   2 KDFFYFRNHLCITFELL-GINLYELMKNnsFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKV 80
Cdd:cd06627    65 IGSVKTKDSLYIILEYVeNGSLASIIKK--FGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG--LVKL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEvLGLPPa 157
Cdd:cd06627   141 ADFGVATKlneVEKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQ-DDHPP- 218
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 158 hftqtasrrqvffdskgLPKNINNNrggkrypdskdltmvvktydssFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06627   219 -----------------LPENISPE----------------------LRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
1-155 4.22e-23

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: 96.95  E-value: 4.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNN--SFHGFNlsiVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtv 78
Cdd:cd07870    63 LHDIIHTKETLTFVFEYMHTDLAQYMIQHpgGLHPYN---VRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGEL-- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQKVYTY---IQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEV-EQLACIMEVLG 153
Cdd:cd07870   138 KLADFGLARAKSIPSQTYsseVVTLWYRPPDVLLGATdYSSALDIWGAGCIFIEMLQGQPAFPGVSDVfEQLEKIWTVLG 217

                  ..
gi 1907169597 154 LP 155
Cdd:cd07870   218 VP 219
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
13-249 6.78e-23

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: 97.85  E-value: 6.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNNSFHgfnlSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFG--SSCYEH 90
Cdd:cd07874    99 LVMELMDANLCQVIQMELDH----ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVV--KSDCTLKILDFGlaRTAGTS 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  91 QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTAsrrqvff 170
Cdd:cd07874   173 FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKL------- 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 171 dsKGLPKNINNNRGG-------KRYPDS--KDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI---HEPRKF 238
Cdd:cd07874   246 --QPTVRNYVENRPKyagltfpKLFPDSlfPADSEHNKLKASQARDLLSKMLVIDPAKRISVDEALQHPYInvwYDPAEV 323
                         250
                  ....*....|.
gi 1907169597 239 KPrPKPQILRK 249
Cdd:cd07874   324 EA-PPPQIYDK 333
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
13-232 1.56e-22

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: 96.03  E-value: 1.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNNSFHgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY---E 89
Cdd:cd07864    93 LVFEYMDHDLMGLLESGLVH-FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQI--KLADFGLARLynsE 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  90 HQKVYT-YIQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLP-PAhftqtasrr 166
Cdd:cd07864   170 ESRPYTnKVITLWYRPPELLLGEErYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPcPA--------- 240
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 167 qVFFDSKGLPkNINNNRGGKRYpdSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd07864   241 -VWPDVIKLP-YFNTMKPKKQY--RRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
9-231 7.92e-22

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: 92.97  E-value: 7.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELL-GINLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSS- 86
Cdd:cd14003    72 NKIYLVMEYAsGGELFDYIVNNG--RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN--LKIIDFGLSn 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  87 -CYEHQKVYTYIQSRFYRSPEVILGHPYNM-AIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTqtas 164
Cdd:cd14003   148 eFRGGSLLKTFCGTPAYAAPEVLLGRKYDGpKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLS---- 223
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597 165 rrqvffdskglpkninnnrggkryPDSKDLtmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14003   224 ------------------------PDARDL--------------IRRMLVVDPSKRITIEEILNHPW 252
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
5-232 1.02e-21

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 92.65  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELL-GINLYELMKNNSfhGFNLSIVRRFTFSILKCLHML-YVEKIIHCDLKPENIVLYQRGQVtvKVID 82
Cdd:cd06623    68 FYKEGEISIVLEYMdGGSLADLLKKVG--KIPEPVLAYIARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGEV--KIAD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FG-SSCYEH--QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTG-YPLFPgeNEVEQLACIMEVLglppah 158
Cdd:cd06623   144 FGiSKVLENtlDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGkFPFLP--PGQPSFFELMQAI------ 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169597 159 ftqtasrrqVFFDSKGLPKNInnnrggkrypdskdltmvvktYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06623   216 ---------CDGPPPSLPAEE---------------------FSPEFRDFISACLQKDPKKRPSAAELLQHPFI 259
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
2-141 1.88e-21

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: 91.90  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   2 KDFFYFRNHLCitfelLGINLYELMKNNSFhgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVI 81
Cdd:cd05572    65 KKYLYMLMEYC-----LGGELWTILRDRGL--FDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYV--KLV 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597  82 DFGSS--CYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENE 141
Cdd:cd05572   136 DFGFAkkLGSGRKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDE 197
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
9-146 2.13e-21

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: 91.45  E-value: 2.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELL-GINLYELMKNNSFHgFNLSIVRRFTFSI---LKCLHMLyveKIIHCDLKPENIVLYQRGqvTVKVIDFG 84
Cdd:cd13999    63 PPLCIVTEYMpGGSLYDLLHKKKIP-LSWSLRLKIALDIargMNYLHSP---PIIHRDLKSLNILLDENF--TVKIADFG 136
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597  85 SSCYEHQK-------VYTYIqsrfYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLA 146
Cdd:cd13999   137 LSRIKNSTtekmtgvVGTPR----WMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAA 201
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
11-249 4.30e-21

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: 92.80  E-value: 4.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELLGINLYELMKNNSFHgfnlSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFG--SSCY 88
Cdd:cd07875   104 VYIVMELMDANLCQVIQMELDH----ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVV--KSDCTLKILDFGlaRTAG 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  89 EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFT---QTASR 165
Cdd:cd07875   178 TSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCPEFMkklQPTVR 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 166 RQVFFDSKGLPKNINNNRGGKRYPDSKDLTmvvKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI---HEPRKFKPrP 242
Cdd:cd07875   258 TYVENRPKYAGYSFEKLFPDVLFPADSEHN---KLKASQARDLLSKMLVIDASKRISVDEALQHPYInvwYDPSEAEA-P 333

                  ....*..
gi 1907169597 243 KPQILRK 249
Cdd:cd07875   334 PPKIPDK 340
PTZ00284 PTZ00284
protein kinase; Provisional
1-234 5.15e-21

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 93.49  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRN---HLCITFELLGINLYE-LMKnnsfHG-FNLSIVRRFTFSILKCLHMLYVE-KIIHCDLKPENIvLYQRG 74
Cdd:PTZ00284  194 MKIQRYFQNetgHMCIVMPKYGPCLLDwIMK----HGpFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENI-LMETS 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  75 QVTV---------------KVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGE 139
Cdd:PTZ00284  269 DTVVdpvtnralppdpcrvRICDLGGCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLYDTH 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 140 NEVEQLACIMEVLGLPPAHFTQ---TASRRQVfFDSKGLPKNINNNRGGKRYPDSKDLTMVVKtyDSSFLDFLRRCLVWE 216
Cdd:PTZ00284  349 DNLEHLHLMEKTLGRLPSEWAGrcgTEEARLL-YNSAGQLRPCTDPKHLARIARARPVREVIR--DDLLCDLIYGLLHYD 425
                         250
                  ....*....|....*...
gi 1907169597 217 PSLRMTPEQALKHAWIHE 234
Cdd:PTZ00284  426 RQKRLNARQMTTHPYVLK 443
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
19-232 1.27e-20

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: 89.78  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  19 GINLYE-LMKNNSfhGFNLSIVRRFTFSILKCL---HMLYVekiIHCDLKPENIVLYQRgQVTVKVIDFG-SSCYEH-QK 92
Cdd:cd14074    86 GGDMYDyIMKHEN--GLNEDLARKYFRQIVSAIsycHKLHV---VHRDLKPENVVFFEK-QGLVKLTDFGfSNKFQPgEK 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  93 VYTYIQSRFYRSPEVILGHPYNM-AIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTqtasrrqvffd 171
Cdd:cd14074   160 LETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVS----------- 228
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907169597 172 skglpkninnnrggkryPDSKDLtmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14074   229 -----------------PECKDL--------------IRRMLIRDPKKRASLEEIENHPWL 258
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
8-232 1.76e-20

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


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 89.28  E-value: 1.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCITFELL-GINLYELMKnnsfHGFNL--SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFG 84
Cdd:cd06626    71 REEVYIFMEYCqEGTLEELLR----HGRILdeAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL--IKLGDFG 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  85 SSCY--------EHQKVYTYIQSRFYRSPEVILGHP---YNMAIDMWSLGCIMAELYTGYPLFPgenEVEQLACIMEVLG 153
Cdd:cd06626   145 SAVKlknntttmAPGEVNSLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWS---ELDNEWAIMYHVG 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 154 L--PPAhftqtasrrqvffdskgLPKNINNNRGGKrypdskdltmvvktydssflDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd06626   222 MghKPP-----------------IPDSLQLSPEGK--------------------DFLSRCLESDPKKRPTASELLDHPF 264

                  .
gi 1907169597 232 I 232
Cdd:cd06626   265 I 265
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
39-232 2.42e-20

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: 88.95  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVL-YQRGQVTVKVIDFGSSCY--EHQKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd14106   110 VRRLMRQILEGVQYLHERNIVHLDLKPQNILLtSEFPLGDIKLCDFGISRVigEGEEIREILGTPDYVAPEILSYEPISL 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEV-LGLPPAHFTQTASRRQvffdskglpkninnnrggkrypdskdl 194
Cdd:cd14106   190 ATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCnLDFPEELFKDVSPLAI--------------------------- 242
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907169597 195 tmvvktydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14106   243 ------------DFIKRLLVKDPEKRLTAKECLEHPWL 268
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
4-229 4.05e-20

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: 88.65  E-value: 4.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   4 FFYFRNHLCItfellginLYELMKNNSFHG-------FNLSIVRRFTFSILKCLHMLY-VEKIIHCDLKPENIVLYQRGQ 75
Cdd:cd06620    72 FLNENNNIII--------CMEYMDCGSLDKilkkkgpFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSKGQ 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  76 VtvKVIDFGSSCYEHQKVY-TYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTG-YPLFPGENEVEQLACIMEVLG 153
Cdd:cd06620   144 I--KLCDFGVSGELINSIAdTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGeFPFAGSNDDDDGYNGPMGILD 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 154 LppahftqtaSRRQVFFDSKGLPKninnnrgGKRYPdsKDLTmvvktydssflDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd06620   222 L---------LQRIVNEPPPRLPK-------DRIFP--KDLR-----------DFVDRCLLKDPRERPSPQLLLDH 268
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
24-232 1.07e-19

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: 87.02  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  24 ELMKNNSFHGF-------NLSIVRRFTFSILKCLHMLY-VEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY-EHQKVY 94
Cdd:cd06605    79 EYMDGGSLDKIlkevgriPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSRGQV--KLCDFGVSGQlVDSLAK 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  95 TYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTG-YPlFPGENE------VEQLACIMEvlGLPPahftqtasrrq 167
Cdd:cd06605   157 TFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGrFP-YPPPNAkpsmmiFELLSYIVD--EPPP----------- 222
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 168 vffdskglpkninnnrggkRYPDSKdltmvvktYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06605   223 -------------------LLPSGK--------FSPDFQDFVSQCLQKDPTERPSYKELMEHPFI 260
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
3-240 2.03e-19

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 86.72  E-value: 2.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVI 81
Cdd:cd06611    69 EAYFYENKLWILIEFCdGGALDSIMLELE-RGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGD--VKLA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  82 DFGSSC---YEHQKVYTYIQSRFYRSPEVIL-----GHPYNMAIDMWSLGCIMAELYTGYPlfPgENEVEQLACIMEVLG 153
Cdd:cd06611   146 DFGVSAknkSTLQKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEP--P-HHELNPMRVLLKILK 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 154 LPPAHFTQtaSRRqvffdskglpkninnnrggkrypdskdltmvvktYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIH 233
Cdd:cd06611   223 SEPPTLDQ--PSK----------------------------------WSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266

                  ....*..
gi 1907169597 234 EPRKFKP 240
Cdd:cd06611   267 DQSDNKA 273
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
1-136 2.14e-19

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: 86.15  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKV 80
Cdd:cd14002    65 MLDSFETKKEFVVVTEYAQGELFQILEDD--GTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVV--KL 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907169597  81 IDFG----SSCYEHqkVYTYIQ-SRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLF 136
Cdd:cd14002   141 CDFGfaraMSCNTL--VLTSIKgTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPF 199
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
41-237 2.77e-19

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 86.32  E-value: 2.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  41 RFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEHQKVY-TYIQSRFYRSPEVILGHPYNMAIDM 119
Cdd:cd06621   109 KIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ--VKLCDFGVSGELVNSLAgTFTGTSYYMAPERIQGGPYSITSDV 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 120 WSLGCIMAELYTGYplFPGENEVEQLACIMEVLglppaHFTQTASRrqvffdskglpkninnnrggkryPDSKDLTMVVK 199
Cdd:cd06621   187 WSLGLTLLEVAQNR--FPFPPEGEPPLGPIELL-----SYIVNMPN-----------------------PELKDEPENGI 236
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907169597 200 TYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI-HEPRK 237
Cdd:cd06621   237 KWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIkAQEKK 275
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
39-231 3.32e-19

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: 85.40  E-value: 3.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSScyehQKVYT--YIQSRF----YRSPEVILGHP 112
Cdd:cd14006    91 VRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLA----RKLNPgeELKEIFgtpeFVAPEIVNGEP 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 113 YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglppahftqtasrrQVFFDSkglpkninnnrggkryPDSK 192
Cdd:cd14006   167 VSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISAC---------------RVDFSE----------------EYFS 215
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907169597 193 DLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14006   216 SVSQEAK-------DFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
2-229 7.00e-19

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: 84.82  E-value: 7.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   2 KDFFYFRNHLCITFELL-GINLYELMKNNSFHGFNLS---IVRRFT--FSILKCLHmlyVEKIIHCDLKPENIVLYQRGq 75
Cdd:cd08215    65 YESFEENGKLCIVMEYAdGGDLAQKIKKQKKKGQPFPeeqILDWFVqiCLALKYLH---SRKILHRDLKTQNIFLTKDG- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  76 vTVKVIDFGSScyehqKVY--------TYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEveqlac 147
Cdd:cd08215   141 -VVKLGDFGIS-----KVLesttdlakTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNL------ 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 148 imevlglppahftqtasrrqvffdsKGLPKNINNnrggKRYPdskdltMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQAL 227
Cdd:cd08215   209 -------------------------PALVYKIVK----GQYP------PIPSQYSSELRDLVNSMLQKDPEKRPSANEIL 253

                  ..
gi 1907169597 228 KH 229
Cdd:cd08215   254 SS 255
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
3-229 1.13e-18

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: 84.18  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSFHgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVI 81
Cdd:cd06614    63 DSYLVGDELWVVMEYMdGGSLTDIITQNPVR-MNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDG--SVKLA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  82 DFG-----SScyEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGcIMA-ELYTGYPLFpgeneveqlacimevLGLP 155
Cdd:cd06614   140 DFGfaaqlTK--EKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLG-IMCiEMAEGEPPY---------------LEEP 201
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597 156 P--AHFTQTasrrqvffdSKGLP--KNINNnrggkrypdskdltmvvktYDSSFLDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd06614   202 PlrALFLIT---------TKGIPplKNPEK-------------------WSPEFKDFLNKCLVKDPEKRPSAEELLQH 251
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1-232 1.16e-18

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: 84.31  E-value: 1.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNSFhgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVT-V 78
Cdd:cd14167    66 LDDIYESGGHLYLIMQLVsGGELFDRIVEKGF--YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSkI 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQK--VYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMevlglpp 156
Cdd:cd14167   144 MISDFGLSKIEGSGsvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQIL------- 216
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 157 ahftqtasRRQVFFDSkglpkninnnrggkryPDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14167   217 --------KAEYEFDS----------------PYWDDISDSAK-------DFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
40-231 1.61e-18

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 83.94  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY--EHQKVYTYIQSRFYRSPEVI-----LGHP 112
Cdd:cd14093   112 RRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNV--KISDFGFATRldEGEKLRELCGTPGYLAPEVLkcsmyDNAP 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 113 -YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEvlglppAHFTqtasrrqvfFDSkglpkninnnrggkryPDS 191
Cdd:cd14093   190 gYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIME------GKYE---------FGS----------------PEW 238
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907169597 192 KDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14093   239 DDISDTAK-------DLISKLLVVDPKKRLTAEEALEHPF 271
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
2-139 3.93e-18

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: 82.91  E-value: 3.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   2 KDFFYFRN--HLCITFELL-GINLYELMKnnSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtv 78
Cdd:cd05611    61 KLYYSFQSkdYLYLVMEYLnGGDCASLIK--TLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHL-- 136
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597  79 KVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGE 139
Cdd:cd05611   137 KLTDFGLSrnGLEKRHNKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAE 199
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
8-146 4.59e-18

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: 82.73  E-value: 4.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCITFEL-LGINLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSS 86
Cdd:cd14010    66 SNHLWLVVEYcTGGDLETLLRQDG--NLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNG--TLKLSDFGLA 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597  87 CYE-------------------HQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENeVEQLA 146
Cdd:cd14010   142 RREgeilkelfgqfsdegnvnkVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAES-FTELV 219
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
1-155 4.88e-18

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: 83.20  E-value: 4.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKV 80
Cdd:cd07869    68 LHDIIHTKETLTLVFEYVHTDLCQYMDKHP-GGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGEL--KL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  81 IDFGSSCYEHQKVYTY---IQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVE-QLACIMEVLGLP 155
Cdd:cd07869   145 ADFGLARAKSVPSHTYsneVVTLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQdQLERIFLVLGTP 224
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1-232 5.58e-18

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 82.73  E-value: 5.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYE-LMKNNSFHGFNLSIVRRFTFSILKCLHMlyvEKIIHCDLKPENIVLYQRGQ-VT 77
Cdd:cd14166    65 LEDIYESTTHYYLVMQLVsGGELFDrILERGVYTEKDASRVINQVLSAVKYLHE---NGIVHRDLKPENLLYLTPDEnSK 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  78 VKVIDFG-SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEvlglpp 156
Cdd:cd14166   142 IMITDFGlSKMEQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKE------ 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 157 AHFTqtasrrqvfFDSkglpkninnnrggkryPDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14166   216 GYYE---------FES----------------PFWDDISESAK-------DFIRHLLEKNPSKRYTCEKALSHPWI 259
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
2-230 6.37e-18

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: 82.05  E-value: 6.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   2 KDFFYFRNHLCITFELLGI-NLYELMKNNSFHG--FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtv 78
Cdd:cd08530    65 KEAFLDGNRLCIVMEYAPFgDLSKLISKRKKKRrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLV-- 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQKV-YTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENeveqlaciMEVLglppa 157
Cdd:cd08530   143 KIGDLGISKVLKKNLaKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEART--------MQEL----- 209
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 158 hftqtasRRQVFfdskglpkninnnRGgkRYPdskdltMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHA 230
Cdd:cd08530   210 -------RYKVC-------------RG--KFP------PIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
5-232 8.37e-18

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: 82.02  E-value: 8.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELL-GINLYELMKN-NSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVID 82
Cdd:cd06610    68 FVVGDELWLVMPLLsGGSLLDIMKSsYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDG--SVKIAD 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FGSS-------CYEHQKVYTYIQSRFYRSPEVI-LGHPYNMAIDMWSLGCIMAELYTGYPlfPGENeveqlacimevlgL 154
Cdd:cd06610   146 FGVSaslatggDRTRKVRKTFVGTPCWMAPEVMeQVRGYDFKADIWSFGITAIELATGAA--PYSK-------------Y 210
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597 155 PPahftqtasrrqvffdSKGLPKNINNNrggkryPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06610   211 PP---------------MKVLMLTLQND------PPSLETGADYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
8-232 2.17e-17

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: 80.48  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCITFELL-GINLYELMKNnsfHG-FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGS 85
Cdd:cd06625    74 EKSLSIFMEYMpGGSVKDEIKA---YGaLTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNV--KLGDFGA 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  86 S------CyEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFpgeNEVEQLACIMEVLglppahf 159
Cdd:cd06625   149 SkrlqtiC-SSTGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPW---AEFEPMAAIFKIA------- 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 160 TQTASRRqvffdskgLPKNInnnrggkrypdskdltmvvktyDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06625   218 TQPTNPQ--------LPPHV----------------------SEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
45-232 2.83e-17

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: 80.00  E-value: 2.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSC---YEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWS 121
Cdd:cd06612   107 QTLKGLEYLHSNKKIHRDIKAGNILLNEEGQA--KLADFGVSGqltDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWS 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 122 LGCIMAELYTGYPLFPGENEVEQLACIMEvlgLPPAHFTQtasrrqvffdskglPKNInnnrggkrypdSKDltmvvkty 201
Cdd:cd06612   185 LGITAIEMAEGKPPYSDIHPMRAIFMIPN---KPPPTLSD--------------PEKW-----------SPE-------- 228
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907169597 202 dssFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06612   229 ---FNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
37-231 3.06e-17

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: 79.96  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTV-KVIDFGSSCYEHQKVY--TYIQSRFYRSPEVILGHPY 113
Cdd:cd14009    92 AVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVlKIADFGFARSLQPASMaeTLCGSPLYMAPEILQFQKY 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 114 NMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASrrqvffdskglpkninnnrggkryPDSKD 193
Cdd:cd14009   172 DAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLS------------------------PDCKD 227
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907169597 194 LtmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14009   228 L--------------LRRLLRRDPAERISFEEFFAHPF 251
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
1-231 6.70e-17

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: 79.44  E-value: 6.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYE-LMKNNS---FHGfnlsivRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQ 75
Cdd:cd14098    66 LIDWYEDDQHIYLVMEYVeGGDLMDfIMAWGAipeQHA------RELTKQILEAMAYTHSMGITHRDLKPENILITQDDP 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  76 VTVKVIDFGSSCYEHQKVY--TYIQSRFYRSPEVILGHP------YNMAIDMWSLGCIMAELYTGYPLFPGENeveQLAC 147
Cdd:cd14098   140 VIVKISDFGLAKVIHTGTFlvTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSS---QLPV 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 148 IMEVlglppahftqtasrrqvffdSKGlpkninnnrggkRYPDSKDLTMVVKtydSSFLDFLRRCLVWEPSLRMTPEQAL 227
Cdd:cd14098   217 EKRI--------------------RKG------------RYTQPPLVDFNIS---EEAIDFILRLLDVDPEKRMTAAQAL 261

                  ....
gi 1907169597 228 KHAW 231
Cdd:cd14098   262 DHPW 265
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
3-232 9.37e-17

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: 78.42  E-value: 9.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSFHgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVI 81
Cdd:cd14103    57 DAFETPREMVLVMEYVaGGELFERVVDDDFE-LTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKII 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  82 DFGSSC-YEHQKVytyIQSRF----YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglpp 156
Cdd:cd14103   136 DFGLARkYDPDKK---LKVLFgtpeFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRA----- 207
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 157 ahftqtasrrQVFFDskglpkninnnrggkrYPDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14103   208 ----------KWDFD----------------DEAFDDISDEAK-------DFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
11-232 9.86e-17

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: 79.13  E-value: 9.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELL-GINLYELMKNNSFHGFNLSIVRrFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSSCYE 89
Cdd:cd14104    71 LVMIFEFIsGVDIFERITTARFELNEREIVS-YVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  90 H--QKV-YTYIQSRFYrSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEvlglppAHFTqtasrr 166
Cdd:cd14104   150 KpgDKFrLQYTSAEFY-APEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRN------AEYA------ 216
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 167 qvfFDSKGLpKNINNNRggkrypdskdltmvvktydssfLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14104   217 ---FDDEAF-KNISIEA----------------------LDFVDRLLVKERKSRMTAQEALNHPWL 256
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
11-232 1.38e-16

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: 78.21  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELL-GINLYELMKNnsFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSScyE 89
Cdd:cd06632    77 LYIFLEYVpGGSIHKLLQR--YGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVV--KLADFGMA--K 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  90 HQKVYTYIQS----RFYRSPEVIL--GHPYNMAIDMWSLGCIMAELYTGYPLFpgeNEVEQLACIMEVlglppahftqta 163
Cdd:cd06632   151 HVEAFSFAKSfkgsPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAIFKI------------ 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 164 srrqvfFDSKGLPKninnnrggkrYPDSkdLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06632   216 ------GNSGELPP----------IPDH--LSPDAK-------DFIRLCLQRDPEDRPTASQLLEHPFV 259
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
13-234 1.69e-16

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 78.62  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNNSFHGFNL--SIVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYE 89
Cdd:cd06617    77 ICMEVMDTSLDKFYKKVYDKGLTIpeDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ--VKLCDFGISGYL 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  90 HQKVYTYIQ--SRFYRSPEVILG----HPYNMAIDMWSLGCIMAELYTG-YPLFPGENEVEQLACIMEvlGLPPAhftqt 162
Cdd:cd06617   155 VDSVAKTIDagCKPYMAPERINPelnqKGYDVKSDVWSLGITMIELATGrFPYDSWKTPFQQLKQVVE--EPSPQ----- 227
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 163 asrrqvffdskgLPKNinnnrggkrypdskdltmvvkTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHE 234
Cdd:cd06617   228 ------------LPAE---------------------KFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFEL 266
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
34-141 1.72e-16

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: 78.41  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSS--------------CYEHQKVYTYIQS 99
Cdd:cd05581    98 LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHI--KITDFGTAkvlgpdsspestkgDADSQIAYNQARA 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907169597 100 R-F-----YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENE 141
Cdd:cd05581   176 AsFvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNE 223
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
31-232 2.15e-16

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: 77.81  E-value: 2.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  31 FHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSS-----CYEHQKVYTYIQSRFYRSP 105
Cdd:cd06629   102 YGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEG--ICKISDFGISkksddIYGNNGATSMQGSVFWMAP 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 106 EVI--LGHPYNMAIDMWSLGCIMAELYTGYPLFPGEnevEQLACIMEVLGL---PPahftqtasrrqvffdskgLPKNIN 180
Cdd:cd06629   180 EVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDD---EAIAAMFKLGNKrsaPP------------------VPEDVN 238
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907169597 181 NNRGGkrypdskdltmvvktydssfLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06629   239 LSPEA--------------------LDFLNACFAIDPRDRPTAAELLSHPFL 270
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
39-232 2.32e-16

