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Conserved domains on  [gi|1178431733|ref|NP_001337269|]
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serine/threonine-protein kinase LATS1 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
598-979 0e+00

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: 806.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd05625      1 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 757
Cdd:cd05625     81 DYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05625    161 QSGDHLRQDSMDFSNEWGDPENCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQ 917
Cdd:cd05625    241 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQ 320
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  918 SASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTLNGWYKNGKHPEHAFYEFTFRRFF 979
Cdd:cd05625    321 SAPYIPKITHPTDTSNFDPVDPDKLWSDDDKEGNVNDTLNGWYKNGKHPEHAFYEFTFRRFF 382
MobB_LATS1 cd21778
Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; ...
524-599 9.91e-51

Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; LATS1, also called WARTS protein kinase, is a serine/threonine-protein kinase that 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. LATS1 belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. LATS proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of LATS1 serine/threonine protein kinase and similar proteins.


:

Pssm-ID: 439273  Cd Length: 76  Bit Score: 172.68  E-value: 9.91e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  524 SRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMDKSM 599
Cdd:cd21778      1 SRVQSYSPQAFKFFMEQHVENVLKSHQQRLHRRKQLENEMAKVGLSEEAQDQMRKMLCQKESNYIRLKRAKMDKSM 76
UBA_like_SF super family cl21463
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ...
11-38 1.50e-12

UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.


The actual alignment was detected with superfamily member cd14397:

Pssm-ID: 473871  Cd Length: 41  Bit Score: 62.74  E-value: 1.50e-12
                           10        20
                   ....*....|....*....|....*...
gi 1178431733   11 QDMVIQALQKTNNRSIEAAIEFISKMSY 38
Cdd:cd14397     14 EDMVIQALQQTNNRSIEAAIEFISKMSY 41
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
343-491 3.18e-04

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.08  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  343 GHEIPTWQPNI---PVRSNSFNNPLGNRASHSANSQPSATTVTAITPAPIQQPV--KSMRVLKPELQTALAPTHPSWIPQ 417
Cdd:PRK10263   348 SVDVPPAQPTVawqPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVqpQQPYYAPAAEQPAQQPYYAPAPEQ 427
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  418 PIQTVQPSPFPEGTASNVTVMPPVAEAPnYQgPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKS 491
Cdd:PRK10263   428 PAQQPYYAPAPEQPVAGNAWQAEEQQST-FA-PQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEET 499
 
Name Accession Description Interval E-value
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
598-979 0e+00

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: 806.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd05625      1 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 757
Cdd:cd05625     81 DYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05625    161 QSGDHLRQDSMDFSNEWGDPENCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQ 917
Cdd:cd05625    241 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQ 320
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  918 SASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTLNGWYKNGKHPEHAFYEFTFRRFF 979
Cdd:cd05625    321 SAPYIPKITHPTDTSNFDPVDPDKLWSDDDKEGNVNDTLNGWYKNGKHPEHAFYEFTFRRFF 382
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
600-905 1.05e-95

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 303.30  E-value: 1.05e-95
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvlLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHdskyyqs 759
Cdd:smart00220   79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE------- 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   760 gdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:smart00220  152 -----------------------------------------KLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELL 190
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733   840 VGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:smart00220  191 TGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKlLVKDPEKRL---TAEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
605-941 3.11e-65

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 223.16  E-value: 3.11e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  605 TLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:PTZ00263    25 TLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgdhpr 764
Cdd:PTZ00263   105 LFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGF-------------------- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  765 qdsmdfsnewgdpsscrcgdrlkplerrAARQHQRclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPP 844
Cdd:PTZ00263   165 ----------------------------AKKVPDR--TFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPP 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  845 FLAQTPLETQMKVI-------NWqtslhippqakLSPEASDLIIKLCR-GPEDRLG--KNGADEIKAHPFFKTIDFSSDL 914
Cdd:PTZ00263   215 FFDDTPFRIYEKILagrlkfpNW-----------FDGRARDLVKGLLQtDHTKRLGtlKGGVADVKNHPYFHGANWDKLY 283
                          330       340       350
                   ....*....|....*....|....*....|
gi 1178431733  915 RQQSASYIP-KITHPTDTSNFD--PVDPDK 941
Cdd:PTZ00263   284 ARYYPAPIPvRVKSPGDTSNFEkyPDSPVD 313
MobB_LATS1 cd21778
Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; ...
524-599 9.91e-51

Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; LATS1, also called WARTS protein kinase, is a serine/threonine-protein kinase that 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. LATS1 belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. LATS proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of LATS1 serine/threonine protein kinase and similar proteins.


