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Conserved domains on  [gi|2032329476|ref|NP_001381708|]
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dual specificity tyrosine-phosphorylation-regulated kinase 4 isoform 5 [Homo sapiens]

Protein Classification

dual specificity tyrosine-phosphorylation-regulated kinase( domain architecture ID 10197782)

dual specificity tyrosine-phosphorylation-regulated kinase (DYRK) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates; it autophosphorylates itself on tyrosine residues and phosphorylates its substrates exclusively on S/T residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
175-515 0e+00

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: 723.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 175 YAELWFLGLEAKKLDTAPEKFSKTSFDDEHGFYLKVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK 254
Cdd:cd14225     1 YPEIWFLGLEAKKIEGVPGAPQNNGYDDENGSYLKVLHDHIAYRYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 255 RFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQ 334
Cdd:cd14225    81 RFHHQALVEVKILDALRRKDRDNSHNVIHMKEYFYFRNHLCITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 335 MLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd14225   161 LLYRERIIHCDLKPENILLRQRGQSSIKVIDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 415 GYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRR 494
Cdd:cd14225   241 GYPLFPGENEVEQLACIMEVLGLPPPELIENAQRRRLFFDSKGNPRCITNSKGKKRRPNSKDLASALKTSDPLFLDFIRR 320
                         330       340
                  ....*....|....*....|.
gi 2032329476 495 CLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14225   321 CLEWDPSKRMTPDEALQHEWI 341
 
Name Accession Description Interval E-value
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
175-515 0e+00

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: 723.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 175 YAELWFLGLEAKKLDTAPEKFSKTSFDDEHGFYLKVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK 254
Cdd:cd14225     1 YPEIWFLGLEAKKIEGVPGAPQNNGYDDENGSYLKVLHDHIAYRYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 255 RFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQ 334
Cdd:cd14225    81 RFHHQALVEVKILDALRRKDRDNSHNVIHMKEYFYFRNHLCITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 335 MLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd14225   161 LLYRERIIHCDLKPENILLRQRGQSSIKVIDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 415 GYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRR 494
Cdd:cd14225   241 GYPLFPGENEVEQLACIMEVLGLPPPELIENAQRRRLFFDSKGNPRCITNSKGKKRRPNSKDLASALKTSDPLFLDFIRR 320
                         330       340
                  ....*....|....*....|.
gi 2032329476 495 CLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14225   321 CLEWDPSKRMTPDEALQHEWI 341
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
219-515 4.60e-79

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 250.91  E-value: 4.60e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK--RFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCI 296
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKikKDRERILREIKILKKLKHP------NIVRLYDVFEDEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  297 TFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH-- 373
Cdd:smart00220  75 VMEYCeGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH--VKLADFGLARQLDpg 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasrrqtff 453
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI--------------------- 209
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476  454 dskgfpknitnnrGKKRYPDSKDLTMVlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:smart00220 210 -------------GKPKPPFPPPEWDI----SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
219-568 3.07e-41

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 155.58  E-value: 3.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV--AKCLDhkNNELVALKIIRNKKRFHQQALMELKILealrkkdkdNTYNVVHMKDFFYF------ 290
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVyeAICID--TSEKVAIKKVLQDPQYKNRELLIMKNL---------NHINIIFLKDYYYTecfkkn 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 -RNHFC-ITFELLGINLYELMK--NNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVKVIDF 366
Cdd:PTZ00036  137 eKNIFLnVVMEFIPQTVHKYMKhyARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNL-LIDPNTHTLKLCDF 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 367 GSS--CYEHQKVYTYIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPpagfi 443
Cdd:PTZ00036  216 GSAknLLAGQRSVSYICSRFYRAPELMLGATnYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGTP----- 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 444 qtaSRRQTffdskgfpKNITNNRGKKRYPD--SKDLTMVL-KTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRN 520
Cdd:PTZ00036  291 ---TEDQL--------KEMNPNYADIKFPDvkPKDLKKVFpKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRD 359
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 521 lkPQPR-PQTLRKSNSFFpsETRKDKVQGCHHSSRKDEITKETTEKTKD 568
Cdd:PTZ00036  360 --PCIKlPKYIDKLPDLF--NFCDAEIKEMSDACRRKIIPKCTYEAYKE 404
Pkinase pfam00069
Protein kinase domain;
219-515 3.49e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 148.93  E-value: 3.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKR---FHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIkkkKDKNILREIKILKKLNHP------NIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLqmlsvekiihcdlkpenivlyqkgqasvkvidfgsscYEHQ 374
Cdd:pfam00069  75 LVLEYVeGGSLFDLLSEK--GAFSEREAKFIMKQILEGL-------------------------------------ESGS 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACImevlglppagfiqtasRRQTFFD 454
Cdd:pfam00069 116 SLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELI----------------IDQPYAF 179
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 455 SKgFPKNItnnrgkkrypdSKDltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:pfam00069 180 PE-LPSNL-----------SEE-----------AKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
213-440 3.35e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 138.99  E-value: 3.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR----NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFF 288
Cdd:COG0515     3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelaADPEARERFRREARALARLNHP------NIVRVYDVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 YFRNHFCITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG 367
Cdd:COG0515    77 EEDGRPYLVMEYVeGESLADLLRRR--GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR--VKLIDFG 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 368 SSCYEHQKVYTYIQSRF----YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPA 440
Cdd:COG0515   153 IARALGGATLTQTGTVVgtpgYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPS 229
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
218-425 9.50e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.82  E-value: 9.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN--------KKRFHQ--QALMELkilealrkkdkdNTYNVVHMKDF 287
Cdd:NF033483    8 RYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRPdlardpefVARFRReaQSAASL------------SHPNIVSVYDV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 288 FYFRNHFCITFELL-GINLYELMKnnnfQGFSLSIVR--RFTLSVLKCLQmLSVEK-IIHCDLKPENIVLYQKGQasVKV 363
Cdd:NF033483   76 GEDGGIPYIVMEYVdGRTLKDYIR----EHGPLSPEEavEIMIQILSALE-HAHRNgIVHRDIKPQNILITKDGR--VKV 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 364 IDFG-------SSCYEHQKVytyIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEV 425
Cdd:NF033483  149 TDFGiaralssTTMTQTNSV---LGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSPV 214
 
Name Accession Description Interval E-value
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
175-515 0e+00

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: 723.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 175 YAELWFLGLEAKKLDTAPEKFSKTSFDDEHGFYLKVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK 254
Cdd:cd14225     1 YPEIWFLGLEAKKIEGVPGAPQNNGYDDENGSYLKVLHDHIAYRYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 255 RFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQ 334
Cdd:cd14225    81 RFHHQALVEVKILDALRRKDRDNSHNVIHMKEYFYFRNHLCITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 335 MLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd14225   161 LLYRERIIHCDLKPENILLRQRGQSSIKVIDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 415 GYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRR 494
Cdd:cd14225   241 GYPLFPGENEVEQLACIMEVLGLPPPELIENAQRRRLFFDSKGNPRCITNSKGKKRRPNSKDLASALKTSDPLFLDFIRR 320
                         330       340
                  ....*....|....*....|.
gi 2032329476 495 CLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14225   321 CLEWDPSKRMTPDEALQHEWI 341
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
205-515 0e+00

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: 606.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 205 GFYLKVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHM 284
Cdd:cd14210     1 GDYKVVLGDHIAYRYEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALVEVKILKHLNDNDPDDKHNIVRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 285 KDFFYFRNHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVI 364
Cdd:cd14210    81 KDSFIFRGHLCIVFELLSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 365 DFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQ 444
Cdd:cd14210   161 DFGSSCFEGEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLGVPPKSLID 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 445 TASRRQTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14210   241 KASRRKKFFDSNGKPRPTTNSKGKKRRPGSKSLAQVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
153-515 0e+00

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: 531.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 153 AAEALKLFKNQLSPYEQSEILGYAELWFLGLEAKKLDTAPEKFSKTSFDDEHGFYLKVLHDHIAYRYEVLETIGKGSFGQ 232
Cdd:cd14224     1 PEQAMKQYMHKLTAYEHHEIFNYPEIYFVGPNAKKRQGVIGGPNNGGYDDEQGSYIHVPHDHIAYRYEVLKVIGKGSFGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 233 VAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNN 312
Cdd:cd14224    81 VVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKQDKDNTMNVIHMLESFTFRNHICMTFELLSMNLYELIKKN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 313 NFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVIL 392
Cdd:cd14224   161 KFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRIYTYIQSRFYRAPEVIL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 393 GHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNIT--------- 463
Cdd:cd14224   241 GARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPPQKLLETSKRAKNFISSKGYPRYCTvttlpdgsv 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 464 ------NNRGKKR-YPDSKDLTMVLK-TYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14224   321 vlnggrSRRGKMRgPPGSKDWVTALKgCDDPLFLDFLKRCLEWDPAARMTPSQALRHPWL 380
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
219-515 2.42e-132

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: 388.55  E-value: 2.42e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITF 298
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNKKDKADKYHIVRLKDVFYFKNHLCIVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYT 378
Cdd:cd14133    81 ELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIIDFGSSCFLTQRLYS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 379 YIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIqtasrrqtffdskgf 458
Cdd:cd14133   161 YIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHML--------------- 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 459 pknitnNRGKKRYPDskdltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14133   226 ------DQGKADDEL--------------FVDFLKKLLEIDPKERPTASQALSHPWL 262
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
218-512 9.25e-126

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: 374.73  E-value: 9.25e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCIT 297
Cdd:cd14226    14 RYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTENKYYIVRLKRHFMFRNHLCLV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVE--KIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQK 375
Cdd:cd14226    94 FELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLCNPKRSAIKIIDFGSSCQLGQR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFD- 454
Cdd:cd14226   174 IYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGMPPVHMLDQAPKARKFFEk 253
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 455 --SKGFPKNITNNRGKKRYPDSKDLTMVLKTyDTS-------------------FLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd14226   254 lpDGTYYLKKTKDGKKYKPPGSRKLHEILGV-ETGgpggrragepghtvedylkFKDLILRMLDYDPKTRITPAEALQH 331
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
219-515 8.95e-123

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: 366.96  E-value: 8.95e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKK-DKDNTYNVVHMKDFFYFRNHFCIT 297
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILTLLNTKyDPEDKHHIVRLLDHFMHHGHLCIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVY 377
Cdd:cd14212    81 FELLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKLIDFGSACFENYTLY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 378 TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFD--S 455
Cdd:cd14212   161 TYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEMLGMPPDWMLEKGKNTNKFFKkvA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 456 KGFPKN---------------------------------ITNNRGKKRYPDSKDLTMVLKtydTSFLDFLRRCLVWEPSL 502
Cdd:cd14212   241 KSGGRStyrlktpeefeaenncklepgkryfkyktlediIMNYPMKKSKKEQIDKEMETR---LAFIDFLKGLLEYDPKK 317
                         330
                  ....*....|...
gi 2032329476 503 RMTPDQALKHAWI 515
Cdd:cd14212   318 RWTPDQALNHPFI 330
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
213-514 1.58e-97

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: 301.79  E-value: 1.58e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRN 292
Cdd:cd14134     8 DLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAAKIEIDVLETLAEKDPNGKSHCVQLRDWFDYRG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVL----------YQKGQ---- 358
Cdd:cd14134    88 HMCIVFELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdyvkvynPKKKRqirv 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 359 ---ASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLAcIME-V 434
Cdd:cd14134   168 pksTDIKLIDFGSATFDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLEHLA-MMErI 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 435 LGLPPAGFIQTASRRQTFFDSKG----FPKNITNNRGKKRYPDSKDLTMVLK-TYDTSFLDFLRRCLVWEPSLRMTPDQA 509
Cdd:cd14134   247 LGPLPKRMIRRAKKGAKYFYFYHgrldWPEGSSSGRSIKRVCKPLKRLMLLVdPEHRLLFDLIRKMLEYDPSKRITAKEA 326

                  ....*
gi 2032329476 510 LKHAW 514
Cdd:cd14134   327 LKHPF 331
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
219-515 1.39e-91

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: 283.36  E-value: 1.39e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRkkDKDNTYNVVHMKDFFYFR--NHFCI 296
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLN--DVEGHPNIVKLLDVFEHRggNHLCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAsVKVIDFGSSCYEHQKV 376
Cdd:cd05118    79 VFELMGMNLYELIKDYP-RGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQ-LKLADFGLARSFTSPP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 YT-YIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPagfiqtasrrqtffd 454
Cdd:cd05118   157 YTpYVATRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGTPE--------------- 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 455 skgfpknitnnrgkkrypdskdltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd05118   222 ---------------------------------ALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
219-515 4.79e-80

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: 256.22  E-value: 4.79e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNtYNVVHMKDFFYFRNHFCITF 298
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENADE-FNFVRAYECFQHKNHTCLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQA--SVKVIDFGSSCYEHQKV 376
Cdd:cd14211    80 EMLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQpyRVKVIDFGSASHVSKAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 -YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDS 455
Cdd:cd14211   160 cSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPAEHLLNAATKTSRFFNR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 456 KGFPKNI-------------TNNRGKKR------------------YPDSKDLtMVLKTYDTSFLDFLRRCLVWEPSLRM 504
Cdd:cd14211   240 DPDSPYPlwrlktpeeheaeTGIKSKEArkyifnclddmaqvngpsDLEGSEL-LAEKADRREFIDLLKRMLTIDQERRI 318
                         330
                  ....*....|.
gi 2032329476 505 TPDQALKHAWI 515
Cdd:cd14211   319 TPGEALNHPFV 329
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
219-515 4.60e-79

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 250.91  E-value: 4.60e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK--RFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCI 296
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKikKDRERILREIKILKKLKHP------NIVRLYDVFEDEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  297 TFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH-- 373
Cdd:smart00220  75 VMEYCeGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH--VKLADFGLARQLDpg 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasrrqtff 453
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI--------------------- 209
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476  454 dskgfpknitnnrGKKRYPDSKDLTMVlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:smart00220 210 -------------GKPKPPFPPPEWDI----SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
218-515 8.87e-74

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: 239.43  E-value: 8.87e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKN-NELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCI 296
Cdd:cd14135     1 RYRVYGYLGKGVFSNVVRARDLARgNQEVAIKIIRNNELMHKAGLKELEILKKLNDADPDDKKHCIRLLRHFEHKNHLCL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGINLYELMKN-NNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgQASVKVIDFGSSCYEHQK 375
Cdd:cd14135    81 VFESLSMNLREVLKKyGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEK-KNTLKLCDFGSASDIGEN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 VYT-YIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFD 454
Cdd:cd14135   160 EITpYLVSRFYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGKFPKKMLRKGQFKDQHFD 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 455 SKGFPKNI----TNNRGKKRYPD----SKDLTMVLKTYDTS----------FLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14135   240 ENLNFIYRevdkVTKKEVRRVMSdikpTKDLKTLLIGKQRLpdedrkkllqLKDLLDKCLMLDPEKRITPNEALQHPFI 318
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
218-515 4.27e-69

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: 227.46  E-value: 4.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKD--NTYNVVHMKDFFYFR---- 291
Cdd:cd14136    11 RYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKCVREADPKdpGREHVVQLLDDFKHTgpng 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVE-KIIHCDLKPENIVLYQKgQASVKVIDFGSSC 370
Cdd:cd14136    91 THVCMVFEVLGPNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCIS-KIEVKIADLGNAC 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF---PGEN---EVEQLACIMEVLGLPPAGFIQ 444
Cdd:cd14136   170 WTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdphSGEDysrDEDHLALIIELLGRIPRSIIL 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 445 TASRRQTFFDSKGFPKNITNnrgKKRYPdskdLTMVLK-TYDTS------FLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14136   250 SGKYSREFFNRKGELRHISK---LKPWP----LEDVLVeKYKWSkeeakeFASFLLPMLEYDPEKRATAAQCLQHPWL 320
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
213-514 9.24e-69

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: 226.81  E-value: 9.24e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKCLDH-KNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFR 291
Cdd:cd14214     9 DWLQERYEIVGDLGEGTFGKVVECLDHaRGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENI--------VLYQKGQA---- 359
Cdd:cd14214    89 GHMCIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENIlfvnsefdTLYNESKSceek 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 360 -----SVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEV 434
Cdd:cd14214   169 svkntSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHLVMMEKI 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 435 LGLPPAGFIQTaSRRQTFFDSKGFPKNITNNRGKKRYPDSKDLtMVLKTYD----TSFLDFLRRCLVWEPSLRMTPDQAL 510
Cdd:cd14214   249 LGPIPSHMIHR-TRKQKYFYKGSLVWDENSSDGRYVSENCKPL-MSYMLGDslehTQLFDLLRRMLEFDPALRITLKEAL 326

                  ....
gi 2032329476 511 KHAW 514
Cdd:cd14214   327 LHPF 330
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
219-515 8.20e-68

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: 224.52  E-value: 8.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNtYNVVHMKDFFYFRNHFCITF 298
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENADE-FNFVRAYECFQHRNHTCLVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQ--KGQASVKVIDFGSSCYEHQKV 376
Cdd:cd14229    81 EMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDpvRQPYRVKVIDFGSASHVSKTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 -YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFF-- 453
Cdd:cd14229   161 cSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLNVGTKTSRFFcr 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 454 -----------------------DSKGFPKNITNNRGKKRYP------DSKDLtMVLKTYDTSFLDFLRRCLVWEPSLRM 504
Cdd:cd14229   241 etdapysswrlktleeheaetgmKSKEARKYIFNSLDDIAHVnmvmdlEGSDL-LAEKADRREFVALLKKMLLIDADLRI 319
                         330
                  ....*....|.
gi 2032329476 505 TPDQALKHAWI 515
Cdd:cd14229   320 TPADTLSHPFV 330
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
218-512 6.90e-64

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: 212.75  E-value: 6.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQqalMELKILEALRKKdkdntyNVVHMKDFFYFR------ 291
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKN---RELQIMRRLKHP------NIVKLKYFFYSSgekkde 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYELMK--NNNFQGFSLSIVRRFT---LSVLKCLQMLSvekIIHCDLKPENI-VLYQKGQasVKVID 365
Cdd:cd14137    76 VYLNLVMEYMPETLYRVIRhySKNKQTIPIIYVKLYSyqlFRGLAYLHSLG---ICHRDIKPQNLlVDPETGV--LKLCD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 366 FGSSCY--EHQKVYTYIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGF 442
Cdd:cd14137   151 FGSAKRlvPGEPNVSYICSRYYRAPELIFGATdYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQ 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 443 IQTASRRQTFFDskgFPKnitnnrgKKRYPdskdLTMVLKTY-DTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd14137   231 IKAMNPNYTEFK---FPQ-------IKPHP----WEKVFPKRtPPDAIDLLSKILVYNPSKRLTALEALAH 287
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
213-512 4.85e-63

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: 211.63  E-value: 4.85e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKCLDH-KNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFR 291
Cdd:cd14213     8 DVLRARYEIVDTLGEGAFGKVVECIDHkMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTDPNSTFRCVQMLEWFDHH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG-------------- 357
Cdd:cd14213    88 GHVCIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDyvvkynpkmkrder 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 358 ---QASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEV 434
Cdd:cd14213   168 tlkNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 435 LGLPPAGFIQTASRRQTFF-DSKGFPKNITNNRG-KKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd14213   248 LGPLPKHMIQKTRKRKYFHhDQLDWDEHSSAGRYvRRRCKPLKEFMLSQDVDHEQLFDLIQKMLEYDPAKRITLDEALKH 327
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
219-515 1.77e-60

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: 205.71  E-value: 1.77e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNtYNVVHMKDFFYFRNHFCITF 298
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADD-YNFVRAYECFQHKNHTCLVF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQA--SVKVIDFGSSCYEHQKV 376
Cdd:cd14227    96 EMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQpyRVKVIDFGSASHVSKAV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 -YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDS 455
Cdd:cd14227   176 cSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNR 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 456 K----------GFPKNITNNRGKKRYPDSK-------DLTMVLKTYD-------------TSFLDFLRRCLVWEPSLRMT 505
Cdd:cd14227   256 DtdspyplwrlKTPEDHEAETGIKSKEARKyifncldDMAQVNMTTDlegsdmlvekadrREFIDLLKKMLTIDADKRIT 335
                         330
                  ....*....|
gi 2032329476 506 PDQALKHAWI 515
Cdd:cd14227   336 PIETLNHPFV 345
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
219-514 3.35e-60

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: 202.38  E-value: 3.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKiiRNKKRFHQ-QALMELKILEALRK-KDKDNtynVVHMKDFFYFRNHFCI 296
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIK--KMKKKFYSwEECMNLREVKSLRKlNEHPN---IVKLKEVFRENDELYF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFG-SSCYEHQK 375
Cdd:cd07830    76 VFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV--SGPEVVKIADFGlAREIRSRP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 VYT-YIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLP-----PAGFiQTASR 448
Cdd:cd07830   154 PYTdYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPtkqdwPEGY-KLASK 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 449 RQtfFDskgFPKNItnnrgkkrypdSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07830   233 LG--FR---FPQFA-----------PTSLHQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
219-515 2.07e-59

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: 203.01  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNtYNVVHMKDFFYFRNHFCITF 298
Cdd:cd14228    17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADE-YNFVRSYECFQHKNHTCLVF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQ--KGQASVKVIDFGSSCYEHQKV 376
Cdd:cd14228    96 EMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDpvRQPYRVKVIDFGSASHVSKAV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 -YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDS 455
Cdd:cd14228   176 cSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTSRFFNR 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 456 K---GFP------------KNITNNRGKKRY--------------PDSKDLTMVLKTYD-TSFLDFLRRCLVWEPSLRMT 505
Cdd:cd14228   256 DpnlGYPlwrlktpeehelETGIKSKEARKYifnclddmaqvnmsTDLEGTDMLAEKADrREYIDLLKKMLTIDADKRIT 335
                         330
                  ....*....|
gi 2032329476 506 PDQALKHAWI 515
Cdd:cd14228   336 PLKTLNHPFV 345
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
213-512 2.78e-59

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: 201.78  E-value: 2.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKCLDHK-NNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFR 291
Cdd:cd14215     8 DWLQERYEIVSTLGEGTFGRVVQCIDHRrGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPENKNLCVQMFDWFDYH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG-------------- 357
Cdd:cd14215    88 GHMCISFELLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDyeltynlekkrder 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 358 ---QASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEV 434
Cdd:cd14215   168 svkSTAIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 435 LGLPPAGFIQTASRRQTFFDSKgfpKNITNNRGKKRY------PDSKDLTMVLKTYDtSFLDFLRRCLVWEPSLRMTPDQ 508
Cdd:cd14215   248 LGPIPSRMIRKTRKQKYFYHGR---LDWDENTSAGRYvrenckPLRRYLTSEAEEHH-QLFDLIESMLEYEPSKRLTLAA 323

                  ....
gi 2032329476 509 ALKH 512
Cdd:cd14215   324 ALKH 327
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
219-515 2.67e-58

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: 197.32  E-value: 2.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKR---FHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEeegIPSTALREISLLKELKHP------NIVKLLDVIHTENKLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG-SSCYEHQ 374
Cdd:cd07829    75 LVFEYCDQDLKKYLDKRP-GPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDG--VLKLADFGlARAFGIP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 -KVYTY-IQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPpagfiqtasrrqt 451
Cdd:cd07829   152 lRTYTHeVVTLWYRAPEILLGsKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTP------------- 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 452 ffDSKGFPkNITNNRGKK----RYPdSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd07829   219 --TEESWP-GVTKLPDYKptfpKWP-KNDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
218-547 6.13e-58

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: 198.13  E-value: 6.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN-------KKRfhqqALMELKILEALRKKdkdntyNVVHMKDFFY- 289
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfddlidAKR----ILREIKILRHLKHE------NIIGLLDILRp 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 -----FrNHFCITFELLGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVI 364
Cdd:cd07834    71 pspeeF-NDVYIVTELMETDLHKVIKSP--QPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILV--NSNCDLKIC 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 365 DFG---SSCYEHQKVY-T-YIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLP 438
Cdd:cd07834   146 DFGlarGVDPDEDKGFlTeYVVTRWYRAPELLLSsKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 439 PAGFIQtasrrqtFFDSKGFPKNItNNRGKKRypdSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQS 518
Cdd:cd07834   226 SEEDLK-------FISSEKARNYL-KSLPKKP---KKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQL 294
                         330       340
                  ....*....|....*....|....*....
gi 2032329476 519 RNLKPQPRPQTLRKSNSFFPSETRKDKVQ 547
Cdd:cd07834   295 HDPEDEPVAKPPFDFPFFDDEELTIEELK 323
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
218-514 3.67e-56

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: 191.76  E-value: 3.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALK---IIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd07833     2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKkfkESEDDEDVKKTALREVKVLRQLRHE------NIVNLKEAFRRKGRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCYEHQ 374
Cdd:cd07833    76 YLVFEYVERTLLELLEASP-GGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESG--VLKLCDFGFARALTA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 K---VYT-YIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLG-LPPagfiqtasR 448
Cdd:cd07833   153 RpasPLTdYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGpLPP--------S 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 449 RQTFFDSKgfpkniTNNRGkKRYPDSKDLTMVLKTYDTSF----LDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07833   225 HQELFSSN------PRFAG-VAFPEPSQPESLERRYPGKVsspaLDFLKACLRMDPKERLTCDELLQHPY 287
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
218-514 2.16e-55

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: 189.85  E-value: 2.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFH---QQALMELKILEALrkkdKDNTYnVVHMKDFFYFRNHF 294
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGgipNQALREIKALQAC----QGHPY-VVKLRDVFPHGTGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG------- 367
Cdd:cd07832    76 VLVFEYMLSSLSEVLRDEE-RPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGV--LKIADFGlarlfse 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 --SSCYEHQkvytyIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPpagfiq 444
Cdd:cd07832   153 edPRLYSHQ-----VATRWYRAPELLYGSRkYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTP------ 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 445 tasRRQTFFDSKGFPknitnNRGKKRYPDSKDLTMVLKTYDTS--FLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07832   222 ---NEKTWPELTSLP-----DYNKITFPESKGIRLEEIFPDCSpeAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
219-514 1.79e-51

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: 179.30  E-value: 1.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN---KKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFC 295
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMeneKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSKGSAKYKGSIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG---SSCYE 372
Cdd:cd07840    81 MVFEYMDHDLTGLLDNPEVK-FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGV--LKLADFGlarPYTKE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTY-IQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPpagfiqTASRRQ 450
Cdd:cd07840   158 NNADYTNrVITLWYRPPELLLGATrYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSP------TEENWP 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 451 TFFDSKGFpKNITNNRGKKRypdskdltmVLKTY-----DTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07840   232 GVSDLPWF-ENLKPKKPYKR---------RLREVfknviDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
219-512 4.85e-49

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: 172.46  E-value: 4.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKiiRNKKRFHQ-QALMELKILEALRKKDKDNtyNVVHMKDFFYFRNHFCIT 297
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIK--CMKKHFKSlEQVNNLREIQALRRLSPHP--NILRLIEVLFDRKTGRLA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 --FELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgqaSVKVIDFGSSCYEHQK 375
Cdd:cd07831    77 lvFELMDMNLYELIKGRK-RPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD---ILKLADFGSCRGIYSK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 V-YT-YIQSRFYRSPEVIL--GHpYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAG---FIQTASR 448
Cdd:cd07831   153 PpYTeYISTRWYRAPECLLtdGY-YGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEvlkKFRKSRH 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 449 RQTFFDSK---GFPKNITNnrgkkrypdskdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd07831   232 MNYNFPSKkgtGLRKLLPN-------------------ASAEGLDLLKKLLAYDPDERITAKQALRH 279
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
213-525 5.15e-49

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: 174.28  E-value: 5.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKII----RNKKRfHQQALMELKILEALRkkDKDNT---YNVV--- 282
Cdd:cd07852     3 KHILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdafRNATD-AQRTFREIMFLQELN--DHPNIiklLNVIrae 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 283 HMKDFFyfrnhfcITFELLGINLYELMKNNNFQgfslSIVRRFTL-SVLKCLQMLSVEKIIHCDLKPENIVLYQKgqASV 361
Cdd:cd07852    80 NDKDIY-------LVFEYMETDLHAVIRANILE----DIHKQYIMyQLLKALKYLHSGGVIHRDLKPSNILLNSD--CRV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 362 KVIDFG--SSCYEHQKVYT------YIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM 432
Cdd:cd07852   147 KLADFGlaRSLSQLEEDDEnpvltdYVATRWYRAPEILLGsTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKII 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 433 EVLGLPPAGFIQTasrrqtfFDSkGFPKNITNNrgkKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd07852   227 EVIGRPSAEDIES-------IQS-PFAATMLES---LPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRH 295
                         330
                  ....*....|...
gi 2032329476 513 AWIHQSRNLKPQP 525
Cdd:cd07852   296 PYVAQFHNPADEP 308
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
218-514 6.23e-47

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: 166.11  E-value: 6.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFH----QQALMELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKII-DKKKLKsedeEMLRREIEILKRLDHP------NIVKLYEVFEDDKN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS-VKVIDFGSSCY 371
Cdd:cd05117    74 LYLVMELCtGGELFDRIVKKGS--FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSpIKIIDFGLAKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 --EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvlglppaGFIQtasrr 449
Cdd:cd05117   152 feEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILK-------GKYS----- 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 450 qtfFDSKGFpKNITNnrgkkrypdskdltmvlktydtSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd05117   220 ---FDSPEW-KNVSE----------------------EAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
219-512 2.21e-46

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: 165.53  E-value: 2.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILealRKKDKDNTYNVVHMKDFFYFRN--- 292
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRvplSEEGIPLSTIREIALL---KQLESFEHPNVVRLLDVCHGPRtdr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 --HFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSc 370
Cdd:cd07838    78 elKLTLVFEHVDQDLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQ--VKLADFGLA- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 yehqKVYTYiQSRF--------YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAgf 442
Cdd:cd07838   155 ----RIYSF-EMALtsvvvtlwYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPSE-- 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 443 iqtasrrqtffdsKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd07838   228 -------------EEWPRNSALPRSSFPSYTPRPFKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQH 284
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
218-527 8.43e-46

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: 164.28  E-value: 8.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKR------FHQQALMELKILEALRKKdkdntyNVVHMKDFFYFR 291
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERkeakdgINFTALREIKLLQELKHP------NIIGLLDVFGHK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSC- 370
Cdd:cd07841    75 SNINLVFEFMETDLEKVIKDKSIV-LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGV--LKLADFGLARs 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 -------YEHQkVYTyiqsRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGF 442
Cdd:cd07841   152 fgspnrkMTHQ-VVT----RWYRAPELLFGaRHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEEN 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 443 IQTASRRQTFFDSKGFPKnitnnrgkkrypdsKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWihqsrnLK 522
Cdd:cd07841   227 WPGVTSLPDYVEFKPFPP--------------TPLKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPY------FS 286

                  ....*
gi 2032329476 523 PQPRP 527
Cdd:cd07841   287 NDPAP 291
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
218-515 3.51e-44

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: 161.35  E-value: 3.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKD--NTYNVVHMKDFFYFR---- 291
Cdd:cd14216    11 RYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETALDEIKLLKSVRNSDPNdpNREMVVQLLDDFKISgvng 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVE-KIIHCDLKPENIVL----------------Y 354
Cdd:cd14216    91 THICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLsvneqyirrlaaeateW 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 355 QKG------------QASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF--- 419
Cdd:cd14216   171 QRNflvnplepknaeKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFeph 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 420 PGEN---EVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITnnrgkKRYPDSKdLTMVLKTYD------TSFLD 490
Cdd:cd14216   251 SGEDysrDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHIT-----KLKPWGL-FEVLVEKYEwsqeeaAGFTD 324
                         330       340
                  ....*....|....*....|....*
gi 2032329476 491 FLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14216   325 FLLPMLELIPEKRATAAECLRHPWL 349
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
218-528 7.04e-44

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: 160.15  E-value: 7.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALK--------IIRNKKRFHqqalmELKILEALRKKdkdntyNVVHMKDFFY 289
Cdd:cd07851    16 RYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKklsrpfqsAIHAKRTYR-----ELRLLKHMKHE------NVIGLLDVFT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 -------FRNHFCITfELLGINLYELMKnnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVK 362
Cdd:cd07851    85 passledFQDVYLVT-HLMGADLNNIVK---CQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAV--NEDCELK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 363 VIDFGSSCYEHQKVYTYIQSRFYRSPEVIL--GHpYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPA 440
Cdd:cd07851   159 ILDFGLARHTDDEMTGYVATRWYRAPEIMLnwMH-YNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPDE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 441 GFIQ--TASRRQTFFdsKGFPKnitnnrgKKRypdsKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQS 518
Cdd:cd07851   238 ELLKkiSSESARNYI--QSLPQ-------MPK----KDFKEVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEY 304
                         330
                  ....*....|
gi 2032329476 519 RNLKPQPRPQ 528
Cdd:cd07851   305 HDPEDEPVAP 314
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
219-514 1.38e-43

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: 157.84  E-value: 1.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRletEDEGVPSTAIREISLLKELNHP------NIVRLLDVVHSENKLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS------ 369
Cdd:cd07835    75 LVFEFLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEG--ALKLADFGLArafgvp 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 --CYEHQKVytyiqSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTA 446
Cdd:cd07835   153 vrTYTHEVV-----TLWYRAPEILLGsKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDEDVWPGV 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 447 SRRQTFFDSkgFPKnitnnrgkkrYPdSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07835   228 TSLPDYKPT--FPK----------WA-RQDLSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
218-517 7.25e-43

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: 157.14  E-value: 7.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQA---LMELKILEALRKKdkdntyNVVHMKDFFY----- 289
Cdd:cd07855     6 RYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAkrtLRELKILRHFKHD------NIIAIRDILRpkvpy 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 --FRNHFCItFELLGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG 367
Cdd:cd07855    80 adFKDVYVV-LDLMESDLHHIIHSD--QPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENC--ELKIGDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 ------SSCYEHQKVYT-YIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPP 439
Cdd:cd07855   155 marglcTSPEEHKYFMTeYVATRWYRAPELMLSlPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 440 AGFIQT--ASRRQTFFDSkgFPkNITNNRGKKRYPDskdltmvlKTYDTsfLDFLRRCLVWEPSLRMTPDQALKHAWIHQ 517
Cdd:cd07855   235 QAVINAigADRVRRYIQN--LP-NKQPVPWETLYPK--------ADQQA--LDLLSQMLRFDPSERITVAEALQHPFLAK 301
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
219-514 1.56e-42

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 154.95  E-value: 1.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCI 296
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHldAEEGTPSTAIREISLMKELKHE------NIVRLHDVIHTENKLML 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGINLYELMKNNNFQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEHQK 375
Cdd:cd07836    76 VFEYMDKDLKKYMDTHGVRGaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGE--LKLADFGLARAFGIP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 VYTY---IQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPpagfiqtasRRQT 451
Cdd:cd07836   154 VNTFsneVVTLWYRAPDVLLGsRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTP---------TEST 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 452 FFDSKGFPKnitNNRGKKRYPdSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07836   225 WPGISQLPE---YKPTFPRYP-PQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
218-512 1.44e-41

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: 152.46  E-value: 1.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN---KKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd07848     2 KFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDseeNEEVKETTLRELKMLRTLKQE------NIVELKEAFRRRGKL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFGSS---CY 371
Cdd:cd07848    76 YLVFEYVEKNMLELLEEMP-NGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLI--SHNDVLKLCDFGFArnlSE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQKVYT-YIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQ 450
Cdd:cd07848   153 GSNANYTeYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQMKLFYSNP 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 451 TF----FDSKGFPKNItnnrgKKRYpdskdltmvLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd07848   233 RFhglrFPAVNHPQSL-----ERRY---------LGILSGVLLDLMKNLLKLNPTDRYLTEQCLNH 284
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
219-568 3.07e-41

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 155.58  E-value: 3.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV--AKCLDhkNNELVALKIIRNKKRFHQQALMELKILealrkkdkdNTYNVVHMKDFFYF------ 290
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVyeAICID--TSEKVAIKKVLQDPQYKNRELLIMKNL---------NHINIIFLKDYYYTecfkkn 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 -RNHFC-ITFELLGINLYELMK--NNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVKVIDF 366
Cdd:PTZ00036  137 eKNIFLnVVMEFIPQTVHKYMKhyARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNL-LIDPNTHTLKLCDF 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 367 GSS--CYEHQKVYTYIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPpagfi 443
Cdd:PTZ00036  216 GSAknLLAGQRSVSYICSRFYRAPELMLGATnYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGTP----- 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 444 qtaSRRQTffdskgfpKNITNNRGKKRYPD--SKDLTMVL-KTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRN 520
Cdd:PTZ00036  291 ---TEDQL--------KEMNPNYADIKFPDvkPKDLKKVFpKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRD 359
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 521 lkPQPR-PQTLRKSNSFFpsETRKDKVQGCHHSSRKDEITKETTEKTKD 568
Cdd:PTZ00036  360 --PCIKlPKYIDKLPDLF--NFCDAEIKEMSDACRRKIIPKCTYEAYKE 404
Pkinase pfam00069
Protein kinase domain;
219-515 3.49e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 148.93  E-value: 3.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKR---FHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIkkkKDKNILREIKILKKLNHP------NIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLqmlsvekiihcdlkpenivlyqkgqasvkvidfgsscYEHQ 374
Cdd:pfam00069  75 LVLEYVeGGSLFDLLSEK--GAFSEREAKFIMKQILEGL-------------------------------------ESGS 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACImevlglppagfiqtasRRQTFFD 454
Cdd:pfam00069 116 SLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELI----------------IDQPYAF 179
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 455 SKgFPKNItnnrgkkrypdSKDltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:pfam00069 180 PE-LPSNL-----------SEE-----------AKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
218-515 4.35e-41

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: 149.98  E-value: 4.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALM-ELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVElsGDSEEELEALErEIRILSSLKHP------NIVRYLGTERTENTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSScYEH 373
Cdd:cd06606    75 NIFLEYVpGGSLASLLKK--FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGV--VKLADFGCA-KRL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSR------FYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLA-CIMEVLGLPPagfiqta 446
Cdd:cd06606   150 AEIATGEGTKslrgtpYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAALfKIGSSGEPPP------- 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 447 srrqtffdskgFPKNItnnrgkkrypdSKDLtmvlktydtsfLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06606   223 -----------IPEHL-----------SEEA-----------KDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
215-515 4.50e-41

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: 152.34  E-value: 4.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIrnKKRFHQQALM-----ELKILEALRKKdkdntyNVVHMKDFFY 289
Cdd:cd07856     8 ITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKI--MKPFSTPVLAkrtyrELKLLKHLRHE------NIISLSDIFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 --FRNHFCITfELLGINLYELMKNNNFQGfslSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFG 367
Cdd:cd07856    80 spLEDIYFVT-ELLGTDLHRLLTSRPLEK---QFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNE--NCDLKICDFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 SSCYEHQKVYTYIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTA 446
Cdd:cd07856   154 LARIQDPQMTGYVSTRYYRAPEIMLTwQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVINTI 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 447 SRRQTFFDSKGFPKnitnnrgKKRYPdskdLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd07856   234 CSENTLRFVQSLPK-------RERVP----FSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
218-512 4.90e-41

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: 150.65  E-value: 4.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKII---RNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd07846     2 KYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFlesEDDKMVKKIAMREIKMLKQLRHE------NLVNLIEVFRRKKRW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGIN-LYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG--SSCY 371
Cdd:cd07846    76 YLVFEFVDHTvLDDLEKYPN--GLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSG--VVKLCDFGfaRTLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQKVYT-YIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGlppagfiQTASRR 449
Cdd:cd07846   152 APGEVYTdYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLG-------NLIPRH 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 450 QTFFDSKGFPKNItnnrgkkRYPDSKDLTMVLKTY---DTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd07846   225 QELFQKNPLFAGV-------RLPEVKEVEPLERRYpklSGVVIDLAKKCLHIDPDKRPSCSELLHH 283
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
225-412 7.39e-41

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: 147.80  E-value: 7.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELL- 301
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPkeKLKKLLEELLREIEILKKLNHP------NIVKLYDVFETENFLYLVMEYCe 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 GINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFGSSCYEHQKVYTYIQ 381
Cdd:cd00180    75 GGSLKDLLKENK-GPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL--DSDGTVKLADFGLAKDLDSDDSLLKT 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2032329476 382 SRF-----YRSPEVILGHPYDVAIDMWSLGCITAEL 412
Cdd:cd00180   152 TGGttppyYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
218-515 6.21e-40

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: 150.17  E-value: 6.21e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYN--VVHMKDFFYFRN--- 292
Cdd:cd14218    11 RYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAVDEIKLLKCVRDSDPSDPKRetIVQLIDDFKISGvng 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 -HFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVE-KIIHCDLKPENIVL----------------Y 354
Cdd:cd14218    91 vHVCMVLEVLGHQLLKWIIKSNYQGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILMcvdegyvrrlaaeatiW 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 355 QKG----------------------------QASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLG 406
Cdd:cd14218   171 QQAgapppsgssvsfgasdflvnplepqnadKIRVKIADLGNACWVHKHFTEDIQTRQYRALEVLIGAEYGTPADIWSTA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 407 CITAELYTGYPLF---PGEN---EVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITNNRGKKRYpdskdlTMV 480
Cdd:cd14218   251 CMAFELATGDYLFephSGEDytrDEDHIAHIVELLGDIPPHFALSGRYSREYFNRRGELRHIKNLKHWGLY------EVL 324
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2032329476 481 LKTYD------TSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14218   325 VEKYEwpleqaAQFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
218-528 3.68e-39

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: 147.41  E-value: 3.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFY----- 289
Cdd:cd07880    16 RYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYrpfQSELFAKRAYRELRLLKHMKHE------NVIGLLDVFTpdlsl 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 --FrNHFCITFELLGINLYELMKNnnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFG 367
Cdd:cd07880    90 drF-HDFYLVMPFMGTDLGKLMKH---EKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNE--DCELKILDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 SSCYEHQKVYTYIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQta 446
Cdd:cd07880   164 LARQTDSEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQ-- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 447 sRRQTfFDSKGFPKNITNNRgkkrypdSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPR 526
Cdd:cd07880   242 -KLQS-EDAKNYVKKLPRFR-------KKDFRSLLPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPEDETE 312

                  ..
gi 2032329476 527 PQ 528
Cdd:cd07880   313 AP 314
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
217-515 4.64e-39

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: 145.44  E-value: 4.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 217 YRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKR---FHQQALMELKILEALRKKdkdntyNVVHMK-------- 285
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEkegFPITSLREINILLKLQHP------NIVTVKevvvgsnl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 286 DFFYfrnhfcITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVID 365
Cdd:cd07843    79 DKIY------MVMEYVEHDLKSLMETMK-QPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGI--LKICD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 366 FGSS--CYEHQKVYTYIQ-SRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLP--- 438
Cdd:cd07843   150 FGLAreYGSPLKPYTQLVvTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPtek 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 439 --PaGFIQTASRRQTFFdskgfpKNITNNRGKKRYPdSKDLTmvlktyDTSFlDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd07843   230 iwP-GFSELPGAKKKTF------TKYPYNQLRKKFP-ALSLS------DNGF-DLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
214-517 5.16e-38

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: 143.98  E-value: 5.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 214 HIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFR 291
Cdd:cd07849     2 DVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpfEHQTYCLRTLREIKILLRFKHENIIGILDIQRPPTFESFK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITfELLGINLYELMKNnnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFG---- 367
Cdd:cd07849    82 DVYIVQ-ELMETDLYKLIKT---QHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLL--NTNCDLKICDFGlari 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 -SSCYEHQKVYT-YIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQ 444
Cdd:cd07849   156 aDPEHDHTGFLTeYVATRWYRAPEIMLNSKgYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQEDLN 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 445 T--ASRRQTFFDSKGFPKNITNNrgkKRYPDSkdltmvlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQ 517
Cdd:cd07849   236 CiiSLKARNYIKSLPFKPKVPWN---KLFPNA----------DPKALDLLDKMLTFNPHKRITVEEALAHPYLEQ 297
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
218-514 5.36e-38

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: 142.19  E-value: 5.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRlddDDEGVPSSALREICLLKELKHK------NIVRLYDVLHSDKKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS----- 369
Cdd:cd07839    75 TLVFEYCDQDLKKYFDSCNGD-IDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGE--LKLADFGLArafgi 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 ---CYEHQKVytyiqSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYT-GYPLFPGENEVEQLACIMEVLGLPPagfIQ 444
Cdd:cd07839   152 pvrCYSAEVV-----TLWYRPPDVLFGAKlYSTSIDMWSAGCIFAELANaGRPLFPGNDVDDQLKRIFRLLGTPT---EE 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 445 TASRRQTFFDSKGFPKnitnnrgkkrYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07839   224 SWPGVSKLPDYKPYPM----------YPATTSLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
218-514 8.08e-38