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: 77.55  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqrgQV-TVKVIDFG-SSCYEHQKVYTYIQ-SRFYRSPEVILGHPYNM 115
Cdd:cd14109   101 VAVFVRQLLLALKHMHDLGIAHLDLRPEDILL----QDdKLKLADFGqSRRLLRGKLTTLIYgSPEFVSPEIVNSYPVTL 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEvlglppahftqtasrrqvffdskglpkninnnrgGKRYPDSKDLT 195
Cdd:cd14109   177 ATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRS----------------------------------GKWSFDSSPLG 222
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 196 MVvkTYDSSflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14109   223 NI--SDDAR--DFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
7-135 3.22e-16

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: 77.67  E-value: 3.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   7 FRNHL-------CITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIvLYQRGQVTVK 79
Cdd:cd14020    73 FTNHYsanvpsrCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNI-LWSAEDECFK 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597  80 VIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPY-----------NMAIDMWSLGCIMAELYTGYPL 135
Cdd:cd14020   152 LIDFGLSFKEGNQDVKYIQTDGYRAPEAELQNCLaqaglqsetecTSAVDLWSLGIVLLEMFSGMKL 218
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
1-136 3.36e-16

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: 76.94  E-value: 3.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVK 79
Cdd:cd14121    60 LKDFQWDEEHIYLIMEYCsGGDLSRFIRSR--RTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLK 137
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597  80 VIDFGSSCY--EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLF 136
Cdd:cd14121   138 LADFGFAQHlkPNDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPF 196
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
1-232 3.43e-16

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: 77.43  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVT-V 78
Cdd:cd14084    76 IEDFFDAEDDYYIVLELMeGGELFDRVVSNK--RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEEClI 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCY--EHQKVYTYIQSRFYRSPEVIL---GHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLAcimevlg 153
Cdd:cd14084   154 KITDFGLSKIlgETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLK------- 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 154 lppahfTQTASRRQVFFDSKGlpKNINNnrggkrypDSKDLtmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14084   227 ------EQILSGKYTFIPKAW--KNVSE--------EAKDL--------------VKKMLVVDPSRRPSIEEALEHPWL 275
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
56-143 4.08e-16

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: 77.20  E-value: 4.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  56 EKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTG 132
Cdd:cd08217   129 GKILHRDLKPANIFLDSDN--NVKLGDFGLARVlshDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCAL 206
                          90
                  ....*....|.
gi 1907169597 133 YPLFPGENEVE 143
Cdd:cd08217   207 HPPFQAANQLE 217
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
42-232 4.50e-16

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 76.98  E-value: 4.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRG--QVTVKVIDFG-----SSCYEHQKVYTYIQsrfYRSPEVILGHPYN 114
Cdd:cd14194   113 FLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpKPRIKIIDFGlahkiDFGNEFKNIFGTPE---FVAPEIVNYEPLG 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 115 MAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglpPAHFTQtasrrQVFFDSKGLPKninnnrggkrypdskdl 194
Cdd:cd14194   190 LEADMWSIGVITYILLSGASPFLGDTKQETLANVSAV----NYEFED-----EYFSNTSALAK----------------- 243
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907169597 195 tmvvktydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14194   244 ------------DFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
37-231 4.58e-16

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: 77.80  E-value: 4.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLY----QRGQVTVKVIDFG----SSCYEHQKVYTYIQSRFYRSPEVI 108
Cdd:cd07867   109 SMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPELL 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 109 LG-HPYNMAIDMWSLGCIMAELYTGYPLFPGENE---------VEQLACIMEVLGLP-----------PAHFTQTASRRQ 167
Cdd:cd07867   189 LGaRHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPadkdwedirkmPEYPTLQKDFRR 268
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169597 168 VFFDSKGLPKNINNNrggKRYPDSKdltmvvktydsSFLdFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07867   269 TTYANSSLIKYMEKH---KVKPDSK-----------VFL-LLQKLLTMDPTKRITSEQALQDPY 317
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
10-249 4.88e-16

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: 76.90  E-value: 4.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  10 HLCITFELL-GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMlyvEKIIHCDLKPENIVLYQRGQVtvKVIDFG-SSC 87
Cdd:cd06609    73 KLWIIMEYCgGGSVLDLLKPGPLDETYIAFILREVLLGLEYLHS---EGKIHRDIKAANILLSEEGDV--KLADFGvSGQ 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  88 YEHQ--KVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYP----LFPgeneveqlaciMEVLGLPPahftq 161
Cdd:cd06609   148 LTSTmsKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPplsdLHP-----------MRVLFLIP----- 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 162 tasrrqvffdskglpkninnnrggKRYPDSKDLTMvvktYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIhepRKFKPR 241
Cdd:cd06609   212 ------------------------KNNPPSLEGNK----FSKPFKDFVELCLNKDPKERPSAKELLKHKFI---KKAKKT 260

                  ....*...
gi 1907169597 242 PKPQILRK 249
Cdd:cd06609   261 SYLTLLIE 268
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
46-163 8.11e-16

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 77.06  E-value: 8.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd05584   109 ITLALGHLHSLGIIYRDLKPENILLDAQGHV--KLTDFGlckESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSL 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907169597 123 GCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTA 163
Cdd:cd05584   187 GALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEA 227
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
3-232 8.83e-16

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: 76.15  E-value: 8.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSFHGFNLSIVRrFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVI 81
Cdd:cd14192    68 DAFESKTNLTLIMEYVdGGELFDRITDESYQLTELDAIL-FTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKII 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  82 DFG-SSCYE-HQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglppahf 159
Cdd:cd14192   147 DFGlARRYKpREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNC-------- 218
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 160 tqtasrrQVFFDSKGLpkninnnrggkrypdsKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14192   219 -------KWDFDAEAF----------------ENLSEEAK-------DFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
9-232 8.95e-16

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


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 76.05  E-value: 8.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELlgINLYELMKNNSFHG---FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGS 85
Cdd:cd14008    79 DKLYLVLEY--CEGGPVMELDSGDRvppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADG--TVKISDFGV 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  86 ScyehQKVY---TYIQSR-----FYrSPEVILG-----HPYnmAIDMWSLGCIMAELYTGYPLFPGENEVEQLacimevl 152
Cdd:cd14008   155 S----EMFEdgnDTLQKTagtpaFL-APELCDGdsktySGK--AADIWALGVTLYCLVFGRLPFNGDNILELY------- 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 153 glppahftqtasrrqvffdskglpKNINNNrgGKRYPDSKDLtmvvktyDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14008   221 ------------------------EAIQNQ--NDEFPIPPEL-------SPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
42-232 2.05e-15

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 75.22  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRG--QVTVKVIDFG-SSCYEHQKVYTYI-QSRFYRSPEVILGHPYNMAI 117
Cdd:cd14105   113 FLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpIPRIKLIDFGlAHKIEDGNEFKNIfGTPEFVAPEIVNYEPLGLEA 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 118 DMWSLGCIMAELYTGYPLFPGENEVEQLACIMEV-LGLPPAHFTQTASrrqvffdskgLPKninnnrggkrypdskdltm 196
Cdd:cd14105   193 DMWSIGVITYILLSGASPFLGDTKQETLANITAVnYDFDDEYFSNTSE----------LAK------------------- 243
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907169597 197 vvktydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14105   244 ----------DFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
39-232 2.63e-15

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: 74.97  E-value: 2.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQV-TVKVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd14197   113 VKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgDIKIVDFGLSriLKNSEELREIMGTPEYVAPEILSYEPIST 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglppahftqtasrrqvffdskglpkNINNNrggkrypdSKDLT 195
Cdd:cd14197   193 ATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQM--------------------------NVSYS--------EEEFE 238
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 196 MVvktyDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14197   239 HL----SESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
39-232 2.77e-15

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


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 74.60  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFG--SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMA 116
Cdd:cd14081   103 ARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN--IKIADFGmaSLQPEGSLLETSCGSPHYACPEVIKGEKYDGR 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 117 I-DMWSLGCIMAELYTGYPLFPGENeVEQLacIMEVlglppahftqtasRRQVFFdskgLPKNINnnrggkryPDSKDLt 195
Cdd:cd14081   181 KaDIWSCGVILYALLVGALPFDDDN-LRQL--LEKV-------------KRGVFH----IPHFIS--------PDAQDL- 231
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 196 mvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14081   232 -------------LRRMLEVNPEKRITIEEIKKHPWF 255
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
37-232 2.83e-15

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: 75.16  E-value: 2.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQKVY-TYIQSRFYRSPEVILGHPYN 114
Cdd:cd06615    99 NILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEI--KLCDFGVSGQLIDSMAnSFVGTRSYMSPERLQGTHYT 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 115 MAIDMWSLGCIMAELYTG-YPLfPGENEVEQ---LACIMEVLGLPPAHFTQT-----ASRRQVFFDskgLPKNINNNRgG 185
Cdd:cd06615   177 VQSDIWSLGLSLVEMAIGrYPI-PPPDAKELeamFGRPVSEGEAKESHRPVSghppdSPRPMAIFE---LLDYIVNEP-P 251
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907169597 186 KRYPDskdltmvvKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06615   252 PKLPS--------GAFSDEFQDFVDKCLKKNPKERADLKELTKHPFI 290
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
9-163 2.96e-15

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: 74.49  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELL-GINLYELMknNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG-SS 86
Cdd:cd06628    79 NHLNIFLEYVpGGSVATLL--NNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKG--GIKISDFGiSK 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  87 CYEHQKVYTYIQ--------SRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPgenEVEQLACIMEVLGL---- 154
Cdd:cd06628   155 KLEANSLSTKNNgarpslqgSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFP---DCTQMQAIFKIGENaspt 231

                  ....*....
gi 1907169597 155 PPAHFTQTA 163
Cdd:cd06628   232 IPSNISSEA 240
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
46-231 3.09e-15

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: 74.33  E-value: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIvLYQRGQVTVKVI--DFGSSCYEHQKVY-TYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd14083   110 VLEAVDYLHSLGIVHRDLKPENL-LYYSPDEDSKIMisDFGLSKMEDSGVMsTACGTPGYVAPEVLAQKPYGKAVDCWSI 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 123 GCIMAELYTGYPLFPGENEVEQLACIMevlglppahftqtasRRQVFFDSkglpkninnnrggkryPDSKDLTMVVKtyd 202
Cdd:cd14083   189 GVISYILLCGYPPFYDENDSKLFAQIL---------------KAEYEFDS----------------PYWDDISDSAK--- 234
                         170       180
                  ....*....|....*....|....*....
gi 1907169597 203 ssflDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14083   235 ----DFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
1-232 5.13e-15

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 74.02  E-value: 5.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNnsfHG-FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtV 78
Cdd:cd14077    78 LRDFLRTPNHYYMLFEYVdGGQLLDYIIS---HGkLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGN--I 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFG-SSCYEHQK-VYTYIQSRFYRSPEVILGHPY-NMAIDMWSLGCIMAELYTGYPLFPGENeveqlacimevlglp 155
Cdd:cd14077   153 KIIDFGlSNLYDPRRlLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDEN--------------- 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597 156 pahftqtasrrqvffdSKGLPKNInnNRGGKRYPdskdltmvvKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14077   218 ----------------MPALHAKI--KKGKVEYP---------SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
38-231 6.74e-15

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: 74.71  E-value: 6.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  38 IVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLY----QRGQVTVKVIDFG----SSCYEHQKVYTYIQSRFYRSPEVIL 109
Cdd:cd07868   125 MVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPELLL 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 110 G-HPYNMAIDMWSLGCIMAELYTGYPLFPGENE---------VEQLACIMEVLGLP-----------PAHFTQTASRRQV 168
Cdd:cd07868   205 GaRHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpyhHDQLDRIFNVMGFPadkdwedikkmPEHSTLMKDFRRN 284
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 169 FFDSKGLPKNINNNrggKRYPDSKDLTMvvktydssfldfLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd07868   285 TYTNCSLIKYMEKH---KVKPDSKAFHL------------LQKLLTMDPIKRITSEQAMQDPY 332
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1-232 1.05e-14

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: 73.39  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYE-LMKNNSFHGFNLSIVRRFTFSILKCLHMLyveKIIHCDLKPENIvLYQRGQVTV 78
Cdd:cd14169    66 LEDIYESPTHLYLAMELVtGGELFDrIIERGSYTEKDASQLIGQVLQAVKYLHQL---GIVHRDLKPENL-LYATPFEDS 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVI--DFGSSCYEHQKVY-TYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMevlglp 155
Cdd:cd14169   142 KIMisDFGLSKIEAQGMLsTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQIL------ 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597 156 pahftqtasRRQVFFDSkglpkninnnrggkryPDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14169   216 ---------KAEYEFDS----------------PYWDDISESAK-------DFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
41-232 1.09e-14

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: 73.07  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  41 RFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVT--VKVIDFG-----SSCYEHQKVYTYIQsrfYRSPEVILGHPY 113
Cdd:cd14196   112 SFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIphIKLIDFGlaheiEDGVEFKNIFGTPE---FVAPEIVNYEPL 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 114 NMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglpPAHFTQtasrrQVFFDSKGLPKninnnrggkrypdskd 193
Cdd:cd14196   189 GLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV----SYDFDE-----EFFSHTSELAK---------------- 243
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907169597 194 ltmvvktydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14196   244 -------------DFIRKLLVKETRKRLTIQEALRHPWI 269
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
38-232 1.17e-14

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 72.99  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  38 IVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG-SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMA 116
Cdd:cd06619    96 VLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQV--KLCDFGvSTQLVNSIAKTYVGTNAYMAPERISGEQYGIH 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 117 IDMWSLGCIMAELYTG---YPLFPGEN----EVEQLACIMEVlglppahftqtasrrqvffDSKGLPkninnnrggkryp 189
Cdd:cd06619   174 SDVWSLGISFMELALGrfpYPQIQKNQgslmPLQLLQCIVDE-------------------DPPVLP------------- 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907169597 190 dskdltmvVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06619   222 --------VGQFSEKFVHFITQCMRKQPKERPAPENLMDHPFI 256
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
30-176 1.23e-14

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: 72.77  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  30 SFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSS------CYEHQKVYTYIQSRFYR 103
Cdd:cd06652    99 SYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNV--KLGDFGASkrlqtiCLSGTGMKSVTGTPYWM 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 104 SPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPgenEVEQLACIMEVLGLP-----PAHFTQTASR--RQVFFDSKGLP 176
Cdd:cd06652   177 SPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKIATQPtnpqlPAHVSDHCRDflKRIFVEAKLRP 253
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
51-232 2.26e-14

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: 71.85  E-value: 2.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  51 HMlYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSSCY--EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAE 128
Cdd:cd14114   115 HM-HENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHldPKESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYV 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 129 LYTGYPLFPGENEVEQLacimevlglppahftQTASRRQVFFDSKGLpKNINnnrggkryPDSKdltmvvktydssflDF 208
Cdd:cd14114   194 LLSGLSPFAGENDDETL---------------RNVKSCDWNFDDSAF-SGIS--------EEAK--------------DF 235
                         170       180
                  ....*....|....*....|....
gi 1907169597 209 LRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14114   236 IRKLLLADPNKRMTIHQALEHPWL 259
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
3-232 2.29e-14

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 71.87  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSFHGFNLSIVRrFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVI 81
Cdd:cd14193    68 DAFESRNDIVLVMEYVdGGELFDRIIDENYNLTELDTIL-FIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKII 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  82 DFG-SSCYE-HQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglppahf 159
Cdd:cd14193   147 DFGlARRYKpREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILAC-------- 218
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 160 tqtasrrQVFFDSKglpkninnnrggkrypDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14193   219 -------QWDFEDE----------------EFADISEEAK-------DFISKLLIKEKSWRMSASEALKHPWL 261
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
10-136 2.52e-14

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: 71.95  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  10 HLCITFELL-GINLYELMKnnSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSS-- 86
Cdd:cd13994    72 KWCLVMEYCpGGDLFTLIE--KADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG--VLKLTDFGTAev 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597  87 ---CYEHQKVYTY--IQSRFYRSPEVILGHPYN-MAIDMWSLGCIMAELYTGYPLF 136
Cdd:cd13994   148 fgmPAEKESPMSAglCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPW 203
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
40-147 2.59e-14

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: 71.65  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG-SSCYEHQKVY-TYIQSRFYRSPEVILGHPYN-MA 116
Cdd:cd14073   104 RRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNG--NAKIADFGlSNLYSKDKLLqTFCGSPLYASPEIVNGTPYQgPE 181
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907169597 117 IDMWSLGCIMAELYTGYPLFPGENE---VEQLAC 147
Cdd:cd14073   182 VDCWSLGVLLYTLVYGTMPFDGSDFkrlVKQISS 215
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
41-232 2.65e-14

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: 71.96  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  41 RFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVT--VKVIDFG-----SSCYEHQKVYTYIQsrfYRSPEVILGHPY 113
Cdd:cd14195   112 QFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNprIKLIDFGiahkiEAGNEFKNIFGTPE---FVAPEIVNYEPL 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 114 NMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglppahftqtasrrqvffdskglpkniNNNRGGKRYPDSKD 193
Cdd:cd14195   189 GLEADMWSIGVITYILLSGASPFLGETKQETLTNISAV----------------------------NYDFDEEYFSNTSE 240
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907169597 194 LTMvvktydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14195   241 LAK----------DFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
48-231 2.68e-14

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 71.90  E-value: 2.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  48 KCLHMLYVEKIIHCDLKPENIvLYQR---GQVTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGC 124
Cdd:cd14185   109 EALVYIHSKHIVHRDLKPENL-LVQHnpdKSTTLKLADFGLAKYVTGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 125 IMAELYTGYPLFPG-ENEVEQLACIMEvLG----LPPahftqtasrrqvFFDskglpkNINNnrggkrypDSKDLtmvvk 199
Cdd:cd14185   188 ILYILLCGFPPFRSpERDQEELFQIIQ-LGhyefLPP------------YWD------NISE--------AAKDL----- 235
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907169597 200 tydssfldfLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14185   236 ---------ISRLLVVDPEKRYTAKQVLQHPW 258
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
5-156 2.96e-14

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: 72.01  E-value: 2.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FY---FRNHLC-ITFELLGI---NLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVLYQRGqv 76
Cdd:cd06616    70 FYgalFREGDCwICMELMDIsldKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNG-- 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  77 TVKVIDFGSScyeHQKVYTYIQS-----RFYRSPEVIL----GHPYNMAIDMWSLGCIMAELYTG-YPlFPGENEV-EQL 145
Cdd:cd06616   148 NIKLCDFGIS---GQLVDSIAKTrdagcRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGkFP-YPKWNSVfDQL 223
                         170
                  ....*....|.
gi 1907169597 146 AciMEVLGLPP 156
Cdd:cd06616   224 T--QVVKGDPP 232
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
45-231 3.04e-14

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: 71.93  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY--EHQKVYTYIQSRFYRSPEVIL-----GHP-YNMA 116
Cdd:cd14181   124 SLLEAVSYLHANNIVHRDLKPENILLDDQLHI--KLSDFGFSCHlePGEKLRELCGTPGYLAPEILKcsmdeTHPgYGKE 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 117 IDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEvlglppahftqtaSRRQvfFDSkglpkninnnrggkryPDSKDLTM 196
Cdd:cd14181   202 VDLWACGVILFTLLAGSPPFWHRRQMLMLRMIME-------------GRYQ--FSS----------------PEWDDRSS 250
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907169597 197 VVKtydssflDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14181   251 TVK-------DLISRLLVVDPEIRLTAEQALQHPF 278
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
59-231 3.91e-14

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: 72.32  E-value: 3.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  59 IHCDLKPENIVLYQRGQVtvKVIDFGSS----------CYEHQKVYTYIQSRF----------------------YRSPE 106
Cdd:cd05573   123 IHRDIKPDNILLDADGHI--KLADFGLCtkmnksgdreSYLNDSVNTLFQDNVlarrrphkqrrvraysavgtpdYIAPE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 107 VILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEqlacimevlglppahftqTASRrqvffdskglpknINNNRGGK 186
Cdd:cd05573   201 VLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVE------------------TYSK-------------IMNWKESL 249
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907169597 187 RYPDSKDltmvvktYDSSFLDFLRRCLVwEPSLRMTP-EQALKHAW 231
Cdd:cd05573   250 VFPDDPD-------VSPEAIDLIRRLLC-DPEDRLGSaEEIKAHPF 287
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
40-232 5.68e-14

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


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 70.67  E-value: 5.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSS--CYEHQKVY---TYIQSRFYRSPEVILGHPYN 114
Cdd:cd14080   105 RIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNN--NVKLSDFGFArlCPDDDGDVlskTFCGSAAYAAPEILQGIPYD 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 115 -MAIDMWSLGCImaeLYtgyplfpgeneveqlacIMEVLGLPpahftqtasrrqvfFDSKGLPKNINN--NRGGKRYPDS 191
Cdd:cd14080   183 pKKYDIWSLGVI---LY-----------------IMLCGSMP--------------FDDSNIKKMLKDqqNRKVRFPSSV 228
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907169597 192 KDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14080   229 KKLSPECK-------DLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
59-156 8.20e-14

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: 71.11  E-value: 8.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  59 IHCDLKPENIVLYQRGQVtvKVIDFGSSCYEH--QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLF 136
Cdd:cd05599   123 IHRDIKPDNLLLDARGHI--KLSDFGLCTGLKksHLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPF 200
                          90       100
                  ....*....|....*....|...
gi 1907169597 137 PGENEVEQLACIM---EVLGLPP 156
Cdd:cd05599   201 CSDDPQETCRKIMnwrETLVFPP 223
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
38-232 8.55e-14

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: 71.24  E-value: 8.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  38 IVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVLYQRGQVtvKVIDFG-SSCYEHQKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd06650   104 ILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEI--KLCDFGvSGQLIDSMANSFVGTRSYMSPERLQGTHYSV 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 116 AIDMWSLGCIMAELYTG-YPLFPGENEVEQLACIMEVLGLPPAhfTQTASRrqvffdSKGLPkninnnrGGKRYPDSKDL 194
Cdd:cd06650   182 QSDIWSMGLSLVEMAVGrYPIPPPDAKELELMFGCQVEGDAAE--TPPRPR------TPGRP-------LSSYGMDSRPP 246
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907169597 195 TMVVKTYD----------------SSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06650   247 MAIFELLDyivnepppklpsgvfsLEFQDFVNKCLIKNPAERADLKQLMVHAFI 300
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
38-140 8.95e-14

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: 70.15  E-value: 8.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  38 IVRRFTfSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtVKVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd08220   103 ILHFFV-QILLALHHVHSKQILHRDLKTQNILLNKKRTV-VKIGDFGISkiLSSKSKAYTVVGTPCYISPELCEGKPYNQ 180
                          90       100
                  ....*....|....*....|....*
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLFPGEN 140
Cdd:cd08220   181 KSDIWALGCVLYELASLKRAFEAAN 205
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
39-225 9.23e-14

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: 70.55  E-value: 9.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTV-KVIDFG--------SSCYEhqkvytYIQSRFYRSPEVIL 109
Cdd:cd13989   104 VRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIyKLIDLGyakeldqgSLCTS------FVGTLQYLAPELFE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 110 GHPYNMAIDMWSLGCIMAELYTGY-PLFPGENEVEQLaciMEVLGLPPAHFTQTASRRQVFFDSKGLPKninnnrggkry 188
Cdd:cd13989   178 SKKYTCTVDYWSFGTLAFECITGYrPFLPNWQPVQWH---GKVKQKKPEHICAYEDLTGEVKFSSELPS----------- 243
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 189 PDSkdLTMVVKTYdssFLDFLRRCLVWEPSLRMTPEQ 225
Cdd:cd13989   244 PNH--LSSILKEY---LESWLQLMLRWDPRQRGGGPQ 275
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
50-155 9.56e-14

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: 70.89  E-value: 9.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIM 126
Cdd:cd05582   110 LDHLHSLGIIYRDLKPENILLDEDGHI--KLTDFGlskESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLM 187
                          90       100       110
                  ....*....|....*....|....*....|
gi 1907169597 127 AELYTGYPLFPGENEVEQLACIMEV-LGLP 155
Cdd:cd05582   188 FEMLTGSLPFQGKDRKETMTMILKAkLGMP 217
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
46-232 1.10e-13

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: 70.53  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQ-VTVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWS 121
Cdd:cd14086   109 ILESVNHCHQNGIVHRDLKPENLLLASKSKgAAVKLADFGLAIEvqgDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWA 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 122 LGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTASrrqvffdskglpkninnnrggkryPDSKDLtmvvkty 201
Cdd:cd14086   189 CGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVT------------------------PEAKDL------- 237
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907169597 202 dssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14086   238 -------INQMLTVNPAKRITAAEALKHPWI 261
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
50-232 1.15e-13

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: 69.72  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCY-EHQKVYTYIQSRFYRSPEVILGHPY-NMAIDMWSLGCIma 127
Cdd:cd14004   122 VKHLHDQGIVHRDIKDENVILDGNG--TIKLIDFGSAAYiKSGPFDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVL-- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 128 eLYTgypLFPGENEVEQLACIMEVLGLPPahftqtasrrqvffdskglpkninnnrggkrYPDSKDLtmvvktydssfLD 207
Cdd:cd14004   198 -LYT---LVFKENPFYNIEEILEADLRIP-------------------------------YAVSEDL-----------ID 231
                         170       180
                  ....*....|....*....|....*
gi 1907169597 208 FLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14004   232 LISRMLNRDVGDRPTIEELLTDPWL 256
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
34-140 1.26e-13

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: 70.30  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPY 113
Cdd:cd05580    98 FPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHI--KITDFGFAKRVKDRTYTLCGTPEYLAPEIILSKGH 175
                          90       100
                  ....*....|....*....|....*..
gi 1907169597 114 NMAIDMWSLGCIMAELYTGYPLFPGEN 140
Cdd:cd05580   176 GKAVDWWALGILIYEMLAGYPPFFDEN 202
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
1-232 1.43e-13

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: 69.50  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvK 79
Cdd:cd14099    66 FHDCFEDEENVYILLELCsNGSLMELLKRR--KALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNV--K 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  80 VIDFGSSC---YEHQKVYTYIQSRFYRSPEVIL---GHPYNmaIDMWSLGCIMAELYTGYPLFpgeneveqlacimevlg 153
Cdd:cd14099   142 IGDFGLAArleYDGERKKTLCGTPNYIAPEVLEkkkGHSFE--VDIWSLGVILYTLLVGKPPF----------------- 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 154 lppahftQTASRRQVFfdskglpKNINNNRggKRYPDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14099   203 -------ETSDVKETY-------KRIKKNE--YSFPSHLSISDEAK-------DLIRSMLQPDPTKRPSLDEILSHPFF 258
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
22-142 1.72e-13