Pssm-ID: 439273  Cd Length: 76  Bit Score: 172.68  E-value: 9.91e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  524 SRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMDKSM 599
Cdd:cd21778      1 SRVQSYSPQAFKFFMEQHVENVLKSHQQRLHRRKQLENEMAKVGLSEEAQDQMRKMLCQKESNYIRLKRAKMDKSM 76
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
603-890 4.06e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 184.83  E-value: 4.06e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:COG0515     12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdh 762
Cdd:COG0515     92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIA----------------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:COG0515    155 -----------------------------RALGGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGR 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1178431733  843 PPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDR 890
Cdd:COG0515    206 PPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRaLAKDPEER 254
Pkinase pfam00069
Protein kinase domain;
600-905 5.33e-49

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 173.20  E-value: 5.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQvAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMgfihrdikpdnilidrdghikltdfglctgfrwthdskyyqs 759
Cdd:pfam00069   80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLESGSSL------------------------------------------ 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:pfam00069  118 -------------------------------------------TTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELL 154
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  840 VGQPPFLAQTPLETQMKVINwQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:pfam00069  155 TGKPPFPGINGNEIYELIID-QPYAFPELPSNLSEEAKDLLKKlLKKDPSKRL---TATQALQHPWF 217
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
660-890 7.44e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 91.40  E-value: 7.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  660 VVRLYYSFQDKDNLYFVMDYIPGgdmMSL--LIRMG--IFPESLARfYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG 735
Cdd:NF033483    69 IVSVYDVGEDGGIPYIVMEYVDG---RTLkdYIREHgpLSPEEAVE-IMIQILSALEHAHRNGIVHRDIKPQNILITKDG 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  736 HIKLTDFGLCtgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerRAARQHQRCLAHSLVGTPNYIAPE 815
Cdd:NF033483   145 RVKVTDFGIA----------------------------------------------RALSSTTMTQTNSVLGTVHYLSPE 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  816 ------VLLRTgytqlcDWWSVGVILFEMLVGQPPFLAQTPLETQMKvinwqtslHI-----PPQA---KLSPEASDLII 881
Cdd:NF033483   179 qarggtVDARS------DIYSLGIVLYEMLTGRPPFDGDSPVSVAYK--------HVqedppPPSElnpGIPQSLDAVVL 244
                          250
                   ....*....|
gi 1178431733  882 K-LCRGPEDR 890
Cdd:NF033483   245 KaTAKDPDDR 254
UBA_LATS1 cd14397
UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large ...
11-38 1.50e-12

UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large tumor suppressor homolog 1 or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. It plays a crucial role in the prevention of tumor formation by controlling mitosis progression. Human LATS1 is the mammalian homologs of Drosophila lats/warts gene that could suppress tumor growth and rescue all developmental defects in flies, including embryonic lethality. It forms a regulatory complex with zyxin, a regulator of actin filament assembly. The LATS1/zyxin complex plays a role in controlling mitosis progression on mitotic apparatus. LATS1 is phosphorylated in a cell-cycle-dependent manner and complexes with CDC2 in early mitosis. It can negatively modulates tumor cell growth by inducing G(2)/M cell cycle transition or apoptosis. It also functions as a mitotic exit network kinase interacting with MOB1A, a protein whose homolog in budding yeast associates with kinases involved in mitotic exit. Moreover, LATS1 acts as a novel cytoskeleton regulator that affects cytokinesis by regulating actin polymerization through inhibiting LIMK1. LATS1 can also inhibit transcription regulation and transformation functions of oncogene YAP by inhibiting its nuclear translocation through phosphorylation. In addition, LATS1 can regulate the transcriptional activity of forkhead L2 (FOXL2) via phosphorylation. It also acts as an acting-binding protein that can negatively regulate the actin polymerization. LATS1 contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