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 142.26  E-value: 8.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKR---FHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:PLN00009    3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEdegVPSTAIREISLLKEMQHG------NIVRLQDVVHSEKRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVKVIDFGSSCYEHQ 374
Cdd:PLN00009   77 YLVFEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNL-LIDRRTNALKLADFGLARAFGI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTY---IQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQ 450
Cdd:PLN00009  156 PVRTFtheVVTLWYRAPEILLGsRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPGVTSLP 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 451 TFFDSkgFPKnitnnrgkkrYPdSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:PLN00009  236 DYKSA--FPK----------WP-PKDLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
218-514 8.48e-38

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: 141.74  E-value: 8.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKiirnkkRF---------HQQALMELKILEALRKKdkdntyNVVHMKDFF 288
Cdd:cd07847     2 KYEKLSKIGEGSYGVVFKCRNRETGQIVAIK------KFveseddpviKKIALREIRMLKQLKHP------NLVNLIEVF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 YFRNHFCITFELLGIN-LYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG 367
Cdd:cd07847    70 RRKRKLHLVFEYCDHTvLNELEKNPR--GVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQ--IKLCDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 ------SSCYEhqkvYT-YIQSRFYRSPEVILGH-PYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLG-LP 438
Cdd:cd07847   146 fariltGPGDD----YTdYVATRWYRAPELLVGDtQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGdLI 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 439 PagfiqtasRRQTFFDSKGFPKNITNNRGKKRYPdskdLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07847   222 P--------RHQQIFSTNQFFKGLSIPEPETREP----LESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
215-515 1.48e-37

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: 142.51  E-value: 1.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNtynVVHMKDFFY--FRN 292
Cdd:cd07858     3 VDTKYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHEN---VIAIKDIMPppHRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HF---CITFELLGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFG-- 367
Cdd:cd07858    80 AFndvYIVYELMDTDLHQIIRSS--QTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLL--NANCDLKICDFGla 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 -SSCYEHQKVYTYIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPA---GF 442
Cdd:cd07858   156 rTTSEKGDFMTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEedlGF 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 443 IQTASRRQtffdskgFPKNITNNRG---KKRYPDSKDLTmvlktydtsfLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd07858   236 IRNEKARR-------YIRSLPYTPRqsfARLFPHANPLA----------IDLLEKMLVFDPSKRITVEEALAHPYL 294
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
218-515 1.74e-37

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: 142.16  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQV--AKCLDHKNNELVALKIIRN---KKRFHQQALMELKILEALRkkDKDNTYNVVHMKDFFY--F 290
Cdd:cd07857     1 RYELIKELGQGAYGIVcsARNAETSEEETVAIKKITNvfsKKILAKRALRELKLLRHFR--GHKNITCLYDMDIVFPgnF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCITfELLGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSC 370
Cdd:cd07857    79 NELYLYE-ELMEADLHQIIRSG--QPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCE--LKICDFGLAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 -------YEHQKVYTYIQSRFYRSPEVILGH-PYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGF 442
Cdd:cd07857   154 gfsenpgENAGFMTEYVATRWYRAPEIMLSFqSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPDEET 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 443 IQ--TASRRQTFFDSKGFP--KNITNNrgkkrYPDSKDLTmvlktydtsfLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd07857   234 LSriGSPKAQNYIRSLPNIpkKPFESI-----FPNANPLA----------LDLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
218-440 3.01e-37

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: 139.26  E-value: 3.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR----NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRpelaEDEEFRERFLREARALARLSHP------NIVRVYDVGEDDGR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYE 372
Cdd:cd14014    75 PYIVMEYVeGGSLADLLRER--GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGR--VKLTDFGIARAL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 373 HQKVYTYIQSR----FYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPA 440
Cdd:cd14014   151 GDSGLTQTGSVlgtpAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPS 222
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
214-514 1.29e-36

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: 139.04  E-value: 1.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 214 HIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFY- 289
Cdd:cd07865     9 DEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLmenEKEGFPITALREIKILQLLKHE------NVVNLIEICRt 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 -------FRNHFCITFELLGINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVK 362
Cdd:cd07865    83 katpynrYKGSIYLVFEFCEHDLAGLLSNKNVK-FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDG--VLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 363 VIDFG------------SSCYEHqKVYTYiqsrFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLA 429
Cdd:cd07865   160 LADFGlarafslaknsqPNRYTN-RVVTL----WYRPPELLLGeRDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 430 CIMEVLG-LPPAgfIQTASRRQTFFDSKGFPKNitnnrGKKRYPDskDLTMVLKtyDTSFLDFLRRCLVWEPSLRMTPDQ 508
Cdd:cd07865   235 LISQLCGsITPE--VWPGVDKLELFKKMELPQG-----QKRKVKE--RLKPYVK--DPYALDLIDKLLVLDPAKRIDADT 303

                  ....*.
gi 2032329476 509 ALKHAW 514
Cdd:cd07865   304 ALNHDF 309
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
218-514 1.35e-36

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: 138.99  E-value: 1.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALK--IIRNKKR-FHQQALMELKILEALRKKdkdntyNVVHMKDFFY----- 289
Cdd:cd07866     9 DYEILGKLGEGTFGEVYKARQIKTGRVVALKkiLMHNEKDgFPITALREIKILKKLKHP------NVVPLIDMAVerpdk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 ---FRNHFCITFELLGINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDF 366
Cdd:cd07866    83 skrKRGSVYMVTPYMDHDLSGLLENPSVK-LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGI--LKIADF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 367 G-------------SSCYEHQKVYT-YIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACI 431
Cdd:cd07866   160 GlarpydgpppnpkGGGGGGTRKYTnLVVTRWYRPPELLLGeRRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 432 MEVLGLPpagfiqTASRRQTFFDSKGFPknitNNRGKKRYPDSkdLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALK 511
Cdd:cd07866   240 FKLCGTP------TEETWPGWRSLPGCE----GVHSFTNYPRT--LEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALE 307

                  ...
gi 2032329476 512 HAW 514
Cdd:cd07866   308 HPY 310
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
218-543 2.40e-36

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: 139.15  E-value: 2.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQA---LMELKILEALRKKDKDNTYNVVHMKDFFYFRNHF 294
Cdd:cd07859     1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDAtriLREIKLLRLLRHPDIVEIKHIMLPPSRREFKDIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 cITFELLGINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVlyQKGQASVKVIDFGSSCYEHQ 374
Cdd:cd07859    81 -VVFELMESDLHQVIKAND--DLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNIL--ANADCKLKICDFGLARVAFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYT------YIQSRFYRSPEVI--LGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTA 446
Cdd:cd07859   156 DTPTaifwtdYVATRWYRAPELCgsFFSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETISRV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 447 SRRQTffdskgfPKNITNNRGKKRYPDSKDLTMVlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPR 526
Cdd:cd07859   236 RNEKA-------RRYLSSMRKKQPVPFSQKFPNA----DPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVEREPS 304
                         330
                  ....*....|....*..
gi 2032329476 527 PQTLRKSNsfFPSETRK 543
Cdd:cd07859   305 AQPITKLE--FEFERRR 319
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
219-515 4.18e-36

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: 136.18  E-value: 4.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM-ELKILEALRKKdkdntyNVVHMKDFFYFRNHFCIT 297
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILnEIAILKKCKHP------NIVKYYGSYLKKDELWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY--EHQ 374
Cdd:cd05122    76 MEFCsGGSLKDLLKNTN-KTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGE--VKLIDFGLSAQlsDGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENeveqlacIMEVLGLPPagfiqtasrrqtffd 454
Cdd:cd05122   153 TRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELP-------PMKALFLIA--------------- 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 455 SKGFPKnitnnrgkkrYPDSkdltmvlKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd05122   211 TNGPPG----------LRNP-------KKWSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
219-512 4.85e-36

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: 136.87  E-value: 4.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRldtETEGVPSTAIREISLLKELNHP------NIVKLLDVIHTENKLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS------ 369
Cdd:cd07860    76 LVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEG--AIKLADFGLArafgvp 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 --CYEHQKVytyiqSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPpagfiqta 446
Cdd:cd07860   154 vrTYTHEVV-----TLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTP-------- 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 447 srrqtffDSKGFPKNITNNRGKKRYPD--SKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd07860   221 -------DEVVWPGVTSMPDYKPSFPKwaRQDFSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAH 281
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
219-527 5.39e-36

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: 137.50  E-value: 5.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKiirnKKRFHQQ-------ALMELKILEALRKKdkdntyNVVHMKDFFYFR 291
Cdd:cd07845     9 FEKLNRIGEGTYGIVYRARDTTSGEIVALK----KVRMDNErdgipisSLREITLLLNLRHP------NIVELKEVVVGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 --NHFCITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG-S 368
Cdd:cd07845    79 hlDSIFLVMEYCEQDLASLLDNMP-TPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC--LKIADFGlA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 369 SCYEH-QKVYT-YIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGfIQT 445
Cdd:cd07845   156 RTYGLpAKPMTpKVVTLWYRAPELLLGcTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNES-IWP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 446 ASRRQTFFDSKGFPKNITNNRgKKRYPDSKDLTMVLktydtsfLDFLrrcLVWEPSLRMTPDQALKHAWIHQsrnlKPQP 525
Cdd:cd07845   235 GFSDLPLVGKFTLPKQPYNNL-KHKFPWLSEAGLRL-------LNFL---LMYDPKKRATAEEALESSYFKE----KPLP 299

                  ..
gi 2032329476 526 RP 527
Cdd:cd07845   300 CE 301
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
218-533 7.25e-36

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: 138.25  E-value: 7.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALK--------IIRNKKRFHqqalmELKILEALRKKdkdntyNVVHMKDFFY 289
Cdd:cd07877    18 RYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKklsrpfqsIIHAKRTYR-----ELRLLKHMKHE------NVIGLLDVFT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 -------FRNHFCITfELLGINLYELMKnnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVK 362
Cdd:cd07877    87 parsleeFNDVYLVT-HLMGADLNNIVK---CQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNE--DCELK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 363 VIDFGSSCYEHQKVYTYIQSRFYRSPEVILG--HpYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPA 440
Cdd:cd07877   161 ILDFGLARHTDDEMTGYVATRWYRAPEIMLNwmH-YNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 441 GFIQTASRRQtffdSKGFPKNITnnrgkkrYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRN 520
Cdd:cd07877   240 ELLKKISSES----ARNYIQSLT-------QMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHD 308
                         330
                  ....*....|...
gi 2032329476 521 LKPQPRPQTLRKS 533
Cdd:cd07877   309 PDDEPVADPYDQS 321
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
218-515 9.90e-36

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: 138.24  E-value: 9.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKD--NTYNVVHMKDFFYFRN--- 292
Cdd:cd14217    13 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLRCVRESDPEdpNKDMVVQLIDDFKISGmng 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 -HFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQML-SVEKIIHCDLKPENIVL----------------Y 354
Cdd:cd14217    93 iHVCMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLhSKCKIIHTDIKPENILMcvddayvrrmaaeateW 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 355 QKGQA---------------------------SVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGC 407
Cdd:cd14217   173 QKAGApppsgsavstapdllvnpldprnadkiRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTAC 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 408 ITAELYTGYPLF---PGEN---EVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITnnrgkKRYPDSKDLTMVL 481
Cdd:cd14217   253 MAFELATGDYLFephSGEDysrDEDHIAHIIELLGCIPRHFALSGKYSREFFNRRGELRHIT-----KLKPWSLFDVLVE 327
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2032329476 482 K-----TYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14217   328 KygwphEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWL 366
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
218-533 2.74e-35

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: 136.33  E-value: 2.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN--KKRFH-QQALMELKILEALRKKdkdntyNVVHMKDFFY----- 289
Cdd:cd07878    16 RYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfQSLIHaRRTYRELRLLKHMKHE------NVIGLLDVFTpatsi 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 --FRNHFCITfELLGINLYELMKnnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFG 367
Cdd:cd07878    90 enFNEVYLVT-NLMGADLNNIVK---CQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNE--DCELRILDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 SSCYEHQKVYTYIQSRFYRSPEVILG--HpYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQT 445
Cdd:cd07878   164 LARQADDEMTGYVATRWYRAPEIMLNwmH-YNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 446 ASRR--QTFFDSkgFPknitnnrgkkrYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKP 523
Cdd:cd07878   243 ISSEhaRKYIQS--LP-----------HMPQQDLKKIFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFSQYHDPED 309
                         330
                  ....*....|
gi 2032329476 524 QPRPQTLRKS 533
Cdd:cd07878   310 EPEAEPYDES 319
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
218-514 2.90e-35

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: 133.80  E-value: 2.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM---ELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKikrEIEIMKLLNHP------NIIKLYEVIETENKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNfqGFSLSIVRRF---TLSVLKCLQMLsveKIIHCDLKPENIVLYQKGQasVKVIDFGSS- 369
Cdd:cd14003    75 YLVMEYAsGGELFDYIVNNG--RLSEDEARRFfqqLISAVDYCHSN---GIVHRDLKLENILLDKNGN--LKIIDFGLSn 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 -CYEHQKVYTYIQSRFYRSPEVILGHPYD-VAIDMWSLGCItaeLY---TGYPLFPGENEVEQLACIMevlglppagfiq 444
Cdd:cd14003   148 eFRGGSLLKTFCGTPAYAAPEVLLGRKYDgPKADVWSLGVI---LYamlTGYLPFDDDNDSKLFRKIL------------ 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 445 tasrrqtffdskgfpknitnnRGKKRYPdskdltmvlKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd14003   213 ---------------------KGKYPIP---------SHLSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
213-440 3.35e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 138.99  E-value: 3.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR----NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFF 288
Cdd:COG0515     3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelaADPEARERFRREARALARLNHP------NIVRVYDVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 YFRNHFCITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG 367
Cdd:COG0515    77 EEDGRPYLVMEYVeGESLADLLRRR--GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR--VKLIDFG 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 368 SSCYEHQKVYTYIQSRF----YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPA 440
Cdd:COG0515   153 IARALGGATLTQTGTVVgtpgYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPS 229
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
219-515 8.25e-35

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: 133.77  E-value: 8.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKDKDNTYNVVHMK----DFFYFR 291
Cdd:cd07864     9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLNHRSVVNLKEIVTDKqdalDFKKDK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY 371
Cdd:cd07864    89 GAFYLVFEYMDHDLMGLLESGLVH-FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQ--IKLADFGLARL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 ---EHQKVYT-YIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTA 446
Cdd:cd07864   166 ynsEESRPYTnKVITLWYRPPELLLGEErYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPAVWPDV 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 447 SRRQTFFDSKgfPKNITNNRGKKRYpdskdltmvlKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd07864   246 IKLPYFNTMK--PKKQYRRRLREEF----------SFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
215-515 1.61e-34

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: 134.14  E-value: 1.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLETIGKGSFGQVAKCLDHKNNELVALK-IIRNKKRFHQQALMELKILealRKKDKDNTYNVVH---------- 283
Cdd:cd07854     3 LGSRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKkIVLTDPQSVKHALREIKII---RRLDHDNIVKVYEvlgpsgsdlt 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 284 --MKDFFYFRNhFCITFELLGINLYELMKNNNFqgfSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgQASV 361
Cdd:cd07854    80 edVGSLTELNS-VYIVQEYMETDLANVLEQGPL---SEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTE-DLVL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 362 KVIDFG-----SSCYEHQKVYTY-IQSRFYRSPEVILgHP--YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIME 433
Cdd:cd07854   155 KIGDFGlarivDPHYSHKGYLSEgLVTKWYRSPRLLL-SPnnYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 434 VLGLppagfIQTASRRQTFfdsKGFPKNITNNRGKKRYPdskdLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHA 513
Cdd:cd07854   234 SVPV-----VREEDRNELL---NVIPSFVRNDGGEPRRP----LRDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHP 301

                  ..
gi 2032329476 514 WI 515
Cdd:cd07854   302 YM 303
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
213-518 1.71e-34

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 133.73  E-value: 1.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLET-IGKGSFGQVAKCLDHKNNELVALKIIRNKK---------------RFHQQALMELKILEALRKKdkd 276
Cdd:PTZ00024    4 FSISERYIQKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEisndvtkdrqlvgmcGIHFTTLRELKIMNEIKHE--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 277 ntyNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQK 356
Cdd:PTZ00024   81 ---NIMGLVDVYVEGDFINLVMDIMASDLKKVVDRKIR--LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 357 GQasVKVIDFG-SSCYEHQKVY------TYIQSR----------FYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPL 418
Cdd:PTZ00024  156 GI--CKIADFGlARRYGYPPYSdtlskdETMQRReemtskvvtlWYRAPELLMGaEKYHFAVDMWSVGCIFAELLTGKPL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 419 FPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFD-SKGFPknitnnrgkkrypdsKDLTMVLKTYDTSFLDFLRRCLV 497
Cdd:PTZ00024  234 FPGENEIDQLGRIFELLGTPNEDNWPQAKKLPLYTEfTPRKP---------------KDLKTIFPNASDDAIDLLQSLLK 298
                         330       340
                  ....*....|....*....|.
gi 2032329476 498 WEPSLRMTPDQALKHAWIHQS 518
Cdd:PTZ00024  299 LNPLERISAKEALKHEYFKSD 319
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
219-512 2.89e-34

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: 131.77  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRlesEEEGVPSTAIREISLLKELQHP------NIVCLEDVLMQENRLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGINLYELMKN-NNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG--SSCYE 372
Cdd:cd07861    76 LVFEFLSMDLKKYLDSlPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKG--VIKLADFGlaRAFGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTY-IQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQ 450
Cdd:cd07861   154 PVRVYTHeVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGVTSLP 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 451 TFFDSkgFPKNITNNrgkkrypdskdLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd07861   234 DYKNT--FPKWKKGS-----------LRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVH 282
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
218-528 1.05e-33

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: 131.95  E-value: 1.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFY----F 290
Cdd:cd07879    16 RYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSrpfQSEIFAKRAYRELTLLKHMQHE------NVIGLLDVFTsavsG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RN--HFCITFELLGINLYELMKNNnfqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGS 368
Cdd:cd07879    90 DEfqDFYLVMPYMQTDLQKIMGHP----LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCE--LKILDFGL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 369 SCYEHQKVYTYIQSRFYRSPEVILG--HpYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTa 446
Cdd:cd07879   164 ARHADAEMTGYVVTRWYRAPEVILNwmH-YNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGPEFVQK- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 447 srrqtfFDSKGFPKNItnnRGKKRYPdSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPR 526
Cdd:cd07879   242 ------LEDKAAKSYI---KSLPKYP-RKDFSTLFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDADEETE 311

                  ..
gi 2032329476 527 PQ 528
Cdd:cd07879   312 QQ 313
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
218-515 1.34e-33

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: 130.08  E-value: 1.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKDKDNtynVVHMKDFfyfrnhf 294
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRvqtNEDGLPLSTVREVALLKRLEAFDHPN---IVRLMDV------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CIT------------FELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVK 362
Cdd:cd07863    71 CATsrtdretkvtlvFEHVDQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQ--VK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 363 VIDFG-SSCYEHQKVYT-YIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPa 440
Cdd:cd07863   149 LADFGlARIYSCQMALTpVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPP- 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 441 gfiqtasrrqtffdSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd07863   228 --------------EDDWPRDVTLPRGAFSPRGPRPVQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
PTZ00284 PTZ00284
protein kinase; Provisional
203-517 5.17e-33

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 132.40  E-value: 5.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 203 EHGFYLKVLHDHI---AYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTY 279
Cdd:PTZ00284  112 EEGHFYVVLGEDIdvsTQRFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDAKIEIQFMEKVRQADPADRF 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 280 NVvhMKDFFYFRN---HFCITFELLGINLYE-LMKNNNFQGFSLSivrRFTLSVLKCLQMLSVE-KIIHCDLKPENIvLY 354
Cdd:PTZ00284  192 PL--MKIQRYFQNetgHMCIVMPKYGPCLLDwIMKHGPFSHRHLA---QIIFQTGVALDYFHTElHLMHTDLKPENI-LM 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 355 QKGQASV---------------KVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:PTZ00284  266 ETSDTVVdpvtnralppdpcrvRICDLGGCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLY 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 420 PGENEVEQLACIMEVLGLPP---AGFIQTASRRQtFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKtyDTSFLDFLRRCL 496
Cdd:PTZ00284  346 DTHDNLEHLHLMEKTLGRLPsewAGRCGTEEARL-LYNSAGQLRPCTDPKHLARIARARPVREVIR--DDLLCDLIYGLL 422
                         330       340
                  ....*....|....*....|.
gi 2032329476 497 VWEPSLRMTPDQALKHAWIHQ 517
Cdd:PTZ00284  423 HYDRQKRLNARQMTTHPYVLK 443
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
218-512 1.07e-32

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: 128.04  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKrfHQQALMELKILEALRkkdkdNTYNVVHMKDFFyfRNHFCIT 297
Cdd:cd14132    19 DYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVK--KKKIKREIKILQNLR-----GGPNIVKLLDVV--KDPQSKT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLginlYELMKNNNF----QGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgQASVKVIDFG-SSCYE 372
Cdd:cd14132    90 PSLI----FEYVNNTDFktlyPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHE-KRKLRLIDWGlAEFYH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVY-TYIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAEL-YTGYPLFPGENEVEQLACIMEVLG------------- 436
Cdd:cd14132   165 PGQEYnVRVASRYYKGPELLVDYQyYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVKIAKVLGtddlyayldkygi 244
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 437 -LPPagfiqtaSRRQTFFDSKGFPKN--ITNNRGKKRYPDSkdltmvlktydtsfLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd14132   245 eLPP-------RLNDILGRHSKKPWErfVNSENQHLVTPEA--------------LDLLDKLLRYDHQERITAKEAMQH 302
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
219-514 3.29e-32

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 125.96  E-value: 3.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKkrfHQQ-----ALMELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLE---HEEgapftAIREASLLKDLKHA------NIVTLHDIIHTKKT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG------ 367
Cdd:cd07844    73 LTLVFEYLDTDLKQYMDDCG-GGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGE--LKLADFGlaraks 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 --SSCYEHQKVytyiqSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEV-EQLACIMEVLGLPpagfi 443
Cdd:cd07844   150 vpSKTYSNEVV-----TLWYRPPDVLLGSTeYSTSLDMWGVGCIFYEMATGRPLFPGSTDVeDQLHKIFRVLGTP----- 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 444 qtasRRQTFfdsKGFPKNITNNRGKKRYPDSKDLTMVLKTYD--TSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07844   220 ----TEETW---PGVSSNPEFKPYSFPFYPPRPLINHAPRLDriPHGEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
219-514 4.66e-32

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: 125.89  E-value: 4.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKkrfHQQ-----ALMELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd07871     7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLE---HEEgapctAIREVSLLKNLKHA------NIVTLHDIIHTERC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELLGINLYELMKN-NNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYE 372
Cdd:cd07871    78 LTLVFEYLDSDLKQYLDNcGNL--MSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGE--LKLADFGLARAK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTY---IQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASR 448
Cdd:cd07871   154 SVPTKTYsneVVTLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTS 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 449 RQTfFDSKGFPKNITNNrgkkrypdskdLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07871   234 NEE-FRSYLFPQYRAQP-----------LINHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSY 287
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
218-517 1.66e-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: 125.22  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKiiRNKKRFHQQ-----ALMELKILEALRKKDKDNTYNVV----HMKDFf 288
Cdd:cd07850     1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIK--KLSRPFQNVthakrAYRELVLMKLVNHKNIIGLLNVFtpqkSLEEF- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 yfrNHFCITFELLGINLYELMKnnnfqgFSLSIVRrftLSVLkCLQMLSVEK------IIHCDLKPENIVLyqKGQASVK 362
Cdd:cd07850    78 ---QDVYLVMELMDANLCQVIQ------MDLDHER---MSYL-LYQMLCGIKhlhsagIIHRDLKPSNIVV--KSDCTLK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 363 VIDFG--SSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPA 440
Cdd:cd07850   143 ILDFGlaRTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGTPSD 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 441 GFIqtaSRRQTFFdskgfpKNITNNRGK-------KRYPDS---KDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQAL 510
Cdd:cd07850   223 EFM---SRLQPTV------RNYVENRPKyagysfeELFPDVlfpPDSEEHNKLKASQARDLLSKMLVIDPEKRISVDDAL 293

                  ....*..
gi 2032329476 511 KHAWIHQ 517
Cdd:cd07850   294 QHPYINV 300
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
218-515 2.39e-31

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: 122.72  E-value: 2.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQ--QALM-ELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSdlKSVMgEIDLLKKLNHP------NIVKYIGSVKTKDSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCY-- 371
Cdd:cd06627    75 YIILEYVeNGSLASIIKK--FGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG--LVKLADFGVATKln 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 -EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvLGLPPagfiqtasrrq 450
Cdd:cd06627   151 eVEKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQ-DDHPP----------- 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 451 tffdskgFPKNITNNrgkkrypdskdltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06627   219 -------LPENISPE----------------------LRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
218-512 3.45e-31

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: 122.19  E-value: 3.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKII---RNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIdlsNMSEKEREEALNEVKLLSKLKHP------NIVKYYESFEENGKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNFQGFSLS---IVRRFT--LSVLKCLQmlsVEKIIHCDLKPENIVLYQKGQasVKVIDFGS 368
Cdd:cd08215    75 CIVMEYAdGGDLAQKIKKQKKKGQPFPeeqILDWFVqiCLALKYLH---SRKILHRDLKTQNIFLTKDGV--VKLGDFGI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 369 ScyehqKVY--------TYIQSRFYRSPEVILGHPYDVAIDMWSLGCItaeLYtgyplfpgeneveqlacimEVLGLPPA 440
Cdd:cd08215   150 S-----KVLesttdlakTVVGTPYYLSPELCENKPYNYKSDIWALGCV---LY-------------------ELCTLKHP 202
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 441 gfiqtasrrqtfFDSKGFP---KNITnnrgKKRYPdskdltMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd08215   203 ------------FEANNLPalvYKIV----KGQYP------PIPSQYSSELRDLVNSMLQKDPEKRPSANEILSS 255
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
225-519 5.54e-31

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: 124.86  E-value: 5.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKkrFH-----QQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITfE 299
Cdd:cd07853     8 IGYGAFGVVWSVTDPRDGKRVALKKMPNV--FQnlvscKRVFRELKMLCFFKHDNVLSALDILQPPHIDPFEEIYVVT-E 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LLGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG--------SSCY 371
Cdd:cd07853    85 LMQSDLHKIIVSP--QPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCV--LKICDFGlarveepdESKH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQKVYTyiqsRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPagfiQTASRRQ 450
Cdd:cd07853   161 MTQEVVT----QYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPS----LEAMRSA 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 451 tffdSKGFPKNITnnRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSR 519
Cdd:cd07853   233 ----CEGARAHIL--RGPHKPPSLPVLYTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEGR 295
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
219-515 6.23e-31

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 121.43  E-value: 6.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRF-----HQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVI-SKSQLqksglEHQLRREIEIQSHLRHP------NILRLYGYFEDKKR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLY-ELMKNNNFqgfSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY 371
Cdd:cd14007    75 IYLILEYApNGELYkELKKQKRF---DEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE--LKLADFGWSVH 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 -EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagfiqtasrrq 450
Cdd:cd14007   150 aPSNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNV---------------- 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 451 tffDSKgFPKNITnnrgkkryPDSKDltmvlktydtsfldFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14007   214 ---DIK-FPSSVS--------PEAKD--------------LISKLLQKDPSKRLSLEQVLNHPWI 252
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
218-515 1.53e-30

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: 120.43  E-value: 1.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKII----RNKKrfhqqalmELKIL----EALRKKDKDNtynVVHMKDFFY 289
Cdd:cd14002     2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIpkrgKSEK--------ELRNLrqeiEILRKLNHPN---IIEMLDSFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNHFCITFELLGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG-- 367
Cdd:cd14002    71 TKKEFVVVTEYAQGELFQILEDD--GTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGV--VKLCDFGfa 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 --SSCYEHqkVYTYIQ-SRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFpGENEVEQLAcimevlglppagfiq 444
Cdd:cd14002   147 raMSCNTL--VLTSIKgTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPF-YTNSIYQLV--------------- 208
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 445 tasrRQTFFDSKGFPKNITNNrgkkrypdskdltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14002   209 ----QMIVKDPVKWPSNMSPE----------------------FKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
219-514 1.64e-30

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: 121.48  E-value: 1.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKkdkdnTYNVVHMKDFFYFRNH-- 293
Cdd:cd07837     3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRlemEEEGVPSTALREVSLLQMLSQ-----SIYIVRLLDVEHVEENgk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 --FCITFELLGINLYELMKNN---NFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVKVIDFGS 368
Cdd:cd07837    78 plLYLVFEYLDTDLKKFIDSYgrgPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNL-LVDKQKGLLKIADLGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 369 S--------CYEHQkvytyIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPp 439
Cdd:cd07837   157 GraftipikSYTHE-----IVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTP- 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 440 agfiqtasrrqtffDSKGFPkNITNNRGKKRYPDSK--DLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd07837   231 --------------NEEVWP-GVSKLRDWHEYPQWKpqDLSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
219-516 7.92e-30

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: 119.72  E-value: 7.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKkrfHQQ-----ALMELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd07873     4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLE---HEEgapctAIREVSLLKDLKHA------NIVTLHDIIHTEKS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH 373
Cdd:cd07873    75 LTLVFEYLDKDLKQYLDDCG-NSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGE--LKLADFGLARAKS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTY---IQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPP----AGFIQT 445
Cdd:cd07873   152 IPTKTYsneVVTLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTeetwPGILSN 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 446 ASrrqtfFDSKGFPknitnnrgkKRYPDSkdLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIH 516
Cdd:cd07873   232 EE-----FKSYNYP---------KYRADA--LHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFH 286
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
218-512 8.09e-30

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: 119.37  E-value: 8.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNN-ELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYF-----R 291
Cdd:cd07862     2 QYECVAEIGEGAYGKVFKARDLKNGgRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLFDVCTVsrtdrE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG-SSC 370
Cdd:cd07862    82 TKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQ--IKLADFGlARI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 YEHQKVYT-YIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPpagfiqtasRR 449
Cdd:cd07862   160 YSFQMALTsVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLP---------GE 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 450 QTFFDSKGFPKNITNNRG----KKRYPDSKDLTMvlktydtsflDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd07862   231 EDWPRDVALPRQAFHSKSaqpiEKFVTDIDELGK----------DLLLKCLTFNPAKRISAYSALSH 287
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
218-514 1.03e-29

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: 119.70  E-value: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQV--AKCLDHKNNELVALKIIRNKKR----FHQQALMELKILEALRKKdkdntyNVVHMKDFFYFR 291
Cdd:cd07842     1 KYEIEGCIGRGTYGRVykAKRKNGKDGKEYAIKKFKGDKEqytgISQSACREIALLRELKHE------NVVSLVEVFLEH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCI--TFELLGINLYELMK---NNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG--QASVKVI 364
Cdd:cd07842    75 ADKSVylLFDYAEHDLWQIIKfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGpeRGVVKIG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 365 DFG---------SSCYEHQKVYTYIqsrFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENE---------V 425
Cdd:cd07842   155 DLGlarlfnaplKPLADLDPVVVTI---WYRAPELLLGaRHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfqR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 426 EQLACIMEVLGLPPAgfiqtasrrQTFFDSKGFP--KNITNNRGKKRYPDSKDLTMV--LKTYDTSFLDFLRRCLVWEPS 501
Cdd:cd07842   232 DQLERIFEVLGTPTE---------KDWPDIKKMPeyDTLKSDTKASTYPNSLLAKWMhkHKKPDSQGFDLLRKLLEYDPT 302
                         330
                  ....*....|...
gi 2032329476 502 LRMTPDQALKHAW 514
Cdd:cd07842   303 KRITAEEALEHPY 315
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
219-512 3.05e-29

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: 116.54  E-value: 3.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALK--IIRNKKRfhQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCI 296
Cdd:cd06614     2 YKNLEKIGEGASGEVYKATDRATGKEVAIKkmRLRKQNK--ELIINEILIMKECKHP------NIVDYYDSYLVGDELWV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG-----SSc 370
Cdd:cd06614    74 VMEYMdGGSLTDIITQNPVR-MNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDG--SVKLADFGfaaqlTK- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 yEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvLGLPPagfIQTASRRq 450
Cdd:cd06614   150 -EKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITT-KGIPP---LKNPEKW- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 451 tffdskgfpknitnnrgkkrypdSKDltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd06614   224 -----------------------SPE-----------FKDFLNKCLVKDPEKRPSAEELLQH 251
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
220-515 1.24e-28

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: 115.00  E-value: 1.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALMELKILealRKKDKDNT---YNVvhmkdfFYFRNHF 294
Cdd:cd06623     4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHvdGDEEFRKQLLRELKTL---RSCESPYVvkcYGA------FYKEGEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQML-SVEKIIHCDLKPENIVLYQKGQasVKVIDFG-SSCY 371
Cdd:cd06623    75 SIVLEYMdGGSLADLLKKVG--KIPEPVLAYIARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGE--VKIADFGiSKVL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EH--QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG-YPLFPGENE--VEQLACIM--EVLGLPPAGFiq 444
Cdd:cd06623   151 ENtlDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGkFPFLPPGQPsfFELMQAICdgPPPSLPAEEF-- 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 445 tasrrqtffdskgfpknitnnrgkkrypdSKDltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06623   229 -----------------------------SPE-----------FRDFISACLQKDPKKRPSAAELLQHPFI 259
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
219-515 6.20e-28

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: 113.13  E-value: 6.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFhQQALMELKILealrkKDKDNTYnVVHMKDFFYFRNHFCITF 298
Cdd:cd06612     5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDL-QEIIKEISIL-----KQCDSPY-IVKYYGSYFKNTDLWIVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGIN-LYELMK--NNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAsvKVIDFGSSC---YE 372
Cdd:cd06612    78 EYCGAGsVSDIMKitNKTLTEEEIAAI---LYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQA--KLADFGVSGqltDT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGcITA-ELYTGYPLFPGENEVEQLACIMEvlgLPPagfiqtasrrQT 451
Cdd:cd06612   153 MAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLG-ITAiEMAEGKPPYSDIHPMRAIFMIPN---KPP----------PT 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 452 FFDSKGFPKNitnnrgkkrypdskdltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06612   219 LSDPEKWSPE--------------------------FNDFVKKCLVKDPEERPSAIQLLQHPFI 256
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
220-520 9.33e-28

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: 112.82  E-value: 9.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHKNNELVALKIIRN--KKRFHQQALMELKILEalrkkdKDNTYNVVHMKDFFYFRNHFCIT 297
Cdd:cd06605     4 EYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLeiDEALQKQILRELDVLH------KCNSPYIVGFYGAFYSEGDISIC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQML-SVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY-EHQ 374
Cdd:cd06605    78 MEYMdGGSLDKILKE--VGRIPERILGKIAVAVVKGLIYLhEKHKIIHRDVKPSNILVNSRGQ--VKLCDFGVSGQlVDS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG-YPlFPGENE------VEQLACIMEvlGLPPagfiqtas 447
Cdd:cd06605   154 LAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGrFP-YPPPNAkpsmmiFELLSYIVD--EPPP-------- 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 448 rrqtffdskgfpknitnnrgkkRYPDSKdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRN 520
Cdd:cd06605   223 ----------------------LLPSGK--------FSPDFQDFVSQCLQKDPTERPSYKELMEHPFIKRYEY 265
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
219-537 3.54e-27

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: 112.39  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKkrfHQQ-----ALMELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd07872     8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLE---HEEgapctAIREVSLLKDLKHA------NIVTLHDIVHTDKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH 373
Cdd:cd07872    79 LTLVFEYLDKDLKQYMDDCG-NIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGE--LKLADFGLARAKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTY---IQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRR 449
Cdd:cd07872   156 VPTKTYsneVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGISSN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 450 QTfFDSKGFPKnitnnrgKKRYPdskdLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIhqsRNLKpqPRPQT 529
Cdd:cd07872   236 DE-FKNYNFPK-------YKPQP----LINHAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYF---RSLG--TRIHS 298

                  ....*...
gi 2032329476 530 LRKSNSFF 537
Cdd:cd07872   299 LPESISIF 306
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
219-438 6.06e-27

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 110.82  E-value: 6.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKII--RNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCI 296
Cdd:cd07870     2 YLNLEKLGEGSYATVYKGISRINGQLVALKVIsmKTEEGVPFTAIREASLLKGLKHA------NIVLLHDIIHTKETLTF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEHQKV 376
Cdd:cd07870    76 VFEYMHTDLAQYMIQHP-GGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE--LKLADFGLARAKSIPS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 377 YTY---IQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEV-EQLACIMEVLGLP 438
Cdd:cd07870   153 QTYsseVVTLWYRPPDVLLGATdYSSALDIWGAGCIFIEMLQGQPAFPGVSDVfEQLEKIWTVLGVP 219
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
219-515 7.30e-27

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: 110.85  E-value: 7.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM-ELKILEALRKKdkdntyNVVHMKDFFYFRNHFCIT 297
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLEnEIAVLKRIKHE------NIVTLEDIYESTTHYYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYE-LMKNNNFQGFSLSIVRRFTLSVLKCLQMLSvekIIHCDLKPENIVLYQKGQAS-VKVIDFG-SSCYEH 373
Cdd:cd14166    79 MQLVsGGELFDrILERGVYTEKDASRVINQVLSAVKYLHENG---IVHRDLKPENLLYLTPDENSkIMITDFGlSKMEQN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvlglppaGFIQTASrrqTFF 453
Cdd:cd14166   156 GIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKE-------GYYEFES---PFW 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 454 DskgfpknitnnrgkkrypdskDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14166   226 D---------------------DISESAK-------DFIRHLLEKNPSKRYTCEKALSHPWI 259
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
225-426 9.07e-27

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: 109.53  E-value: 9.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIR----NKKRFHQQALMELKILEALrkkdkdNTYNVVHMkdFFYF--RNHFCITF 298
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRkkeiIKRKEVEHTLNERNILERV------NHPFIVKL--HYAFqtEEKLYLVL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY---EHQ 374
Cdd:cd05123    73 DYVpGGELFSHLSKEG--RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH--IKLTDFGLAKElssDGD 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVE 426
Cdd:cd05123   149 RTYTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKE 200
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
213-515 1.21e-26

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: 109.75  E-value: 1.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLET-IGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMELKILEALRKKDKDNTyNVVHMKDFFYFR 291
Cdd:cd14106     3 ENINEVYTVESTpLGRGKFAVVRKCIHKETGKEYAAKFLR-KRRRGQDCRNEILHEIAVLELCKDCP-RVVNLHEVYETR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFEL-LGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQK-GQASVKVIDFGSS 369
Cdd:cd14106    81 SELILILELaAGGELQTLLDEE--ECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfPLGDIKLCDFGIS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CY--EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGEneveqlacimevlglppagfiqtaS 447
Cdd:cd14106   159 RVigEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGD------------------------D 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 448 RRQTFFdskgfpkNITNnrGKKRYPDskDLtmvLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14106   215 KQETFL-------NISQ--CNLDFPE--EL---FKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
225-515 1.86e-26

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: 108.93  E-value: 1.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKDKDNTYNV-VHmkdffyfRNHFCITFEL 300
Cdd:cd06626     8 IGEGTFGKVYTAVNLDTGELMAMKEIRfqdNDPKTIKEIADEMKVLEGLDHPNLVRYYGVeVH-------REEVYIFMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 301 L-GINLYELMKnnnfQGFSL--SIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY------ 371
Cdd:cd06626    81 CqEGTLEELLR----HGRILdeAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL--IKLGDFGSAVKlknntt 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 --EHQKVYTYIQSRFYRSPEVILGHP---YDVAIDMWSLGCITAELYTGYPLFPgenEVEQLACIMEVLGL---PPAgfi 443
Cdd:cd06626   155 tmAPGEVNSLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWS---ELDNEWAIMYHVGMghkPPI--- 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 444 qtasrrqtffdskgfpknitnnrgkkryPDSKDLtmvlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06626   229 ----------------------------PDSLQL-------SPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
225-426 1.93e-26

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: 109.23  E-value: 1.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRN----KKRFHQQALMELKILEALRkkdkdNTYnVVHMKDFFYFRNHFCITFEL 300
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKrdmiRKNQVDSVLAERNILSQAQ-----NPF-VVKLYYSFQGKKNLYLVMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 301 L-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY--EHQKVY 377
Cdd:cd05579    75 LpGGDLYSLLEN--VGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGH--LKLTDFGLSKVglVRRQIK 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 378 TYIQSRF----------------YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVE 426
Cdd:cd05579   151 LSIQKKSngapekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEE 215
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
225-515 2.04e-26

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: 108.47  E-value: 2.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIR-NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELL-G 302
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKcRKAKDREDVRNEIEIMNQLRHP------RLLQLYDAFETPREMVLVMEYVaG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 303 INLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSC-YEHQKVytyIQ 381
Cdd:cd14103    75 GELFERVVDDDFE-LTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLARkYDPDKK---LK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 382 SRF----YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagfiqtasrrQTFFDSKG 457
Cdd:cd14103   151 VLFgtpeFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRA---------------KWDFDDEA 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 458 FpKNITNnrgkkrypDSKdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14103   216 F-DDISD--------EAK--------------DFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
225-514 2.67e-26

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: 108.12  E-value: 2.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELL-GI 303
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQHP------RIIQLHEAYESPTELVLILELCsGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNnfqgFSLS--IVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSScyehQKVYT--Y 379
Cdd:cd14006    75 ELLDRLAER----GSLSeeEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLA----RKLNPgeE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 380 IQSRF----YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagfiqtasrRQTFFDS 455
Cdd:cd14006   147 LKEIFgtpeFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISAC--------------RVDFSEE 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 456 kgFPKNITnnrgkkryPDSKdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd14006   213 --YFSSVS--------QEAK--------------DFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
218-517 5.03e-26

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: 108.28  E-value: 5.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK---RFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd14086     2 EYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKlsaRDHQKLEREARICRLLKHP------NIVRLHDSISEEGFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQ-ASVKVIDFGSSCY- 371
Cdd:cd14086    76 YLVFDLVtGGELFEDIVAREF--YSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgAAVKLADFGLAIEv 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 --EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACImevlglppagfiqtasrR 449
Cdd:cd14086   154 qgDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQI-----------------K 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 450 QTFFDskgFPKN----ITnnrgkkryPDSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAWIHQ 517
Cdd:cd14086   217 AGAYD---YPSPewdtVT--------PEAKDL--------------INQMLTVNPAKRITAAEALKHPWICQ 263
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
219-424 7.83e-26

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: 107.30  E-value: 7.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALK------IIRNKKrfHQQALMELKILealrkkDKDNTYNVVHMkdFFYFRN 292
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKvldkrhIIKEKK--VKYVTIEKEVL------SRLAHPGIVKL--YYTFQD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELlginlyELMKNNNFQGF-----SLSI--VRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVID 365
Cdd:cd05581    73 ESKLYFVL------EYAPNGDLLEYirkygSLDEkcTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDM--HIKITD 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 366 FGSS--------------CYEHQKVYTYIQSR-F-----YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENE 424
Cdd:cd05581   145 FGTAkvlgpdsspestkgDADSQIAYNQARAAsFvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNE 223
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
218-515 1.01e-25

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: 106.48  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN----KKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd14099     2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKssltKPKQREKLKSEIKIHRSLKHP------NIVKFHDCFEDEEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSC-- 370
Cdd:cd14099    76 VYILLELCsNGSLMELLKRRK--ALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMN--VKIGDFGLAArl 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 -YEHQKVYTYIQSRFYRSPEVIL---GHPYDVaiDMWSLGCITAELYTGYPLFpgeneveqlacimevlglppagfiQTA 446
Cdd:cd14099   152 eYDGERKKTLCGTPNYIAPEVLEkkkGHSFEV--DIWSLGVILYTLLVGKPPF------------------------ETS 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 447 SRRQTFfdskgfpKNITNNRgkKRYPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14099   206 DVKETY-------KRIKKNE--YSFPSHLSISDEAK-------DLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
225-424 1.80e-25

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: 106.16  E-value: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNK----KRFHQQALMELKILEA--------LRKKDKDNTYnvvhmkdfFYFRN 292
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhivqTRQQEHIFSEKEILEEcnspfivkLYRTFKDKKY--------LYMLM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCitfelLGINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS--C 370
Cdd:cd05572    73 EYC-----LGGELWTILRDRGL--FDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGY--VKLVDFGFAkkL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENE 424
Cdd:cd05572   144 GSGRKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDE 197
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
218-513 1.81e-25

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: 105.94  E-value: 1.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQ---ALMELKILEALrkkdkdNTYNVVHMKDFFYFRNHF 294
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEredSVNEIRLLASV------NHPNIIRYKEAFLDGNRL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGI-NLYELMKNNNFQG--FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY 371
Cdd:cd08530    75 CIVMEYAPFgDLSKLISKRKKKRrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDL--VKIGDLGISKV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQKV-YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENeVEQLA--CIMEVLGLPPAGFiqtasr 448
Cdd:cd08530   153 LKKNLaKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEART-MQELRykVCRGKFPPIPPVY------ 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 449 rqtffdskgfpknitnnrgkkrypdSKDLTmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHA 513
Cdd:cd08530   226 -------------------------SQDLQ-----------QIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
215-514 2.05e-25