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 69.50  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  22 LYELMKNNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENiVLYQRGQVTVKVIDFG-------SSCYEHQKVY 94
Cdd:PHA03390   96 LFDLLKKE--GKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLEN-VLYDRAKDRIYLCDYGlckiigtPSCYDGTLDY 172
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907169597  95 tyiqsrFyrSPEVILGHPYNMAIDMWSLGCIMAELYTG-YPLFPGENEV 142
Cdd:PHA03390  173 ------F--SPEKIKGHNYDVSFDWWAVGVLTYELLTGkHPFKEDEDEE 213
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1-232 1.77e-13

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: 70.08  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNSFHGFN--LSIVRRftfsILKCLHMLYVEKIIHCDLKPENIVLY-QRGQV 76
Cdd:cd14168    73 LEDIYESPNHLYLVMQLVsGGELFDRIVEKGFYTEKdaSTLIRQ----VLDAVYYLHRMGIVHRDLKPENLLYFsQDEES 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  77 TVKVIDFGSSCYEHQK--VYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMevlgl 154
Cdd:cd14168   149 KIMISDFGLSKMEGKGdvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIL----- 223
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597 155 ppahftqtasRRQVFFDSkglpkninnnrggkryPDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14168   224 ----------KADYEFDS----------------PYWDDISDSAK-------DFIRNLMEKDPNKRYTCEQALRHPWI 268
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
9-140 2.25e-13

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: 69.39  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELL-GINLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSC 87
Cdd:cd05612    74 RFLYMLMEYVpGGELFSYLRNSG--RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHI--KLTDFGFAK 149
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907169597  88 YEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGEN 140
Cdd:cd05612   150 KLRDRTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDN 202
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
37-231 2.44e-13

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: 68.85  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRrftfSILKCLHMLYVEKIIHCDLKPENIVLYQRG-QVTVKVIDFGSSCYEHQKV------YTyiqsRFYRSPEVIL 109
Cdd:cd14089   104 EIMR----QIGSAVAHLHSMNIAHRDLKPENLLYSSKGpNAILKLTDFGFAKETTTKKslqtpcYT----PYYVAPEVLG 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 110 GHPYNMAIDMWSLGCIMAELYTGYPLFPGENeveqlacimevlGLPPahftqtasrrqvffdSKGLPKNINNnrGGKRYP 189
Cdd:cd14089   176 PEKYDKSCDMWSLGVIMYILLCGYPPFYSNH------------GLAI---------------SPGMKKRIRN--GQYEFP 226
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907169597 190 DS--KDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14089   227 NPewSNVSEEAK-------DLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
5-149 3.95e-13

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: 68.95  E-value: 3.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELLgiNLYELMKN-NSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDF 83
Cdd:cd05592    65 FQTESHLFFVMEYL--NGGDLMFHiQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHI--KIADF 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597  84 G---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIM 149
Cdd:cd05592   141 GmckENIYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSIC 209
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-232 4.48e-13

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: 68.66  E-value: 4.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELL-GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMlyvEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYE 89
Cdd:cd06917    77 LWIIMDYCeGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHK---DGIIHRDIKAANILVTNTGNV--KLCDFGVAASL 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  90 HQ---KVYTYIQSRFYRSPEVIL-GHPYNMAIDMWSLGCIMAELYTGYPLFPGEneveqlacimevlglpPAHftqtasr 165
Cdd:cd06917   152 NQnssKRSTFVGTPYWMAPEVITeGKYYDTKADIWSLGITTYEMATGNPPYSDV----------------DAL------- 208
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597 166 RQVFFDSKGLPKNINNNrggkrypdskdltmvvkTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06917   209 RAVMLIPKSKPPRLEGN-----------------GYSPLLKEFVAACLDEEPKDRLSADELLKSKWI 258
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
8-229 4.53e-13

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: 68.39  E-value: 4.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrGQvtVKVIDFGSSc 87
Cdd:cd14131    74 DDYLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GR--LKLIDFGIA- 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  88 yehqkvyTYIQS------RF-------YRSPEVILGHPYNMAI----------DMWSLGCIMAELYTGYPLFpgeneveq 144
Cdd:cd14131   150 -------KAIQNdttsivRDsqvgtlnYMSPEAIKDTSASGEGkpkskigrpsDVWSLGCILYQMVYGKTPF-------- 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 145 lacimevlglppAHFTQTASRRQVffdskglpknINNNRGGKRYPD--SKDLtmvvktydssfLDFLRRCLVWEPSLRMT 222
Cdd:cd14131   215 ------------QHITNPIAKLQA----------IIDPNHEIEFPDipNPDL-----------IDVMKRCLQRDPKKRPS 261

                  ....*..
gi 1907169597 223 PEQALKH 229
Cdd:cd14131   262 IPELLNH 268
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
40-140 5.02e-13

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


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 68.06  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEHQKVY--TYIQSRFYRSPEVILGHPY-NMA 116
Cdd:cd14161   105 RHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN--IKIADFGLSNLYNQDKFlqTYCGSPLYASPEIVNGRPYiGPE 182
                          90       100
                  ....*....|....*....|....
gi 1907169597 117 IDMWSLGCIMAELYTGYPLFPGEN 140
Cdd:cd14161   183 VDSWSLGVLLYILVHGTMPFDGHD 206
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
47-193 5.26e-13

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: 68.58  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMLyveKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIM 126
Cdd:cd14209   114 FEYLHSL---DLIYRDLKPENLLIDQQGYI--KVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLI 188
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597 127 AELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQtasrrqvffDSKGLPKNINNNRGGKRYPDSKD 193
Cdd:cd14209   189 YEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSS---------DLKDLLRNLLQVDLTKRFGNLKN 246
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
36-231 5.28e-13

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: 68.12  E-value: 5.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  36 LSIVRRFT-----------FSILKCLHMLyveKIIHCDLKPEN--IVLYQRGQVTVKVIDFGSSCYEHQKVYTYIQSRFY 102
Cdd:cd14095    89 ITSSTKFTerdasrmvtdlAQALKYLHSL---SIVHRDIKPENllVVEHEDGSKSLKLADFGLATEVKEPLFTVCGTPTY 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 103 RSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLF--PGENEVEQLACIM--EVLGLPPahftqtasrrqvFFDskglpkN 178
Cdd:cd14095   166 VAPEILAETGYGLKVDIWAAGVITYILLCGFPPFrsPDRDQEELFDLILagEFEFLSP------------YWD------N 227
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 179 INnnrggkryPDSKDLtmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14095   228 IS--------DSAKDL--------------ISRMLVVDPEKRYSAGQVLDHPW 258
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
3-240 5.92e-13

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: 68.13  E-value: 5.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVID 82
Cdd:cd06643    69 DAFYYENNLWILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGD--IKLAD 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FGSSCYEH---QKVYTYIQSRFYRSPEVIL-----GHPYNMAIDMWSLGCIMAELYTgypLFPGENEVEQLACIMEVLGL 154
Cdd:cd06643   147 FGVSAKNTrtlQRRDSFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQ---IEPPHHELNPMRVLLKIAKS 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 155 PPAHFTQTASrrqvffdskglpkninnnrggkrypdskdltmvvktYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHE 234
Cdd:cd06643   224 EPPTLAQPSR------------------------------------WSPEFKDFLRKCLEKNVDARWTTSQLLQHPFVSV 267

                  ....*.
gi 1907169597 235 PRKFKP 240
Cdd:cd06643   268 LVSNKP 273
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
40-231 6.12e-13

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 67.65  E-value: 6.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVL-YQRGQVtvKVIDFGSSCYEHQKVYT-YIQSRFYRSPEVILGHPYN-MA 116
Cdd:cd14005   110 RIIFRQVVEAVRHCHQRGVLHRDIKDENLLInLRTGEV--KLIDFGCGALLKDSVYTdFDGTRVYSPPEWIRHGRYHgRP 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 117 IDMWSLGCIMAELYTGYplFPGENEVEQLacimevlglppahftqtasRRQVFFdskglpkninnnrggkRYPDSKDLtm 196
Cdd:cd14005   188 ATVWSLGILLYDMLCGD--IPFENDEQIL-------------------RGNVLF----------------RPRLSKEC-- 228
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907169597 197 vvktydssfLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14005   229 ---------CDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
40-234 6.13e-13

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 68.02  E-value: 6.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFGSSC--YEHQKVYTYIQSRFYRSPEVIL-----GHP 112
Cdd:cd14182   113 RKIMRALLEVICALHKLNIVHRDLKPENILL--DDDMNIKLTDFGFSCqlDPGEKLREVCGTPGYLAPEIIEcsmddNHP 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 113 -YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEvlglPPAHFTQtasrrqvffdskglpkninnnrggkryPDS 191
Cdd:cd14182   191 gYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMS----GNYQFGS---------------------------PEW 239
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907169597 192 KDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWIHE 234
Cdd:cd14182   240 DDRSDTVK-------DLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
11-140 6.51e-13

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: 67.58  E-value: 6.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELLGINLYELMKNNsfHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvTVKVIDFGSSCYEH 90
Cdd:cd14164    76 LYIVMEAAATDLLQKIQEV--HHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDR-KIKIADFGFARFVE 152
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907169597  91 ---QKVYTYIQSRFYRSPEVILGHPYN-MAIDMWSLGCIMAELYTGYPLFPGEN 140
Cdd:cd14164   153 dypELSTTFCGSRAYTPPEVILGTPYDpKKYDVWSLGVVLYVMVTGTMPFDETN 206
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
37-176 8.54e-13

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: 67.80  E-value: 8.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSS------CYEHQKVYTYIQSRFYRSPEVILG 110
Cdd:cd06651   111 SVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNV--KLGDFGASkrlqtiCMSGTGIRSVTGTPYWMSPEVISG 188
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 111 HPYNMAIDMWSLGCIMAELYTGYPLFPgenEVEQLACIMEVLGLP-----PAHFTQTASR--RQVFFDSKGLP 176
Cdd:cd06651   189 EGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPtnpqlPSHISEHARDflGCIFVEARHRP 258
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
31-229 8.98e-13

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: 67.25  E-value: 8.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  31 FHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIvLYQRGQVTVKVIDFG---SSCYEHQKVYTYIQSRFYRSPEV 107
Cdd:cd14019    95 YRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNF-LYNRETGKGVLVDFGlaqREEDRPEQRAPRAGTRGFRAPEV 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 108 ILGHPY-NMAIDMWSLGCIMAELYTG-YPLFPGENEVEQLACIMEVLGlppahftqtasrrqvffdskglpkninnnrgg 185
Cdd:cd14019   174 LFKCPHqTTAIDIWSAGVILLSILSGrFPFFFSSDDIDALAEIATIFG-------------------------------- 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907169597 186 krypdskdltmvvktyDSSFLDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd14019   222 ----------------SDEAYDLLDKLLELDPSKRITAEEALKH 249
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
19-232 9.68e-13

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: 67.25  E-value: 9.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  19 GINLYELMKNNSFHgfnLSIVRRFTFSILKCLHMLYVEK--IIHCDLKPENIVLYQRGQVTVKVIDFG-SSCYE-HQKVY 94
Cdd:cd14190    85 GGELFERIVDEDYH---LTEVDAMVFVRQICEGIQFMHQmrVLHLDLKPENILCVNRTGHQVKIIDFGlARRYNpREKLK 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  95 TYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLacimevlglppahftqtasrrqvffdskg 174
Cdd:cd14190   162 VNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETL----------------------------- 212
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597 175 lpkniNNNRGGKRYPDSKDLTMVvktyDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14190   213 -----NNVLMGNWYFDEETFEHV----SDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
47-150 9.78e-13

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 68.01  E-value: 9.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMlyvEKIIHCDLKPENIVLYQRGQVtvKVIDFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLG 123
Cdd:cd05570   109 LQFLHE---RGIIYRDLKLDNVLLDAEGHI--KIADFGmckEGIWGGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALG 183
                          90       100
                  ....*....|....*....|....*..
gi 1907169597 124 CIMAELYTGYPLFPGENEVEQLACIME 150
Cdd:cd05570   184 VLLYEMLAGQSPFEGDDEDELFEAILN 210
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
5-140 1.05e-12

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: 67.98  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELLGINLYELMKNNSFHG-FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVkvIDF 83
Cdd:cd05585    61 FSFQSPEKLYLVLAFINGGELFHHLQREGrFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIAL--CDF 138
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  84 GS---SCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGEN 140
Cdd:cd05585   139 GLcklNMKDDDKTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDEN 198
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
34-141 1.10e-12

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: 67.03  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSI---LKCLHMLyveKIIHCDLKPENIVLYQRGQVtvKVIDFGSS----CYEHQKVYTYIQSRFYRSPE 106
Cdd:cd05583    96 FTESEVRIYIGEIvlaLEHLHKL---GIIYRDIKLENILLDSEGHV--VLTDFGLSkeflPGENDRAYSFCGTIEYMAPE 170
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907169597 107 VILGHP--YNMAIDMWSLGCIMAELYTGYPLFPGENE 141
Cdd:cd05583   171 VVRGGSdgHDKAVDWWSLGVLTYELLTGASPFTVDGE 207
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
2-242 1.25e-12

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: 67.37  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   2 KDFFYFRNHLCITFELL-GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIvLY--QRGQVTV 78
Cdd:cd14170    65 ENLYAGRKCLLIVMECLdGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENL-LYtsKRPNAIL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFG--SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEveqlacimevlglpp 156
Cdd:cd14170   144 KLTDFGfaKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHG--------------- 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 157 ahftqtasrrqvFFDSKGLPKNINNNRGGKRYPDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWIHEPR 236
Cdd:cd14170   209 ------------LAISPGMKTRIRMGQYEFPNPEWSEVSEEVK-------MLIRNLLKTEPTQRMTITEFMNHPWIMQST 269

                  ....*.
gi 1907169597 237 KFKPRP 242
Cdd:cd14170   270 KVPQTP 275
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
37-232 1.25e-12

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 66.80  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRgQVTVKVIDFGSSCYEHQKVYT-YIQSRFYRSPEVILGHPYN- 114
Cdd:cd14101   108 SLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLR-TGDIKLIDFGSGATLKDSMYTdFDGTRVYSPPEWILYHQYHa 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 115 MAIDMWSLGCIMAELYTGYplFPGENEVEQLACIMEVlglpPAHFTqtasrrqvffdskglpkninnnrggkryPDSKDL 194
Cdd:cd14101   187 LPATVWSLGILLYDMVCGD--IPFERDTDILKAKPSF----NKRVS----------------------------NDCRSL 232
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907169597 195 tmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14101   233 --------------IRSCLAYNPSDRPSLEQILLHPWM 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
3-165 1.38e-12

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: 66.67  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVI 81
Cdd:cd08529    66 DSFVDKGKLNIVMEYAeNGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNV--KIG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  82 DFG-SSCYEHQKVY--TYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLP-PA 157
Cdd:cd08529   144 DLGvAKILSDTTNFaqTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPiSA 223

                  ....*...
gi 1907169597 158 HFTQTASR 165
Cdd:cd08529   224 SYSQDLSQ 231
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
50-140 1.51e-12

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: 67.75  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLyveKIIHCDLKPENIVLYQRGQVtvKVIDFGSSC----------------------------------------YE 89
Cdd:cd05600   127 LHQL---GYIHRDLKPENFLIDSSGHI--KLTDFGLASgtlspkkiesmkirleevkntafleltakerrniyramrkED 201
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907169597  90 HQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGEN 140
Cdd:cd05600   202 QNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGST 252
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
39-144 1.53e-12

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: 66.92  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQR-GQVTVKVIDFG------SSCYEHQkvytYIQSRFYRSPEVILGH 111
Cdd:cd14113   105 IRFYLREILEALQYLHNCRIAHLDLKPENILVDQSlSKPTIKLADFGdavqlnTTYYIHQ----LLGSPEFAAPEIILGN 180
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907169597 112 PYNMAIDMWSLGCIMAELYTGYPLFPGENeVEQ 144
Cdd:cd14113   181 PVSLTSDLWSIGVLTYVLLSGVSPFLDES-VEE 212
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
5-148 1.92e-12

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 67.26  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELLgiNLYELMKN-NSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDF 83
Cdd:cd05619    75 FQTKENLFFVMEYL--NGGDLMFHiQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHI--KIADF 150
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597  84 GSsCYEH----QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACI 148
Cdd:cd05619   151 GM-CKENmlgdAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI 218
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
37-176 2.04e-12

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: 66.59  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSS------CYEHQKVYTYIQSRFYRSPEVILG 110
Cdd:cd06653   106 NVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNV--KLGDFGASkriqtiCMSGTGIKSVTGTPYWMSPEVISG 183
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 111 HPYNMAIDMWSLGCIMAELYTGYPLFPgenEVEQLACIMEVLG------LPPAhfTQTASR---RQVFFDSKGLP 176
Cdd:cd06653   184 EGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKIATqptkpqLPDG--VSDACRdflRQIFVEEKRRP 253
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
50-150 2.07e-12

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: 67.03  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEH----QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05587   110 LFFLHSKGIIYRDLKLDNVMLDAEGHI--KIADFGM-CKEGifggKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVL 186
                          90       100
                  ....*....|....*....|....*
gi 1907169597 126 MAELYTGYPLFPGENEVEQLACIME 150
Cdd:cd05587   187 LYEMLAGQPPFDGEDEDELFQSIME 211
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
45-144 2.09e-12

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 66.21  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLYvekIIHCDLKPENIVL--YQRGQVTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd14184   110 SALKYLHGLC---IVHRDIKPENLLVceYPDGTKSLKLGDFGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAA 186
                          90       100
                  ....*....|....*....|..
gi 1907169597 123 GCIMAELYTGYPLFPGENEVEQ 144
Cdd:cd14184   187 GVITYILLCGFPPFRSENNLQE 208
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
47-126 2.09e-12

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: 66.28  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMlyvEKIIHCDLKPENIVLYQRGQV-TVKVIDFGSSCYEHQKVY--TYIQSRFYRSPEVILGHPYNMAIDMWSLG 123
Cdd:cd14082   116 LRYLHS---KNIVHCDLKPENVLLASAEPFpQVKLCDFGFARIIGEKSFrrSVVGTPAYLAPEVLRNKGYNRSLDMWSVG 192

                  ...
gi 1907169597 124 CIM 126
Cdd:cd14082   193 VII 195
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
39-136 2.39e-12

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: 66.19  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVL-YQRGQ------VTVKVIDFGSSCYEHQKVY--TYIQSRFYRSPEVIL 109
Cdd:cd14202   103 IRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsYSGGRksnpnnIRIKIADFGFARYLQNNMMaaTLCGSPMYMAPEVIM 182
                          90       100
                  ....*....|....*....|....*..
gi 1907169597 110 GHPYNMAIDMWSLGCIMAELYTGYPLF 136
Cdd:cd14202   183 SQHYDAKADLWSIGTIIYQCLTGKAPF 209
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
36-169 2.93e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 66.94  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  36 LSIVRrftfSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKviDFGSSCY----EHQKVYTYIQSRFYRSPEVILGH 111
Cdd:PHA03212  185 LAIER----SVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLG--DFGAACFpvdiNANKYYGWAGTIATNAPELLARD 258
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597 112 PYNMAIDMWSLGCIMAELYTGY-PLFP-----GENEVE-QLACIMEVLGLPPAHF--TQTASRRQVF 169
Cdd:PHA03212  259 PYGPAVDIWSAGIVLFEMATCHdSLFEkdgldGDCDSDrQIKLIIRRSGTHPNEFpiDAQANLDEIY 325
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
50-159 4.30e-12

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: 65.36  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVTvKVIDFGSSCYEHQKV---YTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIM 126
Cdd:cd08225   114 LKHIHDRKILHRDIKSQNIFLSKNGMVA-KLGDFGIARQLNDSMelaYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVL 192
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907169597 127 AELYTGYPLFPGeNEVEQLacimeVLGLPPAHF 159
Cdd:cd08225   193 YELCTLKHPFEG-NNLHQL-----VLKICQGYF 219
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
34-230 4.46e-12

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: 65.53  E-value: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtVKVIDFGSSCYEHQKVYTY--IQSRF-----YRSPE 106
Cdd:cd06630   100 FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQR-LRIADFGAAARLASKGTGAgeFQGQLlgtiaFMAPE 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 107 VILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglppAHFTQTASrrqvffdskgLPKNINnnrggk 186
Cdd:cd06630   179 VLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKI-----ASATTPPP----------IPEHLS------ 237
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907169597 187 ryPDSKDLTMvvktydssfldflrRCLVWEPSLRMTPEQALKHA 230
Cdd:cd06630   238 --PGLRDVTL--------------RCLELQPEDRPPARELLKHP 265
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
53-136 5.10e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 65.99  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  53 LYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTG 132
Cdd:PTZ00263  134 LHSKDIIYRDLKPENLLLDNKGHV--KVTDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAG 211

                  ....
gi 1907169597 133 YPLF 136
Cdd:PTZ00263  212 YPPF 215
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
31-141 6.68e-12

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: 65.07  E-value: 6.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  31 FH-------GFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY--EHQKVYTYIQSRF 101
Cdd:cd05605    89 FHiynmgnpGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHV--RISDLGLAVEipEGETIRGRVGTVG 166
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907169597 102 YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENE 141
Cdd:cd05605   167 YMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKE 206
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
47-232 8.24e-12

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: 64.48  E-value: 8.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMLyveKIIHCDLKPENIVLYQRG-QVTVKVIDFGSSCY----EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWS 121
Cdd:cd14087   110 VKYLHGL---GITHRDLKPENLLYYHPGpDSKIMITDFGLASTrkkgPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWA 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 122 LGCIMAELYTGYPLFPGENEVEQlacimevlglppahFTQTASRRQVFFdskglpkninnnrgGKRYPDSKDLTMvvkty 201
Cdd:cd14087   187 VGVIAYILLSGTMPFDDDNRTRL--------------YRQILRAKYSYS--------------GEPWPSVSNLAK----- 233
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907169597 202 dssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14087   234 -----DFIDRLLTVNPGERLSATQALKHPWI 259
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
11-232 9.30e-12

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: 64.69  E-value: 9.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELLGI-NLYELMKNNSFHGFNLSIVRRftfSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY- 88
Cdd:cd06640    77 LWIIMEYLGGgSALDLLRAGPFDEFQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLLSEQGDV--KLADFGVAGQl 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  89 --EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYplfPGENEVEQLACIMEVLGLPPAHFTQTASRr 166
Cdd:cd06640   152 tdTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGE---PPNSDMHPMRVLFLIPKNNPPTLVGDFSK- 227
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 167 qvffdskglpkninnnrggkrypdskdltmvvktydsSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06640   228 -------------------------------------PFKEFIDACLNKDPSFRPTAKELLKHKFI 256
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
9-232 9.95e-12

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 64.64  E-value: 9.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELLGI-NLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSC 87
Cdd:cd06636    92 DQLWLVMEFCGAgSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE--VKLVDFGVSA 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  88 YEHQKV---YTYIQSRFYRSPEVIL-----GHPYNMAIDMWSLGCIMAELYTGYPLFpgeneveqlaCIMEVLglppahf 159
Cdd:cd06636   170 QLDRTVgrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL----------CDMHPM------- 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 160 tqtasrRQVFFdskgLPKNinnnrggkryPDSKdltMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06636   233 ------RALFL----IPRN----------PPPK---LKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
45-144 1.07e-11

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: 64.25  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLyveKIIHCDLKPENIVLY--QRGQVTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd14183   115 SAIKYLHSL---NIVHRDIKPENLLVYehQDGSKSLKLGDFGLATVVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAA 191
                          90       100
                  ....*....|....*....|..
gi 1907169597 123 GCIMAELYTGYPLFPGENEVEQ 144
Cdd:cd14183   192 GVITYILLCGFPPFRGSGDDQE 213
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
51-140 1.07e-11

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 64.21  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  51 HMlYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCY-------EHQKVYTyiqsRFYRSPEVILGHPYNMAIDMWSLG 123
Cdd:cd08224   119 HM-HSKRIMHRDIKPANVFITANG--VVKLGDLGLGRFfsskttaAHSLVGT----PYYMSPERIREQGYDFKSDIWSLG 191
                          90
                  ....*....|....*..
gi 1907169597 124 CIMAELYTGYPLFPGEN 140
Cdd:cd08224   192 CLLYEMAALQSPFYGEK 208
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
50-150 1.13e-11

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 65.02  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEHQ----KVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05616   114 LFFLQSKGIIYRDLKLDNVMLDSEGHI--KIADFGM-CKENIwdgvTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVL 190
                          90       100
                  ....*....|....*....|....*
gi 1907169597 126 MAELYTGYPLFPGENEVEQLACIME 150
Cdd:cd05616   191 LYEMLAGQAPFEGEDEDELFQSIME 215
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
39-136 1.13e-11

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: 64.26  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQ-------VTVKVIDFGSSCYEHQKVY--TYIQSRFYRSPEVIL 109
Cdd:cd14201   107 IRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRkkssvsgIRIKIADFGFARYLQSNMMaaTLCGSPMYMAPEVIM 186
                          90       100
                  ....*....|....*....|....*..
gi 1907169597 110 GHPYNMAIDMWSLGCIMAELYTGYPLF 136
Cdd:cd14201   187 SQHYDAKADLWSIGTVIYQCLVGKPPF 213
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
5-151 1.24e-11

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 64.09  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELL-GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDF 83
Cdd:cd05577    62 FETKDKLCLVLTLMnGGDLKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGH--VRISDL 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597  84 GSSCY--EHQKVYTYIQSRFYRSPEVILGH-PYNMAIDMWSLGCIMAELYTGYPLFPG------ENEVEQLACIMEV 151
Cdd:cd05577   140 GLAVEfkGGKKIKGRVGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQrkekvdKEELKRRTLEMAV 216
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
39-232 1.27e-11