Pssm-ID: 270580  Cd Length: 41  Bit Score: 62.74  E-value: 1.50e-12
                           10        20
                   ....*....|....*....|....*...
gi 1178431733   11 QDMVIQALQKTNNRSIEAAIEFISKMSY 38
Cdd:cd14397     14 EDMVIQALQQTNNRSIEAAIEFISKMSY 41
PRK10263 PRK10263
DNA translocase FtsK; Provisional
343-491 3.18e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.08  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  343 GHEIPTWQPNI---PVRSNSFNNPLGNRASHSANSQPSATTVTAITPAPIQQPV--KSMRVLKPELQTALAPTHPSWIPQ 417
Cdd:PRK10263   348 SVDVPPAQPTVawqPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVqpQQPYYAPAAEQPAQQPYYAPAPEQ 427
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  418 PIQTVQPSPFPEGTASNVTVMPPVAEAPnYQgPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKS 491
Cdd:PRK10263   428 PAQQPYYAPAPEQPVAGNAWQAEEQQST-FA-PQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEET 499
 
Name Accession Description Interval E-value
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
598-979 0e+00

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: 806.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd05625      1 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 757
Cdd:cd05625     81 DYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05625    161 QSGDHLRQDSMDFSNEWGDPENCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQ 917
Cdd:cd05625    241 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQ 320
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  918 SASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTLNGWYKNGKHPEHAFYEFTFRRFF 979
Cdd:cd05625    321 SAPYIPKITHPTDTSNFDPVDPDKLWSDDDKEGNVNDTLNGWYKNGKHPEHAFYEFTFRRFF 382
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
598-979 0e+00

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: 736.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd05598      1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 757
Cdd:cd05598     81 DYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05598    161 L-------------------------------------------AHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYE 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSdLRQQ 917
Cdd:cd05598    198 MLVGQPPFLAQTPAETQLKVINWRTTLKIPHEANLSPEAKDLILRLCCDAEDRLGRNGADEIKAHPFFAGIDWEK-LRKQ 276
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  918 SASYIPKITHPTDTSNFDPVDPDKLWSDDNEeenvnDTLNGWYKNGKHPEHAFYEFTFRRFF 979
Cdd:cd05598    277 KAPYIPTIRHPTDTSNFDPVDPEKLRSSDEE-----PTTPNDPDNGKHPEHAFYEFTFRRFF 333
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
598-979 0e+00

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 707.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd05626      1 SMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 757
Cdd:cd05626     81 DYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWTHNSKYY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05626    161 QKGSHIRQDSMEPSDLWDDVSNCRCGDRLKTLEQRATKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQ 917
Cdd:cd05626    241 MLVGQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCSAEERLGRNGADDIKAHPFFSEVDFSSDIRTQ 320
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  918 SASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVN-DTLNGwyKNGKHPEHAFYEFTFRRFF 979
Cdd:cd05626    321 PAPYVPKISHPMDTSNFDPVEEESPWNDASGDSTRTwDTLCS--PNGKHPEHAFYEFTFRRFF 381
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
598-976 0e+00

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: 579.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd05573      1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 757
Cdd:cd05573     81 EYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGDRESY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDHPRQdsmdfsnewgdpsscrcgDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05573    161 LNDSVNTL------------------FQDNVLARRRPHKQRRVRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYE 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKngADEIKAHPFFKTIDFsSDLRQQ 917
Cdd:cd05573    223 MLYGFPPFYSDSLVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLLCDPEDRLGS--AEEIKAHPFFKGIDW-ENLRES 299
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  918 SASYIPKITHPTDTSNFDPVDPDKLWSDDNEeenvndtlNGWYKNGKHPEHAFYEFTFR 976
Cdd:cd05573    300 PPPFVPELSSPTDTSNFDDFEDDLLLSEYLS--------NGSPLLGKGKQLAFVGFTFK 350
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
600-952 3.13e-164