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 105.92  E-value: 2.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKIlEALRKKDKDNtynVVHMKDFFYFRNHF 294
Cdd:cd14083     1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLENEI-AVLRKIKHPN---IVQLLDIYESKSHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYE-LMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS-VKVIDFGSSCY 371
Cdd:cd14083    77 YLVMELVtGGELFDrIVEKGSYTEKDASHLIR---QVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSkIMISDFGLSKM 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQKVY-TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasRRQ 450
Cdd:cd14083   154 EDSGVMsTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQIL---------------KAE 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 451 TFFDSkgfpknitnnrgkkryPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd14083   219 YEFDS----------------PYWDDISDSAK-------DFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
218-414 2.77e-25

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: 105.16  E-value: 2.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM----ELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd14073     2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVrirrEIEIMSSLNHP------HIIRIYEVFENKDK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMknNNFQGFSLSIVRRF----TLSVLKCLQMlsveKIIHCDLKPENIVLYQKGqaSVKVIDFG- 367
Cdd:cd14073    76 IVIVMEYAsGGELYDYI--SERRRLPEREARRIfrqiVSAVHYCHKN----GVVHRDLKLENILLDQNG--NAKIADFGl 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 368 SSCYEHQKV-YTYIQSRFYRSPEVILGHPYD-VAIDMWSLGCItaeLYT 414
Cdd:cd14073   148 SNLYSKDKLlQTFCGSPLYASPEIVNGTPYQgPEVDCWSLGVL---LYT 193
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
219-515 3.46e-25

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: 105.11  E-value: 3.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKIleALRKKDKDNtyNVVHMKDFFYFRNHFCITF 298
Cdd:cd14167     5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIENEI--AVLHKIKHP--NIVALDDIYESGGHLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS-VKVIDFGSSCYEHQK- 375
Cdd:cd14167    81 QLVsGGELFDRIVEKGF--YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSkIMISDFGLSKIEGSGs 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 -VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasRRQTFFD 454
Cdd:cd14167   159 vMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQIL---------------KAEYEFD 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 455 SkgfpknitnnrgkkryPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14167   224 S----------------PYWDDISDSAK-------DFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
218-516 4.37e-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: 107.04  E-value: 4.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKDKDNTYNV-VHMKDFFYFRNH 293
Cdd:cd07876    22 RYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSrpfQNQTHAKRAYRELVLLKCVNHKNIISLLNVfTPQKSLEEFQDV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FcITFELLGINLYELMKNNnfqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFG---SSC 370
Cdd:cd07876   102 Y-LVMELMDANLCQVIHME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVV--KSDCTLKILDFGlarTAC 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 YEHQkVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIqtASRRQ 450
Cdd:cd07876   175 TNFM-MTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSAEFM--NRLQP 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 451 TFfdskgfpKNITNNRGK-------KRYPD----SKDLTMVLKTYDTSflDFLRRCLVWEPSLRMTPDQALKHAWIH 516
Cdd:cd07876   252 TV-------RNYVENRPQypgisfeELFPDwifpSESERDKLKTSQAR--DLLSKMLVIDPDKRISVDEALRHPYIT 319
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
218-514 5.54e-25

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: 104.86  E-value: 5.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFH------QQALMELKILEALrkkdkdNTYNVVHMKDFFYFR 291
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQI-VKRKVAgndknlQLFQREINILKSL------EHPGIVRLIDWYEDD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSC 370
Cdd:cd14098    74 QHIYLVMEYVeGGDLMDFIMAWG--AIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 YEHQKVY--TYIQSRFYRSPEVILGHP------YDVAIDMWSLGCITAELYTGYPLFPGENeveQLACIMEVlglppagf 442
Cdd:cd14098   152 VIHTGTFlvTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSS---QLPVEKRI-------- 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 443 iqtasrrqtffdskgfpknitnnrGKKRYPDSKDLTMVLKtydTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd14098   221 ------------------------RKGRYTQPPLVDFNIS---EEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
225-429 6.97e-25

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: 103.77  E-value: 6.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQV--AKCldhkNNELVALKIIRNKKRFHQQALM---ELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFE 299
Cdd:cd13999     1 IGSGSFGEVykGKW----RGTDVAIKKLKVEDDNDELLKEfrrEVSILSKLRHP------NIVQFIGACLSPPPLCIVTE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LL-GINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCYEHQK--- 375
Cdd:cd13999    71 YMpGGSLYDLLHKKKIP-LSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENF--TVKIADFGLSRIKNSTtek 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 376 ----VYTYIqsrfYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLA 429
Cdd:cd13999   148 mtgvVGTPR----WMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAA 201
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
222-523 8.25e-25

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: 104.81  E-value: 8.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALMELKILealrkKDKDNTYNVVHMKDFFyfRNHFC---I 296
Cdd:cd06621     6 LSSLGEGAGGSVTKCRLRNTKTIFALKTITtdPNPDVQKQILRELEIN-----KSCASPYIVKYYGAFL--DEQDSsigI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGI----NLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYE 372
Cdd:cd06621    79 AMEYCEGgsldSIYKKVKKKGGR-IGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ--VKLCDFGVSGEL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVY-TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGEneveqlacimevlGLPPAGFIQTASrrqt 451
Cdd:cd06621   156 VNSLAgTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPE-------------GEPPLGPIELLS---- 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 452 ffdskgFPKNITNnrgkkryPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKP 523
Cdd:cd06621   219 ------YIVNMPN-------PELKDEPENGIKWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKV 277
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
218-517 1.39e-24

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: 103.79  E-value: 1.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCIT 297
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHR------NILRLHESFESHEELVMI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNNFQGFSLSIVRrFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEH--Q 374
Cdd:cd14104    75 FEFIsGVDIFERITTARFELNEREIVS-YVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLKpgD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KV-YTYIQSRFYrSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagfiqtasrrQTFF 453
Cdd:cd14104   154 KFrLQYTSAEFY-APEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNA---------------EYAF 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 454 DSKGFpKNITNNRgkkrypdskdltmvlktydtsfLDFLRRCLVWEPSLRMTPDQALKHAWIHQ 517
Cdd:cd14104   218 DDEAF-KNISIEA----------------------LDFVDRLLVKERKSRMTAQEALNHPWLKQ 258
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
219-515 3.46e-24

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: 102.44  E-value: 3.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV--AKCLDhkNNELVALKIIRNKKRfhqQALMElKILEALRKKDKDNTYNVVHMKDFFYFRNHFCI 296
Cdd:cd06610     3 YELIEVIGSGATAVVyaAYCLP--KKEKVAIKRIDLEKC---QTSMD-ELRKEIQAMSQCNHPNVVSYYTSFVVGDELWL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKN-NNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS----- 369
Cdd:cd06610    77 VMPLLsGGSLLDIMKSsYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDG--SVKIADFGVSaslat 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 --CYEHQKVYTYIQSRFYRSPEVI-LGHPYDVAIDMWSLGcITA-ELYTGYPlfPGENeveqlacimevlgLPPagfiqt 445
Cdd:cd06610   155 ggDRTRKVRKTFVGTPCWMAPEVMeQVRGYDFKADIWSFG-ITAiELATGAA--PYSK-------------YPP------ 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 446 asrrqtffdSKGFPKNITNNrgkkryPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06610   213 ---------MKVLMLTLQND------PPSLETGADYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
218-515 4.32e-24

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: 102.32  E-value: 4.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM--ELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:cd06609     2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIEDIqqEIQFLSQCDSP------YITKYYGSFLKGSKLW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-GINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG-SSCYEH 373
Cdd:cd06609    76 IIMEYCgGGSVLDLLKPGPLDETYIAFILR---EVLLGLEYLHSEGKIHRDIKAANILLSEEGD--VKLADFGvSGQLTS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 Q--KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYP----LFPgeneveqlaciMEVLGLPPagfiqtas 447
Cdd:cd06609   151 TmsKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPplsdLHP-----------MRVLFLIP-------- 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 448 rrqtffdsKGFPKNITNNRgkkrypdskdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06609   212 --------KNNPPSLEGNK-----------------FSKPFKDFVELCLNKDPKERPSAKELLKHKFI 254
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
225-432 4.96e-24

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: 101.53  E-value: 4.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKII---RNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELL 301
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEIsrkKLNKKLQENLESEIAILKSIKHP------NIVRLYDVQKTEDFIYLVLEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 -GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASV-KVIDFGSSCYEHQKVY-- 377
Cdd:cd14009    75 aGGDLSQYIRKR--GRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVlKIADFGFARSLQPASMae 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 378 TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM 432
Cdd:cd14009   153 TLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIE 207
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
216-438 7.55e-24

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: 102.46  E-value: 7.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 216 AYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQ--QALMELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd07869     4 ADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTpfTAIREASLLKGLKHA------NIVLLHDIIHTKET 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELLGINLYELMkNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH 373
Cdd:cd07869    78 LTLVFEYVHTDLCQYM-DKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGE--LKLADFGLARAKS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTY---IQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVE-QLACIMEVLGLP 438
Cdd:cd07869   155 VPSHTYsneVVTLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQdQLERIFLVLGTP 224
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
219-515 1.23e-23

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: 100.72  E-value: 1.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV--AKCLDHKNNELVALKIIrNKKR----FHQQAL-MELKILEALRKKdkdntyNVVHMKDFFYFR 291
Cdd:cd14080     2 YRLGKTIGEGSYSKVklAEYTKSGLKEKVACKII-DKKKapkdFLEKFLpRELEILRKLRHP------NIIQVYSIFERG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGI-NLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS- 369
Cdd:cd14080    75 SKVFIFMEYAEHgDLLEYIQKRGA--LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN--VKLSDFGFAr 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 -CYEHQKVY---TYIQSRFYRSPEVILGHPYDVAI-DMWSLGCItaeLYtgyplfpgeneveqlacIMEVLGLPpagfiq 444
Cdd:cd14080   151 lCPDDDGDVlskTFCGSAAYAAPEILQGIPYDPKKyDIWSLGVI---LY-----------------IMLCGSMP------ 204
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 445 tasrrqtfFDSKGFPKNITNNRGKK-RYPDSKdltmvlKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14080   205 --------FDDSNIKKMLKDQQNRKvRFPSSV------KKLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
219-515 1.81e-23

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: 100.04  E-value: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEV--LETIGKGSFGQVAKCLDHKNNELVALKIIRNK-KRFHQQALMELKILEALrkkdkdNTYNVVHMKDFFYFRNHFC 295
Cdd:cd14192     4 YAVcpHEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKgAKEREEVKNEINIMNQL------NHVNLIQLYDAFESKTNLT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-GINLYELMKNNNFQGFSLSIVRrFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFG-SSCYE- 372
Cdd:cd14192    78 LIMEYVdGGELFDRITDESYQLTELDAIL-FTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGlARRYKp 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLacimevlglppaGFIQTASRRqtf 452
Cdd:cd14192   157 REKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETM------------NNIVNCKWD--- 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 453 FDSKGFpKNITNnrgkkrypDSKdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14192   222 FDAEAF-ENLSE--------EAK--------------DFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
219-515 2.05e-23

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: 100.35  E-value: 2.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKIlEALRKKDKDNtynVVHMKDFFYFRNHFCITF 298
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVENEI-AVLRRINHEN---IVSLEDIYESPTHLYLAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVKVI--DFGSSCYEHQK 375
Cdd:cd14169    81 ELVtGGELFDRIIERGS--YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENL-LYATPFEDSKIMisDFGLSKIEAQG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 VY-TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasRRQTFFD 454
Cdd:cd14169   158 MLsTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQIL---------------KAEYEFD 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 455 SkgfpknitnnrgkkryPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14169   223 S----------------PYWDDISESAK-------DFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
215-423 2.18e-23

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: 99.64  E-value: 2.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLETIGKGSFGQVAKCLDhKNNELVALKIIRNKKRFHQQALM----ELKILEALrkkdkdNTYNVVHMKDFFYF 290
Cdd:cd14161     1 LKHRYEFLETLGKGTYGRVKKARD-SSGRLVAIKSIRKDRIKDEQDLLhirrEIEIMSSL------NHPHIISVYEVFEN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCITFELLGI-NLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS 369
Cdd:cd14161    74 SSKIVIVMEYASRgDLYDYISER--QRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANG--NIKIADFGLS 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 370 CYEHQKVY--TYIQSRFYRSPEVILGHPY-DVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd14161   150 NLYNQDKFlqTYCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHD 206
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
225-515 2.26e-23

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: 99.93  E-value: 2.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQalmelKILEALRKKDKDNTYNVVH----MKDFFY----------- 289
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIF-NKSRLRKR-----REGKNDRGKIKNALDDVRReiaiMKKLDHpnivrlyevid 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 --FRNHFCITFELlgINLYELMKNNNFQG---FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVI 364
Cdd:cd14008    75 dpESDKLYLVLEY--CEGGPVMELDSGDRvppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGT--VKIS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 365 DFGSScyehQKVY---TYIQSR-----FYrSPEVILGH--PYDV-AIDMWSLGcITaeLYT---GYPLFPGENEVEQLac 430
Cdd:cd14008   151 DFGVS----EMFEdgnDTLQKTagtpaFL-APELCDGDskTYSGkAADIWALG-VT--LYClvfGRLPFNGDNILELY-- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 431 imevlglppagfiqtasrrqtffdskgfpKNITNNrgKKRYPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQAL 510
Cdd:cd14008   221 -----------------------------EAIQNQ--NDEFPIPPELSPELK-------DLLRRMLEKDPEKRITLKEIK 262

                  ....*
gi 2032329476 511 KHAWI 515
Cdd:cd14008   263 EHPWV 267
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
218-515 2.62e-23

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: 100.16  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFH----------QQALMELKILEALRKKdkdntyNVVHMKDF 287
Cdd:cd14084     7 KYIMSRTLGSGACGEVKLAYDKSTCKKVAIKII-NKRKFTigsrreinkpRNIETEIEILKKLSHP------CIIKIEDF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 288 FYFRNHFCITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS-VKVID 365
Cdd:cd14084    80 FDAEDDYYIVLELMeGGELFDRVVSN--KRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEEClIKITD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 366 FGSSCY--EHQKVYTYIQSRFYRSPEVIL---GHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLAcimevlglppa 440
Cdd:cd14084   158 FGLSKIlgETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLK----------- 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 441 gfIQTASRRQTfFDSKGFpKNITNnrgkkrypDSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14084   227 --EQILSGKYT-FIPKAW-KNVSE--------EAKDL--------------VKKMLVVDPSRRPSIEEALEHPWL 275
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
218-516 4.61e-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: 101.32  E-value: 4.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHF 294
Cdd:cd07874    18 RYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSrpfQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLEEFQDV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGINLYELMKnnnfqgFSLSIVR-RFTLSVLKC-LQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFG--SSC 370
Cdd:cd07874    98 YLVMELMDANLCQVIQ------MELDHERmSYLLYQMLCgIKHLHSAGIIHRDLKPSNIVV--KSDCTLKILDFGlaRTA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTAsrrq 450
Cdd:cd07874   170 GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKL---- 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 451 tffdsKGFPKNITNNRGK-------KRYPDS--KDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIH 516
Cdd:cd07874   246 -----QPTVRNYVENRPKyagltfpKLFPDSlfPADSEHNKLKASQARDLLSKMLVIDPAKRISVDEALQHPYIN 315
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
219-515 6.00e-23

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: 98.61  E-value: 6.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQAL----------MELKILEALRKKDKDntyNVVHMKDFF 288
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIF-KERILVDTWvrdrklgtvpLEIHILDTLNKRSHP---NIVKLLDFF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 YFRNHFCITFEL--LGINLYELM--KNNNFQGFSLSIVRRFTLSVlkclQMLSVEKIIHCDLKPENIVLYQKGqaSVKVI 364
Cdd:cd14004    78 EDDEFYYLVMEKhgSGMDLFDFIerKPNMDEKEAKYIFRQVADAV----KHLHDQGIVHRDIKDENVILDGNG--TIKLI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 365 DFGSSCY-EHQKVYTYIQSRFYRSPEVILGHPYD-VAIDMWSLGCItaeLYTgypLFPGENEVEQLACIMEVlglppagf 442
Cdd:cd14004   152 DFGSAAYiKSGPFDTFVGTIDYAAPEVLRGNPYGgKEQDIWALGVL---LYT---LVFKENPFYNIEEILEA-------- 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 443 iqtasrrqtffDSKgFPKNItnnrgkkrypdSKDLtmvlktydtsfLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14004   218 -----------DLR-IPYAV-----------SEDL-----------IDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
217-515 6.16e-23

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: 98.83  E-value: 6.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 217 YRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM-ELKILEALrkkdkdNTYNVVHMKDFFYFRNHFC 295
Cdd:cd14193     4 YNVNKEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKnEIEVMNQL------NHANLIQLYDAFESRNDIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-GINLYELMKNNNFQGFSLSIVRrFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFG-SSCYE- 372
Cdd:cd14193    78 LVMEYVdGGELFDRIIDENYNLTELDTIL-FIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGlARRYKp 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagfiqtasrrQTF 452
Cdd:cd14193   157 REKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILAC---------------QWD 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 453 FDSKGFpknitnnrgkkrypdsKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14193   222 FEDEEF----------------ADISEEAK-------DFISKLLIKEKSWRMSASEALKHPWL 261
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
222-515 6.33e-23

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: 99.36  E-value: 6.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALMELKILealrKKDKDNTYNVVhmkdfFY---FRNHFC- 295
Cdd:cd06616    11 LGEIGRGAFGTVNKMLHKPSGTIMAVKRIRstVDEKEQKRLLMDLDVV----MRSSDCPYIVK-----FYgalFREGDCw 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGI---NLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVE-KIIHCDLKPENIVLYQKGqaSVKVIDFGSScy 371
Cdd:cd06616    82 ICMELMDIsldKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNG--NIKLCDFGIS-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 eHQKVYTYIQS-----RFYRSPEVIL----GHPYDVAIDMWSLGCITAELYTG-YPlFPGENEV-EQLAciMEVLGLPPa 440
Cdd:cd06616   158 -GQLVDSIAKTrdagcRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGkFP-YPKWNSVfDQLT--QVVKGDPP- 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 441 gfiqtasrrqtffdskgfpknitnnrgkKRYPDSKdltmvlKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06616   233 ----------------------------ILSNSEE------REFSPSFVNFVNLCLIKDESKRPKYKELLKHPFI 273
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
218-515 8.15e-23

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: 98.42  E-value: 8.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM-ELKILEALRKKdkdntyNVVHMKDFFYFRNHFCI 296
Cdd:cd14114     3 HYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRkEIQIMNQLHHP------KLINLHDAFEDDNEMVL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCY---- 371
Cdd:cd14114    77 ILEFLsGGELFERIAAEHYK-MSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHldpk 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQKVYTYIQSrfYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLacimevlglppagfiQTASRRQT 451
Cdd:cd14114   156 ESVKVTTGTAE--FAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETL---------------RNVKSCDW 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 452 FFDSKGFpKNITnnrgkkryPDSKdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14114   219 NFDDSAF-SGIS--------EEAK--------------DFIRKLLLADPNKRMTIHQALEHPWL 259
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
218-512 1.57e-22

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: 97.67  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELvALKIIRNKKRFHQ--QALM-ELKILEALRKKDkdntyNVVHMKDFFYFRN-- 292
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVLNPKKKIY-ALKRVDLEGADEQtlQSYKnEIELLKKLKGSD-----RIIQLYDYEVTDEdd 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgqaSVKVIDFGSScye 372
Cdd:cd14131    76 YLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKG---RLKLIDFGIA--- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 hqkvyTYIQS------RF-------YRSPEVILGHPYDVAI----------DMWSLGCItaeLYtgyplfpgeneveQLa 429
Cdd:cd14131   150 -----KAIQNdttsivRDsqvgtlnYMSPEAIKDTSASGEGkpkskigrpsDVWSLGCI---LY-------------QM- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 430 cimeVLGLPPAGFIQTASRRQtffdskgfpKNITNNRGKKRYPD--SKDLTMVLKtydtsfldflrRCLVWEPSLRMTPD 507
Cdd:cd14131   208 ----VYGKTPFQHITNPIAKL---------QAIIDPNHEIEFPDipNPDLIDVMK-----------RCLQRDPKKRPSIP 263

                  ....*
gi 2032329476 508 QALKH 512
Cdd:cd14131   264 ELLNH 268
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
218-380 1.96e-22

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: 97.14  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRfHQQALMELKILEALRkkdkdNTYNVVHMKDFFYFRNHFCIT 297
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSK-HPQLEYEAKVYKLLQ-----GGPGIPRLYWFGQEGDYNVMV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLYELMKNNNfqgfslsivRRFTL-SVLkCL--QMLS-VEKI-----IHCDLKPENIVL-YQKGQASVKVIDFG 367
Cdd:cd14016    75 MDLLGPSLEDLFNKCG---------RKFSLkTVL-MLadQMISrLEYLhskgyIHRDIKPENFLMgLGKNSNKVYLIDFG 144
                         170
                  ....*....|....
gi 2032329476 368 -SSCYEHQKVYTYI 380
Cdd:cd14016   145 lAKKYRDPRTGKHI 158
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
218-516 2.48e-22

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: 98.96  E-value: 2.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQQALMELKILEALRKKDKDNTYNV-VHMKDFFYFRNH 293
Cdd:cd07875    25 RYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSrpfQNQTHAKRAYRELVLMKCVNHKNIIGLLNVfTPQKSLEEFQDV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FcITFELLGINLYELMKnnnfqgFSLSIVR-RFTLSVLKC-LQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFG--SS 369
Cdd:cd07875   105 Y-IVMELMDANLCQVIQ------MELDHERmSYLLYQMLCgIKHLHSAGIIHRDLKPSNIVV--KSDCTLKILDFGlaRT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRR 449
Cdd:cd07875   176 AGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCPEFMKKLQPT 255
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 450 -QTFFDSKgfPKnITNNRGKKRYPDskdltmVLKTYDTSF--------LDFLRRCLVWEPSLRMTPDQALKHAWIH 516
Cdd:cd07875   256 vRTYVENR--PK-YAGYSFEKLFPD------VLFPADSEHnklkasqaRDLLSKMLVIDASKRISVDEALQHPYIN 322
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
219-523 2.91e-22

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: 97.12  E-value: 2.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM-ELKILEALRKKdkdntyNVVHMKDFFYFRNHFCIT 297
Cdd:cd06611     7 WEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMvEIDILSECKHP------NIVGLYEAYFYENKLWIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FEL-----LGINLYELMKnnnfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSC-- 370
Cdd:cd06611    81 IEFcdggaLDSIMLELER-----GLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGD--VKLADFGVSAkn 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 -YEHQKVYTYIQSRFYRSPEVIL-----GHPYDVAIDMWSLGCITAELYTGYPlfPgENEVEQLACIMEVLGLPPAgfiq 444
Cdd:cd06611   154 kSTLQKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEP--P-HHELNPMRVLLKILKSEPP---- 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 445 tasrrqTFFDSKGFPKnitnnrgkkrypdskdltmvlktydtSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKP 523
Cdd:cd06611   227 ------TLDQPSKWSS--------------------------SFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKA 273
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
219-426 3.26e-22

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 96.46  E-value: 3.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR-----NKKRfhQQALMELKILEALRKK----------DKDNTynVVH 283
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDygkmsEKEK--QQLVSEVNILRELKHPnivryydrivDRANT--TLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 284 --MKdffyfrnhFCItfellGINLYELMKN--NNFQGFSLSIVRRFTLSVLKCLQ-----MLSVEKIIHCDLKPENIVLY 354
Cdd:cd08217    78 ivME--------YCE-----GGDLAQLIKKckKENQYIPEEFIWKIFTQLLLALYechnrSVGGGKILHRDLKPANIFLD 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 355 QKGqaSVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVE 426
Cdd:cd08217   145 SDN--NVKLGDFGLARVlshDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLE 217
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
215-515 3.51e-22

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 96.33  E-value: 3.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLETIGKGSFGqVAKCLDHK-NNELVALKIIRNKK-----RFHqqALMELKILEALRKKDKDNTYNVVHMKDFF 288
Cdd:cd14074     1 IAGLYDLEETLGRGHFA-VVKLARHVfTGEKVAVKVIDKTKlddvsKAH--LFQEVRCMKLVQHPNVVRLYEVIDTQTKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 YfrnhfcITFEL-LGINLYE-LMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgQASVKVIDF 366
Cdd:cd14074    78 Y------LILELgDGGDMYDyIMKHEN--GLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEK-QGLVKLTDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 367 G-SSCYEH-QKVYTYIQSRFYRSPEVILGHPYDV-AIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagfi 443
Cdd:cd14074   149 GfSNKFQPgEKLETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDC--------- 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 444 qtasrRQTffdskgFPKNITnnrgkkryPDSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14074   220 -----KYT------VPAHVS--------PECKDL--------------IRRMLIRDPKKRASLEEIENHPWL 258
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
213-515 1.09e-21

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 95.09  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM-------ELKILEALRKKdkdntyNVVHMK 285
Cdd:cd14194     1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVsredierEVSILKEIQHP------NVITLH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 286 DFFYFRNHFCITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG--QASVK 362
Cdd:cd14194    75 EVYENKTDVILILELVaGGELFDFLAEK--ESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpKPRIK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 363 VIDFG-----SSCYEHQKVYTYIQsrfYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlgl 437
Cdd:cd14194   153 IIDFGlahkiDFGNEFKNIFGTPE---FVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAV--- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 438 ppagfiqTASRRQTFFDSkgfpknitnnrgkkrypdskdltmvlktydTSFL--DFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14194   227 -------NYEFEDEYFSN------------------------------TSALakDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
219-515 1.20e-21

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: 95.25  E-value: 1.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKR-------FHQQALMELKILEALRKKdkdntyNVVHMKDFFYFR 291
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgvSREDIEREVSILRQVLHP------NIITLHDVFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG--QASVKVIDFG- 367
Cdd:cd14105    81 TDVVLILELVaGGELFDFLAEK--ESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpIPRIKLIDFGl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 SSCYEHQKVYTYI-QSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagfiqta 446
Cdd:cd14105   159 AHKIEDGNEFKNIfGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV------------ 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 447 srrQTFFDSKGFPknitnnrgkkrypdskdltmvlktyDTSFL--DFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14105   227 ---NYDFDDEYFS-------------------------NTSELakDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
219-423 1.47e-21

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: 95.34  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALK------IIRNKKRFHqqALMELKILEALRK----------KDKDNTYNVV 282
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKilkkakIIKLKQVEH--VLNEKRILSEVRHpfivnllgsfQDDRNLYMVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 283 HmkdffyfrnhFCITFELLginlYELMKNNNFqgfSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVK 362
Cdd:cd05580    81 E----------YVPGGELF----SLLRRSGRF---PNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDG--HIK 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 363 VIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd05580   142 ITDFGFAKRVKDRTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDEN 202
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
223-419 1.93e-21

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 93.89  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNN-ELVALKIIrNKKRFHQQA----LMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCIT 297
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGArEVVAVKCV-SKSSLNKAStenlLTEIELLKKLKHP------HIVELKDFQWDEEHIYLI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCY--EHQ 374
Cdd:cd14121    74 MEYCsGGDLSRFIRSR--RTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHlkPND 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd14121   152 EAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPF 196
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
220-512 3.48e-21

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: 94.04  E-value: 3.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALMELKILealrkKDKDNTYNVVHMKDFFYFRNHFCIt 297
Cdd:cd06620     8 ETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHidAKSSVRKQILRELQIL-----HECHSPYIVSFYGAFLNENNNIII- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 fellginLYELMKNNNFQG-------FSLSIVRRFTLSVLKCLQML-SVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS 369
Cdd:cd06620    82 -------CMEYMDCGSLDKilkkkgpFPEEVLGKIAVAVLEGLTYLyNVHRIIHRDIKPSNILVNSKGQ--IKLCDFGVS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CYEHQKVY-TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG-YPLFPGENEVEQLACIMEVLGLppagfIQtas 447
Cdd:cd06620   153 GELINSIAdTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGeFPFAGSNDDDDGYNGPMGILDL-----LQ--- 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 448 rRQTFFDSKGFPKnitnnrgKKRYPdsKDLTmvlktydtsflDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd06620   225 -RIVNEPPPRLPK-------DRIFP--KDLR-----------DFVDRCLLKDPRERPSPQLLLDH 268
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
219-517 1.06e-20

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: 92.54  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR-NKKRFHQQALM-ELKILEALRKKDKDNT--YNVVHMKDffyfrNHF 294
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNlDTDDDDVSDIQkEVALLSQLKLGQPKNIikYYGSYLKG-----PSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMlsvEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH 373
Cdd:cd06917    78 WIIMDYCeGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHK---DGIIHRDIKAANILVTNTGN--VKLCDFGVAASLN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 Q---KVYTYIQSRFYRSPEVIL-GHPYDVAIDMWSLGCITAELYTGYPLFPGeneVEQLACIMEVlglppagfiqtasrr 449
Cdd:cd06917   153 QnssKRSTFVGTPYWMAPEVITeGKYYDTKADIWSLGITTYEMATGNPPYSD---VDALRAVMLI--------------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 450 qtffdskgfpknitnnrgkkryPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQ 517
Cdd:cd06917   215 ----------------------PKSKPPRLEGNGYSPLLKEFVAACLDEEPKDRLSADELLKSKWIKQ 260
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
219-423 1.70e-20

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: 91.46  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKR----FHQQALM-ELKILEALRKKdkdntyNVVHMKDFFYFRN- 292
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIV-DRRRaspdFVQKFLPrELSILRRVNHP------NIVQMFECIEVANg 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELLGINLYELMKNNNFQGFSLSivRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQaSVKVIDFGSSCYE 372
Cdd:cd14164    75 RLYIVMEAAATDLLQKIQEVHHIPKDLA--RDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDR-KIKIADFGFARFV 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 373 H---QKVYTYIQSRFYRSPEVILGHPYDV-AIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd14164   152 EdypELSTTFCGSRAYTPPEVILGTPYDPkKYDVWSLGVVLYVMVTGTMPFDETN 206
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
219-515 2.26e-20

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 91.56  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKR-------FHQQALMELKILEALRKKdkdntyNVVHMKDFFYFR 291
Cdd:cd14196     7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREVSILRQVLHP------NIITLHDVYENR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG--QASVKVIDFG- 367
Cdd:cd14196    81 TDVVLILELVsGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipIPHIKLIDFGl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 ----SSCYEHQKVYTYIQsrfYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagfi 443
Cdd:cd14196   159 aheiEDGVEFKNIFGTPE---FVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV--------- 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 444 qtasrrQTFFDSKGFPKniTNNRGKkrypdskdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14196   227 ------SYDFDEEFFSH--TSELAK---------------------DFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
219-515 2.50e-20

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: 91.22  E-value: 2.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRnKKRF--------HQQALMELKILEALRKKdkdntyNVVHMKDFFYF 290
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIK-KRRLsssrrgvsREEIEREVNILREIQHP------NIITLHDIFEN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS--VKVIDFG 367
Cdd:cd14195    80 KTDVVLILELVsGGELFDFLAEK--ESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNprIKLIDFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 -----SSCYEHQKVYTYIQsrfYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagf 442
Cdd:cd14195   158 iahkiEAGNEFKNIFGTPE---FVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAV-------- 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 443 iqtasrrQTFFDSKGFPKniTNNRGKkrypdskdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14195   227 -------NYDFDEEYFSN--TSELAK---------------------DFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
219-515 3.87e-20

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 90.58  E-value: 3.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKII--RNKKRFHQQAlmeLKILEALRKKDKD-----------NTYNVVHMK 285
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprASNAGLKKER---EKRLEKEISRDIRtireaalssllNHPHICRLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 286 DFFYFRNHFCITFELL-GINLYELMknnnFQGFSLS--IVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVK 362
Cdd:cd14077    80 DFLRTPNHYYMLFEYVdGGQLLDYI----ISHGKLKekQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGN--IK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 363 VIDFG-SSCYEHQK-VYTYIQSRFYRSPEVILGHPY-DVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglpp 439
Cdd:cd14077   154 IIDFGlSNLYDPRRlLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIK------- 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 440 agfiqtasrrqtffdskgfpknitnnRGKKRYPdskdltmvlKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14077   227 --------------------------KGKVEYP---------SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
219-518 8.74e-20

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: 90.57  E-value: 8.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALMELKILEalrkkdKDNTYNVVHMKDFFYFRNHFCI 296
Cdd:cd06615     3 FEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHleIKPAIRNQIIRELKVLH------ECNSPYIVGFYGAFYSDGEISI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQML-SVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEHQ 374
Cdd:cd06615    77 CMEHMdGGSLDQVLKK--AGRIPENILGKISIAVLRGLTYLrEKHKIMHRDVKPSNILVNSRGE--IKLCDFGVSGQLID 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVY-TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG-YPLfPGENEVEQ---LACIMEVLGLP-----PAGFIQ 444
Cdd:cd06615   153 SMAnSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrYPI-PPPDAKELeamFGRPVSEGEAKeshrpVSGHPP 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 445 TASRRQTFFDskgFPKNITNNRgKKRYPDskdltmvlKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQS 518
Cdd:cd06615   232 DSPRPMAIFE---LLDYIVNEP-PPKLPS--------GAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRA 293
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
218-514 8.92e-20

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: 89.31  E-value: 8.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQAL--MELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMieNEVAILRRVKHP------NIVQLIEEYDTDTELY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-GINLYElmknnnfqgfSLSIVRRFT-----------LSVLKCLQMLSvekIIHCDLKPEN--IVLYQKGQASV 361
Cdd:cd14095    75 LVMELVkGGDLFD----------AITSSTKFTerdasrmvtdlAQALKYLHSLS---IVHRDIKPENllVVEHEDGSKSL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 362 KVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF--PGENEVEQLACIM--EVLGL 437
Cdd:cd14095   142 KLADFGLATEVKEPLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFrsPDRDQEELFDLILagEFEFL 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 438 PPagfiqtasrrqtFFDskgfpkNITnnrgkkryPDSKDLTMVLktydtsfldflrrcLVWEPSLRMTPDQALKHAW 514
Cdd:cd14095   222 SP------------YWD------NIS--------DSAKDLISRM--------------LVVDPEKRYSAGQVLDHPW 258
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
219-515 9.28e-20

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: 90.07  E-value: 9.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALrkkdkDNTYNVVHMKDFFYFR-----NH 293
Cdd:cd06638    20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKAL-----SDHPNVVKFYGMYYKKdvkngDQ 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMKNNNFQGFSLS--IVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSC 370
Cdd:cd06638    95 LWLVLELCnGGSVTDLVKGFLKRGERMEepIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEG--GVKLVDFGVSA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 Y---EHQKVYTYIQSRFYRSPEVI-----LGHPYDVAIDMWSLGCITAELYTGYPLFPgenEVEQLACIMEVLGLPPAgf 442
Cdd:cd06638   173 QltsTRLRRNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGDPPLA---DLHPMRALFKIPRNPPP-- 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 443 iqtasrrqtffdskgfpknitnnrgKKRYPDskdltmvlkTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06638   248 -------------------------TLHQPE---------LWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
215-427 9.72e-20

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: 89.67  E-value: 9.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKIlEALRKKDKDNTYNVVHMKDFFyfrNHF 294
Cdd:cd14183     4 ISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQNEV-SILRRVKHPNIVLLIEEMDMP---TEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYE-LMKNNNFQGFSLSIVRRFTLSVLKCLQMLSvekIIHCDLKPENIVLY--QKGQASVKVIDFGSSC 370
Cdd:cd14183    80 YLVMELVkGGDLFDaITSTNKYTERDASGMLYNLASAIKYLHSLN---IVHRDIKPENLLVYehQDGSKSLKLGDFGLAT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQ 427
Cdd:cd14183   157 VVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQE 213
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
223-515 1.06e-19

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: 89.00  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIR----NKKRFH--QQALMELKILEALRKKDKDNTYNVVHMKDFFYfrnhfcI 296
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSlvddDKKSREsvKQLEQEIALLSKLRHPNIVQYYGTEREEDNLY------I 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSScyEHQK 375
Cdd:cd06632    80 FLEYVpGGSIHKLLQR--YGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGV--VKLADFGMA--KHVE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 VYTYIQS----RFYRSPEVIL--GHPYDVAIDMWSLGCITAELYTGYPLFpgeNEVEQLACIMEVlglppagfiqtasrr 449
Cdd:cd06632   154 AFSFAKSfkgsPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAIFKI--------------- 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 450 qtfFDSKGFPKnitnnrgkkrYPDSkdLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06632   216 ---GNSGELPP----------IPDH--LSPDAK-------DFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
218-408 1.38e-19

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: 88.95  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMELKILEALRKKD----KDNTYNVVHMKDFFYFRNH 293
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLY-KSGPNSKDGNDFQKLPQLREIDlhrrVSRHPNIITLHDVFETEVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFEL--LGiNLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQaSVKVIDFGSSCY 371
Cdd:cd13993    80 IYIVLEYcpNG-DLFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEG-TVKLCDFGLATT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2032329476 372 EHQKVYTYIQSRFYRSPEVI-----LGHPYDVA-IDMWSLGCI 408
Cdd:cd13993   158 EKISMDFGVGSEFYMAPECFdevgrSLKGYPCAaGDIWSLGII 200
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
220-520 1.75e-19

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: 89.02  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHKNNELVALKIIRN--KKRFHQQALMELKIleALRKKDKDNTynvVHMKDFFYFRNHFCIT 297
Cdd:cd06617     4 EVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRAtvNSQEQKRLLMDLDI--SMRSVDCPYT---VTFYGALFREGDVWIC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLYELMKNNNFQGFSL--SIVRRFTLSVLKCLQML-SVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEHQ 374
Cdd:cd06617    79 MEVMDTSLDKFYKKVYDKGLTIpeDILGKIAVSIVKALEYLhSKLSVIHRDVKPSNVLINRNGQ--VKLCDFGISGYLVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTYIQ--SRFYRSPEVILG----HPYDVAIDMWSLGCITAELYTG-YPLFPGENEVEQLACIMEvlGLPPAgfiqtas 447
Cdd:cd06617   157 SVAKTIDagCKPYMAPERINPelnqKGYDVKSDVWSLGITMIELATGrFPYDSWKTPFQQLKQVVE--EPSPQ------- 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 448 rrqtffdskgFPKNitnnrgkkrypdskdltmvlkTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRN 520
Cdd:cd06617   228 ----------LPAE---------------------KFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHLS 269
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
219-514 2.07e-19

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: 90.04  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNK---KRFHQQALMElkilEALRKKDKDNTYnVVHMkdFFYF--RNH 293
Cdd:cd05573     3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSdmlKREQIAHVRA----ERDILADADSPW-IVRL--HYAFqdEDH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMknNNFQGFSLSIVRrFTLSVLkCLQMLSVEKI--IHCDLKPENIVLYQKGQasVKVIDFGSS- 369
Cdd:cd05573    76 LYLVMEYMpGGDLMNLL--IKYDVFPEETAR-FYIAEL-VLALDSLHKLgfIHRDIKPDNILLDADGH--IKLADFGLCt 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 ---------CYEHQKVYTYIQSRF----------------------YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPL 418
Cdd:cd05573   150 kmnksgdreSYLNDSVNTLFQDNVlarrrphkqrrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 419 FPGENEVEqlacimevlglppagfiqTASRrqtffdskgfpknITNNRGKKRYPDSKDltmvlktYDTSFLDFLRRCLVw 498
Cdd:cd05573   230 FYSDSLVE------------------TYSK-------------IMNWKESLVFPDDPD-------VSPEAIDLIRRLLC- 270
                         330
                  ....*....|....*..
gi 2032329476 499 EPSLRMTP-DQALKHAW 514
Cdd:cd05573   271 DPEDRLGSaEEIKAHPF 287
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
217-419 3.07e-19

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: 88.14  E-value: 3.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 217 YRYEVLETIGKGSFGQVAKCLDHKNNEL-VALKIIRNKKRFHQQALM--ELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd14202     2 FEFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLLgkEIKILKELKHE------NIVALYDFQEIANS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMknNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVL-YQKGQAS------VKVID 365
Cdd:cd14202    76 VYLVMEYCnGGDLADYL--HTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsYSGGRKSnpnnirIKIAD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 366 FGSSCYEHQKVY--TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd14202   154 FGFARYLQNNMMaaTLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPF 209
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
219-417 3.27e-19

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: 88.51  E-value: 3.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALrkkdkDNTYNVVHMKDFFYFRNHFC--- 295
Cdd:cd06639    24 WDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSL-----PNHPNVVKFYGMFYKADQYVggq 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 --ITFELL-GINLYELMKNNNFQGFSL--SIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSC 370
Cdd:cd06639    99 lwLVLELCnGGSVTELVKGLLKCGQRLdeAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG--GVKLVDFGVSA 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 371 Y---EHQKVYTYIQSRFYRSPEVI-----LGHPYDVAIDMWSLGCITAELYTGYP 417
Cdd:cd06639   177 QltsARLRRNTSVGTPFWMAPEVIaceqqYDYSYDARCDVWSLGITAIELADGDP 231
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
218-515 3.58e-19

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 87.59  E-value: 3.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCIT 297
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHT------NIIQLIEVFETKERVYMV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYE--LMKNNnfqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG-QASVKVIDFGSSCY-- 371
Cdd:cd14087    76 MELAtGGELFDriIAKGS----FTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGpDSKIMITDFGLASTrk 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 --EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasrr 449
Cdd:cd14087   152 kgPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQIL----------------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 450 qtffdskgfpknitnnRGKKRYPDS--KDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14087   215 ----------------RAKYSYSGEpwPSVSNLAK-------DFIDRLLTVNPGERLSATQALKHPWI 259
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
219-448 5.08e-19

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: 87.08  E-value: 5.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALK---IIRNKKRFHQQALMELKILEALrkkdkDNTYnVVHMKDFFYFRNHFC 295
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKqidISRMSRKMREEAIDEARVLSKL-----NSPY-VIKYYDSFVDKGKLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG-SSCYEH 373
Cdd:cd08529    76 IVMEYAeNGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN--VKIGDLGvAKILSD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 374 QKVY--TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLP-PAGFIQTASR 448
Cdd:cd08529   154 TTNFaqTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPiSASYSQDLSQ 231
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
219-521 5.15e-19

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: 87.69  E-value: 5.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLdHKN-NELVALKIIRNKKRFHQQalmELKILeaLRkkdkdntY----NVVHMKDFFYFRNH 293
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCI-HKAtGKEYAVKIIDKSKRDPSE---EIEIL--LR-------YgqhpNIITLRDVYDDGNS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL--GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVekiIHCDLKPENIvLY--QKGQA-SVKVIDFG- 367
Cdd:cd14091    69 VYLVTELLrgGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGV---VHRDLKPSNI-LYadESGDPeSLRICDFGf 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 ------------SSCYEHQKVytyiqsrfyrSPEVILGHPYDVAIDMWSLGCItaeLYT---GYPLF---PGENEVEQLA 429
Cdd:cd14091   145 akqlraengllmTPCYTANFV----------APEVLKKQGYDAACDIWSLGVL---LYTmlaGYTPFasgPNDTPEVILA 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 430 CImevlglppagfiqtASRRQTFfdSKGFPKNITnnrgkkryPDSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQA 509
Cdd:cd14091   212 RI--------------GSGKIDL--SGGNWDHVS--------DSAKDL--------------VRKMLHVDPSQRPTAAQV 253
                         330
                  ....*....|..
gi 2032329476 510 LKHAWIHQSRNL 521
Cdd:cd14091   254 LQHPWIRNRDSL 265
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
218-514 5.47e-19

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: 87.41  E-value: 5.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKII---------RNKKRFHQQALMELKILEALRKKDkdntyNVVHMKDFF 288
Cdd:cd14093     4 KYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIditgeksseNEAEELREATRREIEILRQVSGHP-----NIIELHDVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 YfrnhfCITFELLginLYELMKNNNFQGFSLSIV-------RRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasV 361
Cdd:cd14093    79 E-----SPTFIFL---VFELCRKGELFDYLTEVVtlsekktRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN--V 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 362 KVIDFGSSCY--EHQKVYTYIQSRFYRSPEVI-----LGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIME 433
Cdd:cd14093   149 KISDFGFATRldEGEKLRELCGTPGYLAPEVLkcsmyDNAPgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIME 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 434 vlglppagfiqtasrrqtffdskgfpknitnnrGKKRY--PDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALK 511
Cdd:cd14093   229 ---------------------------------GKYEFgsPEWDDISDTAK-------DLISKLLVVDPKKRLTAEEALE 268

                  ...
gi 2032329476 512 HAW 514
Cdd:cd14093   269 HPF 271
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
218-515 6.75e-19

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 86.97  E-value: 6.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILealrkKDKDNTYNVVHMKDFFYFRNHFCIT 297
Cdd:cd06608     7 IFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINIL-----RKFSNHPNIATFYGAFIKKDPPGGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLY-------ELMKNNNFQGFSLS------IVRrftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVI 364
Cdd:cd06608    82 DQLWLVMEYcgggsvtDLVKGLRKKGKRLKeewiayILR----ETLRGLAYLHENKVIHRDIKGQNILLTEEAE--VKLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 365 DFGSSC---YEHQKVYTYIQSRFYRSPEVI-----LGHPYDVAIDMWSLGcITA-ELYTGYPLFPGENEVEQLACImeVL 435
Cdd:cd06608   156 DFGVSAqldSTLGRRNTFIGTPYWMAPEVIacdqqPDASYDARCDVWSLG-ITAiELADGKPPLCDMHPMRALFKI--PR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 436 GLPPagfiqTASRrqtffdskgfPKNITNNrgkkrypdskdltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06608   233 NPPP-----TLKS----------PEKWSKE----------------------FNDFISECLIKNYEQRPFTEELLEHPFI 275
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
220-520 8.06e-19