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: 64.17  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVL---YQRGQVtvKVIDFGSScyehQKVYTYIQSRF------YRSPEVIL 109
Cdd:cd14198   112 IIRLIRQILEGVYYLHQNNIVHLDLKPQNILLssiYPLGDI--KIVDFGMS----RKIGHACELREimgtpeYLAPEILN 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 110 GHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVlglppahftQTASRRQVFFDSKGLPKninnnrggkryp 189
Cdd:cd14198   186 YDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQV---------NVDYSEETFSSVSQLAT------------ 244
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907169597 190 dskdltmvvktydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14198   245 -----------------DFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
46-232 1.31e-11

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: 63.79  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd06647   112 CLQALEFLHSNQVIHRDIKSDNILLGMDGSV--KLTDFGFCAQitpEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSL 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 123 GCIMAELYTGYPLFPGENEVEQLACIMevlglppahftqtasrrqvffdSKGLPKninnnrggkrYPDSKDLTmvvktyd 202
Cdd:cd06647   190 GIMAIEMVEGEPPYLNENPLRALYLIA----------------------TNGTPE----------LQNPEKLS------- 230
                         170       180       190
                  ....*....|....*....|....*....|
gi 1907169597 203 SSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06647   231 AIFRDFLNRCLEMDVEKRGSAKELLQHPFL 260
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
38-232 1.34e-11

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: 64.10  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  38 IVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVLYQRGQvtVKVIDFG-SSCYEHQKVYTYIQSRFYRSPEVILGH---- 111
Cdd:cd06622   103 VLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQ--VKLCDFGvSGNLVASLAKTNIGCQSYMAPERIKSGgpnq 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 112 --PYNMAIDMWSLGCIMAELYTG-YPlFPGE---NEVEQLACIMEvlGLPPahftqtasrrqvffdskGLPKNinnnrgg 185
Cdd:cd06622   181 npTYTVQSDVWSLGLSILEMALGrYP-YPPEtyaNIFAQLSAIVD--GDPP-----------------TLPSG------- 233
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907169597 186 krypdskdltmvvktYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06622   234 ---------------YSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
45-232 1.34e-11

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: 64.00  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWS 121
Cdd:cd06648   111 AVLKALSFLHSQGVIHRDIKSDSILLTSDG--RVKLSDFGfcaQVSKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWS 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 122 LGCIMAELYTGYPLFPGENEVEQLacimevlglppahftqtasrrqvffdskglpKNINNNRGgkryPDSKDLTMVvkty 201
Cdd:cd06648   189 LGIMVIEMVDGEPPYFNEPPLQAM-------------------------------KRIRDNEP----PKLKNLHKV---- 229
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907169597 202 DSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06648   230 SPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
50-232 1.41e-11

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: 63.86  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVTV-KVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIM 126
Cdd:cd14172   116 IQYLHSMNIAHRDVKPENLLYTSKEKDAVlKLTDFGFAkeTTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIM 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 127 AELYTGYPLFpgeneveqlacimevlglppahFTQTAsrrQVFfdSKGLPKNINNNRGGKRYPDSKDLTMVVKtydssfl 206
Cdd:cd14172   196 YILLCGFPPF----------------------YSNTG---QAI--SPGMKRRIRMGQYGFPNPEWAEVSEEAK------- 241
                         170       180
                  ....*....|....*....|....*.
gi 1907169597 207 DFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14172   242 QLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
39-136 1.42e-11

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: 63.93  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRG-------QVTVKVIDFGSSCYEHQKVY--TYIQSRFYRSPEVIL 109
Cdd:cd14120    94 IRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspnDIRLKIADFGFARFLQDGMMaaTLCGSPMYMAPEVIM 173
                          90       100
                  ....*....|....*....|....*..
gi 1907169597 110 GHPYNMAIDMWSLGCIMAELYTGYPLF 136
Cdd:cd14120   174 SLQYDAKADLWSIGTIVYQCLTGKAPF 200
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
47-270 1.45e-11

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


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 64.36  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLG 123
Cdd:cd06656   125 LQALDFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFGFCAQitpEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLG 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 124 CIMAELYTGYPLFPGENEVEQLACIMevlglppahftqtasrrqvffdSKGLPKNINNNRggkrypdskdltmvvktYDS 203
Cdd:cd06656   203 IMAIEMVEGEPPYLNENPLRALYLIA----------------------TNGTPELQNPER-----------------LSA 243
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597 204 SFLDFLRRCLVWEPSLRMTPEQALKHAWIHeprkfkprpkpqiLRKPGASISSEISTEKAEEQQASK 270
Cdd:cd06656   244 VFRDFLNRCLEMDVDRRGSAKELLQHPFLK-------------LAKPLSSLTPLIIAAKEAIKNSSR 297
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
50-150 1.75e-11

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: 64.25  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEHQ----KVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05615   124 LFFLHKKGIIYRDLKLDNVMLDSEGHI--KIADFGM-CKEHMvegvTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVL 200
                          90       100
                  ....*....|....*....|....*
gi 1907169597 126 MAELYTGYPLFPGENEVEQLACIME 150
Cdd:cd05615   201 LYEMLAGQPPFDGEDEDELFQSIME 225
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2-131 2.03e-11

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: 63.45  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   2 KDFFYFRNHLCITFELL-GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKV 80
Cdd:cd08219    64 KESFEADGHLYIVMEYCdGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKV--KL 141
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907169597  81 IDFGSS-CYEHQKVY--TYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYT 131
Cdd:cd08219   142 GDFGSArLLTSPGAYacTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCT 195
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
46-234 2.21e-11

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: 63.69  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIvLY--QRGQVTVKVIDFGSSCYEHQKVY--TYIQSRFYRSPEVILGHPYNMAIDMWS 121
Cdd:cd14085   107 ILEAVAYLHENGIVHRDLKPENL-LYatPAPDAPLKIADFGLSKIVDQQVTmkTVCGTPGYCAPEILRGCAYGPEVDMWS 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 122 LGCIMAELYTGYplfpgeneveqlacimevlglppahftqtasrrQVFFDSKG---LPKNINNNRGGKRYPDSKDLTMVV 198
Cdd:cd14085   186 VGVITYILLCGF---------------------------------EPFYDERGdqyMFKRILNCDYDFVSPWWDDVSLNA 232
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907169597 199 KtydssflDFLRRCLVWEPSLRMTPEQALKHAWIHE 234
Cdd:cd14085   233 K-------DLVKKLIVLDPKKRLTTQQALQHPWVTG 261
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
49-131 3.10e-11

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: 62.91  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  49 CLHMLYV--EKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKV---YTYIQSRFYRSPEVILGHPYNMAIDMWSLG 123
Cdd:cd08218   111 CLALKHVhdRKILHRDIKSQNIFLTKDG--IIKLGDFGIARVLNSTVelaRTCIGTPYYLSPEICENKPYNNKSDIWALG 188

                  ....*...
gi 1907169597 124 CIMAELYT 131
Cdd:cd08218   189 CVLYEMCT 196
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
3-240 3.14e-11

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: 63.13  E-value: 3.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVID 82
Cdd:cd06644    76 GAFYWDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD--IKLAD 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FGSSCYEH---QKVYTYIQSRFYRSPEVILGH-----PYNMAIDMWSLGCIMAELytgyplfpgeNEVEqlacimevlgl 154
Cdd:cd06644   154 FGVSAKNVktlQRRDSFIGTPYWMAPEVVMCEtmkdtPYDYKADIWSLGITLIEM----------AQIE----------- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 155 PPAHftQTASRRQVFFDSKGLPKNINNnrggkrypDSKdltmvvktYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHE 234
Cdd:cd06644   213 PPHH--ELNPMRVLLKIAKSEPPTLSQ--------PSK--------WSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSS 274

                  ....*.
gi 1907169597 235 PRKFKP 240
Cdd:cd06644   275 VTSNRP 280
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
22-126 4.24e-11

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: 62.37  E-value: 4.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  22 LYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqVTVKVIDFGSSCYEHQKVYTYIQSRF 101
Cdd:cd13993    92 LFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDE-GTVKLCDFGLATTEKISMDFGVGSEF 170
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907169597 102 YRSPEVI-----LGHPYN-MAIDMWSLGCIM 126
Cdd:cd13993   171 YMAPECFdevgrSLKGYPcAAGDIWSLGIIL 201
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
46-232 5.42e-11

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: 62.38  E-value: 5.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd06642   110 ILKGLDYLHSERKIHRDIKAANVLLSEQGDV--KLADFGVAGQltdTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSL 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 123 GCIMAELYTGYPLFPGENEveqlaciMEVLGLppahftqtasrrqvffdskgLPKNINNNRGGKrypdskdltmvvktYD 202
Cdd:cd06642   188 GITAIELAKGEPPNSDLHP-------MRVLFL--------------------IPKNSPPTLEGQ--------------HS 226
                         170       180       190
                  ....*....|....*....|....*....|
gi 1907169597 203 SSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06642   227 KPFKEFVEACLNKDPRFRPTAKELLKHKFI 256
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
5-148 5.60e-11

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


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 62.65  E-value: 5.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELLgiNLYELMKNNSFHG-FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDF 83
Cdd:cd05620    65 FQTKEHLFFVMEFL--NGGDLMFHIQDKGrFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHI--KIADF 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597  84 G---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACI 148
Cdd:cd05620   141 GmckENVFGDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI 208
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
50-156 6.50e-11

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: 62.19  E-value: 6.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQ-KVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAE 128
Cdd:cd14117   119 LHYCHEKKVIHRDIKPENLLMGYKGEL--KIADFGWSVHAPSlRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYE 196
                          90       100
                  ....*....|....*....|....*....
gi 1907169597 129 LYTGYPLFPGENEVEQLACIMEV-LGLPP 156
Cdd:cd14117   197 LLVGMPPFESASHTETYRRIVKVdLKFPP 225
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
47-232 6.61e-11

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: 62.43  E-value: 6.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLG 123
Cdd:cd06654   126 LQALEFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFGFCAQitpEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLG 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 124 CIMAELYTGYPLFPGENEVEQLACIMevlglppahftqtasrrqvffdSKGLPKNINNNRggkrypdskdltmvvktYDS 203
Cdd:cd06654   204 IMAIEMIEGEPPYLNENPLRALYLIA----------------------TNGTPELQNPEK-----------------LSA 244
                         170       180
                  ....*....|....*....|....*....
gi 1907169597 204 SFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06654   245 IFRDFLNRCLEMDVEKRGSAKELLQHQFL 273
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
3-146 6.71e-11

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: 61.94  E-value: 6.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSFHGFNLSIVRrFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVI 81
Cdd:cd14191    66 DAFEEKANIVMVLEMVsGGELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLI 144
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597  82 DFGSS--CYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLA 146
Cdd:cd14191   145 DFGLArrLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA 211
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
11-241 7.72e-11

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: 62.17  E-value: 7.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELL-GINL-YELMKNNSfHGFNLS--IVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQR-GQVTVKVIDFGS 85
Cdd:cd14094    80 LYMVFEFMdGADLcFEIVKRAD-AGFVYSeaVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKeNSAPVKLGGFGV 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  86 S-------CYEHQKVYTyiqsRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEveqlacimevlglppaH 158
Cdd:cd14094   159 AiqlgesgLVAGGRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE----------------R 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 159 FTQTASRRQVFFDSKGLPkNINNNrggkrypdSKDLtmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWIHEPRKF 238
Cdd:cd14094   219 LFEGIIKGKYKMNPRQWS-HISES--------AKDL--------------VRRMLMLDPAERITVYEALNHPWIKERDRY 275

                  ...
gi 1907169597 239 KPR 241
Cdd:cd14094   276 AYR 278
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
47-148 9.67e-11

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: 61.66  E-value: 9.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLG 123
Cdd:cd06655   125 LQALEFLHANQVIHRDIKSDNVLLGMDG--SVKLTDFGFCAQitpEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLG 202
                          90       100
                  ....*....|....*....|....*
gi 1907169597 124 CIMAELYTGYPLFPGENEVEQLACI 148
Cdd:cd06655   203 IMAIEMVEGEPPYLNENPLRALYLI 227
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
40-162 9.94e-11

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: 61.91  E-value: 9.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKviDFGSsCYE----HQKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd05603    99 RFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLT--DFGL-CKEgmepEETTSTFCGTPEYLAPEVLRKEPYDR 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLFPGENEVEQLACIM-EVLGLPPAHFTQT 162
Cdd:cd05603   176 TVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILhKPLHLPGGKTVAA 223
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
50-141 1.12e-10

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 61.55  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAEL 129
Cdd:cd05631   115 LEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEM 194
                          90
                  ....*....|..
gi 1907169597 130 YTGYPLFPGENE 141
Cdd:cd05631   195 IQGQSPFRKRKE 206
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
34-132 1.19e-10

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: 61.12  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEH--QKVYTYIQSRFYRSPEVILGH 111
Cdd:cd05578    97 FSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGH--VHITDFNIATKLTdgTLATSTSGTKPYMAPEVFMRA 174
                          90       100
                  ....*....|....*....|.
gi 1907169597 112 PYNMAIDMWSLGCIMAELYTG 132
Cdd:cd05578   175 GYSFAVDWWSLGVTAYEMLRG 195
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
19-131 1.21e-10

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 60.91  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  19 GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCY---EHQKVYT 95
Cdd:cd08221    83 GGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKAD--LVKLGDFGISKVldsESSMAES 160
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907169597  96 YIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYT 131
Cdd:cd08221   161 IVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLT 196
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
44-232 1.25e-10

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 61.50  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  44 FSILKCLHMLYVEKIIHCDLKPENIvLY---QRGQVTVKVIDFG-------------SSCYEHQKVytyiqsrfyrSPEV 107
Cdd:cd14091   101 KTLTKTVEYLHSQGVVHRDLKPSNI-LYadeSGDPESLRICDFGfakqlraengllmTPCYTANFV----------APEV 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 108 ILGHPYNMAIDMWSLGCIMAELYTGYPLF---PGENEVEQLACIMEvlglppahftqtaSRrqvfFD-SKGLPKNINnnr 183
Cdd:cd14091   170 LKKQGYDAACDIWSLGVLLYTMLAGYTPFasgPNDTPEVILARIGS-------------GK----IDlSGGNWDHVS--- 229
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907169597 184 ggkryPDSKDLtmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14091   230 -----DSAKDL--------------VRKMLHVDPSQRPTAAQVLQHPWI 259
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
46-143 1.28e-10

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: 61.52  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTV-KVIDFGSSCYEHQK--VYTYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd14038   110 ISSALRYLHENRIIHRDLKPENIVLQQGEQRLIhKIIDLGYAKELDQGslCTSFVGTLQYLAPELLEQQKYTVTVDYWSF 189
                          90       100
                  ....*....|....*....|..
gi 1907169597 123 GCIMAELYTGY-PLFPGENEVE 143
Cdd:cd14038   190 GTLAFECITGFrPFLPNWQPVQ 211
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
43-134 1.70e-10

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: 60.79  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  43 TFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvkVIDFGSSCYEHQKVYTYIQSR---FYRSPEVILGHPYNMAIDM 119
Cdd:cd13995   102 TKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV---LVDFGLSVQMTEDVYVPKDLRgteIYMSPEVILCRGHNTKADI 178
                          90
                  ....*....|....*
gi 1907169597 120 WSLGCIMAELYTGYP 134
Cdd:cd13995   179 YSLGATIIHMQTGSP 193
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
44-232 1.89e-10

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: 60.82  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  44 FSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMW 120
Cdd:cd06658   125 LSVLRALSYLHNQGVIHRDIKSDSILLTSDGRI--KLSDFGfcaQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIW 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 121 SLGCIMAELYTGYPLFPGENEVEQLACIMEvlGLPPahftqtasrrqvffdskglpkninnnrggkRYPDSKDLTMVVKt 200
Cdd:cd06658   203 SLGIMVIEMIDGEPPYFNEPPLQAMRRIRD--NLPP------------------------------RVKDSHKVSSVLR- 249
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907169597 201 ydsSFLDFLrrcLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06658   250 ---GFLDLM---LVREPSQRATAQELLQHPFL 275
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
49-140 1.94e-10

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: 60.59  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  49 CLHMLYVEK---IIHCDLKPENIVLYQRGQVTVKviDFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd08528   123 VLALRYLHKekqIVHRDLKPNNIMLGEDDKVTIT--DFGlakQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWAL 200
                          90
                  ....*....|....*...
gi 1907169597 123 GCIMAELYTGYPLFPGEN 140
Cdd:cd08528   201 GCILYQMCTLQPPFYSTN 218
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
39-230 1.94e-10

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: 60.45  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVT-VKVIDFGSS----CYEHQKVYTYIQSRFYRSPEVILG-HP 112
Cdd:cd14012   106 ARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGiVKLTDYSLGktllDMCSRGSLDEFKQTYWLPPELAQGsKS 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 113 YNMAIDMWSLGcIMaelytgyplfpgeneVEQLACimevlGLPPahftqtasrrqvffdskglpkninnnrggKRYPDSK 192
Cdd:cd14012   186 PTRKTDVWDLG-LL---------------FLQMLF-----GLDV-----------------------------LEKYTSP 215
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907169597 193 DLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHA 230
Cdd:cd14012   216 NPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
3-233 2.03e-10

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 60.81  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL--GINLYELMKNNSFHGFNLSIVRRftfSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVT-VK 79
Cdd:cd14174    67 EFFEDDTRFYLVFEKLrgGSILAHIQKRKHFNEREASRVVR---DIASALDFLHTKGIAHRDLKPENILCESPDKVSpVK 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  80 VIDF--------GSSC--YEHQKVYTYIQSRFYRSPEVI-----LGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEq 144
Cdd:cd14174   144 ICDFdlgsgvklNSACtpITTPELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTD- 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 145 laCimevlGLPPAHFTQTASRRqvFFDSKglpkninnNRGGKRYPDsKDLTMVvktyDSSFLDFLRRCLVWEPSLRMTPE 224
Cdd:cd14174   223 --C-----GWDRGEVCRVCQNK--LFESI--------QEGKYEFPD-KDWSHI----SSEAKDLISKLLVRDAKERLSAA 280

                  ....*....
gi 1907169597 225 QALKHAWIH 233
Cdd:cd14174   281 QVLQHPWVQ 289
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
39-163 2.13e-10

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: 60.33  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSCYEH---QKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd14189   103 VRYYLKQIISGLKYLHLKGILHRDLKLGNFFINE--NMELKVGDFGLAARLEppeQRKKTICGTPNYLAPEVLLRQGHGP 180
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTA 163
Cdd:cd14189   181 ESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPA 228
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
46-237 2.65e-10

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: 60.47  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd06641   110 ILKGLDYLHSEKKIHRDIKAANVLLSEHGEV--KLADFGVAGQltdTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSL 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 123 GCIMAELYTGYplfPGENEVEQlaciMEVLGLppahftqtasrrqvffdskgLPKNinnnrggkrypdskDLTMVVKTYD 202
Cdd:cd06641   188 GITAIELARGE---PPHSELHP----MKVLFL--------------------IPKN--------------NPPTLEGNYS 226
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907169597 203 SSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEPRK 237
Cdd:cd06641   227 KPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAK 261
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-130 2.88e-10

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: 60.00  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCITFELL-GINLYELM-KNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtVKVIDFGS 85
Cdd:cd13996    76 EPPLYIQMELCeGGTLRDWIdRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ-VKIGDFGL 154
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597  86 SCY-EHQKVYTY----------------IQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELY 130
Cdd:cd13996   155 ATSiGNQKRELNnlnnnnngntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
45-136 3.17e-10

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: 60.36  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLyveKIIHCDLKPENIVLYQRGQVTVKviDFGSsCYE----HQKVYTYIQSRFYRSPEVILGHPYNMAIDMW 120
Cdd:cd05604   108 SALGYLHSI---NIVYRDLKPENILLDSQGHIVLT--DFGL-CKEgisnSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWW 181
                          90
                  ....*....|....*.
gi 1907169597 121 SLGCIMAELYTGYPLF 136
Cdd:cd05604   182 CLGSVLYEMLYGLPPF 197
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
11-157 3.33e-10

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: 59.94  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFEL--LGiNLYELMKNNSFHGFNLS--IVRRFTFSILKCLHMLYVEKIIHCDLKPENIV---LYQRGQVTVKVIDF 83
Cdd:cd14000    83 LMLVLELapLG-SLDHLLQQDSRSFASLGrtLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNSAIIIKIADY 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597  84 GSSCYE-HQKVYTYIQSRFYRSPEVILGHP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQlaCIMEVLGLPPA 157
Cdd:cd14000   162 GISRQCcRMGAKGSEGTPGFRAPEIARGNViYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPN--EFDIHGGLRPP 235
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
50-131 3.45e-10

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: 59.76  E-value: 3.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVtVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAEL 129
Cdd:cd14058   105 LHSMKPKALIHRDLKPPNLLLTNGGTV-LKICDFGTACDISTHMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEV 183

                  ..
gi 1907169597 130 YT 131
Cdd:cd14058   184 IT 185
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
29-232 3.46e-10

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: 59.76  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  29 NSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSS---CYEHQKVYtyiQSRFYRS- 104
Cdd:cd06631    95 ARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNG--VIKLIDFGCAkrlCINLSSGS---QSQLLKSm 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 105 --------PEVILGHPYNMAIDMWSLGCIMAELYTGYPlfpgeneveqlacimevlglPPAHFTQTASRRQVFFDSKGLP 176
Cdd:cd06631   170 rgtpywmaPEVINETGHGRKSDIWSIGCTVFEMATGKP--------------------PWADMNPMAAIFAIGSGRKPVP 229
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 177 kninnnrggkRYPDskdltmvvkTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06631   230 ----------RLPD---------KFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
50-145 3.72e-10

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 60.04  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAEL 129
Cdd:cd05630   115 LEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEM 194
                          90       100
                  ....*....|....*....|..
gi 1907169597 130 YTGYPLFP------GENEVEQL 145
Cdd:cd05630   195 IAGQSPFQqrkkkiKREEVERL 216
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
13-131 3.84e-10

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: 59.66  E-value: 3.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEK--IIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEH 90
Cdd:cd13985    79 LLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR--FKLCDFGSATTEH 156
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597  91 QKVYTY---------IQSR---FYRSPEVI---LGHPYNMAIDMWSLGCImaeLYT 131
Cdd:cd13985   157 YPLERAeevniieeeIQKNttpMYRAPEMIdlySKKPIGEKADIWALGCL---LYK 209
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
45-136 4.61e-10

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: 60.02  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLyveKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEH----QKVYTYIQSRFYRSPEVILGHPYNMAIDMW 120
Cdd:cd05575   107 SALGYLHSL---NIIYRDLKPENILLDSQGHV--VLTDFGL-CKEGiepsDTTSTFCGTPEYLAPEVLRKQPYDRTVDWW 180
                          90
                  ....*....|....*.
gi 1907169597 121 SLGCIMAELYTGYPLF 136
Cdd:cd05575   181 CLGAVLYEMLYGLPPF 196
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
13-237 4.66e-10

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


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 59.70  E-value: 4.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNnSFHGFNLSIVRRFTFSILKCLHMLYVEK-IIHCDLKPENIVLYQRGQvtVKVIDFGSScyeHQ 91
Cdd:cd06618    91 ICMELMSTCLDKLLKR-IQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGN--VKLCDFGIS---GR 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  92 KVYTYIQSR-----FYRSPEVILGHP---YNMAIDMWSLGCIMAELYTGypLFPGENEVEQLACIMEVLGLPPAHftqta 163
Cdd:cd06618   165 LVDSKAKTRsagcaAYMAPERIDPPDnpkYDIRADVWSLGISLVELATG--QFPYRNCKTEFEVLTKILNEEPPS----- 237
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 164 srrqvffdskgLPKNinnnrggkrypdskdltmvvKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI--HEPRK 237
Cdd:cd06618   238 -----------LPPN--------------------EGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIrrYETAE 282
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
3-232 4.90e-10

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: 59.74  E-value: 4.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL--GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMlyvEKIIHCDLKPENIVLYQRGQVT-VK 79
Cdd:cd14090    67 EYFEDDERFYLVFEKMrgGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHD---KGIAHRDLKPENILCESMDKVSpVK 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  80 VIDF--GSSCYEHQKVYTYIQ---------SRFYRSPEVI-----LGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVE 143
Cdd:cd14090   144 ICDFdlGSGIKLSSTSMTPVTtpelltpvgSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGED 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 144 qlaCimevlGLPPAHFTQTAsrRQVFFDSkglpknINNnrGGKRYPDsKDLTMVvktyDSSFLDFLRRCLVWEPSLRMTP 223
Cdd:cd14090   224 ---C-----GWDRGEACQDC--QELLFHS------IQE--GEYEFPE-KEWSHI----SAEAKDLISHLLVRDASQRYTA 280

                  ....*....
gi 1907169597 224 EQALKHAWI 232
Cdd:cd14090   281 EQVLQHPWV 289
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
43-232 5.00e-10

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: 59.48  E-value: 5.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  43 TFSILKCL----HMLYVEKIIHCDLKPENIVLYQ-----RGQVTVKVIDFGSSCYEHQKVYTYIQSR----FYRSPEVIL 109
Cdd:cd14097   102 TRHIIQSLasavAYLHKNDIVHRDLKLENILVKSsiidnNDKLNIKVTDFGLSVQKYGLGEDMLQETcgtpIYMAPEVIS 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 110 GHPYNMAIDMWSLGCIMAELYTGYPLFPGENEvEQLaciMEVLGLPPAHFTQTASRRqvffdSKGLPKNInnnrggkryp 189
Cdd:cd14097   182 AHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSE-EKL---FEEIRKGDLTFTQSVWQS-----VSDAAKNV---------- 242
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907169597 190 dskdltmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14097   243 -------------------LQQLLKVDPAHRMTASELLDNPWI 266
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
56-163 5.03e-10

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: 59.20  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  56 EKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYE-HQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYP 134
Cdd:cd14116   124 KRVIHRDIKPENLLLGSAGEL--KIADFGWSVHApSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKP 201
                          90       100
                  ....*....|....*....|....*....
gi 1907169597 135 LFPGENEVEQLACIMEVLGLPPAHFTQTA 163
Cdd:cd14116   202 PFEANTYQETYKRISRVEFTFPDFVTEGA 230
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
46-150 5.61e-10