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: 485.20  E-value: 3.13e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05599      3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHdskyyqs 759
Cdd:cd05599     83 LPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSH------- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd05599    156 -----------------------------------------LAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEML 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSdLRQQSA 919
Cdd:cd05599    195 IGYPPFCSDDPQETCRKIMNWRETLVFPPEVPISPEAKDLIERLLCDAEHRLGANGVEEIKSHPFFKGVDWDH-IRERPA 273
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1178431733  920 SYIPKITHPTDTSNFDPVDPDKLWSDDNEEENV 952
Cdd:cd05599    274 PILPEVKSILDTSNFDEFEEVDLQIPSSPEAGK 306
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
600-978 2.54e-136

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: 415.02  E-value: 2.54e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05629      3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIMEF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYQ- 758
Cdd:cd05629     83 LPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFHKQHDSAYYQk 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 --SGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARqhqRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd05629    163 llQGKSNKNRIDNRNSVAVDSINLTMSSKDQIATWKKNR---RLMAYSTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSdLRQ 916
Cdd:cd05629    240 ECLIGWPPFCSENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLITNAENRLGRGGAHEIKSHPFFRGVDWDT-IRQ 318
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  917 QSASYIPKITHPTDTSNFdPVdpdklwsdDNEEENVNDTLNGWYKNGKHPEH-----AFYEFTFRRF 978
Cdd:cd05629    319 IRAPFIPQLKSITDTSYF-PT--------DELEQVPEAPALKQAAPAQQEESveldlAFIGYTYKRF 376
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
600-978 9.23e-116

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: 360.91  E-value: 9.23e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05627      4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYQS 759
Cdd:cd05627     84 LPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYRN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 GDHPRQDSMDFSNEwgdpSSCRCGDRLKplerraarQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd05627    164 LTHNPPSDFSFQNM----NSKRKAETWK--------KNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEML 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSdLRQQSA 919
Cdd:cd05627    232 IGYPPFCSETPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFCTDAENRIGSNGVEEIKSHPFFEGVDWEH-IRERPA 310
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  920 SYIPKITHPTDTSNFDpvdpdklwsDDNEEENVNDTLNGWYKNGKHPEHAFYEFTFRRF 978
Cdd:cd05627    311 AIPIEIKSIDDTSNFD---------DFPESDILQPAPNTTEPDYKSKDWVFLNYTYKRF 360
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
588-976 2.37e-114

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: 357.80  E-value: 2.37e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  588 IRLKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSF 667
Cdd:cd05600      1 LRKRRTRLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  668 QDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTG 747
Cdd:cd05600     81 QDPENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 -FRWTHDSKYYQSGDHPRQDSMdfsnewgdpsscrcgDRLKPLERR----AARQHQRCLAHSLVGTPNYIAPEVLLRTGY 822
Cdd:cd05600    161 tLSPKKIESMKIRLEEVKNTAF---------------LELTAKERRniyrAMRKEDQNYANSVVGSPDYMAPEVLRGEGY 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  823 TQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIP------PQAKLSPEASDLIIKLCRGPEDRLGknGA 896
Cdd:cd05600    226 DLTVDYWSLGCILFECLVGFPPFSGSTPNETWANLYHWKKTLQRPvytdpdLEFNLSDEAWDLITKLITDPQDRLQ--SP 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  897 DEIKAHPFFKTIDFSSdLRQQS-ASYIPKITHPTDTSNFD----PVDPDKLW-SDDNEEENVNDTLNGWYKNGKhpeHAF 970
Cdd:cd05600    304 EQIKNHPFFKNIDWDR-LREGSkPPFIPELESEIDTSYFDdfndEADMAKYKdVHEKQKSLEGSGKNGGDNGNR---SLF 379

                   ....*.
gi 1178431733  971 YEFTFR 976
Cdd:cd05600    380 VGFTFR 385
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
606-905 3.16e-113

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: 349.51  E-value: 3.16e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd05123      1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdhprq 765
Cdd:cd05123     81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLA-------------------- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  766 dsmdfsnewgdpsscrcgdrlKPLERRAARqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd05123    141 ---------------------KELSSDGDR------TYTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPF 193
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  846 LAQTPLETQMKVINWQtsLHIPPqaKLSPEASDLIIK-LCRGPEDRLGKNGADEIKAHPFF 905
Cdd:cd05123    194 YAENRKEIYEKILKSP--LKFPE--YVSPEAKSLISGlLQKDPTKRLGSGGAEEIKAHPFF 250
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
600-978 1.48e-111