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: 87.21  E-value: 8.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFhQQALMELKILEalrkkdKDNTYNVVHMKDFFYFRN--HF 294
Cdd:cd06622     4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRlelDESKF-NQIIMELDILH------KAVSPYIVDFYGAFFIEGavYM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGI--NLYElmKNNNFQGFSLSIVRRFTLSVLKCLQMLSVE-KIIHCDLKPENIVLYQKGQasVKVIDFG-SSC 370
Cdd:cd06622    77 CMEYMDAGSldKLYA--GGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQ--VKLCDFGvSGN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVI-LGHP-----YDVAIDMWSLGCITAELYTG-YPlFPGE---NEVEQLACIMEvlGLPPa 440
Cdd:cd06622   153 LVASLAKTNIGCQSYMAPERIkSGGPnqnptYTVQSDVWSLGLSILEMALGrYP-YPPEtyaNIFAQLSAIVD--GDPP- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 441 gfiqtasrrqtffdskgfpknitnnrgkkRYPDSkdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRN 520
Cdd:cd06622   229 -----------------------------TLPSG---------YSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKN 270
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
222-422 9.62e-19

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: 86.38  E-value: 9.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVvhmKDFFYFRN--HFCITFE 299
Cdd:cd05611     1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVA---KLYYSFQSkdYLYLVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS--CYEHQKV 376
Cdd:cd05611    78 YLnGGDCASLIKT--LGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGH--LKLTDFGLSrnGLEKRHN 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 377 YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGE 422
Cdd:cd05611   154 KKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAE 199
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
219-415 1.19e-18

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: 86.16  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN----KKRFHQQALMELKILEALRK----------KDKDNTYNVVhm 284
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKqkciEKDSVRNVLNELEILQELEHpflvnlwysfQDEEDMYMVV-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 285 kDFfyfrnhfcitfeLLGINL-YELMKNNNfqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKV 363
Cdd:cd05578    80 -DL------------LLGGDLrYHLQQKVK---FSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGH--VHI 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 364 IDFGSSCYEH--QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd05578   142 TDFNIATKLTdgTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRG 195
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
218-423 1.43e-18

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: 85.92  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQALM-----ELKILEALRKKdkdntyNVVHMKDFFYFRN 292
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKII-DKEQVAREGMVeqikrEIAIMKLLRHP------NIVELHEVMATKT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG-SSC 370
Cdd:cd14663    74 KIFFVMELVtGGELFSKIAKNG--RLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDG--NLKISDFGlSAL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 371 YEHQK----VYTYIQSRFYRSPEVILGHPYD-VAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd14663   150 SEQFRqdglLHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFDDEN 207
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
218-429 1.65e-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: 85.81  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHqqALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCIT 297
Cdd:cd14010     1 NYVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRPE--VLNEVRLTHELKHP------NVLKFYEWYETSNHLWLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FEL-LGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFGSSCYE---- 372
Cdd:cd14010    73 VEYcTGGDLETLLRQD--GNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL--DGNGTLKLSDFGLARREgeil 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 373 ---------------HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENeVEQLA 429
Cdd:cd14010   149 kelfgqfsdegnvnkVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAES-FTELV 219
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
218-414 2.13e-18

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: 85.41  E-value: 2.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQvAKCLDHKN-NELVALKIIRNKKRFH--QQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd08219     1 QYNVLRVVGEGSFGR-ALLVQHVNsDQKYAMKEIRLPKSSSavEDSRKEAVLLAKMKHP------NIVAFKESFEADGHL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS-CYE 372
Cdd:cd08219    74 YIVMEYCdGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK--VKLGDFGSArLLT 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2032329476 373 HQKVY--TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd08219   152 SPGAYacTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCT 195
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
219-515 2.24e-18

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: 85.00  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQAL-----MELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIV-NKEKLSKESVlmkveREIAIMKLIEHP------NVLKLYDVYENKKY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG--SSC 370
Cdd:cd14081    76 LYLVLEYVsGGELFDYLVKKG--RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN--IKIADFGmaSLQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAI-DMWSLGCITAELYTGYPLFPGENeVEQLacIMEVlglppagfiqtasRR 449
Cdd:cd14081   152 PEGSLLETSCGSPHYACPEVIKGEKYDGRKaDIWSCGVILYALLVGALPFDDDN-LRQL--LEKV-------------KR 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 450 QTFFdskgFPKNITnnrgkkryPDSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14081   216 GVFH----IPHFIS--------PDAQDL--------------LRRMLEVNPEKRITIEEIKKHPWF 255
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
223-515 2.37e-18

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: 85.36  E-value: 2.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIRNK-KRFHQQALMELKILEALrkkdkdNTYNVVHMKDFFYFRNHFCITFELL 301
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQnSKDKEMVLLEIQVMNQL------NHRNLIQLYEAIETPNEIVLFMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 -GINLYELMKNNNF---QGFSLSIVRRFTLSVLKCLQMlsveKIIHCDLKPENIVLYQKGQASVKVIDFG-SSCYE-HQK 375
Cdd:cd14190    84 eGGELFERIVDEDYhltEVDAMVFVRQICEGIQFMHQM----RVLHLDLKPENILCVNRTGHQVKIIDFGlARRYNpREK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppAGfiqtasrrQTFFDS 455
Cdd:cd14190   160 LKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVL-------MG--------NWYFDE 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 456 KGFPKNITNNRgkkrypdskdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14190   225 ETFEHVSDEAK-----------------------DFVSNLIIKERSARMSATQCLKHPWL 261
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
219-523 2.39e-18

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: 85.85  E-value: 2.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM-ELKILEALRKKdkdntyNVVHMKDFFYFRNHFCIT 297
Cdd:cd06643     7 WEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMvEIDILASCDHP------NIVKLLDAFYYENNLWIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCYEH---Q 374
Cdd:cd06643    81 IEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDG--DIKLADFGVSAKNTrtlQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTYIQSRFYRSPEVIL-----GHPYDVAIDMWSLGCITAELYTgypLFPGENEVEQLACIMEVLGLPPAGFIQTASrr 449
Cdd:cd06643   159 RRDSFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQ---IEPPHHELNPMRVLLKIAKSEPPTLAQPSR-- 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 450 qtffdskgfpknitnnrgkkrypdskdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKP 523
Cdd:cd06643   234 ----------------------------------WSPEFKDFLRKCLEKNVDARWTTSQLLQHPFVSVLVSNKP 273
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
218-423 3.00e-18

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: 85.01  E-value: 3.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQV--AKCLDhkNNELVALKIIR------NKKRfhQQALMELKILEALrkkdkdNTYNVVHMKDFFY 289
Cdd:cd08224     1 NYEIEKKIGKGQFSVVyrARCLL--DGRLVALKKVQifemmdAKAR--QDCLKEIDLLQQL------NHPNIIKYLASFI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNHFCITFELL-GINLYELMKNNNFQG--FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDF 366
Cdd:cd08224    71 ENNELNIVLELAdAGDLSRLIKHFKKQKrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANG--VVKLGDL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 367 GSSCY-------EHQKVYTyiqsRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd08224   149 GLGRFfsskttaAHSLVGT----PYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEK 208
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
213-515 3.51e-18

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: 85.48  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKIlEALRKKDKDNtynVVHMKDFFYFRN 292
Cdd:cd14168     6 EDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEI-AVLRKIKHEN---IVALEDIYESPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLY-QKGQASVKVIDFGSSC 370
Cdd:cd14168    82 HLYLVMQLVsGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFsQDEESKIMISDFGLSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 YEHQK--VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasR 448
Cdd:cd14168   160 MEGKGdvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIL---------------K 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 449 RQTFFDSkgfpknitnnrgkkryPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14168   225 ADYEFDS----------------PYWDDISDSAK-------DFIRNLMEKDPNKRYTCEQALRHPWI 268
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
218-427 3.73e-18

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: 84.70  E-value: 3.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKIlEALRKKDKDNTYNVVHMKDFfyfRNHFCIT 297
Cdd:cd14184     2 KYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIENEV-SILRRVKHPNIIMLIEEMDT---PAELYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNNFQGFSLSIVRRFTL-SVLKCLQMLSvekIIHCDLKPENIVL--YQKGQASVKVIDFGSSCYEH 373
Cdd:cd14184    78 MELVkGGDLFDAITSSTKYTERDASAMVYNLaSALKYLHGLC---IVHRDIKPENLLVceYPDGTKSLKLGDFGLATVVE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQ 427
Cdd:cd14184   155 GPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQE 208
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
218-515 4.52e-18

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: 84.59  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKiirnKKRFHQQALMELKILEALRKKDKDNTyNVVHMKDFFYFRNHFCIT 297
Cdd:cd06647     8 KYTRFEKIGQGASGTVYTAIDVATGQEVAIK----QMNLQQQPKKELIINEILVMRENKNP-NIVNYLDSYLVGDELWVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCY---EH 373
Cdd:cd06647    83 MEYLaGGSLTDVVTETCMDEGQIAAVCR---ECLQALEFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFGFCAQitpEQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasrrqtff 453
Cdd:cd06647   158 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA--------------------- 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 454 dskgfpkniTNnrGKKRYPDSKDLTMVlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06647   217 ---------TN--GTPELQNPEKLSAI-------FRDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
225-515 4.89e-18

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: 84.51  E-value: 4.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKII---------RNKKRFHQQALM-ELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVelpsvsaenKDRKKSMLDALQrEIALLRELQHE------NIVQYLGSSSDANHL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMknNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG-SSCYE 372
Cdd:cd06628    82 NIFLEYVpGGSVATLL--NNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKG--GIKISDFGiSKKLE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTYIQ--------SRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPgenEVEQLACIMEV--LGLPPagf 442
Cdd:cd06628   158 ANSLSTKNNgarpslqgSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFP---DCTQMQAIFKIgeNASPT--- 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 443 iqtasrrqtffdskgFPKNITnnrgkkrypdskdltmvlktydTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06628   232 ---------------IPSNIS----------------------SEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
219-512 5.12e-18

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: 84.20  E-value: 5.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV--AKCLDH-----KNNELVALK-IIRNKkrfH-QQALMELKILEALRKKDkdntyNVVHMKDFFY 289
Cdd:cd14019     3 YRIIEKIGEGTFSSVykAEDKLHdlydrNKGRLVALKhIYPTS---SpSRILNELECLERLGGSN-----NVSGLITAFR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNHFCITFELlginlyelMKNNNFQGF----SLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVKVID 365
Cdd:cd14019    75 NEDQVVAVLPY--------IEHDDFRDFyrkmSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNF-LYNRETGKGVLVD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 366 FG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYD-VAIDMWSLGCITAELYTG-YPLFPGENEVEQLACIMEVLGLPPA 440
Cdd:cd14019   146 FGlaqREEDRPEQRAPRAGTRGFRAPEVLFKCPHQtTAIDIWSAGVILLSILSGrFPFFFSSDDIDALAEIATIFGSDEA 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 441 gfiqtasrrqtffdskgfpknitnnrgkkrypdskdltmvlktydtsfLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd14019   226 ------------------------------------------------YDLLDKLLELDPSKRITAEEALKH 249
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
223-515 5.62e-18

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: 84.36  E-value: 5.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQAL-MELKILEALRK-----KDKDNTyNVVHMKDFFYFRNHFCI 296
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADsRQKTVVDALKSeidtlKDLDHP-NIVQYLGFEETEDYFSI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS-----C 370
Cdd:cd06629    86 FLEYVpGGSIGSCLRK--YGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEG--ICKISDFGISkksddI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVI--LGHPYDVAIDMWSLGCITAELYTGYPLFPGEnevEQLACIMEVLGLppagfiqtasr 448
Cdd:cd06629   162 YGNNGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDD---EAIAAMFKLGNK----------- 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 449 rqtffdskgfpknitnnrgKKRYPDSKDLTMvlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06629   228 -------------------RSAPPVPEDVNL-----SPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
219-523 6.42e-18

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: 84.70  E-value: 6.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM-ELKILEALrkkdkdNTYNVVHMKDFFYFRNHFCIT 297
Cdd:cd06644    14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMvEIEILATC------NHPYIVKLLGAFYWDGKLWIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH---Q 374
Cdd:cd06644    88 IEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD--IKLADFGVSAKNVktlQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTYIQSRFYRSPEVILGH-----PYDVAIDMWSLGCITAELYTgypLFPGENEVEQLACIMEVLGLPPAGFIQTASrr 449
Cdd:cd06644   166 RRDSFIGTPYWMAPEVVMCEtmkdtPYDYKADIWSLGITLIEMAQ---IEPPHHELNPMRVLLKIAKSEPPTLSQPSK-- 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 450 qtffdskgfpknitnnrgkkrypdskdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKP 523
Cdd:cd06644   241 ----------------------------------WSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVTSNRP 280
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
219-514 7.59e-18

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: 83.84  E-value: 7.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM--ELKILEALRKKdkdntyNVVHMKDFFYFRNHFCI 296
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIesEILIIKSLSHP------NIVKLFEVYETEKEIYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYE-LMKNNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIVLYQK--GQASVKVIDFGSSCYE 372
Cdd:cd14185    76 ILEYVrGGDLFDaIIESVKFTEHDAALM---IIDLCEALVYIHSKHIVHRDLKPENLLVQHNpdKSTTLKLADFGLAKYV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPG-ENEVEQLACIMEvLG----LPPagfiqtas 447
Cdd:cd14185   153 TGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQ-LGhyefLPP-------- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 448 rrqtFFDskgfpkNITNnrgkkrypDSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd14185   224 ----YWD------NISE--------AAKDL--------------ISRLLVVDPEKRYTAKQVLQHPW 258
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
218-423 1.05e-17

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: 83.24  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKII---RNKKRFHQQALMELKILEALrkkdkdNTYNVVHMKDFFYFRNHF 294
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveQMTKEERQAALNEVKVLSML------HHPNIIEYYESFLEDKAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAsVKVIDFGSS--CY 371
Cdd:cd08220    75 MIVMEYApGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTV-VKIGDFGISkiLS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 372 EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd08220   154 SKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAAN 205
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
219-423 1.05e-17

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: 84.02  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKI--IRNKKRFHQQALM--ELKILEALRKKDKDNTYNVVHMKDFFYfrnhf 294
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVmaIPEVIRLKQEQHVhnEKRVLKEVSHPFIIRLFWTEHDQRFLY----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 cITFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH 373
Cdd:cd05612    78 -MLMEYVpGGELFSYLRNSG--RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGH--IKLTDFGFAKKLR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd05612   153 DRTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDN 202
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
225-515 1.13e-17

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: 83.45  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMELKILEALRKKDKDNTYnVVHMKDFFYFRNHFCITFELL-GI 303
Cdd:cd14197    17 LGRGKFAVVRKCVEKDSGKEFAAKFMR-KRRKGQDCRMEIIHEIAVLELAQANPW-VINLHEVYETASEMILVLEYAaGG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQ-ASVKVIDFGSS--CYEHQKVYTYI 380
Cdd:cd14197    95 EIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPlGDIKIVDFGLSriLKNSEELREIM 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 381 QSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENeveqlacimevlglppagfiqtasRRQTFFDSKGFpk 460
Cdd:cd14197   175 GTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDD------------------------KQETFLNISQM-- 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 461 NITNNrgkkrypdSKDLTMVlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14197   229 NVSYS--------EEEFEHL----SESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
225-434 1.21e-17

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: 83.73  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIrNKKRF-----HQQALMELKILEalrkkdKDNTYNVVHMKDFFYFRNHFCITFE 299
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKL-DKKRIkkkkgETMALNEKIILE------KVSSPFIVSLAYAFETKDKLCLVLT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY--EHQKV 376
Cdd:cd05577    74 LMnGGDLKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGH--VRISDLGLAVEfkGGKKI 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 377 YTYIQSRFYRSPEVILGH-PYDVAIDMWSLGCITAELYTGYPLFPG------ENEVEQLACIMEV 434
Cdd:cd05577   152 KGRVGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQrkekvdKEELKRRTLEMAV 216
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
223-555 1.33e-17

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: 83.89  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIrnKKRF-HQQalmELKILEALRkkdkdNTYNVVHMKDFFYFRNHFCITFELL 301
Cdd:cd14092    12 EALGDGSFSVCRKCVHKKTGQEFAVKIV--SRRLdTSR---EVQLLRLCQ-----GHPNIVKLHEVFQDELHTYLVMELL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 -GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG-QASVKVIDFGSSCY--EHQKVY 377
Cdd:cd14092    82 rGGELLERIRKKK--RFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDdDAEIKIVDFGFARLkpENQPLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 378 TYIQSRFYRSPEVILGHP----YDVAIDMWSLGCItaeLYT---GYPLFPGENEVEQLACIMEVlglppagfIQTASRRq 450
Cdd:cd14092   160 TPCFTLPYAAPEVLKQALstqgYDESCDLWSLGVI---LYTmlsGQVPFQSPSRNESAAEIMKR--------IKSGDFS- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 451 tfFDSKGFpKNITNnrgkkrypDSKDLTMVLKTYDtsfldflrrclvwePSLRMTPDQALKHAWI--HQSRNLKPQPRPQ 528
Cdd:cd14092   228 --FDGEEW-KNVSS--------EAKSLIQGLLTVD--------------PSKRLTMSELRNHPWLqgSSSPSSTPLMTPG 282
                         330       340
                  ....*....|....*....|....*..
gi 2032329476 529 TLrKSNSFFPSETRKDKVQGCHHSSRK 555
Cdd:cd14092   283 VL-SSSAAAVSTALRATFDAFHLAFRE 308
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
225-419 1.57e-17

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: 82.74  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKClDHKN---NELVALKIIRNK------KRFHQQALMELKILEALRKKdkdntyNVVHMKDFFY-FRNHF 294
Cdd:cd13994     1 IGKGATSVVRIV-TKKNprsGVLYAVKEYRRRddeskrKDYVKRLTSEYIISSKLHHP------NIVKVLDLCQdLHGKW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS---- 369
Cdd:cd13994    74 CLVMEYCpGGDLFTLIEKAD--SLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV--LKLTDFGTAevfg 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 370 -CYEHQKVYTY--IQSRFYRSPEVILGHPYD-VAIDMWSLGCITAELYTGYPLF 419
Cdd:cd13994   150 mPAEKESPMSAglCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPW 203
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
218-521 1.74e-17

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: 83.62  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKiirnKKRFHQQALMELKILEALRKKDKDNTyNVVHMKDFFYFRNHFCIT 297
Cdd:cd06656    20 KYTRFEKIGQGASGTVYTAIDIATGQEVAIK----QMNLQQQPKKELIINEILVMRENKNP-NIVNYLDSYLVGDELWVV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCY---EH 373
Cdd:cd06656    95 MEYLaGGSLTDVVTETCMDEGQIAAVCR---ECLQALDFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFGFCAQitpEQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasrrqtff 453
Cdd:cd06656   170 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA--------------------- 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 454 dskgfpkniTNNRGKKRYPDSkdLTMVlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNL 521
Cdd:cd06656   229 ---------TNGTPELQNPER--LSAV-------FRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPL 278
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
222-515 2.86e-17

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: 82.41  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKII--RNKKRFHQQALMELKILEALrkkdkDNTYNVVHMKDFFYFRNHFCITFE 299
Cdd:cd06640     9 LERIGKGSFGEVFKGIDNRTQQVVAIKIIdlEEAEDEIEDIQQEITVLSQC-----DSPYVTKYYGSYLKGTKLWIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LLGINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY---EHQKV 376
Cdd:cd06640    84 LGGGSALDLLRAGPFDEFQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLLSEQGD--VKLADFGVAGQltdTQIKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYplfPGENEVEQLACIMEVLGLPPAGFIQTASRrqtffdsk 456
Cdd:cd06640   159 NTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGE---PPNSDMHPMRVLFLIPKNNPPTLVGDFSK-------- 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 457 gfpknitnnrgkkrypdskdltmvlktydtSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06640   228 ------------------------------PFKEFIDACLNKDPSFRPTAKELLKHKFI 256
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
290-418 3.55e-17

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: 82.29  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNHF-------CITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVK 362
Cdd:cd14020    73 FTNHYsanvpsrCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNI-LWSAEDECFK 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 363 VIDFGSSCYEHQKVYTYIQSRFYRSPEVIL-------GHPYD----VAIDMWSLGCITAELYTGYPL 418
Cdd:cd14020   152 LIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqaGLQSEtectSAVDLWSLGIVLLEMFSGMKL 218
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
225-515 3.98e-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: 81.63  E-value: 3.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQALMELKILEA---LRKkdkdntyNVVHMKDFFYF-----RNHFCI 296
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGRELAVKQV-EIDPINTEASKEVKALECeiqLLK-------NLQHERIVQYYgclqdEKSLSI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS------ 369
Cdd:cd06625    80 FMEYMpGGSVKDEIKA--YGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNG--NVKLGDFGASkrlqti 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CyEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFpgeNEVEQLACIMevlglppagfiqtasrr 449
Cdd:cd06625   156 C-SSTGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPW---AEFEPMAAIF----------------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 450 qtffdskgfpkNITNNRGKKRYPDSkdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06625   215 -----------KIATQPTNPQLPPH---------VSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
220-427 4.15e-17

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: 81.56  E-value: 4.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLEtIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFE 299
Cdd:cd14113    11 EVAE-LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHP------QLVGLLDTFETPTSYILVLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LL--GINLYELMKNNNFqgfSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQK-GQASVKVIDFG------SSC 370
Cdd:cd14113    84 MAdqGRLLDYVVRWGNL---TEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSlSKPTIKLADFGdavqlnTTY 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 371 YEHQkvytYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENeVEQ 427
Cdd:cd14113   161 YIHQ----LLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDES-VEE 212
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
218-521 6.85e-17

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: 81.69  E-value: 6.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKiirnKKRFHQQALMELKILEALRKKDKDNTyNVVHMKDFFYFRNHFCIT 297
Cdd:cd06654    21 KYTRFEKIGQGASGTVYTAMDVATGQEVAIR----QMNLQQQPKKELIINEILVMRENKNP-NIVNYLDSYLVGDELWVV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCY---EH 373
Cdd:cd06654    96 MEYLaGGSLTDVVTETCMDEGQIAAVCR---ECLQALEFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFGFCAQitpEQ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasrrqtff 453
Cdd:cd06654   171 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIA--------------------- 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 454 dskgfpkniTNNRGKKRYPDSkdLTMVlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNL 521
Cdd:cd06654   230 ---------TNGTPELQNPEK--LSAI-------FRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPL 279
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
211-419 7.96e-17

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 82.17  E-value: 7.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 211 LHDhiayrYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK--RFHQQ--ALMELKILEALrkkdkDNTYNVVHMKD 286
Cdd:PTZ00263   17 LSD-----FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREilKMKQVqhVAQEKSILMEL-----SHPFIVNMMCS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 287 F-----FYFRNHFCITFELLGinlyELMKNNNFQGfslSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasV 361
Cdd:PTZ00263   87 FqdenrVYFLLEFVVGGELFT----HLRKAGRFPN---DVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH--V 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 362 KVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:PTZ00263  158 KVTDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF 215
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
218-517 9.20e-17

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: 80.73  E-value: 9.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKII--RNKKRFHQQALMEL-----KILEALRKKDKDNtyNVVHMKDFFYF 290
Cdd:cd14182     4 KYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIdiTGGGSFSPEEVQELreatlKEIDILRKVSGHP--NIIQLKDTYET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCITFELLGI-NLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFGSS 369
Cdd:cd14182    82 NTFFFLVFDLMKKgELFDYLTEK--VTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILL--DDDMNIKLTDFGFS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 C--YEHQKVYTYIQSRFYRSPEVIL-----GHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppAG 441
Cdd:cd14182   158 CqlDPGEKLREVCGTPGYLAPEIIEcsmddNHPgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIM-------SG 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 442 FIQTASrrqtffdskgfpknitnnrgkkryPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWIHQ 517
Cdd:cd14182   231 NYQFGS------------------------PEWDDRSDTVK-------DLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
222-515 9.93e-17

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 80.87  E-value: 9.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKII--RNKKRFHQQALMELKILEALrkkdkDNTYNVVHMKDFFYFRNHFCITFE 299
Cdd:cd06642     9 LERIGKGSFGEVYKGIDNRTKEVVAIKIIdlEEAEDEIEDIQQEITVLSQC-----DSPYITRYYGSYLKGTKLWIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LLGINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS---CYEHQKV 376
Cdd:cd06642    84 LGGGSALDLLKPGPLEETYIATILR---EILKGLDYLHSERKIHRDIKAANVLLSEQG--DVKLADFGVAgqlTDTQIKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEveqlaciMEVLGLPPagfiqtasrrqtffdsK 456
Cdd:cd06642   159 NTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHP-------MRVLFLIP----------------K 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 457 GFPKNITNNrgkkrypdskdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06642   216 NSPPTLEGQ------------------HSKPFKEFVEACLNKDPRFRPTAKELLKHKFI 256
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
219-515 1.01e-16

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 80.43  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR----NKKRFHQQalmELKILEALRKKdkdntyNVVHmkdFF--YFRN 292
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKlepgDDFEIIQQ---EISMLKECRHP------NIVA---YFgsYLRR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 H-FCITFELLGinlyelmknnnfqGFSLSIVRRFT--LS----------VLKCLQMLSVEKIIHCDLKPENIVLYQKGQa 359
Cdd:cd06613    70 DkLWIVMEYCG-------------GGSLQDIYQVTgpLSelqiayvcreTLKGLAYLHSTGKIHRDIKGANILLTEDGD- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 360 sVKVIDFGSSC---YEHQKVYTYIQSRFYRSPEVIL---GHPYDVAIDMWSLGcITA-ELYTGYP----LFPgeneveql 428
Cdd:cd06613   136 -VKLADFGVSAqltATIAKRKSFIGTPYWMAPEVAAverKGGYDGKCDIWALG-ITAiELAELQPpmfdLHP-------- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 429 aciMEVLglppagFIQTASRRQtffdskgfPKNITNnrgKKRYpdSKDltmvlktydtsFLDFLRRCLVWEPSLRMTPDQ 508
Cdd:cd06613   206 ---MRAL------FLIPKSNFD--------PPKLKD---KEKW--SPD-----------FHDFIKKCLTKNPKKRPTATK 252

                  ....*..
gi 2032329476 509 ALKHAWI 515
Cdd:cd06613   253 LLQHPFV 259
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
219-515 1.06e-16

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: 80.82  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMK-------DFFYFR 291
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKksppghdDQLWLV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFellgiNLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFGSSCY 371
Cdd:cd06636    98 MEFCGAG-----SVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE--NAEVKLVDFGVSAQ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQKV---YTYIQSRFYRSPEVIL-----GHPYDVAIDMWSLGCITAELYTGYPLFpgeneveqlaCIMEVLglppagfi 443
Cdd:cd06636   171 LDRTVgrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL----------CDMHPM-------- 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 444 qtasrRQTFFDSKGFPKNITNNRGKKRypdskdltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06636   233 -----RALFLIPRNPPPKLKSKKWSKK-----------------FIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
219-518 2.16e-16

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 80.48  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKII--RNKKRFHQQALMELKILEALrkkdkdNTYNVVHMKDFFYFRNHFCI 296
Cdd:cd06650     7 FEKISELGAGNGGVVFKVSHKPSGLVMARKLIhlEIKPAIRNQIIRELQVLHEC------NSPYIVGFYGAFYSDGEISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVE-KIIHCDLKPENIVLYQKGQasVKVIDFG-SSCYEH 373
Cdd:cd06650    81 CMEHMdGGSLDQVLKKAG--RIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGE--IKLCDFGvSGQLID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG-YPLFPGE-NEVEQL-ACIMEVLGLPPAGFIQTASRRQ 450
Cdd:cd06650   157 SMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGrYPIPPPDaKELELMfGCQVEGDAAETPPRPRTPGRPL 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 451 TFFDSKGFPK-------NITNNRGKKRYPDSkdltmvlkTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQS 518
Cdd:cd06650   237 SSYGMDSRPPmaifellDYIVNEPPPKLPSG--------VFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRS 303
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
223-516 2.26e-16

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: 80.07  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMeLKILEALRKKDKDNtyNVVHMKDFFYFRNHFCITFELL- 301
Cdd:cd14174     8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIE-KNAGHSRSRV-FREVETLYQCQGNK--NILELIEFFEDDTRFYLVFEKLr 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 -GINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS-VKVIDF--------GSSC- 370
Cdd:cd14174    84 gGSILAHIQKRKHFNEREASRVVR---DIASALDFLHTKGIAHRDLKPENILCESPDKVSpVKICDFdlgsgvklNSACt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 -YEHQKVYTYIQSRFYRSPEVI-----LGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEqlaCIMEvlglppAGFIQ 444
Cdd:cd14174   161 pITTPELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTD---CGWD------RGEVC 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 445 TASRRQTFfdskgfpKNItnNRGKKRYPDsKDLTMVlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIH 516
Cdd:cd14174   232 RVCQNKLF-------ESI--QEGKYEFPD-KDWSHI----SSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
219-429 2.32e-16

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: 79.28  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN-KKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCIT 297
Cdd:cd14191     4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAySAKEKENIRQEISIMNCLHHP------KLVQCVDAFEEKANIVMV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNNFQGFSLSIVRrFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSS--CYEHQ 374
Cdd:cd14191    78 LEMVsGGELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLArrLENAG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLA 429
Cdd:cd14191   157 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA 211
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
219-518 2.35e-16

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: 79.73  E-value: 2.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKII--RNKKRFHQQALMELKILEALrkkdkDNTYNVVHMKDFFYFRNHFCI 296
Cdd:cd06641     6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIdlEEAEDEIEDIQQEITVLSQC-----DSPYVTKYYGSYLKDTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS---CYEH 373
Cdd:cd06641    81 MEYLGGGSALDLLEPGPLDETQIATILR---EILKGLDYLHSEKKIHRDIKAANVLLSEHGE--VKLADFGVAgqlTDTQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYplfPGENEVEQlaciMEVLGLPPagfiqtasrrqtff 453
Cdd:cd06641   156 IKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGE---PPHSELHP----MKVLFLIP-------------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 454 dsKGFPKNITNNrgkkrypdskdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQS 518
Cdd:cd06641   215 --KNNPPTLEGN------------------YSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRN 259
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
217-419 2.83e-16

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: 79.28  E-value: 2.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 217 YRYEVLETIGKGSFGQVAKCLDHKNNEL-VALKIIRNKKRFHQQALM--ELKILEALRKKDKDNTYNVVHMKDFFYFRNH 293
Cdd:cd14201     6 FEYSRKDLVGHGAFAVVFKGRHRKKTDWeVAIKSINKKNLSKSQILLgkEIKILKELQHENIVALYDVQEMPNSVFLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCItfellGINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS-------VKVIDF 366
Cdd:cd14201    86 YCN-----GGDLADYLQAKG--TLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKssvsgirIKIADF 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 367 GSSCYEHQKVY--TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd14201   159 GFARYLQSNMMaaTLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPF 213
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
223-514 3.13e-16

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: 78.87  E-value: 3.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKII------RNKKRFHQQAlmelkilealrkkdkDNTYNVVHMKDFF--YFRNHF 294
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKVLrdnpkaRREVELHWRA---------------SGCPHIVRIIDVYenTYQGRK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 C--ITFELL-GINLYELMKNNNFQGFS----LSIVRRFTLSVlkclQMLSVEKIIHCDLKPENIVLYQKG-QASVKVIDF 366
Cdd:cd14089    72 CllVVMECMeGGELFSRIQERADSAFTereaAEIMRQIGSAV----AHLHSMNIAHRDLKPENLLYSSKGpNAILKLTDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 367 GSSCYEHQKV------YTyiqsRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENeveqlacimevlGLPPa 440
Cdd:cd14089   148 GFAKETTTKKslqtpcYT----PYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNH------------GLAI- 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 441 gfiqtasrrqtffdSKGFPKNITNnrGKKRYPDS--KDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd14089   211 --------------SPGMKKRIRN--GQYEFPNPewSNVSEEAK-------DLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
219-514 4.07e-16

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: 78.78  E-value: 4.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITF 298
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLSHR------RLTCLLDQFETRKTLILIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINlyELMKNNNFQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFG----SSCYEH 373
Cdd:cd14107    78 ELCSSE--ELLDRLFLKGvVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGfaqeITPSEH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QkvYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEveqLACIMEVLglppagfiqtasRRQTFF 453
Cdd:cd14107   156 Q--FSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGEND---RATLLNVA------------EGVVSW 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 454 DSkgfpknitnnrgkkryPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd14107   219 DT----------------PEITHLSEDAK-------DFIKRVLQPDPEKRPSASECLSHEW 256
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
218-424 4.08e-16

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: 79.40  E-value: 4.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNN-ELVALKIIRnKKRFHQQALME---LKILEALRKKDKDNTYNVVHMKDFFYFRNH 293
Cdd:cd14096     2 NYRLINKIGEGAFSNVYKAVPLRNTgKPVAIKVVR-KADLSSDNLKGssrANILKEVQIMKRLSHPNIVKLLDFQESDEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL--GINLYELMKnnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVL------------------ 353
Cdd:cd14096    81 YYIVLELAdgGEIFHQIVR---LTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkaddd 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 354 --------YQKGQAS-----VKVIDFG-SSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd14096   158 etkvdegeFIPGVGGggigiVKLADFGlSKQVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPF 237

                  ....*
gi 2032329476 420 PGENE 424
Cdd:cd14096   238 YDESI 242
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
219-431 4.94e-16

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: 78.41  E-value: 4.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITF 298
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHK------SIVRFHDAFEKRRVVIIVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYE-LMKNNNFqgfSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSS--CYEHQK 375
Cdd:cd14108    78 ELCHEELLErITKRPTV---CESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAqeLTPNEP 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 376 VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACI 431
Cdd:cd14108   155 QYCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNI 210
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
218-433 5.19e-16

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: 78.23  E-value: 5.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN------KKRFHQQALMELKILEALrkkdkdNTYNVVHMKDFFYFR 291
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEisvgelQPDETVDANREAKLLSKL------DHPAIVKFHDSFVEK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFEL-----LGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgqaSVKVIDF 366
Cdd:cd08222    75 ESFCIVTEYceggdLDDKISEYKKSG--TTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNN---VIKVGDF 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 367 GSSCY---EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIME 433
Cdd:cd08222   150 GISRIlmgTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVE 219
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
225-506 6.27e-16

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: 78.64  E-value: 6.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIR--------NKKRFHQ--QALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHF 294
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKKCRqelspsdkNRERWCLevQIMKKLNHPNVVSARDVPPELEKLSPNDLPLLAMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CitfelLGINLYELM-KNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASV-KVIDFG----- 367
Cdd:cd13989    81 C-----SGGDLRKVLnQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIyKLIDLGyakel 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 ---SSCYEhqkvytYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGY-PLFPGENEVEQLacimevlglppaGFI 443
Cdd:cd13989   156 dqgSLCTS------FVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYrPFLPNWQPVQWH------------GKV 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 444 QTASrrqtffdskgfPKNIT---NNRGKKRY----PDSKDLTMVLKTYdtsFLDFLRRCLVWEPSLRMTP 506
Cdd:cd13989   218 KQKK-----------PEHICayeDLTGEVKFsselPSPNHLSSILKEY---LESWLQLMLRWDPRQRGGG 273
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
219-515 6.30e-16

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: 79.29  E-value: 6.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRfhqQALMELKILeaLRKKDKDNtynVVHMKDFFYFRNHFCITF 298
Cdd:cd14176    21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR---DPTEEIEIL--LRYGQHPN---IITLKDVYDDGKYVYVVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG--QASVKVIDFGSSCY---E 372
Cdd:cd14176    93 ELMkGGELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnPESIRICDFGFAKQlraE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGY-PLFPGENEVEQlacimEVLGLPPAGfiqtasrrqT 451
Cdd:cd14176   171 NGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYtPFANGPDDTPE-----EILARIGSG---------K 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 452 FFDSKGFPKNITNnrgkkrypDSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14176   237 FSLSGGYWNSVSD--------TAKDL--------------VSKMLHVDPHQRLTAALVLRHPWI 278
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
219-523 6.51e-16

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: 78.37  E-value: 6.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN----KKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd14117     8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKsqieKEGVEHQLRREIEIQSHLRHP------NILRLYNYFHDRKRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL--GINLYELMKNNNFQGFSLSIvrrFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYE 372
Cdd:cd14117    82 YLILEYAprGELYKELQKHGRFDEQRTAT---FMEELADALHYCHEKKVIHRDIKPENLLMGYKGE--LKIADFGWSVHA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQ-KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEV-LGLPPagFIQTASRrq 450
Cdd:cd14117   157 PSlRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVdLKFPP--FLSDGSR-- 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 451 tffdskgfpknitnnrgkkrypdskdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAWI--HQSRNLKP 523
Cdd:cd14117   233 ---------------------------------------DLISKLLRYHPSERLPLKGVMEHPWVkaNSRRVLPP 268
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
218-431 7.99e-16

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: 78.61  E-value: 7.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKrfhqQALMELKILEALRKKDKDNTyNVVHMKDFFYFRNHFCIT 297
Cdd:cd06655    20 KYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQK----QPKKELIINEILVMKELKNP-NIVNFLDSFLVGDELFVV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCY---EH 373
Cdd:cd06655    95 MEYLaGGSLTDVVTETCMDEAQIAAVCR---ECLQALEFLHANQVIHRDIKSDNVLLGMDG--SVKLTDFGFCAQitpEQ 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACI 431
Cdd:cd06655   170 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI 227
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
219-528 8.33e-16

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: 78.52  E-value: 8.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQalmELKILEALRKKDkdntyNVVHMKDFFYFRNHFCITF 298
Cdd:cd14177     6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSE---EIEILMRYGQHP-----NIITLKDVYDDGRYVYLVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL--GINLYELMKNNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQA---SVKVIDFGSSCY-- 371
Cdd:cd14177    78 ELMkgGELLDRILRQKFFSEREASAV---LYTITKTVDYLHCQGVVHRDLKPSNI-LYMDDSAnadSIRICDFGFAKQlr 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 -EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGY-PLFPGENEVEQlacimEVLGLPPAGfiqtasrr 449
Cdd:cd14177   154 gENGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYtPFANGPNDTPE-----EILLRIGSG-------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 450 qTFFDSKGFPKNITNNrgkkrypdSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAWI-HQSRNLKPQPRPQ 528
Cdd:cd14177   221 -KFSLSGGNWDTVSDA--------AKDL--------------LSHMLHVDPHQRYTAEQVLKHSWIaCRDQLPHYQLNRQ 277
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
219-515 8.38e-16

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: 78.35  E-value: 8.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQALM-------ELKILEALRKK---DKDNTYNVVHMKDff 288
Cdd:cd14094     5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIV-DVAKFTSSPGLstedlkrEASICHMLKHPhivELLETYSSDGMLY-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 yfrnhfcITFELL-GINL-YELMK--NNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQK-GQASVKV 363
Cdd:cd14094    82 -------MVFEFMdGADLcFEIVKraDAGFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKeNSAPVKL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 364 IDFGSS-------CYEHQKVYTyiqsRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQlacimevlg 436
Cdd:cd14094   154 GGFGVAiqlgesgLVAGGRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLF--------- 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 437 lppagfiQTASRRQTFFDSKGFPkNITNNrgkkrypdSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14094   221 -------EGIIKGKYKMNPRQWS-HISES--------AKDL--------------VRRMLMLDPAERITVYEALNHPWI 269
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
219-413 1.03e-15

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: 77.72  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQ--QALMELKILEALrkkdkdNTYNVVHmkdfFYF----RN 292
Cdd:cd13996     8 FEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSAseKVLREVKALAKL------NHPNIVR----YYTawveEP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELL-GINLYELM-KNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyQKGQASVKVIDFGSSC 370
Cdd:cd13996    78 PLYIQMELCeGGTLRDWIdRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL-DNDDLQVKIGDFGLAT 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 371 Y-EHQKVYTY----------------IQSRFYRSPEVILGHPYDVAIDMWSLGCITAELY 413
Cdd:cd13996   157 SiGNQKRELNnlnnnnngntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEML 216
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
322-515 1.09e-15

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: 77.17  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 322 VRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgqaSVKVIDFG-SSCYEHQKVYTYIQ-SRFYRSPEVILGHPYDVA 399
Cdd:cd14109   101 VAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD---KLKLADFGqSRRLLRGKLTTLIYgSPEFVSPEIVNSYPVTLA 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 400 IDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvlglppagfiqtasrrqtffdskgfpknitnnrGKKRYpDSKDLTM 479
Cdd:cd14109   178 TDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRS---------------------------------GKWSF-DSSPLGN 223
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2032329476 480 VlkTYDTSflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14109   224 I--SDDAR--DFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
219-424 1.38e-15

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: 77.40  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLetiGKGSFGQVAKCLDHKNNELVALKII---RNKKRFHQQ-ALMELKILEalrkkdKDNTYNVVHMKDFFYFRNHF 294
Cdd:cd05605     5 YRVL---GKGGFGEVCACQVRATGKMYACKKLekkRIKKRKGEAmALNEKQILE------KVNSRFVVSLAYAYETKDAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY-- 371
Cdd:cd05605    76 CLVLTIMnGGDLKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGH--VRISDLGLAVEip 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 372 EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENE 424
Cdd:cd05605   154 EGETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKE 206
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
219-423 1.56e-15

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: 77.16  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNN-ELVALKII--------RNKKRFHQQA---LMELKIL-EALRKKdkdntyNVVHMK 285
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRKKSNGqTLLALKEInmtnpafgRTEQERDKSVgdiISEVNIIkEQLRHP------NIVRYY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 286 DFFYFRNHFCITFELL-GINLYELM-----KNNNFQgfSLSIVRRFTLSVLkCLQMLSVEK-IIHCDLKPENIVLYQKGQ 358
Cdd:cd08528    76 KTFLENDRLYIVMELIeGAPLGEHFsslkeKNEHFT--EDRIWNIFVQMVL-ALRYLHKEKqIVHRDLKPNNIMLGEDDK 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 359 asVKVIDFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd08528   153 --VTITDFGlakQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTN 218
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
222-518 1.56e-15

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: 77.23  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKII--RNKKRFHQQALMELKILEALrkkdkDNTYnVVHMKDFFYFRNHFCITFE 299
Cdd:cd06619     6 QEILGHGNGGTVYKAYHLLTRRILAVKVIplDITVELQKQIMSELEILYKC-----DSPY-IIGFYGAFFVENRISICTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LL---GINLYELMKNNnfqgfslsIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG-SSCYEHQK 375
Cdd:cd06619    80 FMdggSLDVYRKIPEH--------VLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQ--VKLCDFGvSTQLVNSI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG---YPLFPGEN----EVEQLACIMEvlGLPPagfiqtasr 448
Cdd:cd06619   150 AKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGrfpYPQIQKNQgslmPLQLLQCIVD--EDPP--------- 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 449 rqtffdskgfpknitnnrgkkRYPDSKdltmvlktYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQS 518
Cdd:cd06619   219 ---------------------VLPVGQ--------FSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQY 259
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
225-446 2.08e-15

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: 77.61  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMELKILEALRKKDKDNTYnVVHMKdfFYFRNHFCITFELLGIN 304
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIR-KAHIVSRSEVTHTLAERTVLAQVDCPF-IVPLK--FSFQSPEKLYLVLAFIN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 305 LYELMKNNNFQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGS---SCYEHQKVYTYI 380
Cdd:cd05585    78 GGELFHHLQREGrFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGH--IALCDFGLcklNMKDDDKTNTFC 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 381 QSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTA 446
Cdd:cd05585   156 GTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDA 221
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
223-422 2.17e-15

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 77.07  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQA--LMELKILEALRkkdkdNTYNVVHMKDFFYFRNHFCITFEL 300
Cdd:cd14090     8 ELLGEGAYASVQTCINLYTGKEYAVKII-EKHPGHSRSrvFREVETLHQCQ-----GHPNILQLIEYFEDDERFYLVFEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 301 L--GINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS-VKVIDF--GSSCYEHQK 375
Cdd:cd14090    82 MrgGPLLSHIEKRVHFTEQEASLVVR---DIASALDFLHDKGIAHRDLKPENILCESMDKVSpVKICDFdlGSGIKLSST 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 376 VYTYIQ---------SRFYRSPEVI-----LGHPYDVAIDMWSLGCITAELYTGYPLFPGE 422
Cdd:cd14090   159 SMTPVTtpelltpvgSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGR 219
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
225-455 2.32e-15

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: 76.15  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKkdkdntYNVVHMKDFFYFRNHFCITFELLG-- 302
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQH------PQYITLHDTYESPTSYILVLELMDdg 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 303 ------INLYELMKNNnfqgfslsiVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVL-YQKGQASVKVIDFGSSCY--EH 373
Cdd:cd14115    75 rlldylMNHDELMEEK---------VAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEDAVQisGH 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEV-LGLPPAGFIQTASRRQTF 452
Cdd:cd14115   146 RHVHHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVdFSFPDEYFGDVSQAARDF 225