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: 58.97  E-value: 5.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRgqvTVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSL 122
Cdd:cd08222   115 LLLAVQYMHERRILHRDLKAKNIFLKNN---VIKVGDFGISRIlmgTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSL 191
                          90       100
                  ....*....|....*....|....*...
gi 1907169597 123 GCIMAELYTGYPLFPGENEVEQLACIME 150
Cdd:cd08222   192 GCILYEMCCLKHAFDGQNLLSVMYKIVE 219
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
35-136 6.75e-10

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: 58.96  E-value: 6.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  35 NLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENiVLYQRGQVTVKVIDFGSS--------CYEhqkvyTYIQSRFYRSPE 106
Cdd:cd06624   106 NENTIGYYTKQILEGLKYLHDNKIVHRDIKGDN-VLVNTYSGVVKISDFGTSkrlaginpCTE-----TFTGTLQYMAPE 179
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907169597 107 VILGHP--YNMAIDMWSLGCIMAELYTGYPLF 136
Cdd:cd06624   180 VIDKGQrgYGPPADIWSLGCTIIEMATGKPPF 211
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
9-234 6.92e-10

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 59.35  E-value: 6.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELLGI-NLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSC 87
Cdd:cd06637    82 DQLWLVMEFCGAgSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAE--VKLVDFGVSA 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  88 YEHQKV---YTYIQSRFYRSPEVIL-----GHPYNMAIDMWSLGCIMAELYTGYPLFpgeneveqlaCIMEVLglppahf 159
Cdd:cd06637   160 QLDRTVgrrNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPL----------CDMHPM------- 222
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 160 tqtasrRQVFFdskgLPKNinnnrggkryPDSKdltMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHE 234
Cdd:cd06637   223 ------RALFL----IPRN----------PAPR---LKSKKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRD 274
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
38-232 8.33e-10

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


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 59.01  E-value: 8.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  38 IVRRFTFSILKClHMLyveKIIHCDLKPENIVLYQRGQ-VTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEV--------- 107
Cdd:cd14171   114 YTKQIALAVQHC-HSL---NIAHRDLKPENLLLKDNSEdAPIKLCDFGFAKVDQGDLMTPQFTPYYVAPQVleaqrrhrk 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 108 ----ILGHP----YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMevlglppahftqtasRRQVFFDSKGLPKNi 179
Cdd:cd14171   190 ersgIPTSPtpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITKDM---------------KRKIMTGSYEFPEE- 253
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 180 nnnrggkrypDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14171   254 ----------EWSQISEMAK-------DIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
53-136 1.00e-09

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: 58.78  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  53 LYVEKIIHCDLKPENIVLYQRGQVTV-KVIDFGSSCYEHQK--VYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAEL 129
Cdd:cd14039   115 LHENKIIHRDLKPENIVLQEINGKIVhKIIDLGYAKDLDQGslCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFEC 194

                  ....*..
gi 1907169597 130 YTGYPLF 136
Cdd:cd14039   195 IAGFRPF 201
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
40-143 1.07e-09

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: 58.87  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKviDFGSsCYEH----QKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd05602   111 RFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLT--DFGL-CKENiepnGTTSTFCGTPEYLAPEVLHKQPYDR 187
                          90       100
                  ....*....|....*....|....*...
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLFPGENEVE 143
Cdd:cd05602   188 TVDWWCLGAVLYEMLYGLPPFYSRNTAE 215
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
1-132 1.23e-09

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: 58.44  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRN---------HLCITFeLLGINLYEL-------------------MKNNSFHGFNLSIVRRFTFSILKCLHM 52
Cdd:cd14067    51 MKNFSEFRQeasmlhslqHPCIVY-LIGISIHPLcfalelaplgslntvleenHKGSSFMPLGHMLTFKIAYQIAAGLAY 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  53 LYVEKIIHCDLKPENIVLY---QRGQVTVKVIDFGSSCYE-HQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAE 128
Cdd:cd14067   130 LHKKNIIFCDLKSDNILVWsldVQEHINIKLSDYGISRQSfHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYE 209

                  ....
gi 1907169597 129 LYTG 132
Cdd:cd14067   210 LLSG 213
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
45-232 1.24e-09

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 58.46  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQKV---YTYIQSRFYRSPEVILGHPYNMAIDMWS 121
Cdd:cd06659   125 AVLQALAYLHSQGVIHRDIKSDSILLTLDGRV--KLSDFGFCAQISKDVpkrKSLVGTPYWMAPEVISRCPYGTEVDIWS 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 122 LGCIMAELYTGYPLFPGENEVEQLACIMEVlglPPahftqtasrrqvffdskglPKNINNNRggkrypdskdLTMVVKty 201
Cdd:cd06659   203 LGIMVIEMVDGEPPYFSDSPVQAMKRLRDS---PP-------------------PKLKNSHK----------ASPVLR-- 248
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907169597 202 dssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06659   249 -----DFLERMLVRDPQERATAQELLDHPFL 274
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
37-148 1.33e-09

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 57.99  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGHPYN 114
Cdd:cd14108    97 SEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAqeLTPNEPQYCKYGTPEFVAPEIVNQSPVS 176
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907169597 115 MAIDMWSLGCIMAELYTGYPLFPGENEVEQLACI 148
Cdd:cd14108   177 KVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNI 210
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
32-143 1.41e-09

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: 57.93  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  32 HGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSScyehQKVYTYIQ-----SRFYRSPE 106
Cdd:cd14112    94 DYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRA----QKVSKLGKvpvdgDTDWASPE 169
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907169597 107 VILGH-PYNMAIDMWSLGCIMAELYTGYPLFPGENEVE 143
Cdd:cd14112   170 FHNPEtPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDE 207
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
39-231 1.43e-09

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: 57.98  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFG----SSCYEHQkvYTYIQSRFYRSPEVILGHPYN 114
Cdd:cd14107   100 VKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGfaqeITPSEHQ--FSKYGSPEFVAPEIVHQEPVS 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 115 MAIDMWSLGCIMAELYTGYPLFPGENEveqLACIMEVLglppahftqtasRRQVFFDSkglpkninnnrggkryPDSKDL 194
Cdd:cd14107   178 AATDIWALGVIAYLSLTCHSPFAGEND---RATLLNVA------------EGVVSWDT----------------PEITHL 226
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 195 TMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14107   227 SEDAK-------DFIKRVLQPDPEKRPSASECLSHEW 256
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
42-172 1.61e-09

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: 57.66  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQV-TVKVIDFGSSCY--EHQKVYTYIQSRFYRSPEVILGHPYNMAID 118
Cdd:cd14115    94 YIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDAVQisGHRHVHHLLGNPEFAAPEVIQGTPVSLATD 173
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 119 MWSLGCIMAELYTGYPLFPGENEVEQLACIMEV-LGLPPAHFTQTASRRQVFFDS 172
Cdd:cd14115   174 IWSIGVLTYVMLSGVSPFLDESKEETCINVCRVdFSFPDEYFGDVSQAARDFINV 228
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
3-150 1.65e-09

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: 58.08  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRG-QVTVKV 80
Cdd:cd14092    66 EVFQDELHTYLVMELLrGGELLERIRKKK--RFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDdDAEIKI 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597  81 IDFGSSCY--EHQKVYTYIQSRFYRSPEVILGHP----YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIME 150
Cdd:cd14092   144 VDFGFARLkpENQPLKTPCFTLPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMK 219
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
34-141 1.67e-09

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: 58.39  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKviDFGSS----CYEHQKVYTYIQSRFYRSPEVIL 109
Cdd:cd05614   102 FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLT--DFGLSkeflTEEKERTYSFCGTIEYMAPEIIR 179
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907169597 110 GHP-YNMAIDMWSLGCIMAELYTGYPLFPGENE 141
Cdd:cd05614   180 GKSgHGKAVDWWSLGILMFELLTGASPFTLEGE 212
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
8-141 1.69e-09

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: 58.06  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCITFELL-GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSS 86
Cdd:cd05632    74 KDALCLVLTIMnGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK 153
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597  87 CYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENE 141
Cdd:cd05632   154 IPEGESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKE 208
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
37-164 1.77e-09

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: 57.53  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  37 SIVRRFTFS----------ILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFGSSCYEH----QKVYTYIQSRFY 102
Cdd:cd14111    89 SLIDRFRYSeddvvgylvqILQGLEYLHGRRVLHLDIKPDNIMV--TNLNAIKIVDFGSAQSFNplslRQLGRRTGTLEY 166
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 103 RSPEVILGHPYNMAIDMWSLGCIMAELYTG-YPLF---PGENEVEQLACIMEVLGLPPaHFTQTAS 164
Cdd:cd14111   167 MAPEMVKGEPVGPPADIWSIGVLTYIMLSGrSPFEdqdPQETEAKILVAKFDAFKLYP-NVSQSAS 231
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
45-232 1.86e-09

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: 57.73  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWS 121
Cdd:cd06657   124 AVLKALSVLHAQGVIHRDIKSDSILLTHDGRV--KLSDFGfcaQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWS 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 122 LGCIMAELYTGYPLFPGENEVEQLACIMEvlGLPPahftqtasrrqvffdskglpkninnnrggkRYPDSKDLTMVVKty 201
Cdd:cd06657   202 LGIMVIEMVDGEPPYFNEPPLKAMKMIRD--NLPP------------------------------KLKNLHKVSPSLK-- 247
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907169597 202 dssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06657   248 -----GFLDRLLVRDPAQRATAAELLKHPFL 273
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
3-138 2.33e-09

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: 57.73  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL--GINLYELMKNNSFHGFNLSIVRRftfSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVT-VK 79
Cdd:cd14173    67 EFFEEEDKFYLVFEKMrgGSILSHIHRRRHFNELEASVVVQ---DIASALDFLHNKGIAHRDLKPENILCEHPNQVSpVK 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169597  80 VIDFG----------SSCYEHQKVYTYIQSRFYRSPEVILGHP-----YNMAIDMWSLGCIMAELYTGYPLFPG 138
Cdd:cd14173   144 ICDFDlgsgiklnsdCSPISTPELLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVG 217
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
1-155 2.52e-09

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: 57.71  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELlgINLYELMknnsfhgFNLSIVRRFT--------FSILKCLHMLYVEKIIHCDLKPENIVLYQ 72
Cdd:cd05595    60 LKYAFQTHDRLCFVMEY--ANGGELF-------FHLSRERVFTedrarfygAEIVSALEYLHSRDVVYRDIKLENLMLDK 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  73 RGQVtvKVIDFGSsCYE----HQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTG-YPLFPGENEVEQLAC 147
Cdd:cd05595   131 DGHI--KITDFGL-CKEgitdGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHERLFELI 207

                  ....*...
gi 1907169597 148 IMEVLGLP 155
Cdd:cd05595   208 LMEEIRFP 215
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
44-232 3.09e-09

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: 57.33  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  44 FSILKCLHMLYVEKIIHCDLKPENIvLYQRGQV---TVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAI 117
Cdd:cd14177   105 YTITKTVDYLHCQGVVHRDLKPSNI-LYMDDSAnadSIRICDFGFAKQlrgENGLLLTPCYTANFVAPEVLMRQGYDAAC 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 118 DMWSLGCIMAELYTGY-PLFPGENEV-EQLacimeVLGLPPAHFTQTASRRQVFFDSkglpkninnnrggkrypdSKDLt 195
Cdd:cd14177   184 DIWSLGVLLYTMLAGYtPFANGPNDTpEEI-----LLRIGSGKFSLSGGNWDTVSDA------------------AKDL- 239
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 196 mvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14177   240 -------------LSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
21-138 3.32e-09

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: 56.50  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  21 NLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVE---KIIHCDLKPENIVLYQRGqvTVKVIDFGSS-CYEHQKVYTY 96
Cdd:cd14060    68 SLFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADG--VLKICDFGASrFHSHTTHMSL 145
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907169597  97 IQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPG 138
Cdd:cd14060   146 VGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG 187
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
50-232 4.08e-09

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 56.94  E-value: 4.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVI-----LGHPYNMAIDMWS 121
Cdd:cd06638   137 LQHLHVNKTIHRDVKGNNILLTTEG--GVKLVDFGVSAQltsTRLRRNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWS 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 122 LGCIMAELYTGYPLFPgenEVEQLACIMEVLGLPPAHFTQTasrrqvffdskglpkninnnrggkrypdskdltmvvKTY 201
Cdd:cd06638   215 LGITAIELGDGDPPLA---DLHPMRALFKIPRNPPPTLHQP------------------------------------ELW 255
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907169597 202 DSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06638   256 SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
58-142 6.66e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 57.11  E-value: 6.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  58 IIHCDLKPENIVLYQRGQvtVKVIDFG-------SSCYEHQKVytyIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELY 130
Cdd:NF033483  128 IVHRDIKPQNILITKDGR--VKVTDFGiaralssTTMTQTNSV---LGTVHYLSPEQARGGTVDARSDIYSLGIVLYEML 202
                          90
                  ....*....|..
gi 1907169597 131 TGYPLFPGENEV 142
Cdd:NF033483  203 TGRPPFDGDSPV 214
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
47-232 8.17e-09

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


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 55.53  E-value: 8.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYeHQKVYTYIQSRFYRSPEVILGH---PYNMAIDMWSLG 123
Cdd:cd06607   111 LQGLAYLHSHNRIHRDVKAGNILLTEPG--TVKLADFGSASL-VCPANSFVGTPYWMAPEVILAMdegQYDGKVDVWSLG 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 124 --CI-MAELYTgyPLFpGENEVEQLacimevlglppAHFTQTasrrqvffDSKGLPKNinnnrggkrypdskdltmvvkT 200
Cdd:cd06607   188 itCIeLAERKP--PLF-NMNAMSAL-----------YHIAQN--------DSPTLSSG---------------------E 224
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907169597 201 YDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06607   225 WSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFV 256
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
46-140 8.25e-09

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: 55.60  E-value: 8.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGHPYN-MAIDMWSL 122
Cdd:cd14072   108 IVSAVQYCHQKRIVHRDLKAENLLL--DADMNIKIADFGFSneFTPGNKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSL 185
                          90
                  ....*....|....*...
gi 1907169597 123 GCIMAELYTGYPLFPGEN 140
Cdd:cd14072   186 GVILYTLVSGSLPFDGQN 203
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
5-145 1.24e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 55.10  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELL-GINLYELMKNnsFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDF 83
Cdd:cd05609    69 FETKRHLCMVMEYVeGGDCATLLKN--IGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHI--KLTDF 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  84 GSS----------CYE-HQKVYTYI---QSRF----YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENeVEQL 145
Cdd:cd05609   145 GLSkiglmslttnLYEgHIEKDTREfldKQVCgtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDT-PEEL 223
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
40-131 1.31e-08

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: 55.00  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKV-------YTYIQSRFYRSPEVILGHP 112
Cdd:cd14162   103 RRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNN--NLKITDFGFARGVMKTKdgkpklsETYCGSYAYASPEILRGIP 180
                          90       100
                  ....*....|....*....|
gi 1907169597 113 YN-MAIDMWSLGCImaeLYT 131
Cdd:cd14162   181 YDpFLSDIWSMGVV---LYT 197
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
38-137 1.36e-08

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 55.44  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  38 IVRRFTFSILKCLHMLYVE-KIIHCDLKPENIVLYQRGQVtvKVIDFG-SSCYEHQKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd06649   104 ILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEI--KLCDFGvSGQLIDSMANSFVGTRSYMSPERLQGTHYSV 181
                          90       100
                  ....*....|....*....|...
gi 1907169597 116 AIDMWSLGCIMAELYTG-YPLFP 137
Cdd:cd06649   182 QSDIWSMGLSLVELAIGrYPIPP 204
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
5-129 1.75e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 54.89  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFEL-----LGINLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVK 79
Cdd:cd05608    70 FQTKTDLCLVMTImnggdLRYHIYNVDEENP--GFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRIS 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907169597  80 VIDFGSSCYEHQ-KVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAEL 129
Cdd:cd05608   148 DLGLAVELKDGQtKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEM 198
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
11-156 1.78e-08

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: 54.48  E-value: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   11 LCITFELL-GINLYELMKNNSFHGFNLSIVRRFTFSIlkCLHMLYVE--KIIHCDLKPENIVLyqRGQVTVKVIDFGSSC 87
Cdd:smart00221  76 LMIVMEYMpGGDLLDYLRKNRPKELSLSDLLSFALQI--ARGMEYLEskNFIHRDLAARNCLV--GENLVVKISDFGLSR 151
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169597   88 YEHQ-KVYTYIQSRF-YR--SPEVILGHPYNMAIDMWSLGCIMAELYT-GYPLFPGENEVEQLACIMEVLGLPP 156
Cdd:smart00221 152 DLYDdDYYKVKGGKLpIRwmAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYRLPK 225
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-149 1.84e-08

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: 54.94  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  19 GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVkvIDFG----SSCYEHQKVY 94
Cdd:cd05574    85 GGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIML--TDFDlskqSSVTPPPVRK 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  95 TYIQSRF----------------------------YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLA 146
Cdd:cd05574   163 SLRKGSRrssvksieketfvaepsarsnsfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFS 242

                  ...
gi 1907169597 147 CIM 149
Cdd:cd05574   243 NIL 245
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1-185 1.91e-08

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: 55.09  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL--GINLYELMKNNSFhgfNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtv 78
Cdd:cd05593    80 LKYSFQTKDRLCFVMEYVngGELFFHLSRERVF---SEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHI-- 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTG-YPLFPGENEVeqlacIMEVLGL 154
Cdd:cd05593   155 KITDFGlckEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHEK-----LFELILM 229
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907169597 155 PPAHFTQTASRRQVFFDSKGLPKNINNNRGG 185
Cdd:cd05593   230 EDIKFPRTLSADAKSLLSGLLIKDPNKRLGG 260
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
24-138 2.17e-08

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 55.03  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  24 ELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrGQVtVKVIDFG-SSCYEHQKVYTYIQSRF- 101
Cdd:cd05105   224 NLLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQ-GKI-VKICDFGlARDIMHDSNYVSKGSTFl 301
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907169597 102 ---YRSPEVILGHPYNMAIDMWSLGCIMAELYT-GYPLFPG 138
Cdd:cd05105   302 pvkWMAPESIFDNLYTTLSDVWSYGILLWEIFSlGGTPYPG 342
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
50-132 2.19e-08

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: 54.04  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMA 127
Cdd:cd14059    94 MNYLHLHKIIHRDLKSPNVLVTYND--VLKISDFGTSkeLSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLW 171

                  ....*
gi 1907169597 128 ELYTG 132
Cdd:cd14059   172 ELLTG 176
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
46-232 2.45e-08

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: 54.23  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVI-----LGHPYNMAI 117
Cdd:cd06608   122 TLRGLAYLHENKVIHRDIKGQNILLTEEAEV--KLVDFGVSAQldsTLGRRNTFIGTPYWMAPEVIacdqqPDASYDARC 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 118 DMWSLGCIMAELYTGYPLFpgeneveqlaCIMevlglPPAhftqtasrRQVFFdskgLPKNinnnrggkryPDSKdlTMV 197
Cdd:cd06608   200 DVWSLGITAIELADGKPPL----------CDM-----HPM--------RALFK----IPRN----------PPPT--LKS 240
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907169597 198 VKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd06608   241 PEKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
34-149 2.92e-08

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: 54.42  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYE----HQKVYTYIQSRFYRSPEVIL 109
Cdd:cd05591    93 FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHC--KLADFGM-CKEgilnGKTTTTFCGTPDYIAPEILQ 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907169597 110 GHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIM 149
Cdd:cd05591   170 ELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 209
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
34-149 2.99e-08

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: 54.53  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG---SSCYEHQKVYTYIQSRFYRSPEVILG 110
Cdd:cd05590    93 FDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHC--KLADFGmckEGIFNGKTTSTFCGTPDYIAPEILQE 170
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907169597 111 HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIM 149
Cdd:cd05590   171 MLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAIL 209
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
1-249 3.29e-08

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: 54.26  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL--GINLYELMKNNSFHGFNLSIVrrfTFSILKCLHMLYVEKIIHCDLKPENIvLY--QRGQV 76
Cdd:cd14175    60 LKDVYDDGKHVYLVTELMrgGELLDKILRQKFFSEREASSV---LHTICKTVEYLHSQGVVHRDLKPSNI-LYvdESGNP 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  77 -TVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLF---PGENEVEQLACIM 149
Cdd:cd14175   136 eSLRICDFGFAKQlraENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIG 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 150 EvlglppAHFTQTASRRQVFFDSkglpkninnnrggkrypdSKDLtmvvktydssfldfLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd14175   216 S------GKFTLSGGNWNTVSDA------------------AKDL--------------VSKMLHVDPHQRLTAKQVLQH 257
                         250       260
                  ....*....|....*....|
gi 1907169597 230 AWIHEPRKFkprPKPQILRK 249
Cdd:cd14175   258 PWITQKDKL---PQSQLNHQ 274
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
39-136 3.41e-08

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: 53.78  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSC---YEHQKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd14187   109 ARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLND--DMEVKIGDFGLATkveYDGERKKTLCGTPNYIAPEVLSKKGHSF 186
                          90       100
                  ....*....|....*....|.
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLF 136
Cdd:cd14187   187 EVDIWSIGCIMYTLLVGKPPF 207
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
22-245 3.41e-08

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 54.44  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  22 LYELMKNNSFHGFN------LSIVRRftfSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEHQKV-- 93
Cdd:PLN00034  150 LLEFMDGGSLEGTHiadeqfLADVAR---QILSGIAYLHRRHIVHRDIKPSNLLINSAKN--VKIADFGVSRILAQTMdp 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  94 -YTYIQSRFYRSPEVI---LGH-PYN-MAIDMWSLGCIMAELYTG-YPLFPG-ENEVEQLACIMeVLGLPPAHfTQTASR 165
Cdd:PLN00034  225 cNSSVGTIAYMSPERIntdLNHgAYDgYAGDIWSLGVSILEFYLGrFPFGVGrQGDWASLMCAI-CMSQPPEA-PATASR 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 166 rqvffdskglpkninnnrggkrypdskdltmvvktydsSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEPRKFKPRPKPQ 245
Cdd:PLN00034  303 --------------------------------------EFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPN 344
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
34-132 3.50e-08

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: 54.28  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFT-----F---SILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEhQKVYTYIQSRF---- 101
Cdd:cd05571    84 FHLSRERVFSedrtrFygaEIVLALGYLHSQGIVYRDLKLENLLLDKDGHI--KITDFGL-CKE-EISYGATTKTFcgtp 159
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907169597 102 -YRSPEVILGHPYNMAIDMWSLGCIMAELYTG 132
Cdd:cd05571   160 eYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 191
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
40-231 3.51e-08

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: 53.56  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG-SSCYEHQK----VYTYIQSRFYRSPEVILGHPYN 114
Cdd:cd14663   103 RKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDG--NLKISDFGlSALSEQFRqdglLHTTCGTPNYVAPEVLARRGYD 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 115 MAI-DMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTqtasrrqvffdskglpkninnnrggkryPDSKD 193
Cdd:cd14663   181 GAKaDIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFS----------------------------PGAKS 232
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907169597 194 LtmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14663   233 L--------------IKRILDPNPSTRITVEQIMASPW 256
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
5-141 3.75e-08

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: 53.75  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELL-GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDF 83
Cdd:cd05607    71 FETKTHLCLVMSLMnGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGL 150
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597  84 GSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENE 141
Cdd:cd05607   151 AVEVKEGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKE 208
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
41-142 3.85e-08

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: 53.54  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  41 RFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFGSS-------CYEHQKVYTYIQSRfYRSPEVILGHPY 113
Cdd:cd13979   107 LISLDIARALRFCHSHGIVHLDVKPANILI--SEQGVCKLCDFGCSvklgegnEVGTPRSHIGGTYT-YRAPELLKGERV 183
                          90       100
                  ....*....|....*....|....*....
gi 1907169597 114 NMAIDMWSLGCIMAELYTGYPLFPGENEV 142
Cdd:cd13979   184 TPKADIYSFGITLWQMLTRELPYAGLRQH 212
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
50-151 4.12e-08

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 53.84  E-value: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEH----QKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05589   114 LQFLHEHKIVYRDLKLDNLLLDTEGYV--KIADFGL-CKEGmgfgDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVL 190
                          90       100
                  ....*....|....*....|....*...
gi 1907169597 126 MAELYTGYPLFPGENEVEQLACI--MEV 151
Cdd:cd05589   191 IYEMLVGESPFPGDDEEEVFDSIvnDEV 218
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
43-236 4.12e-08

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: 53.89  E-value: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  43 TFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEhQKVYTYIQSRFYRSPEVILGH---PYNMAIDM 119
Cdd:cd06633   127 THGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ--VKLADFGSASIA-SPANSFVGTPYWMAPEVILAMdegQYDGKVDI 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 120 WSLGCIMAELYTGYPLFPGENEVEQLacimevlglppAHFTQTasrrqvffDSKGLPKNinnnrggkrypdskdltmvvk 199
Cdd:cd06633   204 WSLGITCIELAERKPPLFNMNAMSAL-----------YHIAQN--------DSPTLQSN--------------------- 243
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 200 TYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEPR 236
Cdd:cd06633   244 EWTDSFRGFVDYCLQKIPQERPSSAELLRHDFVRRER 280
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
59-139 4.34e-08

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: 53.86  E-value: 4.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  59 IHCDLKPENIVLYQRGQVtvKVIDFG----------SSCYE-HQKVYT--YIqsrfyrSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05598   123 IHRDIKPDNILIDRDGHI--KLTDFGlctgfrwthdSKYYLaHSLVGTpnYI------APEVLLRTGYTQLCDWWSVGVI 194
                          90
                  ....*....|....*...
gi 1907169597 126 MAELYTGYPLF----PGE 139
Cdd:cd05598   195 LYEMLVGQPPFlaqtPAE 212
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
50-149 4.35e-08

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: 53.85  E-value: 4.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHML-YVekiiHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQKvyTYIQSRF------YRSPEVIL------GHPYNMA 116
Cdd:cd05601   118 LHSMgYV----HRDIKPENILIDRTGHI--KLADFGSAAKLSSD--KTVTSKMpvgtpdYIAPEVLTsmnggsKGTYGVE 189
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907169597 117 IDMWSLGCIMAELYTGYPLFPGENEVEQLACIM 149
Cdd:cd05601   190 CDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIM 222
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
39-132 5.03e-08