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: 350.11  E-value: 1.48e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05628      3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYQS 759
Cdd:cd05628     83 LPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 GDHPRQDSMDFSNEwgdpSSCRCGDRLKplerraarQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd05628    163 LNHSLPSDFTFQNM----NSKRKAETWK--------RNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEML 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSdLRQQSA 919
Cdd:cd05628    231 IGYPPFCSETPQETYKKVMNWKETLIFPPEVPISEKAKDLILRFCCEWEHRIGAPGVEEIKTNPFFEGVDWEH-IRERPA 309
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  920 SYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTlngwykNGKHPEHAFYEFTFRRF 978
Cdd:cd05628    310 AIPIEIKSIDDTSNFDEFPDSDILKPSVAVSNHPET------DYKNKDWVFINYTYKRF 362
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
609-909 5.85e-110

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: 341.89  E-value: 5.85e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  609 GAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSL 688
Cdd:cd05579      4 GAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  689 LIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQSGDHPRQDSM 768
Cdd:cd05579     84 LENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGL---------SKVGLVRRQIKLSIQ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  769 DFSNEWGDPSSCRCgdrlkplerraarqhqrclahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQ 848
Cdd:cd05579    155 KKSNGAPEKEDRRI-----------------------VGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAE 211
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  849 TPLETQMKV----INWqtslhiPPQAKLSPEASDLIIKL-CRGPEDRLGKNGADEIKAHPFFKTID 909
Cdd:cd05579    212 TPEEIFQNIlngkIEW------PEDPEVSDEAKDLISKLlTPDPEKRLGAKGIEEIKNHPFFKGID 271
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
604-941 7.03e-109

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: 341.21  E-value: 7.03e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd05601      7 NVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRM-GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsgdh 762
Cdd:cd05601     87 DLLSLLSRYdDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFG------------------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerRAARQHQRCLAHSL--VGTPNYIAPEVLL------RTGYTQLCDWWSVGVI 834
Cdd:cd05601    148 -----------------------------SAAKLSSDKTVTSKmpVGTPDYIAPEVLTsmnggsKGTYGVECDWWSLGIV 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  835 LFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGadeIKAHPFFKTIDFSSdL 914
Cdd:cd05601    199 AYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDPKVSESAVDLIKGLLTDAKERLGYEG---LCCHPFFSGIDWNN-L 274
                          330       340
                   ....*....|....*....|....*..
gi 1178431733  915 RQQSASYIPKITHPTDTSNFDPVDPDK 941
Cdd:cd05601    275 RQTVPPFVPTLTSDDDTSNFDEFEPKK 301
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
600-975 3.20e-107

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: 337.01  E-value: 3.20e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05597      3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdskyyq 758
Cdd:cd05597     83 YCGGDLLTLLSKFEdRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKL---------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhpRQDSMDFSNewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVL--LRTG---YTQLCDWWSVGV 833
Cdd:cd05597    153 -----REDGTVQSS-------------------------------VAVGTPDYISPEILqaMEDGkgrYGPECDWWSLGV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  834 ILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQA-KLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSS 912
Cdd:cd05597    197 CMYEMLYGETPFYAESLVETYGKIMNHKEHFSFPDDEdDVSEEAKDLIRRLICSRERRLGQNGIDDFKKHPFFEGIDWDN 276
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  913 dLRQQSASYIPKITHPTDTSNFDPVDpdklwSDDNEEENVNDTLNGWYKnGKHpeHAFYEFTF 975
Cdd:cd05597    277 -IRDSTPPYIPEVTSPTDTSNFDVDD-----DDLRHTDSLPPPSNAAFS-GLH--LPFVGFTY 330
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
583-951 4.81e-106