                  ...
gi 2032329476 453 FDS 455
Cdd:cd14115   226 INV 228
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
225-414 2.51e-15

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: 77.39  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIrnKKRFHQQALMELKILealrkKDKDNTYNVVHMKDFFYFRNHFCITFELL-GI 303
Cdd:cd14179    15 LGEGSFSICRKCLHKKTNQEYAVKIV--SKRMEANTQREIAAL-----KLCEGHPNIVKLHEVYHDQLHTFLVMELLkGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS-VKVIDFGSSCY---EHQKVYTY 379
Cdd:cd14179    88 ELLERIKKK--QHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSeIKIIDFGFARLkppDNQPLKTP 165
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2032329476 380 IQSRFYRSPEVILGHPYDVAIDMWSLGCItaeLYT 414
Cdd:cd14179   166 CFTLHYAAPELLNYNGYDESCDLWSLGVI---LYT 197
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
222-439 2.72e-15

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 77.44  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFG---QVAKCLDHKNNELVALK------IIRNKK-RFHQQAlmELKILEALRkkdkdntynvvH--MKDFFY 289
Cdd:cd05584     1 LKVLGKGGYGkvfQVRKTTGSDKGKIFAMKvlkkasIVRNQKdTAHTKA--ERNILEAVK-----------HpfIVDLHY 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 -FRNH---FCITFELLGINLYELMKNnnfQGFSLSIVRRFTLS-VLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVI 364
Cdd:cd05584    68 aFQTGgklYLILEYLSGGELFMHLER---EGIFMEDTACFYLAeITLALGHLHSLGIIYRDLKPENILLDAQGH--VKLT 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 365 DFG---SSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEV-LGLPP 439
Cdd:cd05584   143 DFGlckESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGkLNLPP 221
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
215-515 2.97e-15

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: 76.79  E-value: 2.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR---NKKRFHQqalmELKILEALrkkdkdNTYNVVHMKDFFYFR 291
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKktvDKKIVRT----EIGVLLRL------SHPNIIKLKEIFETP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG-QASVKVIDFGSS 369
Cdd:cd14085    71 TEISLVLELVtGGELFDRIVEKGY--YSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPApDAPLKIADFGLS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CYEHQKVY--TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYplfpgeneveqlacimevlglppagfiqtas 447
Cdd:cd14085   149 KIVDQQVTmkTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGF------------------------------- 197
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 448 rrQTFFDSKG---FPKNITNNRGKKRYPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14085   198 --EPFYDERGdqyMFKRILNCDYDFVSPWWDDVSLNAK-------DLVKKLIVLDPKKRLTTQQALQHPWV 259
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
219-416 2.99e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 78.11  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELValkIIRNKKRfhQQALMELKILEALrkkdkdNTYNVVHMKDFFYFRNHFCITF 298
Cdd:PHA03212   94 FSILETFTPGAEGFAFACIDNKTCEHV---VIKAGQR--GGTATEAHILRAI------NHPSIIQLKGTFTYNKFTCLIL 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYELMKNNNFQGFS--LSIVRrftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCY----E 372
Cdd:PHA03212  163 PRYKTDLYCYLAAKRNIAICdiLAIER----SVLRAIQYLHENRIIHRDIKAENIFINHPG--DVCLGDFGAACFpvdiN 236
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGY 416
Cdd:PHA03212  237 ANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
219-408 3.21e-15

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: 75.91  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVL--ETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRF--HQQALM--ELKILEALRKKdkdntyNVVHMKDFFYFRN 292
Cdd:cd14082     3 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKVI-DKLRFptKQESQLrnEVAILQQLSHP------GVVNLECMFETPE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQ-ASVKVIDFGSSCY 371
Cdd:cd14082    76 RVFVVMEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfPQVKLCDFGFARI 155
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2032329476 372 EHQKVY--TYIQSRFYRSPEVILGHPYDVAIDMWSLGCI 408
Cdd:cd14082   156 IGEKSFrrSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVI 194
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
270-425 3.49e-15

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 76.05  E-value: 3.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 270 LRKKDKDNTYNV----VH--MKDFFYFRN-HFCITFE---LL------GINLYELMKNNNFqgFSLSIVRRFTLSVLKCL 333
Cdd:PHA03390   45 VQKIIKAKNFNAiepmVHqlMKDNPNFIKlYYSVTTLkghVLimdyikDGDLFDLLKKEGK--LSEAEVKKIIRQLVEAL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 334 QMLSVEKIIHCDLKPENiVLYQKGQASVKVIDFG-------SSCYEHQKVYtyiqsrFyrSPEVILGHPYDVAIDMWSLG 406
Cdd:PHA03390  123 NDLHKHNIIHNDIKLEN-VLYDRAKDRIYLCDYGlckiigtPSCYDGTLDY------F--SPEKIKGHNYDVSFDWWAVG 193
                         170       180
                  ....*....|....*....|
gi 2032329476 407 CITAELYTG-YPLFPGENEV 425
Cdd:PHA03390  194 VLTYELLTGkHPFKEDEDEE 213
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
219-524 4.33e-15

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 76.22  E-value: 4.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQalmELKILeaLRKKDKDntyNVVHMKDFFYFRNHFCITF 298
Cdd:cd14175     3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSE---EIEIL--LRYGQHP---NIITLKDVYDDGKHVYLVT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL--GINLYELMKNNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIvLY--QKGQA-SVKVIDFGSSCY-- 371
Cdd:cd14175    75 ELMrgGELLDKILRQKFFSEREASSV---LHTICKTVEYLHSQGVVHRDLKPSNI-LYvdESGNPeSLRICDFGFAKQlr 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 -EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF---PGENEVEQLACImevlglppagfiqtAS 447
Cdd:cd14175   151 aENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRI--------------GS 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 448 RRqtfFDSKGFPKNITNNRGKkrypdskdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLkPQ 524
Cdd:cd14175   217 GK---FTLSGGNWNTVSDAAK---------------------DLVSKMLHVDPHQRLTAKQVLQHPWITQKDKL-PQ 268
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
219-439 4.45e-15

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: 76.50  E-value: 4.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRF------HQQAlmELKILEalrkkDKDNTYnVVHMK------D 286
Cdd:cd05599     3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLekeqvaHVRA--ERDILA-----EADNPW-VVKLYysfqdeE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 287 FFYFRNHFCITFELLGInlyeLMKNNNFQgfslSIVRRFTLSVLkclqMLSVEKI-----IHCDLKPENIVLYQKGQasV 361
Cdd:cd05599    75 NLYLIMEFLPGGDMMTL----LMKKDTLT----EEETRFYIAET----VLAIESIhklgyIHRDIKPDNLLLDARGH--I 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 362 KVIDFGSSCYEH--QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM---EVLG 436
Cdd:cd05599   141 KLSDFGLCTGLKksHLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwrETLV 220

                  ...
gi 2032329476 437 LPP 439
Cdd:cd05599   221 FPP 223
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
225-515 4.50e-15

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: 75.73  E-value: 4.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQ---QALMELKILEALRkkdkdNTYNVVHMKDFFYFRNHFCITFELL 301
Cdd:cd14198    16 LGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDcraEILHEIAVLELAK-----SNPRVVNLHEVYETTSEIILILEYA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 -GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVL---YQKGqaSVKVIDFGSScyehQKVY 377
Cdd:cd14198    91 aGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLssiYPLG--DIKIVDFGMS----RKIG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 378 TYIQSRF------YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglppagfiQTASRRQT 451
Cdd:cd14198   165 HACELREimgtpeYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQV---------NVDYSEET 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 452 FFDSKGFPKnitnnrgkkrypdskdltmvlktydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14198   236 FSSVSQLAT-----------------------------DFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
225-433 4.83e-15

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 76.48  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIrnKKRFHQQ------ALMELKILEALRKKDkdntyNVVHMKDFFYFRNHFCITF 298
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVL--KKEVIIEdddvecTMTEKRVLALANRHP-----FLTGLHACFQTEDRLYFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELlgINLYELMknnnfqgFSLSIVRRFTLS--------VLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG--- 367
Cdd:cd05570    76 EY--VNGGDLM-------FHIQRARRFTEErarfyaaeICLALQFLHERGIIYRDLKLDNVLLDAEGH--IKIADFGmck 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 368 SSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIME 433
Cdd:cd05570   145 EGIWGGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILN 210
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
223-515 4.83e-15

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: 76.22  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQA--LMELKILEALRKKDkdntyNVVHMKDFFYFRNHFCITFEL 300
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKIIE-KRPGHSRSrvFREVEMLYQCQGHR-----NVLELIEFFEEEDKFYLVFEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 301 L--GINLYELMKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS-VKVIDFG---------- 367
Cdd:cd14173    82 MrgGSILSHIHRRRHFNELEASVVVQ---DIASALDFLHNKGIAHRDLKPENILCEHPNQVSpVKICDFDlgsgiklnsd 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 SSCYEHQKVYTYIQSRFYRSPEVILGHP-----YDVAIDMWSLGCITAELYTGYPLFPGENEVEqlaCIMEVLGLPPAGf 442
Cdd:cd14173   159 CSPISTPELLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGRCGSD---CGWDRGEACPAC- 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 443 iqtasrRQTFFDSKgfpknitnNRGKKRYPDsKDLTMVlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14173   235 ------QNMLFESI--------QEGKYEFPE-KDWAHI----SCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
225-419 4.91e-15

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: 75.48  E-value: 4.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKN-NELVALKIIRNKKRFHQQALM--ELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELL 301
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKpDLPVAIKCITKKNLSKSQNLLgkEIKILKELSHE------NVVALLDCQETSSSVYLVMEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 -GINLYELMKNnnfQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG-------QASVKVIDFGSSCYE 372
Cdd:cd14120    75 nGGDLADYLQA---KGtLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspnDIRLKIADFGFARFL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 373 HQKVY--TYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd14120   152 QDGMMaaTLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPF 200
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
219-424 5.26e-15

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: 75.80  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLetiGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQ-----ALMELKILEalrkkdKDNTYNVVHMKDFFYFRNH 293
Cdd:cd05631     5 YRVL---GKGGFGEVCACQVRATGKMYACKKLE-KKRIKKRkgeamALNEKRILE------KVNSRFVVSLAYAYETKDA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYE 372
Cdd:cd05631    75 LCLVLTIMnGGDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENE 424
Cdd:cd05631   155 GETVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKE 206
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
218-514 5.60e-15

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: 75.78  E-value: 5.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR-NKKRFHQQALMELKilEALRKKDKDNTYNVVHMKDFFYFRNHFCI 296
Cdd:cd14181    11 KYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvTAERLSPEQLEEVR--SSTLKEIHILRQVSGHPSIITLIDSYESS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLginLYELMKNNNFQGF-------SLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS 369
Cdd:cd14181    89 TFIFL---VFDLMRRGELFDYltekvtlSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLH--IKLSDFGFS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CY--EHQKVYTYIQSRFYRSPEVIL-----GHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvlglppaG 441
Cdd:cd14181   164 CHlePGEKLRELCGTPGYLAPEILKcsmdeTHPgYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIME-------G 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 442 FIQTASrrqtffdskgfpknitnnrgkkryPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd14181   237 RYQFSS------------------------PEWDDRSSTVK-------DLISRLLVVDPEIRLTAEQALQHPF 278
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
218-514 6.04e-15

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 74.97  E-value: 6.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFH--------QQALMELKILEALRKKDKDNtynVVHMKDFFY 289
Cdd:cd14005     1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFV-PKSRVTewamingpVPVPLEIALLLKASKPGVPG---VIRLLDWYE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNHFCITFE--LLGINLYELMKNNNFQGFSLSivRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVKVIDFG 367
Cdd:cd14005    77 RPDGFLLIMErpEPCQDLFDFITERGALSENLA--RIIFRQVVEAVRHCHQRGVLHRDIKDENL-LINLRTGEVKLIDFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 SSCYEHQKVYT-YIQSRFYRSPEVILGHPYD-VAIDMWSLGCITAELYTGYplFPGENEVEQLacimevlglppagfiqt 445
Cdd:cd14005   154 CGALLKDSVYTdFDGTRVYSPPEWIRHGRYHgRPATVWSLGILLYDMLCGD--IPFENDEQIL----------------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 446 asRRQTFFdskgfpknitnnrgkkRYPDSKDLtmvlktydtsfLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd14005   215 --RGNVLF----------------RPRLSKEC-----------CDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
218-504 6.65e-15

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: 76.12  E-value: 6.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKII-------RNK-KRfhqqALMELKILEALrkkdkDNTYnVVHM----- 284
Cdd:cd05574     2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLdkeemikRNKvKR----VLTEREILATL-----DHPF-LPTLyasfq 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 285 -KDFFYFRNHFCitfelLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKV 363
Cdd:cd05574    72 tSTHLCFVMDYC-----PGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGH--IML 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 364 IDFG----SSCYEHQKVYTYIQSRF----------------------------YRSPEVILGHPYDVAIDMWSLGCITAE 411
Cdd:cd05574   145 TDFDlskqSSVTPPPVRKSLRKGSRrssvksieketfvaepsarsnsfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 412 LYTGYPLFPGENeveqlacimevlglppagfiqtasRRQTFfdskgfpKNITNnrGKKRYPDSKDLTMVLKtydtsflDF 491
Cdd:cd05574   225 MLYGTTPFKGSN------------------------RDETF-------SNILK--KELTFPESPPVSSEAK-------DL 264
                         330
                  ....*....|...
gi 2032329476 492 LRRCLVWEPSLRM 504
Cdd:cd05574   265 IRKLLVKDPSKRL 277
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
218-428 7.00e-15

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: 75.44  E-value: 7.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLetiGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQ-----ALMELKILEalrkkdKDNTYNVVHMKDFFYFRN 292
Cdd:cd05630     4 QYRVL---GKGGFGEVCACQVRATGKMYACKKLE-KKRIKKRkgeamALNEKQILE------KVNSRFVVSLAYAYETKD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY 371
Cdd:cd05630    74 ALCLVLTLMnGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGH--IRISDLGLAVH 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 372 --EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFP------GENEVEQL 428
Cdd:cd05630   152 vpEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQqrkkkiKREEVERL 216
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
218-367 1.12e-14

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: 74.60  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRfhQQAL-MELKILEALRKKD---------KDNTYNVVHMkdf 287
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQP--KQVLkMEVAVLKKLQGKPhfcrligcgRTERYNYIVM--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 288 fyfrnhfcitfELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS--VKVID 365
Cdd:cd14017    76 -----------TLLGPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDErtVYILD 144

                  ..
gi 2032329476 366 FG 367
Cdd:cd14017   145 FG 146
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
218-414 1.31e-14

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: 74.29  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALK-IIRNKKRFHQQALMELKILEALRKKDkdntyNVVHMKDFFYFRNH--- 293
Cdd:cd13985     1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKrMYFNDEEQLRVAIKEIEIMKRLCGHP-----NIVQYYDSAILSSEgrk 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 -FCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEK--IIHCDLKPENIVLYQKGQasVKVIDFGSSC 370
Cdd:cd13985    76 eVLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR--FKLCDFGSAT 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 371 YEHQKVYTY---------IQSR---FYRSPEVI---LGHPYDVAIDMWSLGCItaeLYT 414
Cdd:cd13985   154 TEHYPLERAeevniieeeIQKNttpMYRAPEMIdlySKKPIGEKADIWALGCL---LYK 209
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
218-428 1.40e-14

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: 73.96  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKiiRNKKRF-----HQQALMELKILEALRKKDkdntyNVVHMKDFFYFRN 292
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVK--KSKKPFrgpkeRARALREVEAHAALGQHP-----NIVRYYSSWEEGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELLGI-NLYELMKNNNFQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGssc 370
Cdd:cd13997    74 HLYIQMELCENgSLQDALEELSPISkLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKG--TCKIGDFG--- 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 371 yehqkVYTYIQSRF--------YRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQL 428
Cdd:cd13997   149 -----LATRLETSGdveegdsrYLAPELLNENYtHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQL 210
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
220-515 1.42e-14

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: 74.72  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHKNNELVALKIIR------NKKRFhqqaLMELKILealrKKDKDNTYnVVHMKDFFYFRNH 293
Cdd:cd06618    18 ENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRrsgnkeENKRI----LMDLDVV----LKSHDCPY-IVKCYGYFITDSD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEK-IIHCDLKPENIVLYQKGQasVKVIDFGSScye 372
Cdd:cd06618    89 VFICMELMSTCLDKLLKRIQ-GPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGN--VKLCDFGIS--- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTYIQSR-----FYRSPEVILGHP---YDVAIDMWSLGCITAELYTG-YPLFPGENEVEQLACIM--EVLGLPPag 441
Cdd:cd06618   163 GRLVDSKAKTRsagcaAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGqFPYRNCKTEFEVLTKILneEPPSLPP-- 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 442 fiqtasrrqtffdSKGFpknitnnrgkkrypdSKDltmvlktydtsFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06618   241 -------------NEGF---------------SPD-----------FCSFVDLCLTKDHRYRPKYRELLQHPFI 275
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
219-419 1.44e-14

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: 74.75  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVaKCLDHKNN-ELVALKIIRNKK--RFHQ--QALMELKILEAlrkkdkdntynvVHMKDFFYFRNH 293
Cdd:cd14209     3 FDRIKTLGTGSFGRV-MLVRHKETgNYYAMKILDKQKvvKLKQveHTLNEKRILQA------------INFPFLVKLEYS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 F-CITfellgiNLYELMKN-NNFQGFS-LSIVRRFT--------LSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVK 362
Cdd:cd14209    70 FkDNS------NLYMVMEYvPGGEMFShLRRIGRFSepharfyaAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGY--IK 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 363 VIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd14209   142 VTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF 198
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
223-525 1.45e-14

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: 74.69  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYnvvhmKDFFYFRNHFCITFELL- 301
Cdd:cd14170     8 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVY-----ENLYAGRKCLLIVMECLd 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASV-KVIDFG--SSCYEHQKVYT 378
Cdd:cd14170    83 GGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAIlKLTDFGfaKETTSHNSLTT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 379 YIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFpgeneveqlacimevlglppagfiqtaSRRQTFFDSKGF 458
Cdd:cd14170   163 PCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPF---------------------------YSNHGLAISPGM 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 459 PKNItnNRGKKRYPDSKdltmvLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQP 525
Cdd:cd14170   216 KTRI--RMGQYEFPNPE-----WSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTP 275
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
218-414 1.46e-14

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 74.08  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQ---VAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd08218     1 KYVRIKKIGEGSFGKallVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHP------NIVQYQESFEENGNL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMknNNFQGFSLSIVRRFTLSVLKCLQMLSV--EKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCY 371
Cdd:cd08218    75 YIVMDYCdGGDLYKRI--NAQRGVLFPEDQILDWFVQLCLALKHVhdRKILHRDIKSQNIFLTKDG--IIKLGDFGIARV 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 372 EHQKV---YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd08218   151 LNSTVelaRTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCT 196
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
219-520 1.81e-14

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: 74.37  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTY-------NVVHMKDFFYFR 291
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYygafikkNPPGMDDQLWLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFellgiNLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFGSSCY 371
Cdd:cd06637    88 MEFCGAG-----SVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTE--NAEVKLVDFGVSAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQKV---YTYIQSRFYRSPEVIL-----GHPYDVAIDMWSLGCITAELYTGYPLFpgeneveqlaCIMEVLglppagfi 443
Cdd:cd06637   161 LDRTVgrrNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPL----------CDMHPM-------- 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 444 qtasrRQTFFdskgFPKNITnnrgkkryPDSKDltmvlKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRN 520
Cdd:cd06637   223 -----RALFL----IPRNPA--------PRLKS-----KKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQPN 277
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
219-414 2.69e-14

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: 73.10  E-value: 2.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK---RFHQQAL-MELKILEALRKKDKDNTYNVVHMKDFFYfrnhf 294
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKapeDYLQKFLpREIEVIKGLKHPNLICFYEAIETTSRVY----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 cITFELL-GINLYELMKNNNF--QGFSLSIVRRFTLSVLKCLQMlsveKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY 371
Cdd:cd14162    77 -IIMELAeNGDLLDYIRKNGAlpEPQARRWFRQLVAGVEYCHSK----GVVHRDLKCENLLLDKNNN--LKITDFGFARG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 372 EHQKV-------YTYIQSRFYRSPEVILGHPYD-VAIDMWSLGCItaeLYT 414
Cdd:cd14162   150 VMKTKdgkpklsETYCGSYAYASPEILRGIPYDpFLSDIWSMGVV---LYT 197
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
218-423 3.11e-14

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: 73.07  E-value: 3.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKrfhqqalMELKILEALRKK----DKDNTYNVVHMKDFFYFRNH 293
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTK-------MPVKEKEASKKEvillAKMKHPNIVTFFASFQENGR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELlgINLYELMKNNNFQG---FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASvKVIDFGSSC 370
Cdd:cd08225    74 LFIVMEY--CDGGDLMKRINRQRgvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVA-KLGDFGIAR 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 371 YEHQKV---YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd08225   151 QLNDSMelaYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNN 206
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
219-423 4.10e-14

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: 74.30  E-value: 4.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV--AKCLDHKnnELVALKIIrNKKRFHQ-----QALMELKILEALRKK----------DKDNTYNV 281
Cdd:cd05600    13 FQILTQVGQGGYGSVflARKKDTG--EICALKIM-KKKVLFKlnevnHVLTERDILTTTNSPwlvkllyafqDPENVYLA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 282 ---VHMKDFFYFRNHfcitfelLGInlyelMKNNNfqgfslsivRRFTLS-VLKCLQMLSVEKIIHCDLKPENIVLYQKG 357
Cdd:cd05600    90 meyVPGGDFRTLLNN-------SGI-----LSEEH---------ARFYIAeMFAAISSLHQLGYIHRDLKPENFLIDSSG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 358 QasVKVIDFGSSC----------------------------------------YEHQKVYTYIQSRFYRSPEVILGHPYD 397
Cdd:cd05600   149 H--IKLTDFGLASgtlspkkiesmkirleevkntafleltakerrniyramrkEDQNYANSVVGSPDYMAPEVLRGEGYD 226
                         250       260
                  ....*....|....*....|....*.
gi 2032329476 398 VAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd05600   227 LTVDYWSLGCILFECLVGFPPFSGST 252
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
218-418 4.92e-14

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: 72.33  E-value: 4.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGqVAKCL-DHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCI 296
Cdd:cd14665     1 RYELVKDIGSGNFG-VARLMrDKQTKELVAVKYIERGEKIDENVQREIINHRSLRHP------NIVRFKEVILTPTHLAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFG--SSCYEH 373
Cdd:cd14665    74 VMEYAaGGELFERICNAG--RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGysKSSVLH 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAI-DMWSLGCITAELYTG-YPL 418
Cdd:cd14665   152 SQPKSTVGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGaYPF 198
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
225-515 5.26e-14

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: 72.19  E-value: 5.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQAL-------MELKILEALRKKDKDNtyNVVHMKDFFYFRNHFCIT 297
Cdd:cd14101     8 LGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLpgvnpvpNEVALLQSVGGGPGHR--GVIRLLDWFEIPEGFLLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FE--LLGINLYELMKNNNFQGFSLSivRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgQASVKVIDFGSSCYEHQK 375
Cdd:cd14101    86 LErpQHCQDLFDYITERGALDESLA--RRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLR-TGDIKLIDFGSGATLKDS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 376 VYT-YIQSRFYRSPEVILGHPYD-VAIDMWSLGCITAELYTGYplFPGENEVEQLACIMEvlglppagfiqtasrrqtff 453
Cdd:cd14101   163 MYTdFDGTRVYSPPEWILYHQYHaLPATVWSLGILLYDMVCGD--IPFERDTDILKAKPS-------------------- 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 454 dskgFPKNITnnrgkkryPDSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14101   221 ----FNKRVS--------NDCRSL--------------IRSCLAYNPSDRPSLEQILLHPWM 256
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
222-439 5.39e-14

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: 72.20  E-value: 5.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  222 LETIGKGSFGQV----AKCLDHKNNELVALKIIRN-KKRFHQQALM-ELKILEALRKKdkdntyNVVHMKdffyfrnHFC 295
Cdd:smart00221   4 GKKLGEGAFGEVykgtLKGKGDGKEVEVAVKTLKEdASEQQIEEFLrEARIMRKLDHP------NIVKLL-------GVC 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  296 ITFELLGINLyELMKNNNFQGFsLSIVRRFTLSVLKCLQM----------LSVEKIIHCDLKPENIvLYQKGQaSVKVID 365
Cdd:smart00221  71 TEEEPLMIVM-EYMPGGDLLDY-LRKNRPKELSLSDLLSFalqiargmeyLESKNFIHRDLAARNC-LVGENL-VVKISD 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476  366 FGSSCYEHQ-KVYTYIQSRF-YR--SPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPGENEVEQLACIMEVLGLPP 439
Cdd:smart00221 147 FGLSRDLYDdDYYKVKGGKLpIRwmAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYRLPK 225
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
225-514 5.82e-14

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: 73.18  E-value: 5.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQV--AKCLDHKNNELVALKIIRNKKrFHQQALMELKILEALRKKdkdntyNVVHMKDFF--YFRNHFCITFEL 300
Cdd:cd07867    10 VGRGTYGHVykAKRKDGKDEKEYALKQIEGTG-ISMSACREIALLRELKHP------NVIALQKVFlsHSDRKVWLLFDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 301 LGINLYELMK-------NNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG--QASVKVID------ 365
Cdd:cd07867    83 AEHDLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpeRGRVKIADmgfarl 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 366 FGSSCYEHQKVYTYIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENE---------VEQLACIMEVL 435
Cdd:cd07867   163 FNSPLKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVM 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 436 GLPPagfiqtasrRQTFFDSKGFPKNITNNRGKKR--YPDSKDLTMVLKTY---DTSFLDFLRRCLVWEPSLRMTPDQAL 510
Cdd:cd07867   243 GFPA---------DKDWEDIRKMPEYPTLQKDFRRttYANSSLIKYMEKHKvkpDSKVFLLLQKLLTMDPTKRITSEQAL 313

                  ....
gi 2032329476 511 KHAW 514
Cdd:cd07867   314 QDPY 317
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
218-424 7.35e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 72.70  E-value: 7.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLetiGKGSFGQVAKCLDHKNNELVALKIIRNKK----RFHQQALMELKILEalrkkdKDNTYNVVHMKDFFYFRNH 293
Cdd:cd05632     6 QYRVL---GKGGFGEVCACQVRATGKMYACKRLEKKRikkrKGESMALNEKQILE------KVNSQFVVNLAYAYETKDA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYE 372
Cdd:cd05632    77 LCLVLTIMnGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENE 424
Cdd:cd05632   157 GESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKE 208
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
223-515 7.80e-14

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 71.94  E-value: 7.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKIlealrkkdkDNTYNVVHMKDFF--YFRNHFC--ITF 298
Cdd:cd14172    10 QVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRA---------SGGPHIVHILDVYenMHHGKRCllIIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASV-KVIDFGSS--CYEHQ 374
Cdd:cd14172    81 ECMeGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVlKLTDFGFAkeTTVQN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENeveqlacimevlglppAGFIQTASRRQTFFD 454
Cdd:cd14172   161 ALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNT----------------GQAISPGMKRRIRMG 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 455 SKGFPKnitnnrgkkryPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14172   225 QYGFPN-----------PEWAEVSEEAK-------QLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
225-419 7.92e-14

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 72.26  E-value: 7.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIR------NKKRFHQqalmELKILEALrkkdkdNTYNVVHMKDFFYFRNHFCITF 298
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRlelsvkNKDRWCH----EIQIMKKL------NHPNVVKACDVPEEMNFLVNDV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL------GINLYELM-KNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASV-KVIDFGSSC 370
Cdd:cd14039    71 PLLameycsGGDLRKLLnKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVhKIIDLGYAK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 371 YEHQK--VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd14039   151 DLDQGslCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
219-414 1.08e-13

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: 71.31  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKII---RNKKRFHQQALMELKILEALrkkdkdNTYNVVHmkdffYFrNHFC 295
Cdd:cd08221     2 YIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEVnlsRLSEKERRDALNEIDILSLL------NHDNIIT-----YY-NHFL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-------GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGS 368
Cdd:cd08221    70 DGESLFiemeycnGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADL--VKLGDFGI 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 369 SCY---EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd08221   148 SKVldsESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLT 196
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
219-515 1.13e-13

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: 71.35  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK---RFHQQAL-MELKILEALRKKDKDNTYNVVHMKDFFYFrnhf 294
Cdd:cd14165     3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKapdDFVEKFLpRELEILARLNHKSIIKTYEIFETSDGKVY---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 cITFELlGIN--LYELMKNnnfQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFGSS-- 369
Cdd:cd14165    79 -IVMEL-GVQgdLLEFIKL---RGaLPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL--DKDFNIKLTDFGFSkr 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CYEHQKVYTYIQSRF-----YRSPEVILGHPYDVAI-DMWSLGCItaeLYtgyplfpgeneveqlacIMEVLGLPpagfi 443
Cdd:cd14165   152 CLRDENGRIVLSKTFcgsaaYAAPEVLQGIPYDPRIyDIWSLGVI---LY-----------------IMVCGSMP----- 206
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 444 qtasrrqtfFDSKGFPKNITNNRGKK-RYPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14165   207 ---------YDDSNVKKMLKIQKEHRvRFPRSKNLTSECK-------DLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
225-515 1.18e-13

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 71.32  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKiirnKKRFHQQALMELKILEALRKKDKDNTyNVVHMKDFFYFRNHFCITFELL-GI 303
Cdd:cd06648    15 IGEGSTGIVCIATDKSTGRQVAVK----KMDLRKQQRRELLFNEVVIMRDYQHP-NIVEMYSSYLVGDELWVVMEFLeGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG---SSCYEHQKVYTYI 380
Cdd:cd06648    90 ALTDIVTHTRMNEEQIATV---CRAVLKALSFLHSQGVIHRDIKSDSILLTSDGR--VKLSDFGfcaQVSKEVPRRKSLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 381 QSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLacimevlglppagfiqtasrrqtffdskgfpK 460
Cdd:cd06648   165 GTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAM-------------------------------K 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 461 NITNNRGkkryPDSKDLTMVlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06648   214 RIRDNEP----PKLKNLHKV----SPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
225-515 1.82e-13

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: 71.22  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKiirnKKRFHQQALMELKILEALRKKDKDNTyNVVHMKDFFYFRNHFCITFELL-GI 303
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVK----KMDLRKQQRRELLFNEVVIMRDYHHE-NVVDMYNSYLVGDELWVVMEFLeGG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG---SSCYEHQKVYTYI 380
Cdd:cd06658   105 ALTDIVTHTRMNEEQIATV---CLSVLRALSYLHNQGVIHRDIKSDSILLTSDGR--IKLSDFGfcaQVSKEVPKRKSLV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 381 QSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvlGLPPagfiqtasrrqtffdskgfpk 460
Cdd:cd06658   180 GTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRD--NLPP--------------------- 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 461 nitnnrgkkRYPDSKDLTMVLKtydtSFLDFLrrcLVWEPSLRMTPDQALKHAWI 515
Cdd:cd06658   237 ---------RVKDSHKVSSVLR----GFLDLM---LVREPSQRATAQELLQHPFL 275
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
222-439 2.47e-13

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 70.25  E-value: 2.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  222 LETIGKGSFGQV----AKCLDHKNNELVALKIIRNKKRFHQQALM--ELKILEALRKKdkdntyNVVHMKdffyfrnHFC 295
Cdd:smart00219   4 GKKLGEGAFGEVykgkLKGKGGKKKVEVAVKTLKEDASEQQIEEFlrEARIMRKLDHP------NVVKLL-------GVC 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  296 ITFELLGINLyELMKNNNFQGFsLSIVRRfTLSVLKCLQM----------LSVEKIIHCDLKPENIvLYQKGQaSVKVID 365
Cdd:smart00219  71 TEEEPLYIVM-EYMEGGDLLSY-LRKNRP-KLSLSDLLSFalqiargmeyLESKNFIHRDLAARNC-LVGENL-VVKISD 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476  366 FGSSCYEHQKVYTYIQSR----FYRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPGENEVEQLACIMEVLGLPP 439
Cdd:smart00219 146 FGLSRDLYDDDYYRKRGGklpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYRLPQ 224
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
219-434 2.50e-13

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 70.37  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKII----RNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFY--FRN 292
Cdd:cd14116     7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLfkaqLEKAGVEHQLRREVEIQSHLRHP------NILRLYGYFHdaTRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELLGINLYELMKNNNFQGfslsivRRFTLSVLKCLQMLSV---EKIIHCDLKPENIVLYQKGQasVKVIDFGSS 369
Cdd:cd14116    81 YLILEYAPLGTVYRELQKLSKFDE------QRTATYITELANALSYchsKRVIHRDIKPENLLLGSAGE--LKIADFGWS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 370 CYE-HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEV 434
Cdd:cd14116   153 VHApSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRV 218
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
218-515 2.79e-13

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: 70.24  E-value: 2.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVaKCLDHK-NNELVALKIIrNKKRFH----QQALMELKILEALRKKDKDNTYNVVHMKDFFYFRN 292
Cdd:cd14072     1 NYRLLKTIGKGNFAKV-KLARHVlTGREVAIKII-DKTQLNpsslQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELLG-INLYELMKNNNfqgfSLSIVRRFTLSVLKCLQmlsvEKIIHCDLKPENIVLyqKGQASVKVIDFGSS-- 369
Cdd:cd14072    79 EYASGGEVFDyLVAHGRMKEKE----ARAKFRQIVSAVQYCHQ----KRIVHRDLKAENLLL--DADMNIKIADFGFSne 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CYEHQKVYTYIQSRFYRSPEVILGHPYD-VAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMevlglppagfiqtasr 448
Cdd:cd14072   149 FTPGNKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVL---------------- 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 449 rqtffdskgfpknitnnRGKKRYPdskdLTMvlktyDTSFLDFLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14072   213 -----------------RGKYRIP----FYM-----STDCENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
219-433 3.49e-13

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: 70.80  E-value: 3.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMELKILE----ALRKKDKDNT--YNVVHMKDFFYFRN 292
Cdd:cd05616     2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILK-KDVVIQDDDVECTMVEkrvlALSGKPPFLTqlHSCFQTMDRLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELLginlYELMKNNNFQGFSLSIvrrFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYE 372
Cdd:cd05616    81 EYVNGGDLM----YHIQQVGRFKEPHAVF---YAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH--IKIADFGM-CKE 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 373 HQ----KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIME 433
Cdd:cd05616   151 NIwdgvTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIME 215
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
218-414 3.67e-13

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: 69.77  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK---RFHQQALMELKILEALRKKdkdntyNVVHMKD-------F 287
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNaskRERKAAEQEAKLLSKLKHP------NIVSYKEsfegedgF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 288 FYFRNHFCitfelLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG 367
Cdd:cd08223    75 LYIVMGFC-----EGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSN--IIKVGDLG 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 368 ------SSCyehQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd08223   148 iarvleSSS---DMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMAT 197
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
225-514 3.84e-13

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: 70.86  E-value: 3.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQV--AKCLDHKNNELVALKIIRNKKrFHQQALMELKILEALRKKdkdntyNVVHMKDFF--YFRNHFCITFEL 300
Cdd:cd07868    25 VGRGTYGHVykAKRKDGKDDKDYALKQIEGTG-ISMSACREIALLRELKHP------NVISLQKVFlsHADRKVWLLFDY 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 301 LGINLYELMK-------NNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKG--QASVKVID------ 365
Cdd:cd07868    98 AEHDLWHIIKfhraskaNKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpeRGRVKIADmgfarl 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 366 FGSSCYEHQKVYTYIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENE---------VEQLACIMEVL 435
Cdd:cd07868   178 FNSPLKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpyhHDQLDRIFNVM 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 436 GLPPAG---FIQTASRRQTFFdsKGFPKNITNNRGKKRYPDSKDLTMvlktyDTSFLDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd07868   258 GFPADKdweDIKKMPEHSTLM--KDFRRNTYTNCSLIKYMEKHKVKP-----DSKAFHLLQKLLTMDPIKRITSEQAMQD 330

                  ..
gi 2032329476 513 AW 514
Cdd:cd07868   331 PY 332
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
222-522 3.91e-13

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: 70.84  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKIIR-NKKRFH---QQALMELKILEALRKKdkdNT--YNVVHMKDFF-YFRNHF 294
Cdd:cd06633    26 LHEIGHGSFGAVYFATNSHTNEVVAIKKMSySGKQTNekwQDIIKEVKFLQQLKHP---NTieYKGCYLKDHTaWLVMEY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFellGINLYELMKnNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEhQ 374
Cdd:cd06633   103 CLGS---ASDLLEVHK-KPLQEVEIAAI---THGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ--VKLADFGSASIA-S 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 375 KVYTYIQSRFYRSPEVILGH---PYDVAIDMWSLGcitaelytgyplfpgeneveqLACimevlglppagfIQTASRRQT 451
Cdd:cd06633   173 PANSFVGTPYWMAPEVILAMdegQYDGKVDIWSLG---------------------ITC------------IELAERKPP 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 452 FFDSKGFPK--NITNNrgkkrypDSKdlTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLK 522
Cdd:cd06633   220 LFNMNAMSAlyHIAQN-------DSP--TLQSNEWTDSFRGFVDYCLQKIPQERPSSAELLRHDFVRRERPPR 283
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
218-423 5.05e-13

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: 69.33  E-value: 5.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVaKCLDHK-NNELVALKIIRNKKRFHQ--QALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHF 294
Cdd:cd14078     4 YYELHETIGSGGFAKV-KLATHIlTGEKVAIKIMDKKALGDDlpRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGinlYELMKNNnfqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVL--YQKgqasVKVIDFG----- 367
Cdd:cd14078    83 CPGGELFD---YIVAKDR----LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLdeDQN----LKLIDFGlcakp 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 368 SSCYEHQkVYTYIQSRFYRSPEVILGHPY-DVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd14078   152 KGGMDHH-LETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDN 207
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
217-424 5.38e-13

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: 69.93  E-value: 5.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 217 YRYEvLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQ-----ALMELKILEalrkkdKDNTYNVVHMKDFFYFR 291
Cdd:cd05607     3 YFYE-FRVLGKGGFGEVCAVQVKNTGQMYACKKL-DKKRLKKKsgekmALLEKEILE------KVNSPFIVSLAYAFETK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELL-GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSC 370
Cdd:cd05607    75 THLCLVMSLMnGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEV 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENE 424
Cdd:cd05607   155 KEGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKE 208
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
225-518 5.56e-13

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: 70.05  E-value: 5.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKiirnKKRFHQQALMELKILEALRKKDKDNTyNVVHMKDFFYFRNHFCITFELL-GI 303
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKLVAVK----KMDLRKQQRRELLFNEVVIMRDYQHE-NVVEMYNSYLVGDELWVVMEFLeGG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG---SSCYEHQKVYTYI 380
Cdd:cd06657   103 ALTDIVTHTRMNEEQIAAV---CLAVLKALSVLHAQGVIHRDIKSDSILLTHDGR--VKLSDFGfcaQVSKEVPRRKSLV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 381 QSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvlGLPPagfiqtasrrqtffdskgfpk 460
Cdd:cd06657   178 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD--NLPP--------------------- 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 461 nitnnrgkkRYPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWIHQS 518
Cdd:cd06657   235 ---------KLKNLHKVSPSLK-------GFLDRLLVRDPAQRATAAELLKHPFLAKA 276
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
225-513 5.69e-13

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: 69.38  E-value: 5.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKII---RNKKRfHQQALMElKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELL 301
Cdd:cd06630     8 LGTGAFSSCYQARDVKTGTLMAVKQVsfcRNSSS-EQEEVVE-AIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 -GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQaSVKVIDFGSSCYEHQKVYTY- 379
Cdd:cd06630    86 aGGSVASLLSK--YGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQ-RLRIADFGAAARLASKGTGAg 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 380 -IQSRF-----YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvlglppagfIQTASRrqtff 453
Cdd:cd06630   163 eFQGQLlgtiaFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFK---------IASATT----- 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 454 dSKGFPKNITnnrgkkryPDSKDLTMvlktydtsfldflrRCLVWEPSLRMTPDQALKHA 513
Cdd:cd06630   229 -PPPIPEHLS--------PGLRDVTL--------------RCLELQPEDRPPARELLKHP 265
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
219-523 7.60e-13

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: 69.66  E-value: 7.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQalmELKILeaLRKKDKDNtynVVHMKDFFYFRNHFCITF 298
Cdd:cd14178     5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSE---EIEIL--LRYGQHPN---IITLKDVYDDGKFVYLVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL--GINLYELMKNNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQA---SVKVIDFGSSCY-- 371
Cdd:cd14178    77 ELMrgGELLDRILRQKCFSEREASAV---LCTITKTVEYLHSQGVVHRDLKPSNI-LYMDESGnpeSIRICDFGFAKQlr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 -EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGY-PLFPGENEVeqlacimevlglppagfiqtasrr 449
Cdd:cd14178   153 aENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFtPFANGPDDT------------------------ 208
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 450 qtffdskgfPKNITNNRGKKRYpdskdlTMVLKTYDT---SFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKP 523
Cdd:cd14178   209 ---------PEEILARIGSGKY------ALSGGNWDSisdAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREYLSQ 270
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
219-433 1.02e-12

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: 69.64  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMELKILE--ALRKKDKDNTYNVVHMKDFFYFRNHFCI 296
Cdd:cd05615    12 FNFLMVLGKGSFGKVMLAERKGSDELYAIKILK-KDVVIQDDDVECTMVEkrVLALQDKPPFLTQLHSCFQTVDRLYFVM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGINLYELMKNNNFQGFSLSIvrrFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYEHQ-- 374
Cdd:cd05615    91 EYVNGGDLMYHIQQVGKFKEPQAVF---YAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH--IKIADFGM-CKEHMve 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 375 --KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIME 433
Cdd:cd05615   165 gvTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIME 225
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
225-426 1.09e-12

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: 68.84  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIR------NKKRFhqqaLMELKILEALrkkdkdNTYNVVHMK------------D 286
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCRqelspkNRERW----CLEIQIMKRL------NHPNVVAARdvpeglqklapnD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 287 FFYFRNHFCITFELLG-INLYElmknnNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASV-KVI 364
Cdd:cd14038    72 LPLLAMEYCQGGDLRKyLNQFE-----NCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIhKII 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 365 DFGSSCYEHQK--VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGY-PLFPGENEVE 426
Cdd:cd14038   147 DLGYAKELDQGslCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFrPFLPNWQPVQ 211
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
219-415 1.24e-12

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 68.31  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITF 298
Cdd:cd14111     5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLginlYELMknNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFGSSCYEH----Q 374
Cdd:cd14111    85 ELL----HSLI--DRFR-YSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMV--TNLNAIKIVDFGSAQSFNplslR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd14111   156 QLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSG 196
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
218-412 1.31e-12

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: 68.25  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKII----RNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFfYFRNH 293
Cdd:cd06607     2 IFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMsysgKQSTEKWQDIIKEVKFLRQLRHP------NTIEYKGC-YLREH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FC-ITFEL-LG--INLYELMKnnnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS 369
Cdd:cd06607    75 TAwLVMEYcLGsaSDIVEVHK----KPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGT--VKLADFGSA 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 370 CYeHQKVYTYIQSRFYRSPEVILGH---PYDVAIDMWSLGCITAEL 412
Cdd:cd06607   149 SL-VCPANSFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIEL 193
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
225-440 1.45e-12

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 69.23  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNK---KRFHQQALMELK--ILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFE 299
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKtilKKKEQNHIMAERnvLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LLginlYELMKNnnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYE----HQK 375
Cdd:cd05603    83 LF----FHLQRE---RCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGH--VVLTDFGL-CKEgmepEET 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 376 VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM-EVLGLPPA 440
Cdd:cd05603   153 TSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILhKPLHLPGG 218
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
225-424 1.46e-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: 68.19  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQV---AKCLDHKNNELVALKIIR-----NKKRFHQQALMELKILEALRkkdkDNTYNVvhmKDFFYFRNHFCI 296
Cdd:cd05583     2 LGTGAYGKVflvRKVGGHDAGKLYAMKVLKkativQKAKTAEHTMTERQVLEAVR----QSPFLV---TLHYAFQTDAKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGINLYELMKN-NNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS----CY 371
Cdd:cd05583    75 HLILDYVNGGELFTHlYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGH--VVLTDFGLSkeflPG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 372 EHQKVYTYIQSRFYRSPEVILGHP--YDVAIDMWSLGCITAELYTGYPLFPGENE 424
Cdd:cd05583   153 ENDRAYSFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELLTGASPFTVDGE 207
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
225-412 1.66e-12

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: 68.37  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIrNKKRF-----HQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFE 299
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKL-NKKRLkkrkgYEGAMVEKRILAKVHSR------FIVSLAYAFQTKTDLCLVMT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 L-----LGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCY--- 371
Cdd:cd05608    82 ImnggdLRYHIYNVDEEN--PGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDG--NVRISDLGLAVElkd 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2032329476 372 EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAEL 412
Cdd:cd05608   158 GQTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEM 198
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
225-415 1.79e-12