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: 53.28  E-value: 5.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFG-SSCYE----HQKVYTYIQSRFYRSPEVILGHPY 113
Cdd:cd14070   105 ARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDE--NDNIKLIDFGlSNCAGilgySDPFSTQCGSPAYAAPELLARKKY 182
                          90
                  ....*....|....*....
gi 1907169597 114 NMAIDMWSLGCIMAELYTG 132
Cdd:cd14070   183 GPKVDVWSIGVNMYAMLTG 201
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
39-141 5.17e-08

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 53.47  E-value: 5.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKviDFGSS----CYEHQKVYTYIQSRFYRSPEVILG--HP 112
Cdd:cd05613   107 VQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLT--DFGLSkeflLDENERAYSFCGTIEYMAPEIVRGgdSG 184
                          90       100
                  ....*....|....*....|....*....
gi 1907169597 113 YNMAIDMWSLGCIMAELYTGYPLFPGENE 141
Cdd:cd05613   185 HDKAVDWWSLGVLMYELLTGASPFTVDGE 213
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
5-136 5.27e-08

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: 53.91  E-value: 5.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   5 FYFRNHLCITFELLgiNLYELMKNNSFHG-FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDF 83
Cdd:cd05633    77 FHTPDKLCFILDLM--NGGDLHYHLSQHGvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHV--RISDL 152
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597  84 GSSC-YEHQKVYTYIQSRFYRSPEVIL-GHPYNMAIDMWSLGCIMAELYTGYPLF 136
Cdd:cd05633   153 GLACdFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPF 207
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
58-232 5.30e-08

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: 53.25  E-value: 5.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  58 IIHCDLKPENIVLYQrgQVTVKVIDFGSS--CYEHQKVYTYIQSRF-----YRSPEVILGHPYNMAI-DMWSLGCImaeL 129
Cdd:cd14165   123 IVHRDLKCENLLLDK--DFNIKLTDFGFSkrCLRDENGRIVLSKTFcgsaaYAAPEVLQGIPYDPRIyDIWSLGVI---L 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 130 YtgyplfpgeneveqlacIMEVLGLPpahftqtasrrqvfFDSKGLPKNINNNRGGK-RYPDSKDLTMVVKtydssflDF 208
Cdd:cd14165   198 Y-----------------IMVCGSMP--------------YDDSNVKKMLKIQKEHRvRFPRSKNLTSECK-------DL 239
                         170       180
                  ....*....|....*....|....
gi 1907169597 209 LRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14165   240 IYRLLQPDVSQRLCIDEVLSHPWL 263
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
24-156 5.96e-08

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 52.92  E-value: 5.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   24 ELMKNNSFHGFNLSivRRFTFSILKCLH--------MLYVE--KIIHCDLKPENIvLYQRGQVtVKVIDFGSSCYEHQKV 93
Cdd:smart00219  81 EYMEGGDLLSYLRK--NRPKLSLSDLLSfalqiargMEYLEskNFIHRDLAARNC-LVGENLV-VKISDFGLSRDLYDDD 156
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597   94 YTYIQSR----FYRSPEVILGHPYNMAIDMWSLGCIMAELYT-GYPLFPGENEVEQLACIMEVLGLPP 156
Cdd:smart00219 157 YYRKRGGklpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYRLPQ 224
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
13-151 6.19e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 53.51  E-value: 6.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNNSFHG-FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSC-YEH 90
Cdd:cd14223    78 LSFILDLMNGGDLHYHLSQHGvFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGH--VRISDLGLACdFSK 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597  91 QKVYTYIQSRFYRSPEVIL-GHPYNMAIDMWSLGCIMAELYTGYPLF-----PGENEVEQLACIMEV 151
Cdd:cd14223   156 KKPHASVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTMAV 222
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
40-140 7.38e-08

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: 52.77  E-value: 7.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVL--YQRgqvtVKVIDFG-----SSCYEHQkVYTYIQSRFYRSPEVILGHP 112
Cdd:cd14078   104 RVFFRQIVSAVAYVHSQGYAHRDLKPENLLLdeDQN----LKLIDFGlcakpKGGMDHH-LETCCGSPAYAAPELIQGKP 178
                          90       100       110
                  ....*....|....*....|....*....|
gi 1907169597 113 Y--NMAiDMWSLGCIMAELYTGYPLFPGEN 140
Cdd:cd14078   179 YigSEA-DVWSMGVLLYALLCGFLPFDDDN 207
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
46-140 7.40e-08

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 53.72  E-value: 7.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSScyehqKVY----------TYIQSRFYRSPEVILGHPYNM 115
Cdd:PTZ00283  152 VLLAVHHVHSKHMIHRDIKSANILLCSNG--LVKLGDFGFS-----KMYaatvsddvgrTFCGTPYYVAPEIWRRKPYSK 224
                          90       100
                  ....*....|....*....|....*
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLFPGEN 140
Cdd:PTZ00283  225 KADMFSLGVLLYELLTLKRPFDGEN 249
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
44-232 7.73e-08

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: 53.10  E-value: 7.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  44 FSILKCLHMLYVEKIIHCDLKPENIVLYQRG--QVTVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAID 118
Cdd:cd14176   120 FTITKTVEYLHAQGVVHRDLKPSNILYVDESgnPESIRICDFGFAKQlraENGLLMTPCYTANFVAPEVLERQGYDAACD 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 119 MWSLGCIMAELYTGYPLF---PGENEVEQLACImevlglppahftqtASRRqvFFDSKGLPKNINNnrggkrypDSKDLt 195
Cdd:cd14176   200 IWSLGVLLYTMLTGYTPFangPDDTPEEILARI--------------GSGK--FSLSGGYWNSVSD--------TAKDL- 254
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 196 mvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14176   255 -------------VSKMLHVDPHQRLTAALVLRHPWI 278
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
46-168 8.00e-08

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: 52.76  E-value: 8.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEHQKVYTYIQ---------------------SRFYRS 104
Cdd:cd14046   113 ILEGLAYIHSQGIIHRDLKPVNIFLDSNGN--VKIGDFGLATSNKLNVELATQdinkstsaalgssgdltgnvgTALYVA 190
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597 105 PEVILGHP--YNMAIDMWSLGCIMAELYtgYPLFPGENEVEQLACIMEVLGLPPAHFTQTASRRQV 168
Cdd:cd14046   191 PEVQSGTKstYNEKVDMYSLGIIFFEMC--YPFSTGMERVQILTALRSVSIEFPPDFDDNKHSKQA 254
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
40-136 8.50e-08

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: 52.56  E-value: 8.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSC---YEHQKVYTYIQSRFYRSPEVILGHPYNMA 116
Cdd:cd14186   105 RHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTR--NMNIKIADFGLATqlkMPHEKHFTMCGTPNYISPEIATRSAHGLE 182
                          90       100
                  ....*....|....*....|
gi 1907169597 117 IDMWSLGCIMAELYTGYPLF 136
Cdd:cd14186   183 SDVWSLGCMFYTLLVGRPPF 202
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
38-232 9.25e-08

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: 52.28  E-value: 9.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  38 IVRRFTFSILKCLHMLYVEKIIHCDLKPENIVL-YQRGQvtVKVIDFGSSCYEHQKVYT-YIQSRFYRSPEVILGHPYN- 114
Cdd:cd14100   107 LARSFFRQVLEAVRHCHNCGVLHRDIKDENILIdLNTGE--LKLIDFGSGALLKDTVYTdFDGTRVYSPPEWIRFHRYHg 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 115 MAIDMWSLGCIMAELYTGYPLFPGENEVeqlacimevlglppahftqtaSRRQVFFDSKglpkninnnrggkrypdskdl 194
Cdd:cd14100   185 RSAAVWSLGILLYDMVCGDIPFEHDEEI---------------------IRGQVFFRQR--------------------- 222
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907169597 195 tmvvktYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14100   223 ------VSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
56-145 9.65e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 53.59  E-value: 9.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   56 EKIIHCDLKPENIVLYQ---------------RGQVTVKVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGH--PYNMA 116
Cdd:PTZ00266   144 ERVLHRDLKPQNIFLSTgirhigkitaqannlNGRPIAKIGDFGLSknIGIESMAHSCVGTPYYWSPELLLHEtkSYDDK 223
                           90       100
                   ....*....|....*....|....*....
gi 1907169597  117 IDMWSLGCIMAELYTGYPLFPGENEVEQL 145
Cdd:PTZ00266   224 SDMWALGCIIYELCSGKTPFHKANNFSQL 252
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
39-163 9.92e-08

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: 52.32  E-value: 9.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSC----YEHQKvYTYIQSRFYRSPEVILGHPYN 114
Cdd:cd14188   103 VRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINE--NMELKVGDFGLAArlepLEHRR-RTICGTPNYLSPEVLNKQGHG 179
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907169597 115 MAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIMEVLGLPPAHFTQTA 163
Cdd:cd14188   180 CESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPA 228
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
40-231 1.01e-07

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: 52.27  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEHQKVY--TYIQSRFYRSPEVILGHPY-NMA 116
Cdd:cd14079   105 RRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMN--VKIADFGLSNIMRDGEFlkTSCGSPNYAAPEVISGKLYaGPE 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 117 IDMWSLGCIMaelytgYPLFPGEneveqlacimevlgLPpahftqtasrrqvfFDSKGLP---KNInnnRGGKRY----- 188
Cdd:cd14079   183 VDVWSCGVIL------YALLCGS--------------LP--------------FDDEHIPnlfKKI---KSGIYTipshl 225
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907169597 189 -PDSKDLtmvvktydssfldfLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14079   226 sPGARDL--------------IKRMLVVDPLKRITIPEIRQHPW 255
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
44-149 1.07e-07

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: 52.93  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  44 FSILKCLhmLYVEKI-----IHCDLKPENIVLYQRGQVtvKVIDFGSSCYEH---------------------------- 90
Cdd:cd05629   105 FYMAECV--LAIEAVhklgfIHRDIKPDNILIDRGGHI--KLSDFGLSTGFHkqhdsayyqkllqgksnknridnrnsva 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  91 -----------QKVYTYIQSRF-----------YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACI 148
Cdd:cd05629   181 vdsinltmsskDQIATWKKNRRlmaystvgtpdYIAPEIFLQQGYGQECDWWSLGAIMFECLIGWPPFCSENSHETYRKI 260

                  .
gi 1907169597 149 M 149
Cdd:cd05629   261 I 261
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
44-143 1.14e-07

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 53.10  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  44 FSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYTYIQSRF-----YRSPEVILGHPYNMAID 118
Cdd:PTZ00267  176 YQIVLALDEVHSRKMMHRDLKSANIFLMPTG--IIKLGDFGFSKQYSDSVSLDVASSFcgtpyYLAPELWERKRYSKKAD 253
                          90       100
                  ....*....|....*....|....*
gi 1907169597 119 MWSLGCIMAELYTGYPLFPGENEVE 143
Cdd:PTZ00267  254 MWSLGVILYELLTLHRPFKGPSQRE 278
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
40-144 1.26e-07

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: 51.88  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvTVKVIDFGSSCYEHQKVYT-YIQSRFYRSPEVILGHPYN-MAI 117
Cdd:cd14102   108 RGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTG-ELKLIDFGSGALLKDTVYTdFDGTRVYSPPEWIRYHRYHgRSA 186
                          90       100
                  ....*....|....*....|....*..
gi 1907169597 118 DMWSLGCIMAELYTGYPLFPGENEVEQ 144
Cdd:cd14102   187 TVWSLGVLLYDMVCGDIPFEQDEEILR 213
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
58-129 1.32e-07

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: 52.29  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  58 IIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEHQ---------------KVYTYIQsrfYRSPEVI---LGHPYNMAIDM 119
Cdd:cd14037   131 LIHRDLKVENVLISDSGN--YKLCDFGSATTKILppqtkqgvtyveediKKYTTLQ---YRAPEMIdlyRGKPITEKSDI 205
                          90
                  ....*....|
gi 1907169597 120 WSLGCIMAEL 129
Cdd:cd14037   206 WALGCLLYKL 215
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
8-229 1.32e-07

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: 51.89  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCITFELLGINLYELMKNNS------FHGFNLSIVRRFTFSILKCLHMLyveKIIHCDLKPENIVLYQR---GQVTV 78
Cdd:cd13982    67 RQFLYIALELCAASLQDLVESPResklflRPGLEPVRLLRQIASGLAHLHSL---NIVHRDLKPQNILISTPnahGNVRA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQKVYTYIQSRF------YRSPEVILGHPYN---MAIDMWSLGCIMAELYTGyplfpgeneveqlacim 149
Cdd:cd13982   144 MISDFGLCKKLDVGRSSFSRRSGvagtsgWIAPEMLSGSTKRrqtRAVDIFSLGCVFYYVLSG----------------- 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 150 evlGLPPahftqtasrrqvfFDSKgLPKNINNNRGgkRYPDSKDLTMVVKTYDSSflDFLRRCLVWEPSLRMTPEQALKH 229
Cdd:cd13982   207 ---GSHP-------------FGDK-LEREANILKG--KYSLDKLLSLGEHGPEAQ--DLIERMIDFDPEKRPSAEEVLNH 265
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
46-143 1.47e-07

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: 51.95  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVI-DFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGC 124
Cdd:cd14088   108 VLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVIsDFHLAKLENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGV 187
                          90
                  ....*....|....*....
gi 1907169597 125 IMAELYTGYPLFPGENEVE 143
Cdd:cd14088   188 IMYILLSGNPPFYDEAEED 206
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
43-236 1.49e-07

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: 52.36  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  43 TFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEhQKVYTYIQSRFYRSPEVILGH---PYNMAIDM 119
Cdd:cd06635   131 THGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ--VKLADFGSASIA-SPANSFVGTPYWMAPEVILAMdegQYDGKVDV 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 120 WSLGCIMAELytgyplfpgeneveqlacimevlglppahftqtASRRQVFFdskglpkNINNNRGGKRYPDSKDLTMVVK 199
Cdd:cd06635   208 WSLGITCIEL---------------------------------AERKPPLF-------NMNAMSALYHIAQNESPTLQSN 247
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 200 TYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEPR 236
Cdd:cd06635   248 EWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLRER 284
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1-132 1.50e-07

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: 52.35  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYE-LMKNNSFHGFNLSIVRRFTFSILKCLHMLYVekiIHCDLKPENIVLY-QRGQVT 77
Cdd:cd14179    67 LHEVYHDQLHTFLVMELLkGGELLErIKKKQHFSETEASHIMRKLVSAVSHMHDVGV---VHRDLKPENLLFTdESDNSE 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907169597  78 VKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTG 132
Cdd:cd14179   144 IKIIDFGFARLkppDNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSG 201
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
39-161 1.55e-07

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 51.95  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQKV---YTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd08228   108 VWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVV--KLGDLGLGRFFSSKTtaaHSLVGTPYYMSPERIHENGYNF 185
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLFPGE--------NEVEQlaCimEVLGLPPAHFTQ 161
Cdd:cd08228   186 KSDIWSLGCLLYEMAALQSPFYGDkmnlfslcQKIEQ--C--DYPPLPTEHYSE 235
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
40-232 1.61e-07

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: 51.62  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFGSSCY--EHQKVYTYIQSRFYRSPEVILGHPYN-MA 116
Cdd:cd14071   102 RKKFWQILSAVEYCHKRHIVHRDLKAENLLL--DANMNIKIADFGFSNFfkPGELLKTWCGSPPYAAPEVFEGKEYEgPQ 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 117 IDMWSLGCIMAELYTGYPLFPGENeveqlacimevlgLPPAHFTQTASR-RQVFFDSKglpkninnnrggkrypDSKDLt 195
Cdd:cd14071   180 LDIWSLGVVLYVLVCGALPFDGST-------------LQTLRDRVLSGRfRIPFFMST----------------DCEHL- 229
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907169597 196 mvvktydssfldfLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14071   230 -------------IRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
6-134 1.96e-07

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 51.92  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   6 YFRNHLCITFELL-GINLYELMKNNSFHGFNL--SIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVID 82
Cdd:cd06639    94 YVGGQLWLVLELCnGGSVTELVKGLLKCGQRLdeAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG--GVKLVD 171
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FGSSCY---EHQKVYTYIQSRFYRSPEVI-----LGHPYNMAIDMWSLGCIMAELYTGYP 134
Cdd:cd06639   172 FGVSAQltsARLRRNTSVGTPFWMAPEVIaceqqYDYSYDARCDVWSLGITAIELADGDP 231
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
3-141 2.09e-07

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: 51.67  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   3 DFFYFRNHLCITFELL-GINLYELMKNNSFHGFNLSivrRFTFS-ILKCLHMLYVEKIIHCDLKPEN-----IVLYQR-- 73
Cdd:cd14096    73 DFQESDEYYYIVLELAdGGEIFHQIVRLTYFSEDLS---RHVITqVASAVKYLHEIGVVHRDIKPENllfepIPFIPSiv 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  74 --------------GQVT----------VKVIDFG-SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAE 128
Cdd:cd14096   150 klrkadddetkvdeGEFIpgvggggigiVKLADFGlSKQVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYT 229
                         170
                  ....*....|...
gi 1907169597 129 LYTGYPLFPGENE 141
Cdd:cd14096   230 LLCGFPPFYDESI 242
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
59-156 2.24e-07

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: 51.98  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  59 IHCDLKPENIVLYQRGQVtvKVIDFG----------SSCYEH----------------------------QKVYTYIQSR 100
Cdd:cd05627   124 IHRDIKPDNLLLDAKGHV--KLSDFGlctglkkahrTEFYRNlthnppsdfsfqnmnskrkaetwkknrrQLAYSTVGTP 201
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 101 FYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIM---EVLGLPP 156
Cdd:cd05627   202 DYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMnwkETLVFPP 260
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
58-161 2.49e-07

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 51.24  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  58 IIHCDLKPENIVLYQR------GQVTVKVIDFGSScYEHQKVY------TYIqsrfYRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd14061   116 IIHRDLKSSNILILEAienedlENKTLKITDFGLA-REWHKTTrmsaagTYA----WMAPEVIKSSTFSKASDVWSYGVL 190
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907169597 126 MAELYTGYPLFPGeneVEQLACIMEV----LGLP-----PAHFTQ 161
Cdd:cd14061   191 LWELLTGEVPYKG---IDGLAVAYGVavnkLTLPipstcPEPFAQ 232
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
50-132 3.40e-07

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: 50.73  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYTYIQSRF-----YRSPEVILGHPYNMAIDMWSLGC 124
Cdd:cd14066   109 LHEECPPPIIHGDIKSSNILLDEDF--EPKLTDFGLARLIPPSESVSKTSAVkgtigYLAPEYIRTGRVSTKSDVYSFGV 186

                  ....*...
gi 1907169597 125 IMAELYTG 132
Cdd:cd14066   187 VLLELLTG 194
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
16-126 4.06e-07

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 50.59  E-value: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  16 ELLGINLYELMK-NNSFHGFNLSIVRRFTFSILKCLHMLYVEK--IIHCDLKPENIVLYQRGQvtVKVIDFGSSCYE-HQ 91
Cdd:cd14036    86 ELCKGQLVDFVKkVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQ--IKLCDFGSATTEaHY 163
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907169597  92 KVYTYIQSR--------------FYRSPEVI---LGHPYNMAIDMWSLGCIM 126
Cdd:cd14036   164 PDYSWSAQKrslvedeitrnttpMYRTPEMIdlySNYPIGEKQDIWALGCIL 215
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
34-155 5.02e-07

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 50.80  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEK-IIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEHQK----VYTYIQSRFYRSPEVI 108
Cdd:cd05594   122 FSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHI--KITDFGL-CKEGIKdgatMKTFCGTPEYLAPEVL 198
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907169597 109 LGHPYNMAIDMWSLGCIMAELYTG-YPLFPGENEVEQLACIMEVLGLP 155
Cdd:cd05594   199 EDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHEKLFELILMEEIRFP 246
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
59-156 5.19e-07

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 50.81  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  59 IHCDLKPENIVLYQRGQVtvKVIDFG---------------------------SSCYEHQKVYTYIQSRF---------- 101
Cdd:cd05628   123 IHRDIKPDNLLLDSKGHV--KLSDFGlctglkkahrtefyrnlnhslpsdftfQNMNSKRKAETWKRNRRqlafstvgtp 200
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 102 -YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIM---EVLGLPP 156
Cdd:cd05628   201 dYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMnwkETLIFPP 259
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
51-150 5.37e-07

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: 50.03  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  51 HMlYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCY--EHQKVYTYIQSRFYRSPEVI-----LGHPynmaIDMWSLG 123
Cdd:cd14075   116 HM-HENNIIHRDLKAENVFYASNNC--VKVGDFGFSTHakRGETLNTFCGSPPYAAPELFkdehyIGIY----VDIWALG 188
                          90       100
                  ....*....|....*....|....*...
gi 1907169597 124 CIMAELYTGYPLFPGENeVEQL-ACIME 150
Cdd:cd14075   189 VLLYFMVTGVMPFRAET-VAKLkKCILE 215
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
50-149 6.60e-07

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: 50.78  E-value: 6.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEHQKVYTyIQSRF------YRSPEVI------LGHpYNMAI 117
Cdd:cd05624   186 IHSIHQLHYVHRDIKPDNVLLDMNGHI--RLADFGS-CLKMNDDGT-VQSSVavgtpdYISPEILqamedgMGK-YGPEC 260
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907169597 118 DMWSLGCIMAELYTGYPLFPGENEVEQLACIM 149
Cdd:cd05624   261 DWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
25-237 6.62e-07

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: 50.25  E-value: 6.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  25 LMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSSCYEHQK----VYTYIQSR 100
Cdd:cd08226    89 LLKTYFPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMVTNGQrskvVYDFPQFS 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 101 F----YRSPEVILG--HPYNMAIDMWSLGCIMAELYTGYPLFPGENEVEQL------ACIMEVLGLPPAHFTQTASRRQV 168
Cdd:cd08226   169 TsvlpWLSPELLRQdlHGYNVKSDIYSVGITACELARGQVPFQDMRRTQMLlqklkgPPYSPLDIFPFPELESRMKNSQS 248
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597 169 FFDSkGLPKNINNNRGGKRYPDSKDLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEPRK 237
Cdd:cd08226   249 GMDS-GIGESVATSSMTRTMTSERLQTPSSKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVKE 316
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
38-138 6.98e-07

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: 50.03  E-value: 6.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  38 IVRRFTFSILKCLHMLYVEKI---IHCDLKPENIVLYQRGQ------VTVKVIDFGSSCYEHQKVYTYIQSRF-YRSPEV 107
Cdd:cd14147   102 VLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIEnddmehKTLKITDFGLAREWHKTTQMSAAGTYaWMAPEV 181
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907169597 108 ILGHPYNMAIDMWSLGCIMAELYTGYPLFPG 138
Cdd:cd14147   182 IKASTFSKGSDVWSFGVLLWELLTGEVPYRG 212
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
58-136 8.42e-07

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 49.98  E-value: 8.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597  58 IIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLF 136
Cdd:PTZ00426  152 IVYRDLKPENLLLDKDG--FIKMTDFGFAKVVDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
19-131 8.99e-07

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: 49.36  E-value: 8.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  19 GINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG------SSCyehQK 92
Cdd:cd08223    84 GGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSN--IIKVGDLGiarvleSSS---DM 158
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907169597  93 VYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYT 131
Cdd:cd08223   159 ATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMAT 197
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
50-132 9.10e-07

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: 49.65  E-value: 9.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQR------GQVTVKVIDFGSSCYEHQKVYTYIQSRF-YRSPEVILGHPYNMAIDMWSL 122
Cdd:cd14146   118 LHEEAVVPILHRDLKSSNILLLEKiehddiCNKTLKITDFGLAREWHRTTKMSAAGTYaWMAPEVIKSSLFSKGSDIWSY 197
                          90
                  ....*....|
gi 1907169597 123 GCIMAELYTG 132
Cdd:cd14146   198 GVLLWELLTG 207
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
1-168 9.41e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 49.87  E-value: 9.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELLGINLYELMKNNSFHgfnLSIVRRFTF--SILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTV 78
Cdd:PHA03209  122 MKDTLVSGAITCMVLPHYSSDLYTYLTKRSRP---LPIDQALIIekQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCI 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KviDFGSScyehqkVYTYIQSRFY--------RSPEVILGHPYNMAIDMWSLGCIMAELyTGYP--LF---------PGE 139
Cdd:PHA03209  199 G--DLGAA------QFPVVAPAFLglagtvetNAPEVLARDKYNSKADIWSAGIVLFEM-LAYPstIFedppstpeeYVK 269
                         170       180
                  ....*....|....*....|....*....
gi 1907169597 140 NEVEQLACIMEVLGLPPAHFTQTASRRQV 168
Cdd:PHA03209  270 SCHSHLLKIISTLKVHPEEFPRDPGSRLV 298
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
39-145 1.34e-06

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: 48.92  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGsscyehqkVYTYIQSRF--------YRSPEVILG 110
Cdd:cd13997   105 VWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKG--TCKIGDFG--------LATRLETSGdveegdsrYLAPELLNE 174
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907169597 111 HP-YNMAIDMWSLGCIMAELYTGYPLFPGENEVEQL 145
Cdd:cd13997   175 NYtHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQL 210
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
40-136 1.44e-06

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: 49.25  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEH----QKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd05617   119 RFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHI--KLTDYGM-CKEGlgpgDTTSTFCGTPNYIAPEILRGEEYGF 195
                          90       100
                  ....*....|....*....|.
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLF 136
Cdd:cd05617   196 SVDWWALGVLMFEMMAGRSPF 216
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
50-155 1.46e-06

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 48.89  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQR------GQVTVKVIDFGSSCYEHQKVYTYIQSRF-YRSPEVILGHPYNMAIDMWSL 122
Cdd:cd14145   120 LHCEAIVPVIHRDLKSSNILILEKvengdlSNKILKITDFGLAREWHRTTKMSAAGTYaWMAPEVIRSSMFSKGSDVWSY 199
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907169597 123 GCIMAELYTGYPLFPGeneVEQLA----CIMEVLGLP 155
Cdd:cd14145   200 GVLLWELLTGEVPFRG---IDGLAvaygVAMNKLSLP 233
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
45-232 1.50e-06