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 334.73  E-value: 4.81e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  583 KESNYIRLKRAKMDKsmFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVR 662
Cdd:cd05596     13 KPVNEITKLRMNAED--FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANSEWIVQ 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  663 LYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGiFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDF 742
Cdd:cd05596     91 LHYAFQDDKYLYMVMDYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADF 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  743 GLCTgfrwthdskyyqsgdhprqdSMDfsnewgdpsscrcgdrlkplerraARQHQRClaHSLVGTPNYIAPEVLLRTG- 821
Cdd:cd05596    170 GTCM--------------------KMD------------------------KDGLVRS--DTAVGTPDYISPEVLKSQGg 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  822 ---YTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADE 898
Cdd:cd05596    204 dgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKNSLQFPDDVEISKDAKSLICAFLTDREVRLGRNGIEE 283
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  899 IKAHPFFKTIDFSSD-LRQQSASYIPKITHPTDTSNFDpvDPDKlwsDDNEEEN 951
Cdd:cd05596    284 IKAHPFFKNDQWTWDnIRETVPPVVPELSSDIDTSNFD--DIEE---DETPEET 332
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
603-935 6.35e-99

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: 313.36  E-value: 6.35e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd05580      6 LKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdh 762
Cdd:cd05580     86 GELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFA----------------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlKPLERRaarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd05580    149 ------------------------KRVKDR---------TYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGY 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  843 PPFLAQTPLETQMKVINwqTSLHIPPqaKLSPEASDLIIKLC-RGPEDRLG--KNGADEIKAHPFFKTIDFSSDL-RQQS 918
Cdd:cd05580    196 PPFFDENPMKIYEKILE--GKIRFPS--FFDPDAKDLIKRLLvVDLTKRLGnlKNGVEDIKNHPWFAGIDWDALLqRKIP 271
                          330
                   ....*....|....*..
gi 1178431733  919 ASYIPKITHPTDTSNFD 935
Cdd:cd05580    272 APYVPKVRGPGDTSNFD 288
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
600-905 1.05e-95

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 303.30  E-value: 1.05e-95
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvlLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHdskyyqs 759
Cdd:smart00220   79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE------- 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   760 gdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:smart00220  152 -----------------------------------------KLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELL 190
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733   840 VGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:smart00220  191 TGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKlLVKDPEKRL---TAEEALQHPFF 254
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
603-910 5.12e-87

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: 280.52  E-value: 5.12e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDIL-AEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd05611      1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMmIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgd 761
Cdd:cd05611     81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGL----------------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsmdfsnewgdpssCRCGdrlkpLERRAARQhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd05611    144 ------------------SRNG-----LEKRHNKK--------FVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFG 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  842 QPPFLAQTPLETQMKV----INWqtslhiPPQAK--LSPEASDLIIKL-CRGPEDRLGKNGADEIKAHPFFKTIDF 910
Cdd:cd05611    193 YPPFHAETPDAVFDNIlsrrINW------PEEVKefCSPEAVDLINRLlCMDPAKRLGANGYQEIKSHPFFKSINW 262
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
600-924 4.32e-86

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: 279.89  E-value: 4.32e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05574      3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMDY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIR--MGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyY 757
Cdd:cd05574     83 CPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLS-----------K 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDHPRQDSMDFSNEWGDPSSCRcgdrlKPLERRAARQHQRclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05574    152 QSSVTPPPVRKSLRKGSRRSSVKS-----IEKETFVAEPSAR--SNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYE 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQtsLHIPPQAKLSPEASDLIIKLC-RGPEDRLG-KNGADEIKAHPFFKTIDFSSdLR 915
Cdd:cd05574    225 MLYGTTPFKGSNRDETFSNILKKE--LTFPESPPVSSEAKDLIRKLLvKDPSKRLGsKRGASEIKRHPFFRGVNWAL-IR 301

                   ....*....
gi 1178431733  916 QQSASYIPK 924
Cdd:cd05574    302 NMTPPIIPR 310
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
604-949 5.51e-86

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: 279.87  E-value: 5.51e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNE-WVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd05570      1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRHpFLTGLHACFQTEDRLYFVMEYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqsgdh 762
Cdd:cd05570     81 GDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCK---------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfSNEWGDpsscrcgdrlkplerraarqhqrCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd05570    145 --------EGIWGG-----------------------NTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQ 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  843 PPFLAQTPLETQMKVINWQtsLHIPPqaKLSPEASDLIIK-LCRGPEDRLG--KNGADEIKAHPFFKTIDFsSDL--RQQ 917
Cdd:cd05570    194 SPFEGDDEDELFEAILNDE--VLYPR--WLSREAVSILKGlLTKDPARRLGcgPKGEADIKAHPFFRNIDW-DKLekKEV 268
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1178431733  918 SASYIPKITHPTDTSNFD-----------PVDPDKLWSDDNEE 949
Cdd:cd05570    269 EPPFKPKVKSPRDTSNFDpeftsesprltPVDSDLLTNIDQEE 311
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
590-942 1.76e-85