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 68.07  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHkNNELVALKIIR--NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELL- 301
Cdd:cd14066     1 IGSGGFGTVYKGVLE-NGTVVAVKRLNemNCAASKKEFLTELEMLGRLRHP------NLVRLLGYCLESDEKLLVYEYMp 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 GINLYELMKNNNFQG-FSLSIVRRFTLSVLKCLQML---SVEKIIHCDLKPENIVLYQKGQAsvKVIDFGSSCYEHQKVY 377
Cdd:cd14066    74 NGSLEDRLHCHKGSPpLPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILLDEDFEP--KLTDFGLARLIPPSES 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2032329476 378 TYIQSRF-----YRSPEVILGHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd14066   152 VSKTSAVkgtigYLAPEYIRTGRVSTKSDVYSFGVVLLELLTG 194
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
225-438 1.84e-12

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: 67.76  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRnkkrFHQQALMELKILEALrKKDKDNTYNVVHMKDFFYF-------RNHFCIT 297
Cdd:cd06652    10 LGQGAFGRVYLCYDADTGRELAVKQVQ----FDPESPETSKEVNAL-ECEIQLLKNLLHERIVQYYgclrdpqERTLSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS------C 370
Cdd:cd06652    85 MEYMpGGSIKDQLKS--YGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVG--NVKLGDFGASkrlqtiC 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPgenEVEQLACIMEVLGLP 438
Cdd:cd06652   161 LSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKIATQP 225
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
225-425 1.87e-12

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: 68.74  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKII-RNKKRFHQQALMELKILEAlrkkdkdnTYNVVHMKDFFYFRNHFCITFELL-G 302
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIIsRRMEANTQREVAALRLCQS--------HPNIVALHEVLHDQYHTYLVMELLrG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 303 INLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQ-ASVKVIDFGSSCYEHQ---KVYT 378
Cdd:cd14180    86 GELLDRIKKK--ARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgAVLKVIDFGFARLRPQgsrPLQT 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2032329476 379 YIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEV 425
Cdd:cd14180   164 PCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGK 210
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
219-415 2.22e-12

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: 67.53  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQALM------ELKILEALRKKdkdntyNVVHMKDFFYFRN 292
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVI-DKKKAKKDSYVtknlrrEGRIQQMIRHP------NITQLLDILETEN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFEL-LGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFG-SSC 370
Cdd:cd14070    77 SYYLVMELcPGGNLMHRIYDK--KRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDE--NDNIKLIDFGlSNC 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 371 YE----HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd14070   153 AGilgySDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTG 201
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
222-433 2.61e-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: 68.19  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKIIrnKKRFHQQ------ALMELKILeALRKKDKDNT--YNVVHMKDFFYFRNH 293
Cdd:cd05587     1 LMVLGKGSFGKVMLAERKGTDELYAIKIL--KKDVIIQdddvecTMVEKRVL-ALSGKPPFLTqlHSCFQTMDRLYFVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FcitfellgINLYELMKNNNFQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYE 372
Cdd:cd05587    78 Y--------VNGGDLMYHIQQVGkFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGH--IKIADFGM-CKE 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 373 H----QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIME 433
Cdd:cd05587   147 GifggKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIME 211
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
219-428 2.72e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 70.15  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN---KKRFHQQALMELKILEALRKKdkdntyNVVHMKDFF------- 288
Cdd:PTZ00266    15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYrglKEREKSQLVIEVNVMRELKHK------NIVRYIDRFlnkanqk 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  289 -YFRNHFCITFELlGINLYELMKN-NNFQGFSLSIVRRFTLSVLKCLQML----SVEKIIHCDLKPENIVLYQ------- 355
Cdd:PTZ00266    89 lYILMEFCDAGDL-SRNIQKCYKMfGKIEEHAIVDITRQLLHALAYCHNLkdgpNGERVLHRDLKPQNIFLSTgirhigk 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476  356 --------KGQASVKVIDFGSS--CYEHQKVYTYIQSRFYRSPEVILGH--PYDVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:PTZ00266   168 itaqannlNGRPIAKIGDFGLSknIGIESMAHSCVGTPYYWSPELLLHEtkSYDDKSDMWALGCIIYELCSGKTPFHKAN 247

                   ....*
gi 2032329476  424 EVEQL 428
Cdd:PTZ00266   248 NFSQL 252
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
224-419 2.85e-12

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: 68.11  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 224 TIGKGSFGQV--AKcldHKNNE-LVALKIIRNK---KRFHQQALMELKilEALRKkdkdntyNVVH-----------MKD 286
Cdd:cd05575     2 VIGKGSFGKVllAR---HKAEGkLYAVKVLQKKailKRNEVKHIMAER--NVLLK-------NVKHpflvglhysfqTKD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 287 FFYFRNHFCITFELLginlYELMKNNNFqgfSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDF 366
Cdd:cd05575    70 KLYFVLDYVNGGELF----FHLQRERHF---PEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGH--VVLTDF 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 367 GSsCYEH----QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd05575   141 GL-CKEGiepsDTTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
222-419 2.93e-12

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: 68.07  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKIIRNK---KRFHQQALMELKilEALRKKDKDNTYNVVH----MKDFFYFRNHF 294
Cdd:cd05604     1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKvilNRKEQKHIMAER--NVLLKNVKHPFLVGLHysfqTTDKLYFVLDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLginlYELMKNnnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYE-- 372
Cdd:cd05604    79 VNGGELF----FHLQRE---RSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGH--IVLTDFGL-CKEgi 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 373 --HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd05604   149 snSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPF 197
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
219-419 3.29e-12

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: 67.19  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFH-----QQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNH 293
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMI-DKKAMQkagmvQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELlgiNLYelmKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFGSSC--- 370
Cdd:cd14186    82 MCHNGEM---SRY---LKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTR--NMNIKIADFGLATqlk 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd14186   154 MPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPF 202
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
225-535 3.43e-12

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: 67.70  E-value: 3.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKrfhqQALMELKILEALRKKDKDNtYNVVHMKDFFyfrnhfcitfeLLGIN 304
Cdd:cd06659    29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRK----QQRRELLFNEVVIMRDYQH-PNVVEMYKSY-----------LVGEE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 305 LYELMKNnnFQGFSLS-IVRRFTL----------SVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH 373
Cdd:cd06659    93 LWVLMEY--LQGGALTdIVSQTRLneeqiatvceAVLQALAYLHSQGVIHRDIKSDSILLTLDGR--VKLSDFGFCAQIS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKV---YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVlglPPagfiqtasrrq 450
Cdd:cd06659   169 KDVpkrKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDS---PP----------- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 451 tffdskgfPKnitnnrgkkrYPDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQALKHAWIHQSRnlKPQ---PRP 527
Cdd:cd06659   235 --------PK----------LKNSHKASPVLR-------DFLERMLVRDPQERATAQELLDHPFLLQTG--LPEclvPLI 287

                  ....*...
gi 2032329476 528 QTLRKSNS 535
Cdd:cd06659   288 QQYRKRTS 295
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
222-414 3.64e-12

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: 67.35  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKC----LDHKNNELVALKIIRNKKRFHQQAL-MELKILEALRKKdkdntyNVVHMKDFFYF--RNHF 294
Cdd:cd14205     9 LQQLGKGNFGSVEMCrydpLQDNTGEVVAVKKLQHSTEEHLRDFeREIEILKSLQHD------NIVKYKGVCYSagRRNL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFG-SSCYEH 373
Cdd:cd14205    83 RLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILV--ENENRVKIGDFGlTKVLPQ 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 374 QKVYTYIQSR-----FYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd14205   161 DKEYYKVKEPgespiFWYAPESLTESKFSVASDVWSFGVVLYELFT 206
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
225-432 3.75e-12

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: 67.80  E-value: 3.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIrnKKRFHQQ------ALMELKILeALRKKdkdNTYnVVHMKDFFYFRNHFCITF 298
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKAL--KKDVVLEdddvecTMIERRVL-ALASQ---HPF-LTHLFCTFQTESHLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLgiNLYELMKNNNFQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG---SSCYEHQ 374
Cdd:cd05592    76 EYL--NGGDLMFHIQQSGrFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGH--IKIADFGmckENIYGEN 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM 432
Cdd:cd05592   152 KASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSIC 209
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
225-459 3.96e-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: 66.97  E-value: 3.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKII-----RNKKRFHQQAL-MELKILEALRKKDKDNTYNVVhmkdffyfRNH----F 294
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGRELAVKQVpfdpdSQETSKEVNALeCEIQLLKNLRHDRIVQYYGCL--------RDPeekkL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS---- 369
Cdd:cd06653    82 SIFVEYMpGGSVKDQLKA--YGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAG--NVKLGDFGASkriq 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 --CYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPgenEVEQLACIMEVLGLP-----PAGf 442
Cdd:cd06653   158 tiCMSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKIATQPtkpqlPDG- 233
                         250       260
                  ....*....|....*....|
gi 2032329476 443 IQTASR---RQTFFDSKGFP 459
Cdd:cd06653   234 VSDACRdflRQIFVEEKRRP 253
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
215-419 4.41e-12

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: 66.66  E-value: 4.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLET-----IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALME-LKILEALRKKdkdntyNVVHMKDFF 288
Cdd:cd06624     1 LEYEYEYDESgervvLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEeIALHSRLSHK------NIVQYLGSV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 YFRNHFCITFELL-GINLYEL-------MKNNNfqgfslSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENiVLYQKGQAS 360
Cdd:cd06624    75 SEDGFFKIFMEQVpGGSLSALlrskwgpLKDNE------NTIGYYTKQILEGLKYLHDNKIVHRDIKGDN-VLVNTYSGV 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 361 VKVIDFGSS--------CYEhqkvyTYIQSRFYRSPEVILGHP--YDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd06624   148 VKISDFGTSkrlaginpCTE-----TFTGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPF 211
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
222-425 4.92e-12

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: 66.64  E-value: 4.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHknNELVALKIIR--NKKRFHQQAL-MELkilEALRKKdKDNTYNVVHMKDffyfrnhfCITF 298
Cdd:cd13979     8 QEPLGSGGFGSVYKATYK--GETVAVKIVRrrRKNRASRQSFwAEL---NAARLR-HENIVRVLAAET--------GTDF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYELMKNNNFQ------GFSLSIVRR--FTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAsvKVIDFGSS- 369
Cdd:cd13979    74 ASLGLIIMEYCGNGTLQqliyegSEPLPLAHRilISLDIARALRFCHSHGIVHLDVKPANILISEQGVC--KLCDFGCSv 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 370 ------CYEHQKVYTYIQSRfYRSPEVILGHPYDVAIDMWSLGcITA-ELYTGYPLFPGENEV 425
Cdd:cd13979   152 klgegnEVGTPRSHIGGTYT-YRAPELLKGERVTPKADIYSFG-ITLwQMLTRELPYAGLRQH 212
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
223-431 5.34e-12

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: 67.28  E-value: 5.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQ----ALMELKILeALRKkdkDNTYnVVHMKDFFYFRNHFCITF 298
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDdvecTMVEKRVL-ALAW---ENPF-LTHLYCTFQTKEHLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLgiNLYELMKNNNFQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG---SSCYEHQ 374
Cdd:cd05620    76 EFL--NGGDLMFHIQDKGrFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH--IKIADFGmckENVFGDN 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 375 KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACI 431
Cdd:cd05620   152 RASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI 208
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
219-426 6.66e-12

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: 67.35  E-value: 6.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNK---KRFHQQALMELKilEALRKKDKDNTYNVVHmkdfFYFRNHFC 295
Cdd:cd05602     9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKailKKKEEKHIMSER--NVLLKNVKHPFLVGLH----FSFQTTDK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGINLYELMKNNNFQGFSLSIVRRF-TLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYEH- 373
Cdd:cd05602    83 LYFVLDYINGGELFYHLQRERCFLEPRARFyAAEIASALGYLHSLNIVYRDLKPENILLDSQGH--IVLTDFGL-CKENi 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 374 ---QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVE 426
Cdd:cd05602   160 epnGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAE 215
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
219-422 7.35e-12

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: 66.96  E-value: 7.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNK---KR---FHQQAlmELKILealrkKDKDNTYNVvhmKDFFYFRN 292
Cdd:cd05598     3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKdvlKRnqvAHVKA--ERDIL-----AEADNEWVV---KLYYSFQD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELLGINLYELMknnnfqgfSLSI--------VRRFTLSVLKClQMLSVEKI--IHCDLKPENIVLYQKGQasVK 362
Cdd:cd05598    73 KENLYFVMDYIPGGDLM--------SLLIkkgifeedLARFYIAELVC-AIESVHKMgfIHRDIKPDNILIDRDGH--IK 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 363 VIDFG----------SSCYE-HQKVYT--YIqsrfyrSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF----PGE 422
Cdd:cd05598   142 LTDFGlctgfrwthdSKYYLaHSLVGTpnYI------APEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFlaqtPAE 212
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
219-424 7.87e-12

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: 66.87  E-value: 7.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV---AKCLDHKNNELVALKIIRN-----KKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFfyf 290
Cdd:cd05614     2 FELLKVLGTGAYGKVflvRKVSGHDANKLYAMKVLRKaalvqKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDA--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCITFELLGINLYELMKNNNFqgfSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS- 369
Cdd:cd05614    79 KLHLILDYVSGGELFTHLYQRDHF---SEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH--VVLTDFGLSk 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 370 ---CYEHQKVYTYIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENE 424
Cdd:cd05614   154 eflTEEKERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTLEGE 212
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
225-438 9.39e-12

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: 66.66  E-value: 9.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQV---AKCLDHKNNELVALKIIRN---KKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITF 298
Cdd:cd05582     3 LGQGSFGKVflvRKITGPDAGTLYAMKVLKKatlKVRDRVRTKMERDILADVNHP------FIVKLHYAFQTEGKLYLIL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL-GINLY-----ELMknnnfqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG---SS 369
Cdd:cd05582    77 DFLrGGDLFtrlskEVM-------FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGH--IKLTDFGlskES 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEV-LGLP 438
Cdd:cd05582   148 IDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAkLGMP 217
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
218-411 9.78e-12

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 65.91  E-value: 9.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELV-ALKII-------RNKKRfhqqALMELKILEALRKKDKDNtynVVHMKDFFY 289
Cdd:cd14052     1 RFANVELIGSGEFSQVYKVSERVPTGKVyAVKKLkpnyagaKDRLR----RLEEVSILRELTLDGHDN---IVQLIDSWE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNHFCItfellginLYELMKNNNFQGF--SLSIVRRF-TLSVLKCLQMLSV-------EKIIHCDLKPENIVLYQKGqa 359
Cdd:cd14052    74 YHGHLYI--------QTELCENGSLDVFlsELGLLGRLdEFRVWKILVELSLglrfihdHHFVHLDLKPANVLITFEG-- 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 360 SVKVIDFG-SSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAE 411
Cdd:cd14052   144 TLKIGDFGmATVWPLIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
225-515 1.24e-11

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: 65.65  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNtynVVHMKDFFYFRNHFCITFELL-GI 303
Cdd:cd14097     9 LGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAH---IIHLEEVFETPKRMYLVMELCeDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQ-----KGQASVKVIDFGSSCYEHQKVYT 378
Cdd:cd14097    86 ELKELLLRKGF--FSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSsiidnNDKLNIKVTDFGLSVQKYGLGED 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 379 YIQSR----FYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEvlglppAGFIQTASRRQTFFD 454
Cdd:cd14097   164 MLQETcgtpIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRK------GDLTFTQSVWQSVSD 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 455 SKgfpKNItnnrgkkrypdskdLTMVLKTydtsfldflrrclvwEPSLRMTPDQALKHAWI 515
Cdd:cd14097   238 AA---KNV--------------LQQLLKV---------------DPAHRMTASELLDNPWI 266
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
219-412 1.31e-11

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: 65.43  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR----NKKRFHQQALMELKILEALrkkdkdNTYNVVHMKDFFYFRNHF 294
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifemMDAKARQDCVKEIDLLKQL------NHPNVIKYLDSFIEDNEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGI-NLYELMKNNNFQGFSL--SIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCY 371
Cdd:cd08228    78 NIVLELADAgDLSQMIKYFKKQKRLIpeRTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGV--VKLGDLGLGRF 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2032329476 372 EHQKV---YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAEL 412
Cdd:cd08228   156 FSSKTtaaHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEM 199
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
218-408 1.43e-11

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: 65.42  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR--------NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFY 289
Cdd:cd13990     1 RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKIHQlnkdwseeKKQNYIKHALREYEIHKSLDHP------RIVKLYDVFE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNH-FCITFELL-GINL-YELMKNNNF-QGFSLSIVRRfTLSVLKCLQMLSvEKIIHCDLKPENIVLYQKGQA-SVKVI 364
Cdd:cd13990    75 IDTDsFCTVLEYCdGNDLdFYLKQHKSIpEREARSIIMQ-VVSALKYLNEIK-PPIIHYDLKPGNILLHSGNVSgEIKIT 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 365 DFGSS-------------CYEHQKVYTYiqsrFYRSPEVILGHPYDVAI----DMWSLGCI 408
Cdd:cd13990   153 DFGLSkimddesynsdgmELTSQGAGTY----WYLPPECFVVGKTPPKIsskvDVWSVGVI 209
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
219-515 1.44e-11

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 65.11  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGqVAKCLDHKNNEL-VALKIIrNKKRFHQQALM----ELKILEALRKKDKDNTYNVVHMKDFFYFRNH 293
Cdd:cd14071     2 YDIERTIGKGNFA-VVKLARHRITKTeVAIKII-DKSQLDEENLKkiyrEVQIMKMLNHPHIIKLYQVMETKDMLYLVTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELlginlYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFGSSCY-- 371
Cdd:cd14071    80 YASNGEI-----FDYLAQHG--RMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL--DANMNIKIADFGFSNFfk 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQKVYTYIQSRFYRSPEVILGHPYD-VAIDMWSLGCITAELYTGYPLFPGENeveqLACIMEVLglppagfiqTASR-R 449
Cdd:cd14071   151 PGELLKTWCGSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGST----LQTLRDRV---------LSGRfR 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 450 QTFFDSKgfpknitnnrgkkrypDSKDLtmvlktydtsfldfLRRCLVWEPSLRMTPDQALKHAWI 515
Cdd:cd14071   218 IPFFMST----------------DCEHL--------------IRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
219-419 1.46e-11

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: 66.24  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK-RFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCIT 297
Cdd:cd05633     7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRiKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAsvKVIDFGSSC-YEHQK 375
Cdd:cd05633    87 LDLMnGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHV--RISDLGLACdFSKKK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2032329476 376 VYTYIQSRFYRSPEVIL-GHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd05633   163 PHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPF 207
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
225-423 1.72e-11

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: 64.97  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKK--RF---HQQALMELKILEALRKKdkdntyNVVHMKDFFYfrNH----FC 295
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKlrRIpngEANVKREIQILRRLNHR------NVIKLVDVLY--NEekqkLY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG----SSCY 371
Cdd:cd14119    73 MVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDG--TLKISDFGvaeaLDLF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 372 EHQKVYTYIQ-SRFYRSPEVILGHPY--DVAIDMWSLGCITAELYTG-YPlFPGEN 423
Cdd:cd14119   151 AEDDTCTTSQgSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGkYP-FEGDN 205
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
225-434 3.62e-11

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


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 64.38  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQ-----ALMElKILEALRKKDKDNTYnVVHMKDFFYFRNHFCITFE 299
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCL-DKKRIKMKqgetlALNE-RIMLSLVSTGGDCPF-IVCMTYAFQTPDKLCFILD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LL-GINL-YELMKNNNFqgfSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSC-YEHQKV 376
Cdd:cd05606    79 LMnGGDLhYHLSQHGVF---SEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGH--VRISDLGLACdFSKKKP 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 377 YTYIQSRFYRSPEVIL-GHPYDVAIDMWSLGCITAELYTGYPLF-----PGENEVEQLACIMEV 434
Cdd:cd05606   154 HASVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFrqhktKDKHEIDRMTLTMNV 217
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
218-406 4.02e-11

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: 63.63  E-value: 4.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGqVAKCL-DHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCI 296
Cdd:cd14662     1 RYELVKDIGSGNFG-VARLMrNKETKELVAVKYIERGLKIDENVQREIINHRSLRHP------NIIRFKEVVLTPTHLAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFG--SSCYEH 373
Cdd:cd14662    74 VMEYAaGGELFERICNAG--RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGysKSSVLH 151
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAI-DMWSLG 406
Cdd:cd14662   152 SQPKSTVGTPAYIAPEVLSRKEYDGKVaDVWSCG 185
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
219-413 5.17e-11

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 63.44  E-value: 5.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVaKCLDHK-NNELVALKIIrNKKRFhQQALM------ELKILEALRKKDKDNTYNVVHMKDFFyfr 291
Cdd:cd14079     4 YILGKTLGVGSFGKV-KLAEHElTGHKVAVKIL-NRQKI-KSLDMeekirrEIQILKLFRHPHIIRLYEVIETPTDI--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 nhFCITFELLGINLYELMKNNNfqGFSLSIVRRFTLsvlkclQMLS-VE-----KIIHCDLKPENIVLyqKGQASVKVID 365
Cdd:cd14079    78 --FMVMEYVSGGELFDYIVQKG--RLSEDEARRFFQ------QIISgVEychrhMVVHRDLKPENLLL--DSNMNVKIAD 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 366 FGSSCYEHQKVY--TYIQSRFYRSPEVILGHPY-DVAIDMWSLGCItaeLY 413
Cdd:cd14079   146 FGLSNIMRDGEFlkTSCGSPNYAAPEVISGKLYaGPEVDVWSCGVI---LY 193
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
219-451 5.38e-11

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: 63.54  E-value: 5.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR-NKKRFHQQALM-ELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCI 296
Cdd:cd14046     8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKlRSESKNNSRILrEVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TfellgINLYELMKNNNFQgfSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEHQKV 376
Cdd:cd14046    88 K-----STLRDLIDSGLFQ--DTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN--VKIGDFGLATSNKLNV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 YTYIQ---------------------SRFYRSPEVILGHP--YDVAIDMWSLGCITAELYtgYPLFPGENEVEQLACIME 433
Cdd:cd14046   159 ELATQdinkstsaalgssgdltgnvgTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC--YPFSTGMERVQILTALRS 236
                         250
                  ....*....|....*...
gi 2032329476 434 VLGLPPAGFIQTASRRQT 451
Cdd:cd14046   237 VSIEFPPDFDDNKHSKQA 254
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
219-415 6.11e-11

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: 63.12  E-value: 6.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKII---RNKKRFHQQALMELKILEALRKKdkdntyNVVHM------KDFFY 289
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVdmkRAPGDCPENIKKEVCIQKMLSHK------NVVRFyghrreGEFQY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNHFCItfellGINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG-S 368
Cdd:cd14069    77 LFLEYAS-----GGELFDKIEPDV--GMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDN--LKISDFGlA 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 369 SCYEHQKVYTYIQSRF----YRSPEVILGHPYDVA-IDMWSLGCITAELYTG 415
Cdd:cd14069   148 TVFRYKGKERLLNKMCgtlpYVAPELLAKKKYRAEpVDVWSCGIVLFAMLAG 199
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
219-428 7.33e-11

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: 63.19  E-value: 7.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAkCLDHKN-NELVALK-------IIRNKKrfhQQALMELKILEAlrkkdKDNTYnVVHMKDFFYF 290
Cdd:cd05609     2 FETIKLISNGAYGAVY-LVRHREtRQRFAMKkinkqnlILRNQI---QQVFVERDILTF-----AENPF-VVSMYCSFET 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCITFELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS 369
Cdd:cd05609    72 KRHLCMVMEYVeGGDCATLLKN--IGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGH--IKLTDFGLS 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 370 ----------CYE-HQKVYTYI---QSRF----YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENeVEQL 428
Cdd:cd05609   148 kiglmslttnLYEgHIEKDTREfldKQVCgtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDT-PEEL 223
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
219-434 8.58e-11

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: 63.53  E-value: 8.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQ----ALMELKILEALRKKDkdnTYNVVHMKDFFYFRNHF 294
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTGD---CPFIVCMSYAFHTPDKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSC-YE 372
Cdd:cd14223    79 SFILDLMnGGDLHYHLSQHGV--FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGH--VRISDLGLACdFS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 373 HQKVYTYIQSRFYRSPEVIL-GHPYDVAIDMWSLGCITAELYTGYPLF-----PGENEVEQLACIMEV 434
Cdd:cd14223   155 KKKPHASVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTMAV 222
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
222-412 9.09e-11

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: 63.50  E-value: 9.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKII----RNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDfFYFRNH--FC 295
Cdd:cd06634    20 LREIGHGSFGAVYFARDVRNNEVVAIKKMsysgKQSNEKWQDIIKEVKFLQKLRHP------NTIEYRG-CYLREHtaWL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLG--INLYELMKnNNFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYeH 373
Cdd:cd06634    93 VMEYCLGsaSDLLEVHK-KPLQEVEIAAI---THGALQGLAYLHSHNMIHRDVKAGNILLTEPGL--VKLGDFGSASI-M 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGH---PYDVAIDMWSLGCITAEL 412
Cdd:cd06634   166 APANSFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIEL 207
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
218-425 9.50e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.82  E-value: 9.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN--------KKRFHQ--QALMELkilealrkkdkdNTYNVVHMKDF 287
Cdd:NF033483    8 RYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRPdlardpefVARFRReaQSAASL------------SHPNIVSVYDV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 288 FYFRNHFCITFELL-GINLYELMKnnnfQGFSLSIVR--RFTLSVLKCLQmLSVEK-IIHCDLKPENIVLYQKGQasVKV 363
Cdd:NF033483   76 GEDGGIPYIVMEYVdGRTLKDYIR----EHGPLSPEEavEIMIQILSALE-HAHRNgIVHRDIKPQNILITKDGR--VKV 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 364 IDFG-------SSCYEHQKVytyIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEV 425
Cdd:NF033483  149 TDFGiaralssTTMTQTNSV---LGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSPV 214
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
225-431 9.80e-11

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: 63.40  E-value: 9.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNkkrfhQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELLGiN 304
Cdd:cd05619    13 LGKGSFGKVFLAELKGTNQFFAIKALKK-----DVVLMDDDVECTMVEK------RVLSLAWEHPFLTHLFCTFQTKE-N 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 305 LYELMK--NNNFQGFSLSIVRRFTLS--------VLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYEH- 373
Cdd:cd05619    81 LFFVMEylNGGDLMFHIQSCHKFDLPratfyaaeIICGLQFLHSKGIVYRDLKLDNILLDKDGH--IKIADFGM-CKENm 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 374 ---QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACI 431
Cdd:cd05619   158 lgdAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI 218
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
225-438 1.11e-10

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: 62.79  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQAlMELKILEALRKKDKdntyNVVHMKDFFYF---RNH----FCIT 297
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETS-KEVSALECEIQLLK----NLQHERIVQYYgclRDRaektLTIF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSS------C 370
Cdd:cd06651    90 MEYMpGGSVKDQLKA--YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG--NVKLGDFGASkrlqtiC 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPgenEVEQLACIMEVLGLP 438
Cdd:cd06651   166 MSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQP 230
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
222-519 1.39e-10

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: 63.15  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKII----RNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFfYFRNH--FC 295
Cdd:cd06635    30 LREIGHGSFGAVYFARDVRTSEVVAIKKMsysgKQSNEKWQDIIKEVKFLQRIKHP------NSIEYKGC-YLREHtaWL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGI--NLYELMKNNnFQGFSLSIVrrfTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEh 373
Cdd:cd06635   103 VMEYCLGSasDLLEVHKKP-LQEIEIAAI---THGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ--VKLADFGSASIA- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGH---PYDVAIDMWSLGCITAELytgyplfpgeneveqlacimevlglppagfiqtASRRQ 450
Cdd:cd06635   176 SPANSFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIEL---------------------------------AERKP 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 451 TFFdskgfpkNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSR 519
Cdd:cd06635   223 PLF-------NMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLRER 284
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
219-438 1.50e-10

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 63.18  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNK----KRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHF 294
Cdd:cd05593    17 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEviiaKDEVAHTLTESRVLKNTRHP------FLTSLKYSFQTKDRL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL--GINLYELMKNnnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG---SS 369
Cdd:cd05593    91 CFVMEYVngGELFFHLSRE---RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH--IKITDFGlckEG 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG-YPLFPGENEVEQLACIMEVLGLP 438
Cdd:cd05593   166 ITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHEKLFELILMEDIKFP 235
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
219-518 1.53e-10

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: 63.14  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKcLDHKNNELV-ALKII--RNKKRFHQQALMELKILEALrkkdkdNTYNVVHMKDFFYFRNHFC 295
Cdd:cd06649     7 FERISELGAGNGGVVTK-VQHKPSGLImARKLIhlEIKPAIRNQIIRELQVLHEC------NSPYIVGFYGAFYSDGEIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVE-KIIHCDLKPENIVLYQKGQasVKVIDFG-SSCYE 372
Cdd:cd06649    80 ICMEHMdGGSLDQVLKEA--KRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGE--IKLCDFGvSGQLI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG-YPLFP-----------------GENEVEQLACIMEV 434
Cdd:cd06649   156 DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGrYPIPPpdakeleaifgrpvvdgEEGEPHSISPRPRP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 435 LGLPPAGFIQTASRRQTFFDSKGFpkniTNNRGKKRYPDSkdltmvlkTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAW 514
Cdd:cd06649   236 PGRPVSGHGMDSRPAMAIFELLDY----IVNEPPPKLPNG--------VFTPDFQEFVNKCLIKNPAERADLKMLMNHTF 303

                  ....
gi 2032329476 515 IHQS 518
Cdd:cd06649   304 IKRS 307
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
225-529 1.72e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 62.92  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKII--RNKKRFHQQALMELKILealrkKDKDNTyNVVHMKDFFYFRNHFCItfellg 302
Cdd:PLN00034   82 IGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQICREIEIL-----RDVNHP-NVVKCHDMFDHNGEIQV------ 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 303 inLYELMKNNNFQG------FSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEHQKV 376
Cdd:PLN00034  150 --LLEFMDGGSLEGthiadeQFLADVAR---QILSGIAYLHRRHIVHRDIKPSNLLINSAKN--VKIADFGVSRILAQTM 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 ---YTYIQSRFYRSPEVI---LGH-PYD-VAIDMWSLGCITAELYTG-YPLFPG-ENEVEQLACIMeVLGLPPAGfIQTA 446
Cdd:PLN00034  223 dpcNSSVGTIAYMSPERIntdLNHgAYDgYAGDIWSLGVSILEFYLGrFPFGVGrQGDWASLMCAI-CMSQPPEA-PATA 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 447 SRrqtffdskgfpknitnnrgkkrypdskdltmvlktydtSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPR 526
Cdd:PLN00034  301 SR--------------------------------------EFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGG 342

                  ...
gi 2032329476 527 PQT 529
Cdd:PLN00034  343 PNL 345
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
219-410 1.74e-10

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: 61.86  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITF 298
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSHP------RIAQLHSAYLSPRHLVLIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGIN--LYELMKNNNfqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS-CYEHQK 375
Cdd:cd14110    79 ELCSGPelLYNLAERNS---YSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNL--LKIVDLGNAqPFNQGK 153
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2032329476 376 VYTYIQSRFY---RSPEVILGHPYDVAIDMWSLGcITA 410
Cdd:cd14110   154 VLMTDKKGDYvetMAPELLEGQGAGPQTDIWAIG-VTA 190
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
218-426 1.91e-10

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: 61.78  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKN--NELVALKIiRNKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:cd14112     4 RFSFGSEIFRGRFSVIVKAVDSTTetDAHCAVKI-FEVSDEASEAVREFESLRTLQHE------NVQRLIAAFKPSNFAY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSScyehQK 375
Cdd:cd14112    77 LVMEKLQEDVFTRFSSNDY--YSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRA----QK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 376 VYTYIQ-----SRFYRSPEVILGH-PYDVAIDMWSLGCITAELYTGYPLFPGENEVE 426
Cdd:cd14112   151 VSKLGKvpvdgDTDWASPEFHNPEtPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDE 207
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
219-424 2.33e-10

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: 61.94  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV---AKCLDHKNNELVALKIIR-----NKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFfyf 290
Cdd:cd05613     2 FELLKVLGTGAYGKVflvRKVSGHDAGKLYAMKVLKkativQKAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDT--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCITFellgINLYELMKN-NNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS 369
Cdd:cd05613    79 KLHLILDY----INGGELFTHlSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGH--VVLTDFGLS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 370 ----CYEHQKVYTYIQSRFYRSPEVILG--HPYDVAIDMWSLGCITAELYTGYPLFPGENE 424
Cdd:cd05613   153 keflLDENERAYSFCGTIEYMAPEIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGE 213
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
219-515 3.19e-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: 61.71  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVL--ETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALME---------LKILEALRkkdkdntyNVVHMKDF 287
Cdd:cd14171     6 YEVNwtQKLGTGISGPVRVCVKKSTGERFALKILLDRPKARTEVRLHmmcsghpniVQIYDVYA--------NSVQFPGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 288 FYFRNHFCITFELL-GINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQ-ASVKVID 365
Cdd:cd14171    78 SSPRARLLIVMELMeGGELFDRISQH--RHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdAPIKLCD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 366 FGSSCYEHQKVYTYIQSRFYRSPEV-------------ILGHP----YDVAIDMWSLGCITAELYTGYPLFPGENeveql 428
Cdd:cd14171   156 FGFAKVDQGDLMTPQFTPYYVAPQVleaqrrhrkersgIPTSPtpytYDKSCDMWSLGVIIYIMLCGYPPFYSEH----- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 429 acimevlglpPAGFIQTASRRQTFFDSKGFPKNitnnrgkkrypDSKDLTMVLKtydtsflDFLRRCLVWEPSLRMTPDQ 508
Cdd:cd14171   231 ----------PSRTITKDMKRKIMTGSYEFPEE-----------EWSQISEMAK-------DIVRKLLCVDPEERMTIEE 282

                  ....*..
gi 2032329476 509 ALKHAWI 515
Cdd:cd14171   283 VLHHPWL 289
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
225-438 3.91e-10

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: 61.56  E-value: 3.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNK----KRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFEL 300
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILRKEviiaKDEVAHTVTESRVLQNTRHP------FLTALKYAFQTHDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 301 lgINLYELMknnnfqgFSLSIVRRFT--------LSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYE 372
Cdd:cd05595    77 --ANGGELF-------FHLSRERVFTedrarfygAEIVSALEYLHSRDVVYRDIKLENLMLDKDGH--IKITDFGL-CKE 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 373 ----HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG-YPLFPGENEVEQLACIMEVLGLP 438
Cdd:cd05595   145 gitdGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHERLFELILMEEIRFP 215
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
223-515 5.68e-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: 60.53  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAkCLDHKNNELVALKII----RNKKRFHQQALM---ELKILEALRKKD---------KDNTYNVvhmkd 286
Cdd:cd06631     7 NVLGKGAYGTVY-CGLTSTGQLIAVKQVeldtSDKEKAEKEYEKlqeEVDLLKTLKHVNivgylgtclEDNVVSI----- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 287 FFYFrnhfcitfeLLGINLYELMknNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDF 366
Cdd:cd06631    81 FMEF---------VPGGSIASIL--ARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGV--IKLIDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 367 GSS---CYEHQKVYtyiQSRFYRS---------PEVILGHPYDVAIDMWSLGCITAELYTGYPlfPGENeveqlacimev 434
Cdd:cd06631   148 GCAkrlCINLSSGS---QSQLLKSmrgtpywmaPEVINETGHGRKSDIWSIGCTVFEMATGKP--PWAD----------- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 435 lgLPPAGFIqtasrrqtFFdskgfpknITNNRG-KKRYPDskdltmvlkTYDTSFLDFLRRCLVWEPSLRMTPDQALKHA 513
Cdd:cd06631   212 --MNPMAAI--------FA--------IGSGRKpVPRLPD---------KFSPEARDFVHACLTRDQDERPSAEQLLKHP 264

                  ..
gi 2032329476 514 WI 515
Cdd:cd06631   265 FI 266
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
220-420 6.13e-10

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: 60.06  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKClDHKNNElVALKIIRNKKRFHQQALMELKILEALRKKdkdntyNVVHMkdffyfrnhfcITFE 299
Cdd:cd05039     9 KLGELIGKGEFGDVMLG-DYRGQK-VAVKCLKDDSTAAQAFLAEASVMTTLRHP------NLVQL-----------LGVV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LLGINLY---ELMKNNNFQGFSLS-----IVRR----FTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAsvKVIDFG 367
Cdd:cd05039    70 LEGNGLYivtEYMAKGSLVDYLRSrgravITRKdqlgFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVA--KVSDFG 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 SSCYEHQKVYTyiqSRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT----GYPLFP 420
Cdd:cd05039   148 LAKEASSNQDG---GKLpikWTAPEALREKKFSTKSDVWSFGILLWEIYSfgrvPYPRIP 204
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
225-440 7.19e-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: 60.32  E-value: 7.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQV--AKCldhkNNELVALKIIRNKKRFHQQALMELKILEALRKKDKdntynvvhMKDFFYFR---------NH 293
Cdd:cd14000     2 LGDGGFGSVyrASY----KGEPVAVKIFNKHTSSNFANVPADTMLRHLRATDA--------MKNFRLLRqeltvlshlHH 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFeLLGINLYELM---------------KNNNFQGFSLS--IVRRFTLSVLKCLQMLSVEKIIHCDLKPENIV---L 353
Cdd:cd14000    70 PSIVY-LLGIGIHPLMlvlelaplgsldhllQQDSRSFASLGrtLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 354 YQKGQASVKVIDFGSSCYE-HQKVYTYIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGENEVEQlaCI 431
Cdd:cd14000   149 YPNSAIIIKIADYGISRQCcRMGAKGSEGTPGFRAPEIARGNViYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPN--EF 226

                  ....*....
gi 2032329476 432 MEVLGLPPA 440
Cdd:cd14000   227 DIHGGLRPP 235
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
219-439 9.32e-10

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: 60.84  E-value: 9.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRkKDKDNTYNVVHMKDFFYFRNHFCITF 298
Cdd:cd05627     4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDIL-VEADGAWVVKMFYSFQDKRNLYLIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYE-LMKNNNFQGFSLSIVRRFTLSVLKCLQMLSvekIIHCDLKPENIVLYQKGQasVKVIDFG---------- 367
Cdd:cd05627    83 FLPGGDMMTlLMKKDTLSEEATQFYIAETVLAIDAIHQLG---FIHRDIKPDNLLLDAKGH--VKLSDFGlctglkkahr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 SSCYEH----------------------------QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd05627   158 TEFYRNlthnppsdfsfqnmnskrkaetwkknrrQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPF 237
                         250       260
                  ....*....|....*....|...
gi 2032329476 420 PGENEVEQLACIM---EVLGLPP 439
Cdd:cd05627   238 CSETPQETYRKVMnwkETLVFPP 260
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
218-426 1.03e-09

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: 59.65  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALK--IIRNKKRFHQQALMELKILEALRKkdkdntYNVVHMKDFFYFRNHFC 295
Cdd:cd14088     2 RYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkfLKRDGRKVRKAAKNEINILKMVKH------PNILQLVDVFETRKEYF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELL-GINLYELMKNnnfQGF-----SLSIVRRftlsVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVI-DFGS 368
Cdd:cd14088    76 IFLELAtGREVFDWILD---QGYyserdTSNVIRQ----VLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVIsDFHL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 369 SCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVE 426
Cdd:cd14088   149 AKLENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEED 206
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
218-419 1.08e-09

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: 59.56  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN----KKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNH 293
Cdd:cd14187     8 RYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKslllKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELLginlyELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENivLYQKGQASVKVIDFGSSC--- 370
Cdd:cd14187    88 LCRRRSLL-----ELHKRR--KALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGN--LFLNDDMEVKIGDFGLATkve 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVI--LGHPYDVaiDMWSLGCITAELYTGYPLF 419
Cdd:cd14187   159 YDGERKKTLCGTPNYIAPEVLskKGHSFEV--DIWSIGCIMYTLLVGKPPF 207
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
219-438 1.28e-09

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: 59.37  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLdHKNNELVALKIIRNKKRFHQQALM-ELKILEALRKKDKDNTYNVVHMKDFFYfrnhfcIT 297
Cdd:cd05148     8 FTLERKLGSGYFGEVWEGL-WKNRVRVAIKILKSDDLLKQQDFQkEVQALKRLRHKHLISLFAVCSVGEPVY------II 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGI-NLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqkGQASV-KVIDFGSSCYEHQK 375
Cdd:cd05148    81 TELMEKgSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILV---GEDLVcKVADFGLARLIKED 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 376 VYTYIQSRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT--GYPlFPGENEVEQLACIMEVLGLP 438
Cdd:cd05148   158 VYLSSDKKIpykWTAPEAASHGTFSTKSDVWSFGILLYEMFTygQVP-YPGMNNHEVYDQITAGYRMP 224
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
219-408 1.65e-09

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 58.85  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNK---KRFHQQAL-MELKILEALRKKDKDNTYNVVHMKDffyfrNHF 294
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSggpEEFIQRFLpRELQIVERLDHKNIIHVYEMLESAD-----GKI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNnnfQG-FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgqaSVKVIDFGSSCY- 371
Cdd:cd14163    77 YLVMELAeDGDVFDCVLH---GGpLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF---TLKLTDFGFAKQl 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2032329476 372 --EHQKV-YTYIQSRFYRSPEVILGHPYDVAI-DMWSLGCI 408
Cdd:cd14163   151 pkGGRELsQTFCGSTAYAAPEVLQGVPHDSRKgDIWSMGVV 191
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
219-432 1.78e-09

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: 59.63  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM----ELKILeALRK-----------KDKDNTYNVVh 283
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSffeeERDIM-AKANspwitklqyafQDSENLYLVM- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 284 mkDFfyfrnhfcitfeLLGINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKV 363
Cdd:cd05601    81 --EY------------HPGGDLLSLLSRYDDI-FEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGH--IKL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 364 IDFGSSCYEHQKvyTYIQSRF------YRSPEVIL------GHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACI 431
Cdd:cd05601   144 ADFGSAAKLSSD--KTVTSKMpvgtpdYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNI 221

                  .
gi 2032329476 432 M 432
Cdd:cd05601   222 M 222
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
219-434 1.94e-09

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: 59.62  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrnKK-----RFHQQALM-ELKILEALrkkdkdNTYN---VVHMKDFFY 289
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKAL--KKgdiiaRDEVESLMcEKRIFETV------NSARhpfLVNLFACFQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNHFCITFEllginlY----ELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVID 365
Cdd:cd05589    73 TPEHVCFVME------YaaggDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY--VKIAD 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 366 FGSsCYEH----QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACI--MEV 434
Cdd:cd05589   145 FGL-CKEGmgfgDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIvnDEV 218
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
326-417 2.63e-09

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: 58.48  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 326 TLSVLKCLQMLSVEKIIHCDLKPENIVLYqkgQASVKVIDFGSSCYEHQKVYTYIQSR---FYRSPEVILGHPYDVAIDM 402
Cdd:cd13995   102 TKHVLKGLDFLHSKNIIHHDIKPSNIVFM---STKAVLVDFGLSVQMTEDVYVPKDLRgteIYMSPEVILCRGHNTKADI 178
                          90
                  ....*....|....*
gi 2032329476 403 WSLGCITAELYTGYP 417
Cdd:cd13995   179 YSLGATIIHMQTGSP 193
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
225-432 3.04e-09

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: 58.77  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMELKILEalrKKDKDNTYNVVHMKDFFY-FRNHFCITFELLGI 303
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVLK-KDVILQDDDVECTMTE---KRILSLARNHPFLTQLYCcFQTPDRLFFVMEFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMknnnfqgFSLSIVRRF--------TLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAsvKVIDFG---SSCYE 372
Cdd:cd05590    79 NGGDLM-------FHIQKSRRFdeararfyAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHC--KLADFGmckEGIFN 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM 432
Cdd:cd05590   150 GKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAIL 209
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
225-432 3.12e-09

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: 58.66  E-value: 3.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQ-----ALMELKILeALRKKDKDNT--YNVVHMKDFFYFRNHFcit 297
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVLK-KDVILQDddvdcTMTEKRIL-ALAAKHPFLTalHSCFQTKDRLFFVMEY--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 fellgINLYELMknnnFQ-----GFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYE 372
Cdd:cd05591    78 -----VNGGDLM----FQiqrarKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGH--CKLADFGM-CKE 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 373 ----HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM 432
Cdd:cd05591   146 gilnGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 209
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
223-421 3.44e-09