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: 49.24  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMLYVEKIIHCDLKPENIvLY--QRGQV-TVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYNMAID 118
Cdd:cd14178   105 TITKTVEYLHSQGVVHRDLKPSNI-LYmdESGNPeSIRICDFGFAKQlraENGLLMTPCYTANFVAPEVLKRQGYDAACD 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 119 MWSLGCIMAELYTGYPLF---PGENEVEQLACImevlglppahftqtasrrqvffdskglpkninnnrGGKRYpdskdlT 195
Cdd:cd14178   184 IWSLGILLYTMLAGFTPFangPDDTPEEILARI-----------------------------------GSGKY------A 222
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907169597 196 MVVKTYDS---SFLDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14178   223 LSGGNWDSisdAAKDIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
42-126 1.52e-06

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: 49.09  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQ-RGQVTVKVIDFGSS--C-------YEHQKVYTYIQSR-----FYRSPE 106
Cdd:cd13977   139 FMLQLSSALAFLHRNQIVHRDLKPDNILISHkRGEPILKVADFGLSkvCsgsglnpEEPANVNKHFLSSacgsdFYMAPE 218
                          90       100
                  ....*....|....*....|
gi 1907169597 107 VILGHpYNMAIDMWSLGCIM 126
Cdd:cd13977   219 VWEGH-YTAKADIFALGIII 237
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
57-136 1.76e-06

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: 48.86  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  57 KIIHCDLKPENIVLYQRGQVtvKVIDFGSSC------YEHQKVYTYIQSRF--------YRSPEVILGHPYNMAIDMWSL 122
Cdd:cd14011   135 KLVHGNICPESVVINSNGEW--KLAGFDFCIsseqatDQFPYFREYDPNLPplaqpnlnYLAPEYILSKTCDPASDMFSL 212
                          90
                  ....*....|....*
gi 1907169597 123 GCIMAELY-TGYPLF 136
Cdd:cd14011   213 GVLIYAIYnKGKPLF 227
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
45-137 2.23e-06

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: 48.56  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  45 SILKCLHMlyvEKIIHCDLKPENIVLYQRGQvTVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPY-NMAIDMW 120
Cdd:cd13974   143 RVVEALHK---KNIVHRDLKLGNMVLNKRTR-KITITNFCLGKHlvsEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMW 218
                          90
                  ....*....|....*...
gi 1907169597 121 SLGCImaeLYTG-YPLFP 137
Cdd:cd13974   219 ALGVV---LFTMlYGQFP 233
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
39-129 2.43e-06

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 48.49  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKV---YTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd08229   130 VWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG--VVKLGDLGLGRFFSSKTtaaHSLVGTPYYMSPERIHENGYNF 207
                          90
                  ....*....|....
gi 1907169597 116 AIDMWSLGCIMAEL 129
Cdd:cd08229   208 KSDIWSLGCLLYEM 221
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
58-142 2.59e-06

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: 48.33  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  58 IIHCDLKPENIVLYQRGQ-VTVKVIDFGSSCYEHQK---VYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGY 133
Cdd:cd14180   122 VVHRDLKPENILYADESDgAVLKVIDFGFARLRPQGsrpLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQ 201

                  ....*....
gi 1907169597 134 PLFPGENEV 142
Cdd:cd14180   202 VPFQSKRGK 210
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
35-134 2.71e-06

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 47.99  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  35 NLSIVRRFTFSILKCLHMLYVEK--IIHCDLKPENI-VLYQRGQvtVKVIDFGSSCY-EHQKVYTYIQSRFYRSPEVILG 110
Cdd:cd13983   100 KLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIfINGNTGE--VKIGDLGLATLlRQSFAKSVIGTPEFMAPEMYEE 177
                          90       100
                  ....*....|....*....|....*
gi 1907169597 111 HpYNMAIDMWSLGCIMAELYTG-YP 134
Cdd:cd13983   178 H-YDEKVDIYAFGMCLLEMATGeYP 201
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
12-97 2.84e-06

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: 47.84  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  12 CITFELLGINLYELMKNNSfhgfnlsivRRFTF-----------SILKCLHMlyvEKIIHCDLKPENIVL-YQRGQVTVK 79
Cdd:cd14016    72 VMVMDLLGPSLEDLFNKCG---------RKFSLktvlmladqmiSRLEYLHS---KGYIHRDIKPENFLMgLGKNSNKVY 139
                          90
                  ....*....|....*....
gi 1907169597  80 VIDFG-SSCYEHQKVYTYI 97
Cdd:cd14016   140 LIDFGlAKKYRDPRTGKHI 158
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
49-146 2.97e-06

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: 47.83  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  49 CLHMLYVEK--IIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYTYIQ-SRF---YRSPEVILGHPYNMAIDMWSL 122
Cdd:cd05059   110 CEAMEYLESngFIHRDLAARNCLVGEQN--VVKVSDFGLARYVLDDEYTSSVgTKFpvkWSPPEVFMYSKFSSKSDVWSF 187
                          90       100
                  ....*....|....*....|....*...
gi 1907169597 123 GCIMAELYTG----YPLFPGENEVEQLA 146
Cdd:cd05059   188 GVLMWEVFSEgkmpYERFSNSEVVEHIS 215
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
50-140 3.17e-06

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: 48.34  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQVTvkVIDFGSS---CYEHQKVYTYIQSRFYRSPEVILGHP-YNMAIDMWSLGCI 125
Cdd:cd05586   109 LEHLHKNDIVYRDLKPENILLDANGHIA--LCDFGLSkadLTDNKTTNTFCGTTEYLAPEVLLDEKgYTKMVDFWSLGVL 186
                          90
                  ....*....|....*
gi 1907169597 126 MAELYTGYPLFPGEN 140
Cdd:cd05586   187 VFEMCCGWSPFYAED 201
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
50-150 3.58e-06

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 48.11  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHML-YVekiiHCDLKPENIVLYQRGQVtvKVIDFGSsCYEHQKVYTyIQSRF------YRSPEVIL----GH-PYNMAI 117
Cdd:cd05597   118 IHQLgYV----HRDIKPDNVLLDRNGHI--RLADFGS-CLKLREDGT-VQSSVavgtpdYISPEILQamedGKgRYGPEC 189
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907169597 118 DMWSLGCIMAELYTGYPLFPGENEVEQLACIME 150
Cdd:cd05597   190 DWWSLGVCMYEMLYGETPFYAESLVETYGKIMN 222
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
42-147 3.69e-06

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 48.05  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSScyehQKVYT---YIQ---SRF---YRSPEVILGHP 112
Cdd:cd05103   184 YSFQVAKGMEFLASRKCIHRDLAARNILLSENN--VVKICDFGLA----RDIYKdpdYVRkgdARLplkWMAPETIFDRV 257
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907169597 113 YNMAIDMWSLGCIMAELYT-GYPLFPGENEVEQLAC 147
Cdd:cd05103   258 YTIQSDVWSFGVLLWEIFSlGASPYPGVKIDEEFCR 293
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
21-159 4.23e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 48.15  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  21 NLYELMKNNSFHGFN---LSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKviDFGSSC-YEHQKV--- 93
Cdd:PHA03210  248 DLYSFMYDEAFDWKDrplLKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLG--DFGTAMpFEKEREafd 325
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  94 YTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTgYPLFP----GENEVEQLACIMEVLGLPPAHF 159
Cdd:PHA03210  326 YGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLS-HDFCPigdgGGKPGKQLLKIIDSLSVCDEEF 394
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
9-232 4.34e-06

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 47.35  E-value: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELLgiNLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCY 88
Cdd:cd14118    89 DNLYMVFELV--DKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGH--VKIADFGVSNE 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  89 EH---QKVYTYIQSRFYRSPEVILGHPYNM---AIDMWSLGCIMAELYTGYPLFPGENeveqlacIMevlglppahftqt 162
Cdd:cd14118   165 FEgddALLSSTAGTPAFMAPEALSESRKKFsgkALDIWAMGVTLYCFVFGRCPFEDDH-------IL------------- 224
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 163 asrrqvffdskGLPKNINNNRggKRYPDSKDLTMVVKtydssflDFLRRCLVWEPSLRMTPEQALKHAWI 232
Cdd:cd14118   225 -----------GLHEKIKTDP--VVFPDDPVVSEQLK-------DLILRMLDKNPSERITLPEIKEHPWV 274
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
58-128 5.24e-06

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: 47.42  E-value: 5.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597  58 IIHCDLKPENIVLYQRGqvTVKVIDFG-SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAE 128
Cdd:cd14052   127 FVHLDLKPANVLITFEG--TLKIGDFGmATVWPLIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
46-152 6.56e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 47.58  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFGSSCYehqkVYTYIQSRFY---------RSPEVILGHPYNMA 116
Cdd:PHA03211  269 LLSAIDYIHGEGIIHRDIKTENVLV--NGPEDICLGDFGAACF----ARGSWSTPFHygiagtvdtNAPEVLAGDPYTPS 342
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907169597 117 IDMWSLGCIMAE--LYTGyPLFPGENEVEQLACIMEVL 152
Cdd:PHA03211  343 VDIWSAGLVIFEaaVHTA-SLFSASRGDERRPYDAQIL 379
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
21-222 7.00e-06

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: 46.85  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  21 NLYELMKNNSFHgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG--SSCYEHQKVYTYIQ 98
Cdd:cd05079    94 SLKEYLPRNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQV--KIGDFGltKAIETDKEYYTVKD 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  99 SR----FYRSPEVILGHPYNMAIDMWSLGCIMAELYTgYplfpGENEVEQLACIMEVLGlpPAHFTQTASRRqvffdskg 174
Cdd:cd05079   171 DLdspvFWYAPECLIQSKFYIASDVWSFGVTLYELLT-Y----CDSESSPMTLFLKMIG--PTHGQMTVTRL-------- 235
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907169597 175 lpknINNNRGGKRYPDSKDLTmvvktydSSFLDFLRRCLVWEPSLRMT 222
Cdd:cd05079   236 ----VRVLEEGKRLPRPPNCP-------EEVYQLMRKCWEFQPSKRTT 272
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
40-136 7.42e-06

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 47.03  E-value: 7.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEHQK----VYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd05588    99 RFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHI--KLTDYGM-CKEGLRpgdtTSTFCGTPNYIAPEILRGEDYGF 175
                          90       100
                  ....*....|....*....|.
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLF 136
Cdd:cd05588   176 SVDWWALGVLMFEMLAGRSPF 196
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
42-138 7.72e-06

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 46.92  E-value: 7.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG--SSCYEHQKVYTYIQSRF---YRSPEVILGHPYNMA 116
Cdd:cd14207   185 YSFQVARGMEFLSSRKCIHRDLAARNILLSENN--VVKICDFGlaRDIYKNPDYVRKGDARLplkWMAPESIFDKIYSTK 262
                          90       100
                  ....*....|....*....|...
gi 1907169597 117 IDMWSLGCIMAELYT-GYPLFPG 138
Cdd:cd14207   263 SDVWSYGVLLWEIFSlGASPYPG 285
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
46-166 8.08e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 47.15  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKviDFGSSCY--EHQ---KVYTYIQSRFYRSPEVILGHPYNMAIDMW 120
Cdd:PHA03207  194 LLEALAYLHGRGIIHRDVKTENIFLDEPENAVLG--DFGAACKldAHPdtpQCYGWSGTLETNSPELLALDPYCAKTDIW 271
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907169597 121 SLGCIMAELYT-GYPLFPGENEV--EQLACIMEVLGLPPAHFTQTASRR 166
Cdd:PHA03207  272 SAGLVLFEMSVkNVTLFGKQVKSssSQLRSIIRCMQVHPLEFPQNGSTN 320
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
8-161 9.32e-06

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: 46.53  E-value: 9.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCItfellgINLYELMKNNS-------FHGFNLSIVRRFTFSILKCLHMLY--VEKIIHCDLKPENIVLyQRGQVTV 78
Cdd:cd14033    74 RGHKCI------ILVTELMTSGTlktylkrFREMKLKLLQRWSRQILKGLHFLHsrCPPILHRDLKCDNIFI-TGPTGSV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  79 KVIDFGSSCYEHQK-VYTYIQSRFYRSPEvILGHPYNMAIDMWSLGCIMAELYTG-YPLFPGENEVEQLACIMEvlGLPP 156
Cdd:cd14033   147 KIGDLGLATLKRASfAKSVIGTPEFMAPE-MYEEKYDEAVDVYAFGMCILEMATSeYPYSECQNAAQIYRKVTS--GIKP 223

                  ....*
gi 1907169597 157 AHFTQ 161
Cdd:cd14033   224 DSFYK 228
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
24-146 1.06e-05

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: 46.41  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  24 ELMKNNSFHGFNLSIVRRFTFSIL------KCLHMLYVE--KIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYT 95
Cdd:cd05113    79 EYMANGCLLNYLREMRKRFQTQQLlemckdVCEAMEYLEskQFLHRDLAARNCLVNDQG--VVKVSDFGLSRYVLDDEYT 156
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169597  96 Y-IQSRF---YRSPEVILGHPYNMAIDMWSLGCIMAELYT----GYPLFPGENEVEQLA 146
Cdd:cd05113   157 SsVGSKFpvrWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlgkmPYERFTNSETVEHVS 215
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
33-132 1.21e-05

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: 46.10  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  33 GFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIV---LYQRGQVTVKVIDFGSSCY-EHQKVYTYIQSRFYRSPEVI 108
Cdd:cd14068    82 SLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLlftLYPNCAIIAKIADYGIAQYcCRMGIKTSEGTPGFRAPEVA 161
                          90       100
                  ....*....|....*....|....*
gi 1907169597 109 LGH-PYNMAIDMWSLGCIMAELYTG 132
Cdd:cd14068   162 RGNvIYNQQADVYSFGLLLYDILTC 186
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
46-169 1.27e-05

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: 46.02  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCY-----EHQKVYTYIQS----------RFYRSPEVILG 110
Cdd:cd14048   127 IASAVEYLHSKGLIHRDLKPSNVFFSLDD--VVKVGDFGLVTAmdqgePEQTVLTPMPAyakhtgqvgtRLYMSPEQIHG 204
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 111 HPYNMAIDMWSLGCIMAELytgypLFPGENEVEQLACIMEVLGLP-PAHFTQTASRRQVF 169
Cdd:cd14048   205 NQYSEKVDIFALGLILFEL-----IYSFSTQMERIRTLTDVRKLKfPALFTNKYPEERDM 259
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
43-129 1.34e-05

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: 46.17  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  43 TFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYeHQKVYTYIQSRFYRSPEVILGH---PYNMAIDM 119
Cdd:cd06634   121 THGALQGLAYLHSHNMIHRDVKAGNILLTEPGL--VKLGDFGSASI-MAPANSFVGTPYWMAPEVILAMdegQYDGKVDV 197
                          90
                  ....*....|
gi 1907169597 120 WSLGCIMAEL 129
Cdd:cd06634   198 WSLGITCIEL 207
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
39-139 1.34e-05

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: 45.78  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFGSScyehQKVYTYIQSRF----YRSPEV---ILGH 111
Cdd:cd13987    93 VKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLT----RRVGSTVKRVSgtipYTAPEVceaKKNE 168
                          90       100       110
                  ....*....|....*....|....*....|
gi 1907169597 112 PY--NMAIDMWSLGCIMAELYTGYplFPGE 139
Cdd:cd13987   169 GFvvDPSIDVWAFGVLLFCCLTGN--FPWE 196
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
52-145 1.47e-05

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: 45.68  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVEKI--IHCDLKPENIVLYQRgqVTVKVIDFGSSCYEHQKVYTYIQ-SRF---YRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd14203   104 MAYIERMnyIHRDLRAANILVGDN--LVCKIADFGLARLIEDNEYTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGIL 181
                          90       100
                  ....*....|....*....|.
gi 1907169597 126 MAELYT-GYPLFPGENEVEQL 145
Cdd:cd14203   182 LTELVTkGRVPYPGMNNREVL 202
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
39-135 1.51e-05

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: 46.00  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAID 118
Cdd:cd05576   115 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGH--IQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETEACD 192
                          90
                  ....*....|....*..
gi 1907169597 119 MWSLGCIMAELYTGYPL 135
Cdd:cd05576   193 WWSLGALLFELLTGKAL 209
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
53-132 1.77e-05

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: 45.78  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  53 LYVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSCYE-----HQKVYTYIQSRFYRSPEVIL---GHPYNMAIDMWSLGC 124
Cdd:cd14150   112 LHAKNIIHRDLKSNNIFLHE--GLTVKIGDFGLATVKtrwsgSQQVEQPSGSILWMAPEVIRmqdTNPYSFQSDVYAYGV 189

                  ....*...
gi 1907169597 125 IMAELYTG 132
Cdd:cd14150   190 VLYELMSG 197
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
53-132 1.90e-05

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


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 45.46  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  53 LYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG--------SSCYEHQKVYTYIqsrFYRSPEVIL---GHPYNMAIDMWS 121
Cdd:cd14062   105 LHAKNIIHRDLKSNNIFLHEDL--TVKIGDFGlatvktrwSGSQQFEQPTGSI---LWMAPEVIRmqdENPYSFQSDVYA 179
                          90
                  ....*....|.
gi 1907169597 122 LGCIMAELYTG 132
Cdd:cd14062   180 FGIVLYELLTG 190
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
19-132 1.92e-05

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: 45.79  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  19 GINLYELM--KNNSFHGFNLSIVRRFTFSILKCLHmlyVEKIIHCDLKPENIVLYQrgQVTVKVIDFGSSCYE-----HQ 91
Cdd:cd14149    91 GSSLYKHLhvQETKFQMFQLIDIARQTAQGMDYLH---AKNIIHRDMKSNNIFLHE--GLTVKIGDFGLATVKsrwsgSQ 165
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907169597  92 KVYTYIQSRFYRSPEVIL---GHPYNMAIDMWSLGCIMAELYTG 132
Cdd:cd14149   166 QVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTG 209
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
47-131 2.02e-05

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: 45.36  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMLYVEKIIHCDLKPENIVLYQRGQVTvkVIDFGSSCyehqKVYTYIQSR----------------FYRSPEviLG 110
Cdd:cd13986   119 LKAMHEPELVPYAHRDIKPGNVLLSEDDEPI--LMDLGSMN----PARIEIEGRrealalqdwaaehctmPYRAPE--LF 190
                          90       100
                  ....*....|....*....|....*.
gi 1907169597 111 HPYNMAI-----DMWSLGCImaeLYT 131
Cdd:cd13986   191 DVKSHCTidektDIWSLGCT---LYA 213
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
49-131 2.15e-05

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: 45.33  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  49 CLHMLYVEK--IIHCDLKPENiVLYQRGQVtVKVIDFGSSCYEHQKVYTYIQ-SRF---YRSPEVILGHPYNMAIDMWSL 122
Cdd:cd05112   110 CEGMAYLEEasVIHRDLAARN-CLVGENQV-VKVSDFGMTRFVLDDQYTSSTgTKFpvkWSSPEVFSFSRYSSKSDVWSF 187

                  ....*....
gi 1907169597 123 GCIMAELYT 131
Cdd:cd05112   188 GVLMWEVFS 196
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
50-155 2.77e-05

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: 44.98  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQ------VTVKVIDFGSSCYEHQKVYTYIQSRF-YRSPEVILGHPYNMAIDMWSL 122
Cdd:cd14148   108 LHNEAIVPIIHRDLKSSNILILEPIEnddlsgKTLKITDFGLAREWHKTTKMSAAGTYaWMAPEVIRLSLFSKSSDVWSF 187
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907169597 123 GCIMAELYTGYPLFpgeNEVEQLA----CIMEVLGLP 155
Cdd:cd14148   188 GVLLWELLTGEVPY---REIDALAvaygVAMNKLTLP 221
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
50-132 2.82e-05

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: 45.01  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  50 LHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFG-SSCYEHQKVYTYIQSRF----YRSPEVILGHPYNMA-IDMWSLG 123
Cdd:cd14069   113 LKYLHSCGITHRDIKPENLLLDENDN--LKISDFGlATVFRYKGKERLLNKMCgtlpYVAPELLAKKKYRAEpVDVWSCG 190

                  ....*....
gi 1907169597 124 CIMAELYTG 132
Cdd:cd14069   191 IVLFAMLAG 199
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
11-135 2.94e-05

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: 44.91  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELLginlYELMKNNSFhgfNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFGSS-CYE 89
Cdd:cd14110    80 LCSGPELL----YNLAERNSY---SEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMII--TEKNLLKIVDLGNAqPFN 150
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907169597  90 HQKVYTYIQSRFY---RSPEVILGHPYNMAIDMWSLGC---IMaeLYTGYPL 135
Cdd:cd14110   151 QGKVLMTDKKGDYvetMAPELLEGQGAGPQTDIWAIGVtafIM--LSADYPV 200
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
40-136 3.30e-05

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 45.41  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  40 RRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFGSsCYEH----QKVYTYIQSRFYRSPEVILGHPYNM 115
Cdd:cd05618   124 RFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHI--KLTDYGM-CKEGlrpgDTTSTFCGTPNYIAPEILRGEDYGF 200
                          90       100
                  ....*....|....*....|.
gi 1907169597 116 AIDMWSLGCIMAELYTGYPLF 136
Cdd:cd05618   201 SVDWWALGVLMFEMMAGRSPF 221
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
27-129 3.39e-05

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: 44.79  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  27 KNNSFHGFNLSIVRRFtFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFG--SSCYEHQKVYTYIQSRFYRS 104
Cdd:cd14047   108 KRNGEKLDKVLALEIF-EQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK--VKIGDFGlvTSLKNDGKRTKSKGTLSYMS 184
                          90       100
                  ....*....|....*....|....*
gi 1907169597 105 PEVILGHPYNMAIDMWSLGCIMAEL 129
Cdd:cd14047   185 PEQISSQDYGKEVDIYALGLILFEL 209
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
34-131 3.60e-05

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: 44.62  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLyqRGQVTVKVIDFG-SSCYEHQKVYTYIQSR-----FYRSPEV 107
Cdd:cd14205   105 IDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILV--ENENRVKIGDFGlTKVLPQDKEYYKVKEPgespiFWYAPES 182
                          90       100
                  ....*....|....*....|....
gi 1907169597 108 ILGHPYNMAIDMWSLGCIMAELYT 131
Cdd:cd14205   183 LTESKFSVASDVWSFGVVLYELFT 206
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
42-131 3.66e-05

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: 44.61  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYTYIQ---SRfYRSPEVILGHpYNMAID 118
Cdd:cd14050   105 ILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDG--VCKLGDFGLVVELDKEDIHDAQegdPR-YMAPELLQGS-FTKAAD 180
                          90
                  ....*....|...
gi 1907169597 119 MWSLGCIMAELYT 131
Cdd:cd14050   181 IFSLGITILELAC 193
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
47-132 4.14e-05

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 44.42  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  47 LKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVkVIDFGSSCYEH-----QKVYT--YIQ-SRFYRSPEVILGHPYNMAID 118
Cdd:cd13991   108 LEGLEYLHSRKILHGDVKADNVLLSSDGSDAF-LCDFGHAECLDpdglgKSLFTgdYIPgTETHMAPEVVLGKPCDAKVD 186
                          90
                  ....*....|....
gi 1907169597 119 MWSLGCIMAELYTG 132
Cdd:cd13991   187 VWSSCCMMLHMLNG 200
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
27-144 4.29e-05

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: 44.42  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  27 KNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvTVKVIDFGSSC----YEHQKVYTYIQSR-- 100
Cdd:cd14049   110 KSAPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDI-HVRIGDFGLACpdilQDGNDSTTMSRLNgl 188
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907169597 101 ---------FYRSPEVILGHPYNMAIDMWSLGCIMAELYTgyplfPGENEVEQ 144
Cdd:cd14049   189 thtsgvgtcLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ-----PFGTEMER 236
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
24-134 4.67e-05

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: 44.36  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  24 ELMKNNSFHGF------NLSIVRRFTFSILKCLHMLYVEK--IIHCDLKPENIVLYQRGQVtvKVIDFGSSCYEHQKVYT 95
Cdd:cd05041    73 ELVPGGSLLTFlrkkgaRLTVKQLLQMCLDAAAGMEYLESknCIHRDLAARNCLVGENNVL--KISDFGMSREEEDGEYT 150
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907169597  96 yIQSRF------YRSPEVILGHPYNMAIDMWSLGCIMAELYTG----YP 134
Cdd:cd05041   151 -VSDGLkqipikWTAPEALNYGRYTSESDVWSFGILLWEIFSLgatpYP 198
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
19-129 5.50e-05

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: 44.00  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  19 GINLYELMKNNSFHGFNLSIvrRFTFSILKCLHMLYVEKIIHCDLKPEN-IVLYQRGQVTVKVIDFG------SSCYEHQ 91
Cdd:cd14155    72 GGNLEQLLDSNEPLSWTVRV--KLALDIARGLSYLHSKGIFHRDLTSKNcLIKRDENGYTAVVGDFGlaekipDYSDGKE 149
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907169597  92 KVYTyIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAEL 129
Cdd:cd14155   150 KLAV-VGSPYWMAPEVLRGEPYNEKADVFSYGIILCEI 186
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
13-129 5.76e-05

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: 44.02  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  13 ITFELLGINLYELMKNnsfHGFNLSIVRRFTFS--ILKCLHMLYVEKIIHCDLKPEN-IVLYQRGQVTVKVIDFG----- 84
Cdd:cd14065    66 ITEYVNGGTLEELLKS---MDEQLPWSQRVSLAkdIASGMAYLHSKNIIHRDLNSKNcLVREANRGRNAVVADFGlarem 142
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907169597  85 ----SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAEL 129
Cdd:cd14065   143 pdekTKKPDRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEI 191
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
44-137 6.43e-05

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: 43.88  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  44 FSILKCLHMLYVE--KIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYTyiqSRF---YRSPEVILGHPYNMAID 118
Cdd:cd05039   107 FALDVCEGMEYLEskKFVHRDLAARNVLVSEDN--VAKVSDFGLAKEASSNQDG---GKLpikWTAPEALREKKFSTKSD 181
                          90       100
                  ....*....|....*....|...
gi 1907169597 119 MWSLGCIMAELYT----GYPLFP 137
Cdd:cd05039   182 VWSFGILLWEIYSfgrvPYPRIP 204
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
35-182 6.87e-05

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: 43.80  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  35 NLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQrGQVtVKVIDFGSS--CYEHQKVYTYIQSRF---YRSPEVIL 109
Cdd:cd05045   125 TMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAE-GRK-MKISDFGLSrdVYEEDSYVKRSKGRIpvkWMAIESLF 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 110 GHPYNMAIDMWSLGCIMAELYT----GYPLFPGENEVEQLA----------CIMEVLGLPPAHFTQTASRRQVFFD-SKG 174
Cdd:cd05045   203 DHIYTTQSDVWSFGVLLWEIVTlggnPYPGIAPERLFNLLKtgyrmerpenCSEEMYNLMLTCWKQEPDKRPTFADiSKE 282

                  ....*...
gi 1907169597 175 LPKNINNN 182
Cdd:cd05045   283 LEKMMVKS 290
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
13-84 7.18e-05

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 43.79  E-value: 7.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169597  13 ITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQV--TVKVIDFG 84
Cdd:cd14017    73 IVMTLLGPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDerTVYILDFG 146
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
59-149 8.02e-05

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: 44.24  E-value: 8.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  59 IHCDLKPENIVLYQRGQVtvKVIDFGSsCYEHQKVYTyIQSRF------YRSPEVILGHP-----YNMAIDMWSLGCIMA 127
Cdd:cd05623   195 VHRDIKPDNILMDMNGHI--RLADFGS-CLKLMEDGT-VQSSVavgtpdYISPEILQAMEdgkgkYGPECDWWSLGVCMY 270
                          90       100
                  ....*....|....*....|..
gi 1907169597 128 ELYTGYPLFPGENEVEQLACIM 149
Cdd:cd05623   271 EMLYGETPFYAESLVETYGKIM 292
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
22-138 8.25e-05

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: 43.68  E-value: 8.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  22 LYELMKNNSFHGF--------------NLSIVRRFTFSILKCLHMLYVE--KIIHCDLKPENIVLYQRGqvTVKVIDFGS 85
Cdd:cd00192    74 VMEYMEGGDLLDFlrksrpvfpspepsTLSLKDLLSFAIQIAKGMEYLAskKFVHRDLAARNCLVGEDL--VVKISDFGL 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  86 SCYEHQKVYTYIQSRF-----YRSPEVILGHPYNMAIDMWSLGCIMAELYT--GYPlFPG 138
Cdd:cd00192   152 SRDIYDDDYYRKKTGGklpirWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlgATP-YPG 210
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
22-137 9.55e-05

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: 43.52  E-value: 9.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  22 LYELMKNNSFHGF----------NLSIVRRFTFSILKCLHMLYV-------------EKIIHCDLKPENIVLYQRgqVTV 78
Cdd:cd05048    86 LFEYMAHGDLHEFlvrhsphsdvGVSSDDDGTASSLDQSDFLHIaiqiaagmeylssHHYVHRDLAARNCLVGDG--LTV 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907169597  79 KVIDFGSS--CYEHQkvYTYIQSRF-----YRSPEVILGHPYNMAIDMWSLGCIMAELYTgYPLFP 137
Cdd:cd05048   164 KISDFGLSrdIYSSD--YYRVQSKSllpvrWMPPEAILYGKFTTESDVWSFGVVLWEIFS-YGLQP 226
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
10-135 1.00e-04

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: 43.44  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  10 HLCITFELL-GINLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFG--SS 86
Cdd:cd14665    70 HLAIVMEYAaGGELFERICNAG--RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGysKS 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907169597  87 CYEHQKVYTYIQSRFYRSPEVILGHPYNMAI-DMWSLGCIMAELYTG-YPL 135
Cdd:cd14665   148 SVLHSQPKSTVGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGaYPF 198
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
53-153 1.03e-04

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: 43.51  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  53 LYVEKIIHCDLKPENIVLYQrgQVTVKVIDFG--------SSCYEHQKVYTYIqsrFYRSPEVIL---GHPYNMAIDMWS 121
Cdd:cd14151   120 LHAKSIIHRDLKSNNIFLHE--DLTVKIGDFGlatvksrwSGSHQFEQLSGSI---LWMAPEVIRmqdKNPYSFQSDVYA 194
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907169597 122 LGCIMAELYTGYPLFPGENEVEQlacIMEVLG 153
Cdd:cd14151   195 FGIVLYELMTGQLPYSNINNRDQ---IIFMVG 223
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
7-231 1.03e-04

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: 43.01  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   7 FRNH----LCITFELLGINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVID 82
Cdd:cd14119    63 LYNEekqkLYMVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDG--TLKISD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  83 FG----SSCYEHQKVYTYIQ-SRFYRSPEVILGHPY--NMAIDMWSLGCIMAELYTG-YPlFPGENeveqlacIMEvlgl 154
Cdd:cd14119   141 FGvaeaLDLFAEDDTCTTSQgSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGkYP-FEGDN-------IYK---- 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169597 155 ppahftqtasrrqvffdskgLPKNINNNrggkrypdskDLTMvVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAW 231
Cdd:cd14119   209 --------------------LFENIGKG----------EYTI-PDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQHPW 254
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
42-138 1.90e-04

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 42.66  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSScyehQKVYT---YIQSRFYR------SPEVILGHP 112
Cdd:cd05102   177 YSFQVARGMEFLASRKCIHRDLAARNILLSENN--VVKICDFGLA----RDIYKdpdYVRKGSARlplkwmAPESIFDKV 250
                          90       100
                  ....*....|....*....|....*..
gi 1907169597 113 YNMAIDMWSLGCIMAELYT-GYPLFPG 138
Cdd:cd05102   251 YTTQSDVWSFGVLLWEIFSlGASPYPG 277
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
42-137 1.98e-04

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 42.69  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENiVLYQRGQVtVKVIDFG-SSCYEHQKVYTYIQSRF----YRSPEVILGHPYNMA 116
Cdd:cd05107   244 FSYQVANGMEFLASKNCVHRDLAARN-VLICEGKL-VKICDFGlARDIMRDSNYISKGSTFlplkWMAPESIFNNLYTTL 321
                          90       100
                  ....*....|....*....|....*
gi 1907169597 117 IDMWSLGCIMAELY----TGYPLFP 137
Cdd:cd05107   322 SDVWSFGILLWEIFtlggTPYPELP 346
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
24-138 2.18e-04

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 42.10  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  24 ELMKNNSFHGF------NLSIVRRFTFSILKCLHMLYVE--KIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYT 95
Cdd:pfam07714  81 EYMPGGDLLDFlrkhkrKLTLKDLLSMALQIAKGMEYLEskNFVHRDLAARNCLVSENL--VVKISDFGLSRDIYDDDYY 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907169597  96 YIQSR-----FYRSPEVILGHPYNMAIDMWSLGCIMAELYT-GYPLFPG 138
Cdd:pfam07714 159 RKRGGgklpiKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPG 207
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
49-131 2.30e-04

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: 42.19  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  49 CLHMLYV--EKIIHCDLKPENIVLYQRGQVtvKVIDFG-SSCYEHQKVYTYIQSR-----FYRSPEVILGHPYNMAIDMW 120
Cdd:cd05081   118 CKGMEYLgsRRCVHRDLAARNILVESEAHV--KIADFGlAKLLPLDKDYYVVREPgqspiFWYAPESLSDNIFSRQSDVW 195
                          90
                  ....*....|.
gi 1907169597 121 SLGCIMAELYT 131
Cdd:cd05081   196 SFGVVLYELFT 206
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
39-84 2.68e-04

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: 40.50  E-value: 2.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907169597  39 VRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG 84
Cdd:cd13968    93 VESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDG--NVKLIDFG 136
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
9-123 3.47e-04

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: 41.87  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELlgINLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFG-SSC 87
Cdd:cd14199   100 DHLYMVFEL--VKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGH--IKIADFGvSNE 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907169597  88 YEHQKVY--TYIQSRFYRSPEVILGHPYNM---AIDMWSLG 123
Cdd:cd14199   176 FEGSDALltNTVGTPAFMAPETLSETRKIFsgkALDVWAMG 216
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
38-86 3.85e-04

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 42.09  E-value: 3.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907169597  38 IVRRFTFSILKCLHMLYVEKIIHCDLKPENIvLYQRGQVTVKVIDFGSS 86
Cdd:PLN03225  256 IIQTIMRQILFALDGLHSTGIVHRDVKPQNI-IFSEGSGSFKIIDLGAA 303
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
22-131 4.08e-04

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: 41.54  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  22 LYELMKNNS-----FHGFNLSIVRRFTFsilkcLHM-------LYVEKIIHCDLKPENIVLyqRGQVTVKVIDFGSSC-Y 88
Cdd:cd14053    80 LCDYLKGNViswneLCKIAESMARGLAY-----LHEdipatngGHKPSIAHRDFKSKNVLL--KSDLTACIADFGLALkF 152
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907169597  89 EHQKVY--TYIQ--SRFYRSPEVILGhPYN------MAIDMWSLGCIMAELYT 131
Cdd:cd14053   153 EPGKSCgdTHGQvgTRRYMAPEVLEG-AINftrdafLRIDMYAMGLVLWELLS 204
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
49-131 4.11e-04

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: 41.39  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  49 CLHMLYVEK--IIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYTY-IQSRF---YRSPEVILGHPYNMAIDMWSL 122
Cdd:cd05114   110 CEGMEYLERnnFIHRDLAARNCLVNDTG--VVKVSDFGMTRYVLDDQYTSsSGAKFpvkWSPPEVFNYSKFSSKSDVWSF 187

                  ....*....
gi 1907169597 123 GCIMAELYT 131
Cdd:cd05114   188 GVLMWEVFT 196
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
52-145 4.32e-04

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: 41.59  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVEKI--IHCDLKPENIVLyqRGQVTVKVIDFGSSCYEHQKVYTYIQ-SRF---YRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05070   118 MAYIERMnyIHRDLRSANILV--GNGLICKIADFGLARLIEDNEYTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGIL 195
                          90       100
                  ....*....|....*....|.
gi 1907169597 126 MAELYT-GYPLFPGENEVEQL 145
Cdd:cd05070   196 LTELVTkGRVPYPGMNNREVL 216
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
59-149 4.33e-04

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: 41.59  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  59 IHCDLKPENIVLYQRGQVtvKVIDFGSsCY---EHQKVY--TYIQSRFYRSPEVIL--GHP--YNMAIDMWSLGCIMAEL 129
Cdd:cd05596   147 VHRDVKPDNMLLDASGHL--KLADFGT-CMkmdKDGLVRsdTAVGTPDYISPEVLKsqGGDgvYGRECDWWSVGVFLYEM 223
                          90       100
                  ....*....|....*....|
gi 1907169597 130 YTGYPLFPGENEVEQLACIM 149
Cdd:cd05596   224 LVGDTPFYADSLVGTYGKIM 243
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
21-155 4.82e-04

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: 41.18  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  21 NLYELMKNNSfhGFNLSIVRRFTFSILKCLHMLYVEK--IIHCDLKPENIVLYQrgQVTVKVIDFGSSCYEHQKVYTYIQ 98
Cdd:cd05072    88 SLLDFLKSDE--GGKVLLPKLIDFSAQIAEGMAYIERknYIHRDLRAANVLVSE--SLMCKIADFGLARVIEDNEYTARE 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169597  99 -SRF---YRSPEVILGHPYNMAIDMWSLGCIMAELYT-GYPLFPGENEVEQLACIMEVLGLP 155
Cdd:cd05072   164 gAKFpikWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGYRMP 225
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
42-150 5.15e-04

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: 41.52  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFGSSCYEHQ----KVYTYIQSRFYRSPEVILGHP----Y 113
Cdd:cd05621   156 YTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGH--LKLADFGTCMKMDEtgmvHCDTAVGTPDYISPEVLKSQGgdgyY 233
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907169597 114 NMAIDMWSLGCIMAELYTGYPLFPGENEVEQLACIME 150
Cdd:cd05621   234 GRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMD 270
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
43-138 5.43e-04

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: 41.15  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  43 TFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYtYIQSRFYR------SPEVILGHPYNMA 116
Cdd:cd05101   152 TYQLARGMEYLASQKCIHRDLAARNVLVTENN--VMKIADFGLARDINNIDY-YKKTTNGRlpvkwmAPEALFDRVYTHQ 228
                          90       100
                  ....*....|....*....|....
gi 1907169597 117 IDMWSLGCIMAELYT--GYPlFPG 138
Cdd:cd05101   229 SDVWSFGVLMWEIFTlgGSP-YPG 251
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
34-139 6.24e-04

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 41.02  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  34 FNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG------------------SSCYEHQKVYT 95
Cdd:cd05610   101 FDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHI--KLTDFGlskvtlnrelnmmdilttPSMAKPKNDYS 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  96 YIQSRF--------------------------------------YRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFP 137
Cdd:cd05610   179 RTPGQVlslisslgfntptpyrtpksvrrgaarvegerilgtpdYLAPELLLGKPHGPAVDWWALGVCLFEFLTGIPPFN 258

                  ..
gi 1907169597 138 GE 139
Cdd:cd05610   259 DE 260
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
42-138 7.06e-04

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 40.94  E-value: 7.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFG--SSCYEHQKVYTYIQSRF---YRSPEVILGHPYNMA 116
Cdd:cd05054   143 YSFQVARGMEFLASRKCIHRDLAARNILLSENN--VVKICDFGlaRDIYKDPDYVRKGDARLplkWMAPESIFDKVYTTQ 220
                          90       100
                  ....*....|....*....|...
gi 1907169597 117 IDMWSLGCIMAELYT-GYPLFPG 138
Cdd:cd05054   221 SDVWSFGVLLWEIFSlGASPYPG 243
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
7-131 8.80e-04

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: 40.24  E-value: 8.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   7 FRNHLCITFELLGI-NLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGqvTVKVIDFGS 85
Cdd:cd05083    69 LHNGLYIVMELMSKgNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDG--VAKISDFGL 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907169597  86 SCYEHQKVYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYT 131
Cdd:cd05083   147 AKVGSMGVDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFS 192
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
52-155 1.18e-03

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: 40.11  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVE--KIIHCDLKPENIVLYQrgQVTVKVIDFGSSCYEHQKVYTYIQSRF---YRSPEVILGHPYNMAIDMWSLGCIM 126
Cdd:cd05148   117 MAYLEeqNSIHRDLAARNILVGE--DLVCKVADFGLARLIKEDVYLSSDKKIpykWTAPEAASHGTFSTKSDVWSFGILL 194
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907169597 127 AELYT--GYPlFPGENEVEQLACIMEVLGLP 155
Cdd:cd05148   195 YEMFTygQVP-YPGMNNHEVYDQITAGYRMP 224
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
52-148 1.19e-03

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: 40.08  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVEK--IIHCDLKPENIVLYQRGqvTVKVIDFG-SSCYEHQKVYT-YIQSRF---YRSPEVILGHPYNMAIDMWSLGC 124
Cdd:cd05068   117 MAYLESqnYIHRDLAARNVLVGENN--ICKVADFGlARVIKVEDEYEaREGAKFpikWTAPEAANYNRFSIKSDVWSFGI 194
                          90       100
                  ....*....|....*....|....*
gi 1907169597 125 IMAELYT-GYPLFPGENEVEQLACI 148
Cdd:cd05068   195 LLTEIVTyGRIPYPGMTNAEVLQQV 219
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
52-138 1.19e-03

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: 40.05  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVEKI--IHCDLKPENIVLYQrgQVTVKVIDFGSSCYEHQKVYTYIQ-SRF---YRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05069   121 MAYIERMnyIHRDLRAANILVGD--NLVCKIADFGLARLIEDNEYTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGIL 198
                          90
                  ....*....|....
gi 1907169597 126 MAELYT-GYPLFPG 138
Cdd:cd05069   199 LTELVTkGRVPYPG 212
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
8-131 1.25e-03

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: 40.06  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   8 RNHLCITFELLGI-NLYELMKNNSfHGFNLSIVRRFTFSIlkCLHMLYVE--KIIHCDLKPENIVLYQRGQVtvKVIDFG 84
Cdd:cd05038    80 RRSLRLIMEYLPSgSLRDYLQRHR-DQIDLKRLLLFASQI--CKGMEYLGsqRYIHRDLAARNILVESEDLV--KISDFG 154
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907169597  85 -SSCYEHQKVYTYIQSR-----FYRSPEVILGHPYNMAIDMWSLGCIMAELYT 131
Cdd:cd05038   155 lAKVLPEDKEYYYVKEPgespiFWYAPECLRESRFSSASDVWSFGVTLYELFT 207
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
20-86 1.25e-03

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 40.03  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  20 INLYELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYqRGQVT--------------VKVIDFGS 85
Cdd:cd13981    89 LDVVNKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLR-LEICAdwpgegengwlskgLKLIDFGR 167

                  .
gi 1907169597  86 S 86
Cdd:cd13981   168 S 168
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
52-138 1.39e-03

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: 40.06  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVEKI--IHCDLKPENIVLYQrgQVTVKVIDFGSSCYEHQKVYTYIQ-SRF---YRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05071   118 MAYVERMnyVHRDLRAANILVGE--NLVCKVADFGLARLIEDNEYTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGIL 195
                          90
                  ....*....|....
gi 1907169597 126 MAELYT-GYPLFPG 138
Cdd:cd05071   196 LTELTTkGRVPYPG 209
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
9-123 1.54e-03

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: 39.93  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   9 NHLCITFELLGINlyELMKNNSFHGFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQvtVKVIDFG-SSC 87
Cdd:cd14200    98 DNLYMVFDLLRKG--PVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGH--VKIADFGvSNQ 173
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907169597  88 YE--HQKVYTYIQSRFYRSPEVIL--GHPYN-MAIDMWSLG 123
Cdd:cd14200   174 FEgnDALLSSTAGTPAFMAPETLSdsGQSFSgKALDVWAMG 214
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
52-139 1.59e-03

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: 39.95  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVE--KIIHCDLKPENIVLYQRGqvTVKVIDFGSSCYEHQKVYtYIQSRFYR------SPEVILGHPYNMAIDMWSLG 123
Cdd:cd05099   147 MEYLEsrRCIHRDLAARNVLVTEDN--VMKIADFGLARGVHDIDY-YKKTSNGRlpvkwmAPEALFDRVYTHQSDVWSFG 223
                          90       100
                  ....*....|....*....|
gi 1907169597 124 CIMAELYT----GYPLFPGE 139
Cdd:cd05099   224 ILMWEIFTlggsPYPGIPVE 243
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
11-131 2.03e-03

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 39.30  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  11 LCITFELLGINLYELMKNNSFHG---FNLSIVRRFTFSILKCLHMLYVEK-IIHCDLKPENIVLyqRGQV-TVKVIDFGS 85
Cdd:cd14001    81 LCLAMEYGGKSLNDLIEERYEAGlgpFPAATILKVALSIARALEYLHNEKkILHGDIKSGNVLI--KGDFeSVKLCDFGV 158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597  86 S--------CYEHQKVYtYIQSRFYRSPEVIL-GHPYNMAIDMWSLGCIMAELYT 131
Cdd:cd14001   159 SlpltenleVDSDPKAQ-YVGTEPWKAKEALEeGGVITDKADIFAYGLVLWEMMT 212
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
41-156 2.33e-03

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: 39.64  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  41 RFTFSILKC-LHMLYVEKIIHCDLKPENIVLYQRGQVtvKVIDFG----------------------------------S 85
Cdd:cd05625   104 RFYIAELTCaVESVHKMGFIHRDIKPDNILIDRDGHI--KLTDFGlctgfrwthdskyyqsgdhlrqdsmdfsnewgdpE 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  86 SCY--------------EHQK--VYTYIQSRFYRSPEVILGHPYNMAIDMWSLGCIMAELYTGYPLFPGENEVE-QLACI 148
Cdd:cd05625   182 NCRcgdrlkplerraarQHQRclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLEtQMKVI 261
                         170
                  ....*....|
gi 1907169597 149 --MEVLGLPP 156
Cdd:cd05625   262 nwQTSLHIPP 271
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
52-146 3.29e-03

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


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 38.42  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVEK--IIHCDLKPENIvLYQRGQVtVKVIDFGSSCYEHQKVYTYIQ-SRF---YRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05034   105 MAYLESrnYIHRDLAARNI-LVGENNV-CKVADFGLARLIEDDEYTAREgAKFpikWTAPEAALYGRFTIKSDVWSFGIL 182
                          90       100
                  ....*....|....*....|....*
gi 1907169597 126 MAELYT-G---YPLFPGENEVEQLA 146
Cdd:cd05034   183 LYEIVTyGrvpYPGMTNREVLEQVE 207
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
52-131 4.09e-03

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: 38.48  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVE--KIIHCDLKPENIVLyqRGQVTVKVIDFGSS--CYEHQkvytyiqsrFYR------------SPEVILGHPYNM 115
Cdd:cd05032   132 MAYLAakKFVHRDLAARNCMV--AEDLTVKIGDFGMTrdIYETD---------YYRkggkgllpvrwmAPESLKDGVFTT 200
                          90
                  ....*....|....*.
gi 1907169597 116 AIDMWSLGCIMAELYT 131
Cdd:cd05032   201 KSDVWSFGVVLWEMAT 216
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
41-134 4.17e-03

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: 38.21  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  41 RFTFSILKC-LHMLYVEKIIHCDLKPENIVLYQRGQVTVKVIDFG--SSCYEHQKVYTYIQSRFYRSPEVILGHPYNMAI 117
Cdd:cd14662    99 RYFFQQLISgVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGysKSSVLHSQPKSTVGTPAYIAPEVLSRKEYDGKV 178
                          90
                  ....*....|....*....
gi 1907169597 118 -DMWSLGCIMAELYTG-YP 134
Cdd:cd14662   179 aDVWSCGVTLYVMLVGaYP 197
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
42-138 4.53e-03

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


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 38.73  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  42 FTFSILKCLHMLYVEKIIHCDLKPENIVLYQrGQVTvKVIDFGSScYEHQKVYTYI---QSRF---YRSPEVILGHPYNM 115
Cdd:cd05104   219 FSYQVAKGMEFLASKNCIHRDLAARNILLTH-GRIT-KICDFGLA-RDIRNDSNYVvkgNARLpvkWMAPESIFECVYTF 295
                          90       100
                  ....*....|....*....|....
gi 1907169597 116 AIDMWSLGCIMAELYT-GYPLFPG 138
Cdd:cd05104   296 ESDVWSYGILLWEIFSlGSSPYPG 319
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
57-125 4.83e-03

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: 38.07  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  57 KIIHCDLKPENIVLYQRGQV-TVKVIDFGSS-------------CYEHQKVYTYiqsrFYRSPEVILGHPYNMAI----D 118
Cdd:cd13990   127 PIIHYDLKPGNILLHSGNVSgEIKITDFGLSkimddesynsdgmELTSQGAGTY----WYLPPECFVVGKTPPKIsskvD 202

                  ....*..
gi 1907169597 119 MWSLGCI 125
Cdd:cd13990   203 VWSVGVI 209
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
52-143 5.01e-03

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: 38.08  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  52 MLYVEK--IIHCDLKPENIVLYQrgQVTVKVIDFGSSCYEHQKVYTYIQ-SRF---YRSPEVILGHPYNMAIDMWSLGCI 125
Cdd:cd05073   120 MAFIEQrnYIHRDLRAANILVSA--SLVCKIADFGLARVIEDNEYTAREgAKFpikWTAPEAINFGSFTIKSDVWSFGIL 197
                          90
                  ....*....|....*....
gi 1907169597 126 MAELYT-GYPLFPGENEVE 143
Cdd:cd05073   198 LMEIVTyGRIPYPGMSNPE 216
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
1-232 5.19e-03

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: 38.23  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597   1 MKDFFYFRNHLCITFELL-GINLYELMKNNSFhgFNLSIVRRFTFSILKCLHMLYVEKIIHCDLKPENIVLYQRGQVTVK 79
Cdd:cd14076    71 LLDVLKTKKYIGIVLEFVsGGELFDYILARRR--LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVIT 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  80 viDFG-SSCYEHQK---VYTYIQSRFYRSPE-VILGHPYN-MAIDMWSLGCIMAELYTGY------PLFP-GENEVEQLA 146
Cdd:cd14076   149 --DFGfANTFDHFNgdlMSTSCGSPCYAAPElVVSDSMYAgRKADIWSCGVILYAMLAGYlpfdddPHNPnGDNVPRLYR 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 147 CIMEVLGLPPAHFTqtasrrqvffdskglpkninnnrggkryPDSKDLtmvvktydssfldfLRRCLVWEPSLRMTPEQA 226
Cdd:cd14076   227 YICNTPLIFPEYVT----------------------------PKARDL--------------LRRILVPNPRKRIRLSAI 264

                  ....*.
gi 1907169597 227 LKHAWI 232
Cdd:cd14076   265 MRHAWL 270
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
46-248 5.75e-03

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: 38.00  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597  46 ILKCL----HMLYVekiiHCDLKPENIVLYQRGQVTVKVIDFGSSCYEHQK----VYTY----IQSRFYRSPEVILGH-- 111
Cdd:cd08227   110 VLKALdyihHMGYV----HRSVKASHILISVDGKVYLSGLRSNLSMINHGQrlrvVHDFpkysVKVLPWLSPEVLQQNlq 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169597 112 PYNMAIDMWSLGCIMAELYTGYPLFPG----ENEVEQLA----CIMEVLGLPPAHFTQTASRRQVffdSKGLPKNINNNR 183
Cdd:cd08227   186 GYDAKSDIYSVGITACELANGHVPFKDmpatQMLLEKLNgtvpCLLDTTTIPAEELTMKPSRSGA---NSGLGESTTVST 262
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169597 184 GGKRYPDSKdLTMVVKTYDSSFLDFLRRCLVWEPSLRMTPEQALKHAWIHEPRKFKPRPKPQILR 248
Cdd:cd08227   263 PRPSNGESS-SHPYNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLR 326
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
58-90 7.29e-03

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 37.62  E-value: 7.29e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907169597  58 IIHCDLKPENiVLYQRGQVTVkVIDFGSSCYEH 90
Cdd:cd05153   181 VIHADLFRDN-VLFDGDRLSG-IIDFYDACYDP 211
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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