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: 57.93  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKC-LDHKNNE--LVALKIIRNKKRFHQQA--LMELKILEALRKKdkdntyNVVHMkdffYfrnHFCIT 297
Cdd:cd00192     1 KKLGEGAFGEVYKGkLKGGDGKtvDVAVKTLKEDASESERKdfLKEARVMKKLGHP------NVVRL----L---GVCTE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGInLYELMKNNNFQGF------SLSIVRRFTLSVLKCLQM----------LSVEKIIHCDLKPENIVLYQKGQasV 361
Cdd:cd00192    68 EEPLYL-VMEYMEGGDLLDFlrksrpVFPSPEPSTLSLKDLLSFaiqiakgmeyLASKKFVHRDLAARNCLVGEDLV--V 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 362 KVIDFGSSCYEHQKVYTYIQSRF-----YRSPEVILGHPYDVAIDMWSLGCITAELYT--GYPlFPG 421
Cdd:cd00192   145 KISDFGLSRDIYDDDYYRKKTGGklpirWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlgATP-YPG 210
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
225-407 3.45e-09

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: 58.14  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM----ELKILEALRKKDK--DNTY------------NVVHM-- 284
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQAGFFrrppPRRKPGALGKPLDplDRVYreiailkkldhpNVVKLve 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 285 ------KDFFYfrnhfcITFELLgiNLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQ 358
Cdd:cd14118    82 vlddpnEDNLY------MVFELV--DKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGH 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 359 asVKVIDFGSSCYEH---QKVYTYIQSRFYRSPEVILGHPYDV---AIDMWSLGC 407
Cdd:cd14118   154 --VKIADFGVSNEFEgddALLSSTAGTPAFMAPEALSESRKKFsgkALDIWAMGV 206
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
218-446 3.49e-09

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: 58.10  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK--RFHQQALM--ELKILEALRKKdkdntyNVVHMKDFFYFRNH 293
Cdd:cd14188     2 RYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRvsKPHQREKIdkEIELHRILHHK------HVVQFYHYFEDKEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELLG-INLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSC-- 370
Cdd:cd14188    76 IYILLEYCSrRSMAHILKARKV--LTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENME--LKVGDFGLAArl 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 371 --YEHQKvYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTA 446
Cdd:cd14188   152 epLEHRR-RTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPA 228
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
209-438 4.53e-09

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: 58.50  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 209 KVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNK----KRFHQQALMELKILEALRKKdkdntyNVVHM 284
Cdd:cd05594    17 KPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivaKDEVAHTLTENRVLQNSRHP------FLTAL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 285 KDFFYFRNHFCITFELL--GINLYELMKNnnfQGFSLSIVRRFTLSVLKCLQMLSVEK-IIHCDLKPENIVLYQKGQasV 361
Cdd:cd05594    91 KYSFQTHDRLCFVMEYAngGELFFHLSRE---RVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGH--I 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 362 KVIDFGSsCYEHQK----VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG-YPLFPGENEVEQLACIMEVLG 436
Cdd:cd05594   166 KITDFGL-CKEGIKdgatMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDHEKLFELILMEEIR 244

                  ..
gi 2032329476 437 LP 438
Cdd:cd05594   245 FP 246
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
223-417 5.55e-09

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: 57.24  E-value: 5.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKN------NELVALKIIRN-KKRFHQqalmELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEgievawNEIKLRKLPKAeRQRFKQ----EIEILKSLKHP------NIIKFYDSWESKSKKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFellginLYELMKN-------NNFQGFSLSIVRRFTLSVLKCLQMLSVEK--IIHCDLKPENIVLyQKGQASVKVIDF 366
Cdd:cd13983    77 VIF------ITELMTSgtlkqylKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFI-NGNTGEVKIGDL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 367 GSSCY-EHQKVYTYIQSRFYRSPEVILGHpYDVAIDMWSLGCITAELYTG-YP 417
Cdd:cd13983   150 GLATLlRQSFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGeYP 201
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
219-419 6.53e-09

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 58.07  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAkCLDHKNNEL--VALK------IIRNKKRFHqqALMELKILEALRKKDKDNTYNVVHMKDFFYF 290
Cdd:PTZ00426   32 FNFIRTLGTGSFGRVI-LATYKNEDFppVAIKrfekskIIKQKQVDH--VFSERKILNYINHPFCVNLYGSFKDESYLYL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCItfellGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSC 370
Cdd:PTZ00426  109 VLEFVI-----GGEFFTFLRRN--KRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDG--FIKMTDFGFAK 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 371 YEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:PTZ00426  180 VVDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
219-432 7.40e-09

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: 57.94  E-value: 7.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKileALRK--KDKDNTYnVVHMKDFFYFRNHFCI 296
Cdd:cd05629     3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVK---AERDvlAESDSPW-VVSLYYSFQDAQYLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH-- 373
Cdd:cd05629    79 IMEFLpGGDLMTMLIK--YDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGH--IKLSDFGLSTGFHkq 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 374 -------------------------------------QKVYTYIQSRF-----------YRSPEVILGHPYDVAIDMWSL 405
Cdd:cd05629   155 hdsayyqkllqgksnknridnrnsvavdsinltmsskDQIATWKKNRRlmaystvgtpdYIAPEIFLQQGYGQECDWWSL 234
                         250       260
                  ....*....|....*....|....*..
gi 2032329476 406 GCITAELYTGYPLFPGENEVEQLACIM 432
Cdd:cd05629   235 GAIMFECLIGWPPFCSENSHETYRKII 261
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
219-425 7.70e-09

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: 56.90  E-value: 7.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQ--------QALMELKILealrKKDKDNTYNVVHMKDFFYF 290
Cdd:cd14100     2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHV-EKDRVSEwgelpngtRVPMEIVLL----KKVGSGFRGVIRLLDWFER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCITFELLGI--NLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVKVIDFGS 368
Cdd:cd14100    77 PDSFVLVLERPEPvqDLFDFITERG--ALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENI-LIDLNTGELKLIDFGS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 369 SCYEHQKVYT-YIQSRFYRSPEVILGHPYD-VAIDMWSLGCITAELYTGYPLFPGENEV 425
Cdd:cd14100   154 GALLKDTVYTdFDGTRVYSPPEWIRFHRYHgRSAAVWSLGILLYDMVCGDIPFEHDEEI 212
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
218-367 7.74e-09

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 56.99  E-value: 7.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKiIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFrnhfcIT 297
Cdd:cd14129     1 RWKVLRKIGGGGFGEIYDALDLLTRENVALK-VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNY-----VV 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 298 FELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVK--VIDFG 367
Cdd:cd14129    75 MQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKcyMLDFG 146
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
225-440 8.39e-09

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: 56.86  E-value: 8.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKK--RFHQQA--LMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFEL 300
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRvaKPHQREkiVNEIELHRDLHHK------HVVKFSHHFEDAENIYIFLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 301 LG-INLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH---QKV 376
Cdd:cd14189    83 CSrKSLAHIWKARH--TLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENME--LKVGDFGLAARLEppeQRK 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 377 YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPA 440
Cdd:cd14189   159 KTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPA 222
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
196-417 1.04e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 57.58  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 196 SKTSFDDEHGFY------LKVLHDhiaYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKkrfhqQALMELKILEA 269
Cdd:PHA03209   42 SESDDDDDDGLIptkqkaREVVAS---LGYTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQKG-----TTLIEAMLLQN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 270 LrkkdkdNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFQgfsLSIVRRFTL--SVLKCLQMLSVEKIIHCDLK 347
Cdd:PHA03209  114 V------NHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRSRP---LPIDQALIIekQILEGLRYLHAQRIIHRDVK 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 348 PENIVLyqKGQASVKVIDFGSScyehqkVYTYIQSRFY--------RSPEVILGHPYDVAIDMWSLGCITAELyTGYP 417
Cdd:PHA03209  185 TENIFI--NDVDQVCIGDLGAA------QFPVVAPAFLglagtvetNAPEVLARDKYNSKADIWSAGIVLFEM-LAYP 253
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
212-427 1.08e-08

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 56.99  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 212 HDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR--------NKKRFHQQALMELKIlealrKKDKDNTyNVVH 283
Cdd:cd14041     1 HPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQlnknwrdeKKENYHKHACREYRI-----HKELDHP-RIVK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 284 MKDFFYF-RNHFCITFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEK--IIHCDLKPENIVLYQ-KGQ 358
Cdd:cd14041    75 LYDYFSLdTDSFCTVLEYCeGNDLDFYLKQHKL--MSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNgTAC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 359 ASVKVIDFGSSCYEHQKVYTYIQ----------SRFYRSPE--VILGHPYDVA--IDMWSLGCITAELYTGYPLFpGENE 424
Cdd:cd14041   153 GEIKITDFGLSKIMDDDSYNSVDgmeltsqgagTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFYQCLYGRKPF-GHNQ 231

                  ...
gi 2032329476 425 VEQ 427
Cdd:cd14041   232 SQQ 234
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
219-416 1.14e-08

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: 56.72  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV-----AKCLDHKNNELVALKIIRN---KKRFHQQALM-ELKILEALRKKdkdntyNVVHMKDFFY 289
Cdd:cd14076     3 YILGRTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRdtqQENCQTSKIMrEINILKGLTHP------NIVRLLDVLK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 290 FRNHFCITFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFG- 367
Cdd:cd14076    77 TKKYIGIVLEFVsGGELFDYILARRR--LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDK--NRNLVITDFGf 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 368 SSCYEHQK---VYTYIQSRFYRSPE-VILGHPYD-VAIDMWSLGCITAELYTGY 416
Cdd:cd14076   153 ANTFDHFNgdlMSTSCGSPCYAAPElVVSDSMYAgRKADIWSCGVILYAMLAGY 206
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
225-367 1.14e-08

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 53.99  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALM-ELKILEALRKKDKdntyNVVHMKDFFYFRNHFCITFELL-G 302
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLEsEMDILRRLKGLEL----NIPKVLVTEDVDGPNILLMELVkG 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 303 INLYELMknnnfQGFSLS--IVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFG 367
Cdd:cd13968    77 GTLIAYT-----QEEELDekDVESIMYQLAECMRLLHSFHLIHRDLNNDNILL--SEDGNVKLIDFG 136
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
225-414 1.16e-08

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: 56.29  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLdhKNNELVALKII---RNKKRFhqqaLMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELL 301
Cdd:cd14058     1 VGRGSFGVVCKAR--WRNQIVAVKIIeseSEKKAF----EVEVRQLSRVDHP------NIIKLYGACSNQKPVCLVMEYA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 -GINLYELMKNNNFQ-GFSLSIVRRFTLSVLKCLQML---SVEKIIHCDLKPENIVLYQKGQAsVKVIDFGSSCYEHQKV 376
Cdd:cd14058    69 eGGSLYNVLHGKEPKpIYTAAHAMSWALQCAKGVAYLhsmKPKALIHRDLKPPNLLLTNGGTV-LKICDFGTACDISTHM 147
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2032329476 377 YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd14058   148 TNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVIT 185
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
222-421 1.21e-08

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 56.35  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQV----AKCLDHKNNELVALKIIRNKKRFHQQA--LMELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:pfam07714   4 GEKLGEGAFGEVykgtLKGEGENTKIKVAVKTLKEGADEEEREdfLEEASIMKKLDHP------NIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFEL--LGiNLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH 373
Cdd:pfam07714  78 IVTEYmpGG-DLLDFLRKHK-RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLV--VKISDFGLSRDIY 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 374 QKVYTYIQSR-----FYRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPG 421
Cdd:pfam07714 154 DDDYYRKRGGgklpiKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPG 207
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
218-369 1.42e-08

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: 56.51  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQ---------------------------QALMELKIleaL 270
Cdd:cd14199     3 QYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQagfprrppprgaraapegctqprgpieRVYQEIAI---L 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 271 RKKDKDNTYNVVHMKDFFYfRNHFCITFELlgINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPEN 350
Cdd:cd14199    80 KKLDHPNVVKLVEVLDDPS-EDHLYMVFEL--VKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSN 156
                         170
                  ....*....|....*....
gi 2032329476 351 IVLYQKGQasVKVIDFGSS 369
Cdd:cd14199   157 LLVGEDGH--IKIADFGVS 173
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
225-444 1.54e-08

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: 56.16  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNN------ELVALKIIR-NKKRFHQqalmELKILEALRKKdkdntyNVVHMKDFF--YFRNHFC 295
Cdd:cd14033     9 IGRGSFKTVYRGLDTETTvevawcELQTRKLSKgERQRFSE----EVEMLKGLQHP------NIVRFYDSWksTVRGHKC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ItfellgINLYELMKNNN-------FQGFSLSIVRRFTLSVLKCLQML--SVEKIIHCDLKPENIVLyQKGQASVKVIDF 366
Cdd:cd14033    79 I------ILVTELMTSGTlktylkrFREMKLKLLQRWSRQILKGLHFLhsRCPPILHRDLKCDNIFI-TGPTGSVKIGDL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 367 GSSCYEHQK-VYTYIQSRFYRSPEvILGHPYDVAIDMWSLGCITAELYTG-YPLFPGENEVEQLACIMEvlGLPPAGFIQ 444
Cdd:cd14033   152 GLATLKRASfAKSVIGTPEFMAPE-MYEEKYDEAVDVYAFGMCILEMATSeYPYSECQNAAQIYRKVTS--GIKPDSFYK 228
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
228-415 1.57e-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: 55.58  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 228 GSFGQVAKCLDHKNNELVALKIIRNKKRfhqqalMELKILEALrkkdkdNTYNVVHMKDFFYFRNHFCITFELLGI-NLY 306
Cdd:cd14059     2 GSGAQGAVFLGKFRGEEVAVKKVRDEKE------TDIKHLRKL------NHPNIIKFKGVCTQAPCYCILMEYCPYgQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 307 ELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFGSS--CYEHQKVYTYIQSRF 384
Cdd:cd14059    70 EVLRAG--REITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLV--TYNDVLKISDFGTSkeLSEKSTKMSFAGTVA 145
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2032329476 385 YRSPEVILGHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd14059   146 WMAPEVIRNEPCSEKVDIWSFGVVLWELLTG 176
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
219-439 1.79e-08

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: 56.97  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELK-----ILEAlrkkdkdNTYNVVHMKDFFYFRNH 293
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRaerdiLVEA-------DSLWVVKMFYSFQDKLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFELL--GINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSvekIIHCDLKPENIVLYQKGQasVKVIDFG---- 367
Cdd:cd05628    76 LYLIMEFLpgGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLG---FIHRDIKPDNLLLDSKGH--VKLSDFGlctg 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 -----------------------SSCYEHQKVYTYIQSRF-----------YRSPEVILGHPYDVAIDMWSLGCITAELY 413
Cdd:cd05628   151 lkkahrtefyrnlnhslpsdftfQNMNSKRKAETWKRNRRqlafstvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEML 230
                         250       260
                  ....*....|....*....|....*....
gi 2032329476 414 TGYPLFPGENEVEQLACIM---EVLGLPP 439
Cdd:cd05628   231 IGYPPFCSETPQETYKKVMnwkETLIFPP 259
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
226-421 2.22e-08

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: 55.35  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 226 GKGSFGQVAKCLDHKNNELVALKIIRNKKRfhqqalmELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELLGI-N 304
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIEK-------EAEILSVLSHR------NIIQFYGAILEAPNYGIVTEYASYgS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 305 LYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVE---KIIHCDLKPENIVLYQKGqaSVKVIDFGSS-CYEHQKVYTYI 380
Cdd:cd14060    69 LFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADG--VLKICDFGASrFHSHTTHMSLV 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2032329476 381 QSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPG 421
Cdd:cd14060   147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG 187
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
218-383 4.80e-08

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; 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. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 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: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 54.82  E-value: 4.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRfHQQALMELKILEALRkkdkdNTYNVVHMKDFFYFRNHFCIT 297
Cdd:cd14128     1 KYRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKAR-HPQLLYESKLYKILQ-----GGVGIPHIRWYGQEKDYNVLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLYELMknnNFqgfslsIVRRFTLSVLKCL--QMLS------VEKIIHCDLKPENIVLYQKGQAS-VKVIDFG- 367
Cdd:cd14128    75 MDLLGPSLEDLF---NF------CSRRFTMKTVLMLadQMIGrieyvhNKNFIHRDIKPDNFLMGIGRHCNkLFLIDFGl 145
                         170
                  ....*....|....*.
gi 2032329476 368 SSCYEHQKVYTYIQSR 383
Cdd:cd14128   146 AKKYRDSRTRQHIPYR 161
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
225-423 5.19e-08

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: 55.27  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNK----KRFHQQALMELKILeaLRKKDKDNTYnVVHMKdfFYFRNH---FCIT 297
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKvivaKKEVAHTIGERNIL--VRTALDESPF-IVGLK--FSFQTPtdlYLVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLY-ELMKNNNfqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS---CYEH 373
Cdd:cd05586    76 DYMSGGELFwHLQKEGR---FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGH--IALCDFGLSkadLTDN 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHP-YDVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:cd05586   151 KTTNTFCGTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAED 201
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
225-415 5.42e-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: 55.05  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNK----KRFHQQALMELKILEALRkkdkdntynvvH-----MKDFFYFRNHFC 295
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILKKEviiaKDEVAHTLTENRVLQNTR-----------HpfltsLKYSFQTNDRLC 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELlgINLYELMknnnfqgFSLSIVRRFT--------LSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG 367
Cdd:cd05571    72 FVMEY--VNGGELF-------FHLSRERVFSedrtrfygAEIVLALGYLHSQGIVYRDLKLENLLLDKDGH--IKITDFG 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 368 SsCYEhQKVYTYIQSRF-----YRSPEVILGHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd05571   141 L-CKE-EISYGATTKTFcgtpeYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 191
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
217-413 7.38e-08

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: 54.21  E-value: 7.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 217 YRYEVLETIGKGSFGQVAKCLDHKNNELVALK--IIRNKkrfHQQALM--ELKILEALRK-------------KDKDNTY 279
Cdd:cd14037     3 HHVTIEKYLAEGGFAHVYLVKTSNGGNRAALKrvYVNDE---HDLNVCkrEIEIMKRLSGhknivgyidssanRSGNGVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 280 NV-VHMkdffyfrnHFCitfelLGINLYELMKNNNFQGFS----LSIVRRFTLSVlKCLQMLSVeKIIHCDLKPENIVLY 354
Cdd:cd14037    80 EVlLLM--------EYC-----KGGGVIDLMNQRLQTGLTeseiLKIFCDVCEAV-AAMHYLKP-PLIHRDLKVENVLIS 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 355 QKGqaSVKVIDFGSSCYEHQ---------------KVYTYIQsrfYRSPEVI---LGHPYDVAIDMWSLGCItaeLY 413
Cdd:cd14037   145 DSG--NYKLCDFGSATTKILppqtkqgvtyveediKKYTTLQ---YRAPEMIdlyRGKPITEKSDIWALGCL---LY 213
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
219-432 7.63e-08

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 55.01  E-value: 7.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAkCLDHKNNELV-ALKIIrNKKRFHQQALMelkileALRKKDKDNTYN-----VVHMKDFFYFRN 292
Cdd:cd05624    74 FEIIKVIGRGAFGEVA-VVKMKNTERIyAMKIL-NKWEMLKRAET------ACFREERNVLVNgdcqwITTLHYAFQDEN 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFEL-LGINLYELMknNNFQGFSLSIVRRFTLSVLkCLQMLSVEKI--IHCDLKPENIVLYQKGQasVKVIDFGSs 369
Cdd:cd05624   146 YLYLVMDYyVGGDLLTLL--SKFEDKLPEDMARFYIGEM-VLAIHSIHQLhyVHRDIKPDNVLLDMNGH--IRLADFGS- 219
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 370 CYEHQKVYTyIQSRF------YRSPEVI------LGHpYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM 432
Cdd:cd05624   220 CLKMNDDGT-VQSSVavgtpdYISPEILqamedgMGK-YGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
220-415 7.69e-08

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: 53.87  E-value: 7.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHKNnelVALKIIRNKKRFHQQALMELKILEALRKKdkdNTYNVVHMKDFFYFRNHFCITFE 299
Cdd:cd14150     3 SMLKRIGTGSFGTVFRGKWHGD---VAVKILKVTEPTPEQLQAFKNEMQVLRKT---RHVNILLFMGFMTRPNFAIITQW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LLGINLYELMK--NNNFQGFSLSIVRRFTLsvlKCLQMLSVEKIIHCDLKPENIVLYQKgqASVKVIDFGSSCYE----- 372
Cdd:cd14150    77 CEGSSLYRHLHvtETRFDTMQLIDVARQTA---QGMDYLHAKNIIHRDLKSNNIFLHEG--LTVKIGDFGLATVKtrwsg 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 373 HQKVYTYIQSRFYRSPEVIL---GHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd14150   152 SQQVEQPSGSILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMSG 197
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
307-421 7.97e-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: 7.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 307 ELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkGQAsVKVIDFG-SSCYEHQKVYTYIQSRF- 384
Cdd:cd05105   224 NLLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQ-GKI-VKICDFGlARDIMHDSNYVSKGSTFl 301
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2032329476 385 ---YRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPG 421
Cdd:cd05105   302 pvkWMAPESIFDNLYTTLSDVWSYGILLWEIFSlGGTPYPG 342
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
223-417 8.20e-08

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: 53.60  E-value: 8.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIR------NKKRFHQQAlmelkilEALRKKDKDNTYNVVHMkdffyfrnhfCI 296
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRetlppdLKRKFLQEA-------RILKQYDHPNIVKLIGV----------CV 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGInLYELMKNNNFqgfsLSIVRR--FTLSVLKCLQM----------LSVEKIIHCDLKPENIVLYQKGQasVKVI 364
Cdd:cd05041    64 QKQPIMI-VMELVPGGSL----LTFLRKkgARLTVKQLLQMcldaaagmeyLESKNCIHRDLAARNCLVGENNV--LKIS 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 365 DFGSSCYEHQKVYTyIQSRF------YRSPEVILGHPYDVAIDMWSLGCITAELYTG----YP 417
Cdd:cd05041   137 DFGMSREEEDGEYT-VSDGLkqipikWTAPEALNYGRYTSESDVWSFGILLWEIFSLgatpYP 198
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
219-433 8.60e-08

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: 53.88  E-value: 8.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQALM----ELKILEALRKKDKDNTYNVVHMkdffYFRNHF 294
Cdd:cd14075     4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKIL-DKTKLDQKTQRllsrEISSMEKLHHPNIIRLYEVVET----LSKLHL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGinlyELMKNNNFQGfslsivrRFTLSVLKCL--QMLSVEK------IIHCDLKPENIVLYQKGQasVKVIDF 366
Cdd:cd14075    79 VMEYASGG----ELYTKISTEG-------KLSESEAKPLfaQIVSAVKhmhennIIHRDLKAENVFYASNNC--VKVGDF 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 367 GSSCY--EHQKVYTYIQSRFYRSPEVILG-HPYDVAIDMWSLGCITAELYTGYPLFPGENeVEQL-ACIME 433
Cdd:cd14075   146 GFSTHakRGETLNTFCGSPPYAAPELFKDeHYIGIYVDIWALGVLLYFMVTGVMPFRAET-VAKLkKCILE 215
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
219-427 8.91e-08

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: 54.05  E-value: 8.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKK---RFHQQALMELKILEALrkkdkdNTYNVV--------HMKDF 287
Cdd:cd14049     8 FEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKvtkRDCMKVLREVKVLAGL------QHPNIVgyhtawmeHVQLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 288 FYfrnhfcITFELLGINLYELMKNNN----FQGFS--------LSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQ 355
Cdd:cd14049    82 LY------IQMQLCELSLWDWIVERNkrpcEEEFKsapytpvdVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 356 KGQaSVKVIDFGSSC----YEHQKVYTYIQSR-----------FYRSPEVILGHPYDVAIDMWSLGCITAELYTgyplfP 420
Cdd:cd14049   156 SDI-HVRIGDFGLACpdilQDGNDSTTMSRLNglthtsgvgtcLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ-----P 229

                  ....*..
gi 2032329476 421 GENEVEQ 427
Cdd:cd14049   230 FGTEMER 236
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
213-435 9.10e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 55.08  E-value: 9.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 213 DHIAYRYEVLETIGKGSFGQVAKC--------------------LDHKNNELVAlKIIRNKKRFHQQALME--------- 263
Cdd:PHA03210  144 DEFLAHFRVIDDLPAGAFGKIFICalrasteeaearrgvnstnqGKPKCERLIA-KRVKAGSRAAIQLENEilalgrlnh 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 264 ---LKILEALRKKDkdNTYNVVHMKDFfyfrnhfcitfellgiNLYELMKNNNFQGFS---LSIVRRFTLSVLKCLQMLS 337
Cdd:PHA03210  223 eniLKIEEILRSEA--NTYMITQKYDF----------------DLYSFMYDEAFDWKDrplLKQTRAIMKQLLCAVEYIH 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 338 VEKIIHCDLKPENIVLyqKGQASVKVIDFGSSC-YEHQKV---YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELY 413
Cdd:PHA03210  285 DKKLIHRDIKLENIFL--NCDGKIVLGDFGTAMpFEKEREafdYGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDML 362
                         250       260
                  ....*....|....*....|....*.
gi 2032329476 414 TgYPLFP----GENEVEQLACIMEVL 435
Cdd:PHA03210  363 S-HDFCPigdgGGKPGKQLLKIIDSL 387
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
322-513 9.19e-08

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


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 53.52  E-value: 9.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 322 VRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQK-GQASVKVIDFGSS----CYEHQKVYTYIQSRFYRSPEVILG-HP 395
Cdd:cd14012   106 ARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDaGTGIVKLTDYSLGktllDMCSRGSLDEFKQTYWLPPELAQGsKS 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 396 YDVAIDMWSLGcitaelytgyplfpgeneveqlacimevlglppAGFIQTASRRQTFfdskgfpknitnnrgkkRYPDSK 475
Cdd:cd14012   186 PTRKTDVWDLG---------------------------------LLFLQMLFGLDVL-----------------EKYTSP 215
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2032329476 476 DLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHA 513
Cdd:cd14012   216 NPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
212-427 9.31e-08

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 54.29  E-value: 9.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 212 HDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR--------NKKRFHQQALMELKIlealrKKDKDNTyNVVH 283
Cdd:cd14040     1 HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQlnkswrdeKKENYHKHACREYRI-----HKELDHP-RIVK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 284 MKDFFYF-RNHFCITFELL-GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEK--IIHCDLKPENIVLYQ-KGQ 358
Cdd:cd14040    75 LYDYFSLdTDTFCTVLEYCeGNDLDFYLKQHKL--MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDgTAC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 359 ASVKVIDFGSSCYEHQKVYTY---------IQSRFYRSPE--VILGHPYDVA--IDMWSLGCITAELYTGYPLFpGENEV 425
Cdd:cd14040   153 GEIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQCLYGRKPF-GHNQS 231

                  ..
gi 2032329476 426 EQ 427
Cdd:cd14040   232 QQ 233
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
219-427 1.21e-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: 53.42  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQ-----QALMELKILeaLRKKDKDNTYNVVHMKDFFYFRNH 293
Cdd:cd14102     2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVV-KERVTEwgtlnGVMVPLEIV--LLKKVGSGFRGVIKLLDWYERPDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFEL--LGINLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKgQASVKVIDFGSSCY 371
Cdd:cd14102    79 FLIVMERpePVKDLFDFITEKG--ALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLR-TGELKLIDFGSGAL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 372 EHQKVYT-YIQSRFYRSPEVILGHPYD-VAIDMWSLGCITAELYTGYPLFPGENEVEQ 427
Cdd:cd14102   156 LKDTVYTdFDGTRVYSPPEWIRYHRYHgRSATVWSLGVLLYDMVCGDIPFEQDEEILR 213
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
214-414 1.38e-07

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: 53.36  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 214 HIAYryevLETIGKGSFGQVAKC----LDHKNNELVALKIIRNKKRFHQQALM-ELKILEALRKKdkdntyNVVHMKDFF 288
Cdd:cd05081     5 HLKY----ISQLGKGNFGSVELCrydpLGDNTGALVAVKQLQHSGPDQQRDFQrEIQILKALHSD------FIVKYRGVS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 YF--RNHFCITFELL--GINLYELMKNNNFQGFSLSIVrrFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVI 364
Cdd:cd05081    75 YGpgRRSLRLVMEYLpsGCLRDFLQRHRARLDASRLLL--YSSQICKGMEYLGSRRCVHRDLAARNILV--ESEAHVKIA 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 365 DFG-SSCYEHQKVYTYIQSR-----FYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd05081   151 DFGlAKLLPLDKDYYVVREPgqspiFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
225-412 1.46e-07

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 53.04  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALK-IIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFrnhfcITFELLGI 303
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKeLIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNF-----ITEYIKGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG--------SSCYEH-- 373
Cdd:cd14221    76 TLRGIIKSMDSH-YPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENK--SVVVADFGlarlmvdeKTQPEGlr 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 374 -------QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAEL 412
Cdd:cd14221   153 slkkpdrKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEI 198
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
218-408 1.53e-07

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: 53.71  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIR-NKKRFHQQALMELKILEALRKKDKdntyNVVHMKDFFYFRNHFC- 295
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRcNAPENVELALREFWALSSIQRQHP----NVIQLEECVLQRDGLAq 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ----------ITFELLGINL-----------------YELMKNNNFQGFSLSivRR--------FTLSVLKCLQMLSVEK 340
Cdd:cd13977    77 rmshgssksdLYLLLVETSLkgercfdprsacylwfvMEFCDGGDMNEYLLS--RRpdrqtntsFMLQLSSALAFLHRNQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 341 IIHCDLKPENIVLYQK-GQASVKVIDFGSS--C-------YEHQKVYTYIQSR-----FYRSPEVILGHpYDVAIDMWSL 405
Cdd:cd13977   155 IVHRDLKPDNILISHKrGEPILKVADFGLSkvCsgsglnpEEPANVNKHFLSSacgsdFYMAPEVWEGH-YTAKADIFAL 233

                  ...
gi 2032329476 406 GCI 408
Cdd:cd13977   234 GII 236
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
225-412 1.54e-07

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: 52.88  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIirnKKRFHQQA--LMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFELL- 301
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKE---LKRFDEQRsfLKEVKLMRRLSHP------NILRFIGVCVKDNKLNFITEYVn 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 GINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPEN-IVLYQKGQASVKVIDFG---------SSCY 371
Cdd:cd14065    72 GGTLEELLKSMDEQ-LPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNcLVREANRGRNAVVADFGlarempdekTKKP 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2032329476 372 EHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAEL 412
Cdd:cd14065   151 DRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEI 191
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
219-432 1.79e-07

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 53.86  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVakcldhknnelvalKIIRNKKRFHQQALMELKILEALRKKD-------KD-----NTYNVVHMkd 286
Cdd:cd05622    75 YEVVKVIGRGAFGEV--------------QLVRHKSTRKVYAMKLLSKFEMIKRSDsaffweeRDimafaNSPWVVQL-- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 287 FFYFRN--HFCITFELL-GINLYELMKNNNFQGfslSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKV 363
Cdd:cd05622   139 FYAFQDdrYLYMVMEYMpGGDLVNLMSNYDVPE---KWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH--LKL 213
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 364 IDFGsSCYEHQK-----VYTYIQSRFYRSPEVILGHP----YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM 432
Cdd:cd05622   214 ADFG-TCMKMNKegmvrCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 290
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
225-422 2.49e-07

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: 52.33  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDK-DNTYNVVHMKDFFYFrnhFCITFELLGi 303
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHiIKTYDVAFETEDYYV---FAQEYAPYG- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNNfqGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSScyehQKVYTYIQSR 383
Cdd:cd13987    77 DLFSIIPPQV--GLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLT----RRVGSTVKRV 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2032329476 384 FYRSP-------EVILGHPYDV--AIDMWSLGCITAELYTGYplFPGE 422
Cdd:cd13987   151 SGTIPytapevcEAKKNEGFVVdpSIDVWAFGVLLFCCLTGN--FPWE 196
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
218-408 2.51e-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: 52.51  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALK-IIRNKKRFHQQALMELKILEALRKKDkdntyNVVHM--------KDFF 288
Cdd:cd14036     1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKrLLSNEEEKNKAIIQEINFMKKLSGHP-----NIVQFcsaasigkEESD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 YFRNHFCITFELLGINLYELMKNNNFQG-FSLSIVRRFTLSVLKCLQMLSVEK--IIHCDLKPENIVLYQKGQasVKVID 365
Cdd:cd14036    76 QGQAEYLLLTELCKGQLVDFVKKVEAPGpFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQ--IKLCD 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 366 FGSSCYE-HQKVYTYIQSR--------------FYRSPEVI---LGHPYDVAIDMWSLGCI 408
Cdd:cd14036   154 FGSATTEaHYPDYSWSAQKrslvedeitrnttpMYRTPEMIdlySNYPIGEKQDIWALGCI 214
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
219-406 2.63e-07

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: 52.31  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKiiRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITF 298
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVK--RSRSRFRGEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELLGINLYELMKNnnFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCYEHQKVYT 378
Cdd:cd14050    81 ELCDTSLQQYCEE--THSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDG--VCKLGDFGLVVELDKEDIH 156
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2032329476 379 YIQ---SRfYRSPEVILGHpYDVAIDMWSLG 406
Cdd:cd14050   157 DAQegdPR-YMAPELLQGS-FTKAADIFSLG 185
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
219-412 2.89e-07

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: 52.11  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKC---LDHKNNELVALKIIRNKKRFHQQALMELKILEALRK----KDKDNTYNVVHMKDFFYFR 291
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAkhrIDGKTYAIKRVKLNNEKAEREVKALAKLDHPNIVRYngcwDGFDYDPETSSSNSSRSKT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINLYE--LMKNNNFQGFSLSIVRRFtLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG-- 367
Cdd:cd14047    88 KCLFIQMEFCEKGTLEswIEKRNGEKLDKVLALEIF-EQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK--VKIGDFGlv 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2032329476 368 SSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAEL 412
Cdd:cd14047   165 TSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFEL 209
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
218-367 2.90e-07

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 52.34  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKiIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFrnhfcIT 297
Cdd:cd14130     1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNY-----VV 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 298 FELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVK--VIDFG 367
Cdd:cd14130    75 MQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFG 146
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
219-369 3.88e-07

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 52.36  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQV--AKCLDH-KNNELVALKIIRNKKRFhqQALMELKILEALRKKDKDNTYNVVH----MKDFFYFR 291
Cdd:cd13981     2 YVISKELGEGGYASVylAKDDDEqSDGSLVALKVEKPPSIW--EFYICDQLHSRLKNSRLRESISGAHsahlFQDESILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGINlyELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQA------------ 359
Cdd:cd13981    80 MDYSSQGTLLDVV--NKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEICAdwpgegengwls 157
                         170
                  ....*....|.
gi 2032329476 360 -SVKVIDFGSS 369
Cdd:cd13981   158 kGLKLIDFGRS 168
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
284-415 4.55e-07

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: 51.89  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 284 MKDFFYFRN---------HFCITFeLLGINLYEL-------------------MKNNNFQGFSLSIVRRFTLSVLKCLQM 335
Cdd:cd14067    51 MKNFSEFRQeasmlhslqHPCIVY-LIGISIHPLcfalelaplgslntvleenHKGSSFMPLGHMLTFKIAYQIAAGLAY 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 336 LSVEKIIHCDLKPENIVLY---QKGQASVKVIDFGSSCYE-HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAE 411
Cdd:cd14067   130 LHKKNIIFCDLKSDNILVWsldVQEHINIKLSDYGISRQSfHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYE 209

                  ....
gi 2032329476 412 LYTG 415
Cdd:cd14067   210 LLSG 213
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
219-419 4.93e-07

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 52.33  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYnVVHMKDFFYFRNHFCITF 298
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPF-LVGLHSCFQTTSRLFLVI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELlgINLYELMKNNNFQ-GFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYEH---- 373
Cdd:cd05617    96 EY--VNGGDLMFHMQRQrKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGH--IKLTDYGM-CKEGlgpg 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd05617   171 DTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
223-512 5.69e-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: 51.50  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQV--AKCLDHKNnelVALKiiRNKKRFHQQALMELKILEAlrkkdKDNTYNVVHM------KDFFYfrnhf 294
Cdd:cd13982     7 KVLGYGSEGTIvfRGTFDGRP---VAVK--RLLPEFFDFADREVQLLRE-----SDEHPNVIRYfctekdRQFLY----- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 cITFELLGINLYELMKN-NNFQGF---SLSIVR--RFTLSVLKCLQMLsveKIIHCDLKPENIVLYQ---KGQASVKVID 365
Cdd:cd13982    72 -IALELCAASLQDLVESpRESKLFlrpGLEPVRllRQIASGLAHLHSL---NIVHRDLKPQNILISTpnaHGNVRAMISD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 366 FGSSCYEHQKVYTYIQSRF------YRSPEVILGHPYD---VAIDMWSLGCITAELYTGyplfpgeneveqlacimevlG 436
Cdd:cd13982   148 FGLCKKLDVGRSSFSRRSGvagtsgWIAPEMLSGSTKRrqtRAVDIFSLGCVFYYVLSG--------------------G 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 437 LPPAGFIQtasRRQtffdskgfpKNITnnrgKKRYPDSKDLTMVLKTYDTSflDFLRRCLVWEPSLRMTPDQALKH 512
Cdd:cd13982   208 SHPFGDKL---ERE---------ANIL----KGKYSLDKLLSLGEHGPEAQ--DLIERMIDFDPEKRPSAEEVLNH 265
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
215-415 6.31e-07

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: 51.57  E-value: 6.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 215 IAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKkdkdntYNVVHMKDFFYFRNHF 294
Cdd:cd14149    10 EASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRH------VNILLFMGYMTKDNLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGINLYELM--KNNNFQGFSLSIVRRFTLsvlKCLQMLSVEKIIHCDLKPENIVLYQKgqASVKVIDFGSSCYE 372
Cdd:cd14149    84 IVTQWCEGSSLYKHLhvQETKFQMFQLIDIARQTA---QGMDYLHAKNIIHRDMKSNNIFLHEG--LTVKIGDFGLATVK 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 373 -----HQKVYTYIQSRFYRSPEVIL---GHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd14149   159 srwsgSQQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTG 209
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
311-419 6.42e-07

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: 51.55  E-value: 6.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 311 NNNFQGFSLS--IVRRFTLSVLKCLQML-SVEKIIHCDLKPENIVLYQKGQAsvKVIDFGSSC------YEHQKVYTYIQ 381
Cdd:cd14011   103 PPELQDYKLYdvEIKYGLLQISEALSFLhNDVKLVHGNICPESVVINSNGEW--KLAGFDFCIsseqatDQFPYFREYDP 180
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2032329476 382 SRF--------YRSPEVILGHPYDVAIDMWSLGCITAELY-TGYPLF 419
Cdd:cd14011   181 NLPplaqpnlnYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLF 227
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
219-432 6.78e-07

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: 51.94  E-value: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQALMelkileALRKKDKDNTYN-----VVHMKDFFYFRNH 293
Cdd:cd05623    74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKIL-NKWEMLKRAET------ACFREERDVLVNgdsqwITTLHYAFQDDNN 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 294 FCITFEL-LGINLYELMknNNFQGFSLSIVRRFTLSVLkCLQMLSVEKI--IHCDLKPENIVLYQKGQasVKVIDFGSsC 370
Cdd:cd05623   147 LYLVMDYyVGGDLLTLL--SKFEDRLPEDMARFYLAEM-VLAIDSVHQLhyVHRDIKPDNILMDMNGH--IRLADFGS-C 220
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 371 YEHQKVYTyIQSRF------YRSPEVILGHP-----YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIM 432
Cdd:cd05623   221 LKLMEDGT-VQSSVavgtpdYISPEILQAMEdgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
219-412 7.79e-07

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: 51.19  E-value: 7.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR----NKKRFHQQALMELKILEALrkkdkdNTYNVVHMKDFFYFRNHF 294
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQifdlMDAKARADCIKEIDLLKQL------NHPNVIKYYASFIEDNEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGI-NLYELMKNNNFQGFSL--SIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCY 371
Cdd:cd08229   100 NIVLELADAgDLSRMIKHFKKQKRLIpeKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG--VVKLGDLGLGRF 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2032329476 372 EHQKV---YTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAEL 412
Cdd:cd08229   178 FSSKTtaaHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEM 221
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
220-520 9.17e-07

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 51.14  E-value: 9.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFG----QVAKCLdhKNNELVALKII----RNKKRFhQQALMELKILEALRKKdkdntyNVVHMKDFFYFR 291
Cdd:cd08216     1 ELLYEIGKCFKGggvvHLAKHK--PTNTLVAVKKInlesDSKEDL-KFLQQEILTSRQLQHP------NILPYVTSFVVD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 292 NHFCITFELLGI-NLYELMKNNNFQGFSlSIVRRFTL-SVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSS 369
Cdd:cd08216    72 NDLYVVTPLMAYgSCRDLLKTHFPEGLP-ELAIAFILrDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CYEHQK----VYTY----IQSRFYRSPEV----ILGhpYDVAIDMWSLGCITAELYTGYplFPGENEVEQLACIMEVLGL 437
Cdd:cd08216   151 MVKHGKrqrvVHDFpkssEKNLPWLSPEVlqqnLLG--YNEKSDIYSVGITACELANGV--VPFSDMPATQMLLEKVRGT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 438 PPAGFIQTasrrqTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQ 517
Cdd:cd08216   227 TPQLLDCS-----TYPLEEDSMSQSEDSSTEHPNNRDTRDIPYQRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQ 301

                  ...
gi 2032329476 518 SRN 520
Cdd:cd08216   302 CRR 304
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
225-414 9.83e-07

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: 50.84  E-value: 9.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKC----LDHKNNELVALKIIR-NKKRFHQQAL-MELKILEALRKKdkdntyNVVHMKDFFY--FRNHFCI 296
Cdd:cd05038    12 LGEGHFGSVELCrydpLGDNTGEQVAVKSLQpSGEEQHMSDFkREIEILRTLDHE------YIVKYKGVCEspGRRSLRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELLGI-NLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFG-SSCYEHQ 374
Cdd:cd05038    86 IMEYLPSgSLRDYLQRHRDQ-IDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILV--ESEDLVKISDFGlAKVLPED 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2032329476 375 KVYTYIQSR-----FYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd05038   163 KEYYYVKEPgespiFWYAPECLRESRFSSASDVWSFGVTLYELFT 207
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
218-367 1.17e-06

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 50.44  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRfHQQALMELKILEAL---------RKKDKDNTYNVVHMkdff 288
Cdd:cd14125     1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTK-HPQLLYESKLYKILqggvgipnvRWYGVEGDYNVMVM---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 289 yfrnhfcitfELLGINLYELMknnNFQGfslsivRRFTLSVLKCL--QMLS-VEKI-----IHCDLKPENIV--LYQKGQ 358
Cdd:cd14125    76 ----------DLLGPSLEDLF---NFCS------RKFSLKTVLMLadQMISrIEYVhsknfIHRDIKPDNFLmgLGKKGN 136

                  ....*....
gi 2032329476 359 AsVKVIDFG 367
Cdd:cd14125   137 L-VYIIDFG 144
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
223-414 1.51e-06

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: 49.87  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKclDHKNNELVALKIIRNKKRfHQQALMELKILEALRKKDKDNTYNVVhmkdffyFRNHFCITFELLG 302
Cdd:cd05083    12 EIIGEGEFGAVLQ--GEYMGQKVAVKNIKCDVT-AQAFLEETAVMTKLQHKNLVRLLGVI-------LHNGLYIVMELMS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 303 I-NLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAsvKVIDFGSSCYEHQKVYTYIQ 381
Cdd:cd05083    82 KgNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVA--KISDFGLAKVGSMGVDNSRL 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2032329476 382 SRFYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd05083   160 PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFS 192
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
225-438 2.42e-06

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: 49.31  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLdhKNNELVALKIIR-----NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFE 299
Cdd:cd14061     2 IGVGGFGKVYRGI--WRGEEVAVKAARqdpdeDISVTLENVRQEARLFWMLRHP------NIIALRGVCLQPPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LlginlyelmknnnFQGFSLSIV---RRFTLSVL--------KCLQMLSVEK---IIHCDLKPENIVLYQK------GQA 359
Cdd:cd14061    74 Y-------------ARGGALNRVlagRKIPPHVLvdwaiqiaRGMNYLHNEApvpIIHRDLKSSNILILEAienedlENK 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 360 SVKVIDFGSScYEHQKVY------TYIqsrfYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGeneVEQLACIME 433
Cdd:cd14061   141 TLKITDFGLA-REWHKTTrmsaagTYA----WMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKG---IDGLAVAYG 212

                  ....*....
gi 2032329476 434 V----LGLP 438
Cdd:cd14061   213 VavnkLTLP 221
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
219-433 3.60e-06

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: 49.61  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVaKCLDHKNNELV-ALKIIRN---KKRFHQQALMELKILEALRkkdkdNTYNVVHMKDFFYFRNHF 294
Cdd:cd05621    54 YDVVKVIGRGAFGEV-QLVRHKASQKVyAMKLLSKfemIKRSDSAFFWEERDIMAFA-----NSPWVVQLFCAFQDDKYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELL-GINLYELMKNNNFQGfslSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEH 373
Cdd:cd05621   128 YMVMEYMpGGDLVNLMSNYDVPE---KWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGH--LKLADFGTCMKMD 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 374 Q----KVYTYIQSRFYRSPEVILGHP----YDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIME 433
Cdd:cd05621   203 EtgmvHCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMD 270
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
218-396 3.64e-06

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 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. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal 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: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 49.03  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKiirnkkrfhqqalMELKILEALRKKDKDNTYNVVH----MKDFFYFRN- 292
Cdd:cd14127     1 HYKVGKKIGEGSFGVIFEGTNLLNGQQVAIK-------------FEPRKSDAPQLRDEYRTYKLLAgcpgIPNVYYFGQe 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 --HFCITFELLGINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQAS---VKVIDFG 367
Cdd:cd14127    68 glHNILVIDLLGPSLEDLFDLCG-RKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRPGTKNanvIHVVDFG 146
                         170       180
                  ....*....|....*....|....*....
gi 2032329476 368 sscyehqkvytyiQSRFYRSPEVILGHPY 396
Cdd:cd14127   147 -------------MAKQYRDPKTKQHIPY 162
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
219-422 4.84e-06

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 49.11  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRN----KKRFHQQALMELKILeALRKkdkdnTYNVVHMKDFFYFRNHF 294
Cdd:cd05610     6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKadmiNKNMVHQVQAERDAL-ALSK-----SPFIVHLYYSLQSANNV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFE-LLGINLYELMknNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG------ 367
Cdd:cd05610    80 YLVMEyLIGGDVKSLL--HIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGH--IKLTDFGlskvtl 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 ------------SSCYEHQKVYTYIQSRF--------------------------------------YRSPEVILGHPYD 397
Cdd:cd05610   156 nrelnmmdilttPSMAKPKNDYSRTPGQVlslisslgfntptpyrtpksvrrgaarvegerilgtpdYLAPELLLGKPHG 235
                         250       260
                  ....*....|....*....|....*
gi 2032329476 398 VAIDMWSLGCITAELYTGYPLFPGE 422
Cdd:cd05610   236 PAVDWWALGVCLFEFLTGIPPFNDE 260
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
340-426 1.32e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 48.09  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 340 KIIHCDLKPENIVLYQKGqaSVKVIDFGSSCYEHQKVYTYIQSRF-----YRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:PTZ00267  189 KMMHRDLKSANIFLMPTG--IIKLGDFGFSKQYSDSVSLDVASSFcgtpyYLAPELWERKRYSKKADMWSLGVILYELLT 266
                          90
                  ....*....|..
gi 2032329476 415 GYPLFPGENEVE 426
Cdd:PTZ00267  267 LHRPFKGPSQRE 278
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
222-439 1.37e-05

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: 47.73  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRkKDKDNTYNVvhmKDFFYFRNHFCITFELL 301
Cdd:cd05625     6 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDIL-AEADNEWVV---RLYYSFQDKDNLYFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 GINLYELMKNNNFQGFSLSIVRRFTLSVLKClQMLSVEKI--IHCDLKPENIVLYQKGQasVKVIDFG------------ 367
Cdd:cd05625    82 YIPGGDMMSLLIRMGVFPEDLARFYIAELTC-AVESVHKMgfIHRDIKPDNILIDRDGH--IKLTDFGlctgfrwthdsk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 368 ----------------------SSC--------------YEHQK--VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCIT 409
Cdd:cd05625   159 yyqsgdhlrqdsmdfsnewgdpENCrcgdrlkplerraaRQHQRclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2032329476 410 AELYTGYPLFPGENEVE-QLACI--MEVLGLPP 439
Cdd:cd05625   239 FEMLVGQPPFLAQTPLEtQMKVInwQTSLHIPP 271
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
327-423 1.47e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 47.94  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 327 LSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSScyehqKVY----------TYIQSRFYRSPEVILGHPY 396
Cdd:PTZ00283  150 IQVLLAVHHVHSKHMIHRDIKSANILLCSNGL--VKLGDFGFS-----KMYaatvsddvgrTFCGTPYYVAPEIWRRKPY 222
                          90       100
                  ....*....|....*....|....*..
gi 2032329476 397 DVAIDMWSLGCITAELYTGYPLFPGEN 423
Cdd:PTZ00283  223 SKKADMFSLGVLLYELLTLKRPFDGEN 249
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
225-415 1.62e-05

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 47.10  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIrNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRnHFCITFELL-GI 303
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVF-NNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEELTTR-HKVLVMELCpCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKN-NNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENI--VLYQKGQASVKVIDFGSS--CYEHQKVYT 378
Cdd:cd13988    79 SLYTVLEEpSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNImrVIGEDGQSVYKLTDFGAAreLEDDEQFVS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2032329476 379 YIQSRFYRSPEV----IL----GHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd13988   159 LYGTEEYLHPDMyeraVLrkdhQKKYGATVDLWSIGVTFYHAATG 203
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
225-414 2.41e-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: 46.48  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNElVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVhmkdffYFRNHFCITFELLGIN 304
Cdd:cd05112    12 IGSGQFGLVHLGYWLNKDK-VAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVC------LEQAPICLVFEFMEHG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 305 -LYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqkGQASV-KVIDFGSSCYEHQKVYTYIQ- 381
Cdd:cd05112    85 cLSDYLRTQRGL-FSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLV---GENQVvKVSDFGMTRFVLDDQYTSSTg 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2032329476 382 SRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd05112   161 TKFpvkWSSPEVFSFSRYSSKSDVWSFGVLMWEVFS 196
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
218-512 2.62e-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: 46.52  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQalmelkilEALRKKD---KDNTYNVVHMKDF--FYFRN 292
Cdd:cd13986     1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVK--------EAMREIEnyrLFNHPNILRLLDSqiVKEAG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 293 HFCITFELL----GINLYELMKNNNFQG--FSLSIVRRFTLSV---LKCLQMLSVEKIIHCDLKPENIVLYQKGQAsvkV 363
Cdd:cd13986    73 GKKEVYLLLpyykRGSLQDEIERRLVKGtfFPEDRILHIFLGIcrgLKAMHEPELVPYAHRDIKPGNVLLSEDDEP---I 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 364 I-DFGSSCyehqKVYTYIQSR----------------FYRSPE---VILGHPYDVAIDMWSLGCItaeLYtgyplfpgen 423
Cdd:cd13986   150 LmDLGSMN----PARIEIEGRrealalqdwaaehctmPYRAPElfdVKSHCTIDEKTDIWSLGCT---LY---------- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 424 eveqlaCIMevLGLPPagfiqtasrrqtfFD---SKGFPKNITNNRGKKRYPDSkdltmvlKTYDTSFLDFLRRCLVWEP 500
Cdd:cd13986   213 ------ALM--YGESP-------------FErifQKGDSLALAVLSGNYSFPDN-------SRYSEELHQLVKSMLVVNP 264
                         330
                  ....*....|..
gi 2032329476 501 SLRMTPDQALKH 512
Cdd:cd13986   265 AERPSIDDLLSR 276
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
220-438 2.66e-05

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 46.19  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHkNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFrnhfcITFE 299
Cdd:cd05072    10 KLVKKLGAGQFGEVWMGYYN-NSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYI-----ITEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFGSSCYEHQKVYTY 379
Cdd:cd05072    84 MAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSE--SLMCKIADFGLARVIEDNEYTA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 380 IQ-SRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPGENEVEQLACIMEVLGLP 438
Cdd:cd05072   162 REgAKFpikWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGYRMP 225
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
225-415 2.71e-05

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: 46.18  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKClDHKNNElVALKIIR-----NKKRFHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFE 299
Cdd:cd14146     2 IGVGGFGKVYRA-TWKGQE-VAVKAARqdpdeDIKATAESVRQEAKLFSMLRHP------NIIKLEGVCLEEPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LL-GINLYELMKNNNFQGFSLS-------IVRRFTLSVLKCLQMLSVEK---IIHCDLKPENIVLYQK------GQASVK 362
Cdd:cd14146    74 FArGGTLNRALAAANAAPGPRRarripphILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiehddiCNKTLK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 363 VIDFGSSCYEHQKVYTYIQSRF-YRSPEVILGHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd14146   154 ITDFGLAREWHRTTKMSAAGTYaWMAPEVIKSSLFSKGSDIWSYGVLLWELLTG 207
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
222-429 2.82e-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: 46.03  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGqVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKdffyfRNHFCITfell 301
Cdd:cd05113     9 LKELGTGQFG-VVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQ-----RPIFIIT---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 ginlyELMKNNNFQGFSLSIVRRFTLS--------VLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCYEH 373
Cdd:cd05113    79 -----EYMANGCLLNYLREMRKRFQTQqllemckdVCEAMEYLESKQFLHRDLAARNCLVNDQG--VVKVSDFGLSRYVL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 374 QKVYTY-IQSRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT----GYPLFPGENEVEQLA 429
Cdd:cd05113   152 DDEYTSsVGSKFpvrWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlgkmPYERFTNSETVEHVS 215
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
334-435 2.87e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 46.81  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 334 QMLSV------EKIIHCDLKPENIVLyqKGQASVKVIDFGSSCYehqkVYTYIQSRFY---------RSPEVILGHPYDV 398
Cdd:PHA03211  268 QLLSAidyihgEGIIHRDIKTENVLV--NGPEDICLGDFGAACF----ARGSWSTPFHygiagtvdtNAPEVLAGDPYTP 341
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2032329476 399 AIDMWSLGCITAE--LYTGyPLFPGENEVEQLACIMEVL 435
Cdd:PHA03211  342 SVDIWSAGLVIFEaaVHTA-SLFSASRGDERRPYDAQIL 379
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
220-431 3.19e-05

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: 45.86  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLdHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFrnhfcITfe 299
Cdd:cd05068    11 KLLRKLGSGQFGEVWEGL-WNNTTPVAVKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYI-----IT-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 llginlyELMKNNNFQGFSLSIVRRFTLS--------VLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG-SSC 370
Cdd:cd05068    83 -------ELMKHGSLLEYLQGKGRSLQLPqlidmaaqVASGMAYLESQNYIHRDLAARNVLVGENN--ICKVADFGlARV 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 371 YEHQKVYT-YIQSRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPGENEVEQLACI 431
Cdd:cd05068   154 IKVEDEYEaREGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQV 219
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
218-449 3.29e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 46.76  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQVAKCLDHKNNEL--VALKIIRNKKRFHQqalmELKILEALRKKdkdntyNVVHMKDFFYFRNHFC 295
Cdd:PHA03207   93 QYNILSSLTPGSEGEVFVCTKHGDEQRkkVIVKAVTGGKTPGR----EIDILKTISHR------AIINLIHAYRWKSTVC 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFELLGINLYELMKNNNfqgfSLSIVRRFTLS--VLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKviDFGSSCY-- 371
Cdd:PHA03207  163 MVMPKYKCDLFTYVDRSG----PLPLEQAITIQrrLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLG--DFGAACKld 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 372 EHQ---KVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPGENEV--EQLACIMEVLGLPPAGFIQT 445
Cdd:PHA03207  237 AHPdtpQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVkNVTLFGKQVKSssSQLRSIIRCMQVHPLEFPQN 316

                  ....
gi 2032329476 446 ASRR 449
Cdd:PHA03207  317 GSTN 320
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
325-430 3.67e-05

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: 46.13  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 325 FTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSScyehQKVYT---YIQ---SRF---YRSPEVILGHP 395
Cdd:cd05103   184 YSFQVAKGMEFLASRKCIHRDLAARNILLSENN--VVKICDFGLA----RDIYKdpdYVRkgdARLplkWMAPETIFDRV 257
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2032329476 396 YDVAIDMWSLGCITAELYT-GYPLFPGENEVEQLAC 430
Cdd:cd05103   258 YTIQSDVWSFGVLLWEIFSlGASPYPGVKIDEEFCR 293
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
223-414 3.77e-05

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 45.69  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNNELVALKIIRN------KKRFhqqaLMELKILEALRKKDKDNTYNVVHMKDFFYFrnhfci 296
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRADNTPVAVKSCREtlppdlKAKF----LQEARILKQYSHPNIVRLIGVCTQKQPIYI------ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 tfellginLYELMKNNNFQGF--------SLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGS 368
Cdd:cd05084    72 --------VMELVQGGDFLTFlrtegprlKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKN--VLKISDFGM 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2032329476 369 SCYEHQKVYT------YIQSRfYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd05084   142 SREEEDGVYAatggmkQIPVK-WTAPEALNYGRYSSESDVWSFGILLWETFS 192
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
223-414 3.84e-05

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 46.14  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKC--------------LDHKNNE--LVALKIIRN--KKRFHQQALMELKILEalRKKDKdntyNVVHM 284
Cdd:cd05095    11 EKLGEGQFGEVHLCeaegmekfmdkdfaLEVSENQpvLVAVKMLRAdaNKNARNDFLKEIKIMS--RLKDP----NIIRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 285 KdffyfrnHFCITFELLGInLYELMKNNNFQGF-------------------SLSIVRRFTLSVLKCLQMLSVEKIIHCD 345
Cdd:cd05095    85 L-------AVCITDDPLCM-ITEYMENGDLNQFlsrqqpegqlalpsnaltvSYSDLRFMAAQIASGMKYLSSLNFVHRD 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032329476 346 LKPENIVLYQkgQASVKVIDFGSSCYEHQKVYTYIQSRF-----YRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd05095   157 LATRNCLVGK--NYTIKIADFGMSRNLYSGDYYRIQGRAvlpirWMSWESILLGKFTTASDVWAFGVTLWETLT 228
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
219-412 5.43e-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: 45.25  E-value: 5.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIR--NKKRFHQQALMELKILEALR-------------------KKDKDN 277
Cdd:cd14048     8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRlpNNELAREKVLREVRALAKLDhpgivryfnawlerppegwQEKMDE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 278 TYnvvhmkdfFYFRNHFCITfellgINLYELMKNN-NFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQK 356
Cdd:cd14048    88 VY--------LYIQMQLCRK-----ENLKDWMNRRcTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLD 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 357 GqaSVKVIDFGSSCY-----EHQKVYTYIQS----------RFYRSPEVILGHPYDVAIDMWSLGCITAEL 412
Cdd:cd14048   155 D--VVKVGDFGLVTAmdqgePEQTVLTPMPAyakhtgqvgtRLYMSPEQIHGNQYSEKVDIFALGLILFEL 223
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
225-415 5.50e-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: 45.19  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMELKILEALRKKDkdnTYNVVHMKDFFyfrnhfCITFELL-GI 303
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKVR-LEVFRAEELMACAGLTSPRVVP---LYGAVREGPWV------NIFMDLKeGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNNFQGFSLSIvrRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVkVIDFGSSCYEH-----QKVYT 378
Cdd:cd13991    84 SLGQLIKEQGCLPEDRAL--HYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAF-LCDFGHAECLDpdglgKSLFT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2032329476 379 --YIQ-SRFYRSPEVILGHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd13991   161 gdYIPgTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNG 200
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
325-421 6.07e-05

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: 45.76  E-value: 6.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 325 FTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG--SSCYEHQKVYTYIQSRF---YRSPEVILGHPYDVA 399
Cdd:cd14207   185 YSFQVARGMEFLSSRKCIHRDLAARNILLSENN--VVKICDFGlaRDIYKNPDYVRKGDARLplkWMAPESIFDKIYSTK 262
                          90       100
                  ....*....|....*....|...
gi 2032329476 400 IDMWSLGCITAELYT-GYPLFPG 421
Cdd:cd14207   263 SDVWSYGVLLWEIFSlGASPYPG 285
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
219-433 8.21e-05

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: 45.03  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIrNK----KRFHQQALMELKilEALRKKDKD---NTYNVVHMKDFFYF- 290
Cdd:cd05597     3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKIL-NKwemlKRAETACFREER--DVLVNGDRRwitKLHYAFQDENYLYLv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 291 RNHFCitfellGINLYELMknNNFQGFSLSIVRRFTLSVLkCLQMLSVEKI--IHCDLKPENIVLYQKGQasVKVIDFGS 368
Cdd:cd05597    80 MDYYC------GGDLLTLL--SKFEDRLPEEMARFYLAEM-VLAIDSIHQLgyVHRDIKPDNVLLDRNGH--IRLADFGS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032329476 369 sCYEHQKVYTyIQSRF------YRSPEVIL----GH-PYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIME 433
Cdd:cd05597   149 -CLKLREDGT-VQSSVavgtpdYISPEILQamedGKgRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMN 222
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
308-519 8.97e-05

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: 44.86  E-value: 8.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 308 LMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQK----VYTYIQSR 383
Cdd:cd08226    89 LLKTYFPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMVTNGQrskvVYDFPQFS 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 384 F----YRSPEVILG--HPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLacIMEVLGLP-----PAGFIQTASR---R 449
Cdd:cd08226   169 TsvlpWLSPELLRQdlHGYNVKSDIYSVGITACELARGQVPFQDMRRTQML--LQKLKGPPyspldIFPFPELESRmknS 246
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 450 QTFFDSkGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSR 519
Cdd:cd08226   247 QSGMDS-GIGESVATSSMTRTMTSERLQTPSSKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVK 315
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
225-414 1.03e-04

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: 44.53  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCL----DHKNNELVALKIIRNKKRFHQQALMELKIlEALRkkdkdNTY--NVVHMKDFFY--FRNHFCI 296
Cdd:cd05079    12 LGEGHFGKVELCRydpeGDNTGEQVAVKSLKPESGGNHIADLKKEI-EILR-----NLYheNIVKYKGICTedGGNGIKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 297 TFELL-GINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFG--SSCYEH 373
Cdd:cd05079    86 IMEFLpSGSLKEYLPRNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ--VKIGDFGltKAIETD 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2032329476 374 QKVYTYIQSR----FYRSPEVILGHPYDVAIDMWSLGCITAELYT 414
Cdd:cd05079   163 KEYYTVKDDLdspvFWYAPECLIQSKFYIASDVWSFGVTLYELLT 207
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
220-428 1.15e-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: 44.29  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHKNNElVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFyfrnhfCITFE 299
Cdd:cd05070    12 QLIKRLGNGQFGEVWMGTWNGNTK-VAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIY------IVTEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LLGINLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKI--IHCDLKPENIVLyqkGQASV-KVIDFGSSCYEHQKV 376
Cdd:cd05070    85 MSKGSLLDFLKDG--EGRALKLPNLVDMAAQVAAGMAYIERMnyIHRDLRSANILV---GNGLIcKIADFGLARLIEDNE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 377 YTYIQ-SRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPGENEVEQL 428
Cdd:cd05070   160 YTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVL 216
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
341-438 1.27e-04

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: 44.26  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 341 IIHCDLKPENIVLYQK------GQASVKVIDFGSSCYEHQKVYTYIQSRF-YRSPEVILGHPYDVAIDMWSLGCITAELY 413
Cdd:cd14145   128 VIHRDLKSSNILILEKvengdlSNKILKITDFGLAREWHRTTKMSAAGTYaWMAPEVIRSSMFSKGSDVWSYGVLLWELL 207
                          90       100
                  ....*....|....*....|....*....
gi 2032329476 414 TGYPLFPGeneVEQLA----CIMEVLGLP 438
Cdd:cd14145   208 TGEVPFRG---IDGLAvaygVAMNKLSLP 233
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
218-421 1.28e-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: 44.40  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVLETIGKGSFGQV--AKCLDHKNN---ELVALKIIRNKKRFHQQ-ALM-ELKILE-------------ALRKKDKD- 276
Cdd:cd05054     8 RLKLGKPLGRGAFGKViqASAFGIDKSatcRTVAVKMLKEGATASEHkALMtELKILIhighhlnvvnllgACTKPGGPl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 277 ------------NTYNVVHMKDFFYFRNHFCITFELlGINLYELMKnnnfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHC 344
Cdd:cd05054    88 mvivefckfgnlSNYLRSKREEFVPYRDKGARDVEE-EEDDDELYK----EPLTLEDLICYSFQVARGMEFLASRKCIHR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 345 DLKPENIVLYQKGqaSVKVIDFGSScyehQKVYT---YIQSRFYR------SPEVILGHPYDVAIDMWSLGCITAELYT- 414
Cdd:cd05054   163 DLAARNILLSENN--VVKICDFGLA----RDIYKdpdYVRKGDARlplkwmAPESIFDKVYTTQSDVWSFGVLLWEIFSl 236

                  ....*..
gi 2032329476 415 GYPLFPG 421
Cdd:cd05054   237 GASPYPG 243
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
311-465 1.41e-04

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: 44.18  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 311 NNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENiVLYQKGQaSVKVIDFGSS--CYEHQKVYTYIQSRF---Y 385
Cdd:cd05045   118 NPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARN-VLVAEGR-KMKISDFGLSrdVYEEDSYVKRSKGRIpvkW 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 386 RSPEVILGHPYDVAIDMWSLGCITAELYT----GYPLFPGENEVEQLA----------CIMEVLGLPPAGFIQTASRRQT 451
Cdd:cd05045   196 MAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnPYPGIAPERLFNLLKtgyrmerpenCSEEMYNLMLTCWKQEPDKRPT 275
                         170
                  ....*....|....*
gi 2032329476 452 FFD-SKGFPKNITNN 465
Cdd:cd05045   276 FADiSKELEKMMVKS 290
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
225-428 1.82e-04

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: 43.75  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNElVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFyfrnhfcITFELLGI- 303
Cdd:cd14203     3 LGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIY-------IVTEFMSKg 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNnfQGFSLSIVRRFTLSVLKCLQMLSVEKI--IHCDLKPENIVLyqkGQASV-KVIDFGSSCYEHQKVYTYI 380
Cdd:cd14203    75 SLLDFLKDG--EGKYLKLPQLVDMAAQIASGMAYIERMnyIHRDLRAANILV---GDNLVcKIADFGLARLIEDNEYTAR 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 381 Q-SRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPGENEVEQL 428
Cdd:cd14203   150 QgAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVL 202
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
220-415 1.85e-04

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 43.88  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLDHKNnelVALKIIrNKKRFHQQALMELK-ILEALRKKDKDNTynVVHMKDFFYfRNHFCITF 298
Cdd:cd14063     3 EIKEVIGKGRFGRVHRGRWHGD---VAIKLL-NIDYLNEEQLEAFKeEVAAYKNTRHDNL--VLFMGACMD-PPHLAIVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELL-GINLYELMKNNNfQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQasVKVIDFGSScyehqKVY 377
Cdd:cd14063    76 SLCkGRTLYSLIHERK-EKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNI-FLENGR--VVITDFGLF-----SLS 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 378 TYIQSR-------------FYRSPEVI--------LGH--PYDVAIDMWSLGCITAELYTG 415
Cdd:cd14063   147 GLLQPGrredtlvipngwlCYLAPEIIralspdldFEEslPFTKASDVYAFGTVWYELLAG 207
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
328-420 2.19e-04

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: 43.55  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 328 SVLKCLQMLSVEKIIHCDLKPENIVLyQKGQASVKVIDFGSSCY---EHQKVYTYIQSRFYRSPEVILGHPY-DVAIDMW 403
Cdd:cd13974   140 DVVRVVEALHKKNIVHRDLKLGNMVL-NKRTRKITITNFCLGKHlvsEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMW 218
                          90
                  ....*....|....*...
gi 2032329476 404 SLGCItaeLYTG-YPLFP 420
Cdd:cd13974   219 ALGVV---LFTMlYGQFP 233
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
225-412 2.20e-04

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: 43.23  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIirNKKRFHQ-QALMELKILEALRKKDKDNTYNV-VHMKDFfyfrnHfCITFELLG 302
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKM--NTLSSNRaNMLREVQLMNRLSHPNILRFMGVcVHQGQL-----H-ALTEYING 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 303 INLYELMKNNNFQGFSLSIvrRFTLSVLKCLQMLSVEKIIHCDLKPEN-IVLYQKGQASVKVIDFG------SSCYEHQK 375
Cdd:cd14155    73 GNLEQLLDSNEPLSWTVRV--KLALDIARGLSYLHSKGIFHRDLTSKNcLIKRDENGYTAVVGDFGlaekipDYSDGKEK 150
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2032329476 376 VYTyIQSRFYRSPEVILGHPYDVAIDMWSLGCITAEL 412
Cdd:cd14155   151 LAV-VGSPYWMAPEVLRGEPYNEKADVFSYGIILCEI 186
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
223-426 3.06e-04

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 43.04  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKC--------LDHKNNE------LVALKIIRN--KKRFHQQALMELKILEALrkkdkdNTYNVVHMKD 286
Cdd:cd05097    11 EKLGEGQFGEVHLCeaeglaefLGEGAPEfdgqpvLVAVKMLRAdvTKTARNDFLKEIKIMSRL------KNPNIIRLLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 287 FFYFRNHFCITFELL---GINLY--------ELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyq 355
Cdd:cd05097    85 VCVSDDPLCMITEYMengDLNQFlsqreiesTFTHANNIPSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLV-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 356 KGQASVKVIDFGSSCYEHQKVYTYIQSRF-----YRSPEVILGHPYDVAIDMWSLGCITAELYT-----GYPLFPGENEV 425
Cdd:cd05097   163 GNHYTIKIADFGMSRNLYSGDYYRIQGRAvlpirWMAWESILLGKFTTASDVWAFGVTLWEMFTlckeqPYSLLSDEQVI 242

                  .
gi 2032329476 426 E 426
Cdd:cd05097   243 E 243
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
246-414 3.30e-04

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 43.16  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 246 ALKIIRNKKRFHQQALM------ELKILEALRKKdkdntyNVVHMKDFFYFRN-HFCITFELLGINLYELMKNNNFQG-- 316
Cdd:cd14001    32 AVKKINSKCDKGQRSLYqerlkeEAKILKSLNHP------NIVGFRAFTKSEDgSLCLAMEYGGKSLNDLIEERYEAGlg 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 317 -FSLSIVRRFTLSVLKCLQMLSVEK-IIHCDLKPENIVLyqKGQ-ASVKVIDFGSS--------CYEHQKVYtYIQSRFY 385
Cdd:cd14001   106 pFPAATILKVALSIARALEYLHNEKkILHGDIKSGNVLI--KGDfESVKLCDFGVSlpltenleVDSDPKAQ-YVGTEPW 182
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2032329476 386 RSPEVILGhpyDVAI----DMWSLGCITAELYT 414
Cdd:cd14001   183 KAKEALEE---GGVItdkaDIFAYGLVLWEMMT 212
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
216-356 3.32e-04

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 43.09  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 216 AYRYEVLETIGKGSFGQVAKCLDHKNNELVALKiiRNKKRF-----HQQALMELKILEALRKKDK-DNTYNVVHMKDFFY 289
Cdd:cd14138     4 ATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIK--RSKKPLagsvdEQNALREVYAHAVLGQHSHvVRYYSAWAEDDHML 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 290 FRNHFCItfellGINLYELMKNNN--FQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQK 356
Cdd:cd14138    82 IQNEYCN-----GGSLADAISENYriMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRT 145
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
341-421 3.85e-04

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: 42.71  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 341 IIHCDLKPENIVLYQKGQA------SVKVIDFGSSCYEHQKVYTYIQSRF-YRSPEVILGHPYDVAIDMWSLGCITAELY 413
Cdd:cd14147   125 VIHRDLKSNNILLLQPIENddmehkTLKITDFGLAREWHKTTQMSAAGTYaWMAPEVIKASTFSKGSDVWSFGVLLWELL 204

                  ....*...
gi 2032329476 414 TGYPLFPG 421
Cdd:cd14147   205 TGEVPYRG 212
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
225-426 5.28e-04

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: 42.32  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNElVALKIIRNKKRFHQQALMELKILEALrKKDKDNTYNVVHMKDFFYFRNHFCITFELLgin 304
Cdd:cd05073    19 LGAGQFGEVWMATYNKHTK-VAVKTMKPGSMSVEAFLAEANVMKTL-QHDKLVKLHAVVTKEPIYIITEFMAKGSLL--- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 305 lyELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqKGQASVKVIDFGSSCYEHQKVYTYIQ-SR 383
Cdd:cd05073    94 --DFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILV--SASLVCKIADFGLARVIEDNEYTAREgAK 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2032329476 384 F---YRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPGENEVE 426
Cdd:cd05073   170 FpikWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPE 216
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
219-419 5.89e-04

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: 42.71  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRnKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITF 298
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVK-KELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 299 ELlgINLYELMKNNNFQGFSLSIVRRFTLSVLK-CLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYEH---- 373
Cdd:cd05618   101 EY--VNGGDLMFHMQRQRKLPEEHARFYSAEISlALNYLHERGIIYRDLKLDNVLLDSEGH--IKLTDYGM-CKEGlrpg 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 374 QKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLF 419
Cdd:cd05618   176 DTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
225-444 6.04e-04

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 41.90  E-value: 6.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLdhKNNELVALKIIRNKKR-----FHQQALMELKILEALRKKdkdntyNVVHMKDFFYFRNHFCITFE 299
Cdd:cd14148     2 IGVGGFGKVYKGL--WRGEEVAVKAARQDPDediavTAENVRQEARLFWMLQHP------NIIALRGVCLNPPHLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LL-GINLYELMKNNNFQGfslSIVRRFTLSVLKCLQMLSVEK---IIHCDLKPENIVLYQKGQ------ASVKVIDFGSS 369
Cdd:cd14148    74 YArGGALNRALAGKKVPP---HVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPIEnddlsgKTLKITDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 370 CYEHQKVYTYIQSRF-YRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFpgeNEVEQLA----CIMEVLGLP-----P 439
Cdd:cd14148   151 REWHKTTKMSAAGTYaWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY---REIDALAvaygVAMNKLTLPipstcP 227

                  ....*
gi 2032329476 440 AGFIQ 444
Cdd:cd14148   228 EPFAR 232
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
222-351 6.30e-04

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 42.01  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKiiRNKK-----RFHQQALMELKILEALRKKDkdntyNVV----------HMkd 286
Cdd:cd14051     5 VEKIGSGEFGSVYKCINRLDGCVYAIK--KSKKpvagsVDEQNALNEVYAHAVLGKHP-----HVVryysawaeddHM-- 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 287 ffYFRNHFCItfellGINLYELMKNNNFQG--FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENI 351
Cdd:cd14051    76 --IIQNEYCN-----GGSLADAISENEKAGerFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNI 135
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
219-367 7.89e-04

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 42.03  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 219 YEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALmELKILEALRKKDKdntynvvhMKDFFYF---RNHFC 295
Cdd:cd14126     2 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHL-EYRFYKLLGQAEG--------LPQVYYFgpcGKYNA 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 296 ITFELLGINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVL---YQKGQASVKVIDFG 367
Cdd:cd14126    73 MVLELLGPSLEDLFDLCDRT-FSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIgrqSTKKQHVIHIIDFG 146
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
322-418 8.14e-04

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: 41.76  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 322 VRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAID 401
Cdd:cd05576   115 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGH--IQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETEACD 192
                          90
                  ....*....|....*..
gi 2032329476 402 MWSLGCITAELYTGYPL 418
Cdd:cd05576   193 WWSLGALLFELLTGKAL 209
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
225-415 8.42e-04

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: 41.61  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNnelVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNV--VHMKDFFYFRNHFCitfelLG 302
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFmgYMTKPQLAIVTQWC-----EG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 303 INLYEL--MKNNNFQGFSLSIVRRftlSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFG--------SSCYE 372
Cdd:cd14062    73 SSLYKHlhVLETKFEMLQLIDIAR---QTAQGMDYLHAKNIIHRDLKSNNIFLHEDL--TVKIGDFGlatvktrwSGSQQ 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 373 HQKVYTYIqsrFYRSPEVIL---GHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd14062   148 FEQPTGSI---LWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLTG 190
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
333-419 1.08e-03

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: 41.64  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 333 LQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSsCYEHQK----VYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCI 408
Cdd:cd05588   109 LNFLHEKGIIYRDLKLDNVLLDSEGH--IKLTDYGM-CKEGLRpgdtTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVL 185
                          90
                  ....*....|.
gi 2032329476 409 TAELYTGYPLF 419
Cdd:cd05588   186 MFEMLAGRSPF 196
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
225-421 1.11e-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: 41.21  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNElVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFyfrnhfcITFELLGI- 303
Cdd:cd05069    20 LGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIY-------IVTEFMGKg 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFGSSCYEHQKVYTYIQ-S 382
Cdd:cd05069    92 SLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGD--NLVCKIADFGLARLIEDNEYTARQgA 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2032329476 383 RF---YRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPG 421
Cdd:cd05069   170 KFpikWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPG 212
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
223-421 1.29e-03

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 41.14  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKClDHKNNELVALKIIrnKKRFHQQalMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELL- 301
Cdd:cd05085     2 ELLGKGNFGEVYKG-TLKDKTPVAVKTC--KEDLPQE--LKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVp 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 GINLYELMKNNNFQgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqkGQASV-KVIDFGSSCYEHQKVYTYI 380
Cdd:cd05085    77 GGDFLSFLRKKKDE-LKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLV---GENNAlKISDFGMSRQEDDGVYSSS 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2032329476 381 QSR----FYRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPG 421
Cdd:cd05085   153 GLKqipiKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPG 198
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
222-365 1.37e-03

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 41.07  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGQVAKCLDHKNNELVALKiiRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELL 301
Cdd:cd14139     5 LEKIGVGEFGSVYKCIKRLDGCVYAIK--RSMRPFAGSSNEQLALHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYC 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 302 -GINLYELMKNNNFQG--FSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVID 365
Cdd:cd14139    83 nGGSLQDAISENTKSGnhFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKMQSSSGVGE 149
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
222-429 1.40e-03

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: 40.89  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 222 LETIGKGSFGqVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMkdffyfRNHFCITFELL 301
Cdd:cd05059     9 LKELGSGQFG-VVHLGKWRGKIDVAIKMIKEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTK------QRPIFIVTEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 302 --GINLYELMKNNNFqgFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCYEHQKVYTY 379
Cdd:cd05059    82 anGCLLNYLRERRGK--FQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQN--VVKVSDFGLARYVLDDEYTS 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032329476 380 IQ-SRF---YRSPEVILGHPYDVAIDMWSLGCITAELYTG----YPLFPGENEVEQLA 429
Cdd:cd05059   158 SVgTKFpvkWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEgkmpYERFSNSEVVEHIS 215
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
325-420 1.41e-03

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: 41.53  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 325 FTLSVLKCLQMLSVEKIIHCDLKPENiVLYQKGQAsVKVIDFG-SSCYEHQKVYTYIQSRF----YRSPEVILGHPYDVA 399
Cdd:cd05107   244 FSYQVANGMEFLASKNCVHRDLAARN-VLICEGKL-VKICDFGlARDIMRDSNYISKGSTFlplkWMAPESIFNNLYTTL 321
                          90       100
                  ....*....|....*....|....*
gi 2032329476 400 IDMWSLGCITAELY----TGYPLFP 420
Cdd:cd05107   322 SDVWSFGILLWEIFtlggTPYPELP 346
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
316-415 1.59e-03

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: 40.71  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 316 GFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIV---LYQKGQASVKVIDFGSSCY-EHQKVYTYIQSRFYRSPEVI 391
Cdd:cd14068    82 SLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLlftLYPNCAIIAKIADYGIAQYcCRMGIKTSEGTPGFRAPEVA 161
                          90       100
                  ....*....|....*....|....*
gi 2032329476 392 LGH-PYDVAIDMWSLGCITAELYTG 415
Cdd:cd14068   162 RGNvIYNQQADVYSFGLLLYDILTC 186
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
321-369 1.82e-03

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 41.32  E-value: 1.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2032329476 321 IVRRFTLSVLKCLQMLSVEKIIHCDLKPENIvLYQKGQASVKVIDFGSS 369
Cdd:PLN03225  256 IIQTIMRQILFALDGLHSTGIVHRDVKPQNI-IFSEGSGSFKIIDLGAA 303
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
325-421 1.83e-03

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: 40.73  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 325 FTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSScyehQKVYT---YIQSRFYR------SPEVILGHP 395
Cdd:cd05102   177 YSFQVARGMEFLASRKCIHRDLAARNILLSENN--VVKICDFGLA----RDIYKdpdYVRKGSARlplkwmAPESIFDKV 250
                          90       100
                  ....*....|....*....|....*..
gi 2032329476 396 YDVAIDMWSLGCITAELYT-GYPLFPG 421
Cdd:cd05102   251 YTTQSDVWSFGVLLWEIFSlGASPYPG 277
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
220-421 2.21e-03

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 40.26  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKCLdHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFyfrnhfCITFE 299
Cdd:cd05067    10 KLVERLGAGQFGEVWMGY-YNGHTKVAIKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIY------IITEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 300 LLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFGSSCYEHQKVYTY 379
Cdd:cd05067    83 MENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSD--TLSCKIADFGLARLIEDNEYTA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2032329476 380 IQ-SRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPG 421
Cdd:cd05067   161 REgAKFpikWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPG 207
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
225-415 2.26e-03

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


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 40.17  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKcLDHKNNELVALK-IIRNKKRFHQQAL-MELKILEALRKKdkdntyNVVHMKDffYFRNHfciTFELLg 302
Cdd:cd14664     1 IGRGGAGTVYK-GVMPNGTLVAVKrLKGEGTQGGDHGFqAEIQTLGMIRHR------NIVRLRG--YCSNP---TTNLL- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 303 inLYELMKNNNFQGF---------SLSIVRRFTLSV-----LKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKviDFGS 368
Cdd:cd14664    68 --VYEYMPNGSLGELlhsrpesqpPLDWETRQRIALgsargLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVA--DFGL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2032329476 369 S---CYEHQKVYTYIQSRF-YRSPEVILGHPYDVAIDMWSLGCITAELYTG 415
Cdd:cd14664   144 AklmDDKDSHVMSSVAGSYgYIAPEYAYTGKVSEKSDVYSYGVVLLELITG 194
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
333-420 2.56e-03

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 40.05  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 333 LQMLSVEKIIHCDLKPENIVLYQKGQasVKVIDFGSS--CYEHQkvYTYIQSRF-----YRSPEVILGHPYDVAIDMWSL 405
Cdd:cd05048   137 MEYLSSHHYVHRDLAARNCLVGDGLT--VKISDFGLSrdIYSSD--YYRVQSKSllpvrWMPPEAILYGKFTTESDVWSF 212
                          90
                  ....*....|....*
gi 2032329476 406 GCITAELYTgYPLFP 420
Cdd:cd05048   213 GVVLWEIFS-YGLQP 226
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
218-421 2.80e-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: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 218 RYEVleTIGKGSFGQVAKCLDHKNNElVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFyfrnhfCIT 297
Cdd:cd05071    12 RLEV--KLGQGCFGEVWMGTWNGTTR-VAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIY------IVT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 298 FELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLyqkGQASV-KVIDFGSSCYEHQKV 376
Cdd:cd05071    83 EYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILV---GENLVcKVADFGLARLIEDNE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2032329476 377 YTYIQ-SRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT-GYPLFPG 421
Cdd:cd05071   160 YTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPG 209
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
225-446 4.35e-03

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 39.65  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKK-------RFHQQALMelkiLEALRKKdkdntyNVVHMKDFF--YFRNHFC 295
Cdd:cd14030    33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKlskserqRFKEEAGM----LKGLQHP------NIVRFYDSWesTVKGKKC 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 296 ITFellginLYELMKNNN-------FQGFSLSIVRRFTLSVLKCLQMLSVEK--IIHCDLKPENIVLyQKGQASVKVIDF 366
Cdd:cd14030   103 IVL------VTELMTSGTlktylkrFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI-TGPTGSVKIGDL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 367 GSSCYEHQK-VYTYIQSRFYRSPEvILGHPYDVAIDMWSLGCITAELYTG-YPLFPGENEVEQLACIMEvlGLPPAGFIQ 444
Cdd:cd14030   176 GLATLKRASfAKSVIGTPEFMAPE-MYEEKYDESVDVYAFGMCMLEMATSeYPYSECQNAAQIYRRVTS--GVKPASFDK 252

                  ..
gi 2032329476 445 TA 446
Cdd:cd14030   253 VA 254
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
387-531 5.44e-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: 39.54  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 387 SPEVILGH--PYDVAIDMWSLGCITAELYTGYPLFPG----ENEVEQLA----CIMEVLGLPPAGFIQTASRRQTffdSK 456
Cdd:cd08227   176 SPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFKDmpatQMLLEKLNgtvpCLLDTTTIPAEELTMKPSRSGA---NS 252
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032329476 457 GFPKNITNNRGKKRYPDSKdLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPRPQTLR 531
Cdd:cd08227   253 GLGESTTVSTPRPSNGESS-SHPYNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLR 326
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
225-429 5.99e-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: 38.80  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNElVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFrnhfcITfellgin 304
Cdd:cd05034     3 LGAGQFGEVWMGVWNGTTK-VAVKTLKPGTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYI-----VT------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 305 lyELMKNNNFQGFsLSIVRRFTLSVLKCLQM----------LSVEKIIHCDLKPENIVLYQKGqaSVKVIDFGSSCYEHQ 374
Cdd:cd05034    70 --ELMSKGSLLDY-LRTGEGRALRLPQLIDMaaqiasgmayLESRNYIHRDLAARNILVGENN--VCKVADFGLARLIED 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032329476 375 KVYTYIQ-SRF---YRSPEVILGHPYDVAIDMWSLGCITAELYT-G---YPLFPGENEVEQLA 429
Cdd:cd05034   145 DEYTAREgAKFpikWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGrvpYPGMTNREVLEQVE 207
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
220-420 6.34e-03

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 39.04  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 220 EVLETIGKGSFGQVAKC-----LDHKNNELVALKIIRNKKRFHQQALMELkilEALRKKDKDNTyNVVHMKDFFYFRNHF 294
Cdd:cd05050     8 EYVRDIGQGAFGRVFQArapglLPYEPFTMVAVKMLKEEASADMQADFQR---EAALMAEFDHP-NIVKLLGVCAVGKPM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 295 CITFELLGI-NLYELMKNN----------NFQGFSLSIVRRFTLSVLKCLQM----------LSVEKIIHCDLKPENIVL 353
Cdd:cd05050    84 CLLFEYMAYgDLNEFLRHRspraqcslshSTSSARKCGLNPLPLSCTEQLCIakqvaagmayLSERKFVHRDLATRNCLV 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032329476 354 yqKGQASVKVIDFGSScyehQKVYTyiqSRFYRS------------PEVILGHPYDVAIDMWSLGCITAELYTgYPLFP 420
Cdd:cd05050   164 --GENMVVKIADFGLS----RNIYS---ADYYKAsendaipirwmpPESIFYNRYTTESDVWAYGVVLWEIFS-YGMQP 232
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
214-431 7.67e-03

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 38.60  E-value: 7.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 214 HIAYRYEVL-ETIGKGSFGQV--AKC---LDHKNNELVALKIIRN------KKRFHQQAlmelKILEALRKKDKDNTYNV 281
Cdd:cd05049     1 HIKRDTIVLkRELGEGAFGKVflGECynlEPEQDKMLVAVKTLKDasspdaRKDFEREA----ELLTNLQHENIVKFYGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 282 VHMKDFFYfrnhfcITFELL---GINLY--------ELMKNNNFQGFSLSIVRRFTLSVLKCLQM--LSVEKIIHCDLKP 348
Cdd:cd05049    77 CTEGDPLL------MVFEYMehgDLNKFlrshgpdaAFLASEDSAPGELTLSQLLHIAVQIASGMvyLASQHFVHRDLAT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 349 ENIVLYQKgqASVKVIDFGSScyehQKVYTyiqSRFYR------------SPEVILGHPYDVAIDMWSLGCITAELYT-- 414
Cdd:cd05049   151 RNCLVGTN--LVVKIGDFGMS----RDIYS---TDYYRvgghtmlpirwmPPESILYRKFTTESDVWSFGVVLWEIFTyg 221
                         250
                  ....*....|....*..
gi 2032329476 415 GYPLFPGENEvEQLACI 431
Cdd:cd05049   222 KQPWFQLSNT-EVIECI 237
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
225-420 8.26e-03

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 38.65  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 225 IGKGSFGQVAKCLDHKNNELVALKIIRNKkrfhqqaLMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELL-GI 303
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKND-------VDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVsGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 304 NLYELMKNnnfQGFSLSIVRRFTLS--VLKCLQMLSVEKIIHCDLKPENIVLYQK--GQASVkVIDFGSS-------CYE 372
Cdd:cd14156    74 CLEELLAR---EELPLSWREKVELAcdISRGMVYLHSKNIYHRDLNSKNCLIRVTprGREAV-VTDFGLArevgempAND 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2032329476 373 HQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFP 420
Cdd:cd14156   150 PERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPADP 197
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
223-436 9.34e-03

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: 38.50  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 223 ETIGKGSFGQVAKCLDHKNnelVALKIIRNKKRFHQQALMELKILEALRKKdkdNTYNVVHMKDFFYFRNHFCITFELLG 302
Cdd:cd14151    14 QRIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKT---RHVNILLFMGYSTKPQLAIVTQWCEG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032329476 303 INLYELMK--NNNFQGFSLSIVRRFTLsvlKCLQMLSVEKIIHCDLKPENIVLYQkgQASVKVIDFG--------SSCYE 372
Cdd:cd14151    88 SSLYHHLHiiETKFEMIKLIDIARQTA---QGMDYLHAKSIIHRDLKSNNIFLHE--DLTVKIGDFGlatvksrwSGSHQ 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032329476 373 HQKVYTYIqsrFYRSPEVIL---GHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQlacIMEVLG 436
Cdd:cd14151   163 FEQLSGSI---LWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ---IIFMVG 223
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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