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: 281.90  E-value: 1.76e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  590 LKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQD 669
Cdd:cd05624     64 VKEMQLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQD 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  670 KDNLYFVMDYIPGGDMMSLLIRM-GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGF 748
Cdd:cd05624    144 ENYLYLVMDYYVGGDLLTLLSKFeDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKM 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdskyyqSGDHPRQDSMdfsnewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVL--LRTG---YT 823
Cdd:cd05624    224 ----------NDDGTVQSSV------------------------------------AVGTPDYISPEILqaMEDGmgkYG 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  824 QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQ-AKLSPEASDLIIKLCRGPEDRLGKNGADEIKAH 902
Cdd:cd05624    258 PECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHvTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKH 337
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1178431733  903 PFFKTIDFsSDLRQQSASYIPKITHPTDTSNFDpVDPDKL 942
Cdd:cd05624    338 AFFEGLNW-ENIRNLEAPYIPDVSSPSDTSNFD-VDDDVL 375
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
586-941 1.70e-83

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: 276.12  E-value: 1.70e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  586 NYIRLKRAKMDKSMFVKIktLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYY 665
Cdd:cd05622     63 NKIRDLRMKAEDYEVVKV--IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFY 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  666 SFQDKDNLYFVMDYIPGGDMMSLLIRMGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC 745
Cdd:cd05622    141 AFQDDRYLYMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  746 tgfrwthdskyyqsgdhprqdsMDFSNEwgdpSSCRCgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTG---- 821
Cdd:cd05622    220 ----------------------MKMNKE----GMVRC--------------------DTAVGTPDYISPEVLKSQGgdgy 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  822 YTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKA 901
Cdd:cd05622    254 YGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKR 333
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1178431733  902 HPFFKTIDFS-SDLRQQSASYIPKITHPTDTSNFDPVDPDK 941
Cdd:cd05622    334 HLFFKNDQWAwETLRDTVAPVVPDLSSDIDTSNFDDLEEDK 374
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
589-942 6.08e-83

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: 274.97  E-value: 6.08e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  589 RLKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQ 668
Cdd:cd05623     63 KVKQMRLHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYAFQ 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  669 DKDNLYFVMDYIPGGDMMSLLIRM-GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtg 747
Cdd:cd05623    143 DDNNLYLVMDYYVGGDLLTLLSKFeDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSC-- 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 frwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrLKPLERRAArqhQRCLAhslVGTPNYIAPEVLL-----RTGY 822
Cdd:cd05623    221 --------------------------------------LKLMEDGTV---QSSVA---VGTPDYISPEILQamedgKGKY 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  823 TQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQ-AKLSPEASDLIIKLCRGPEDRLGKNGADEIKA 901
Cdd:cd05623    257 GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQvTDVSENAKDLIRRLICSREHRLGQNGIEDFKN 336
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1178431733  902 HPFFKTIDFsSDLRQQSASYIPKITHPTDTSNFDpVDPDKL 942
Cdd:cd05623    337 HPFFVGIDW-DNIRNCEAPYIPEVSSPTDTSNFD-VDDDCL 375
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
589-941 2.00e-82

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: 272.26  E-value: 2.00e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  589 RLKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQ 668
Cdd:cd05621     43 KIRELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQ 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  669 DKDNLYFVMDYIPGGDMMSLLIRMGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgf 748
Cdd:cd05621    123 DDKYLYMVMEYMPGGDLVNLMSNYDV-PEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCM-- 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdsKYYQSGdhprqdsmdfsnewgdpsSCRCgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTG----YTQ 824
Cdd:cd05621    200 ------KMDETG------------------MVHC--------------------DTAVGTPDYISPEVLKSQGgdgyYGR 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  825 LCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPF 904
Cdd:cd05621    236 ECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNFPDDVEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPF 315
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1178431733  905 FKTIDFS-SDLRQQSASYIPKITHPTDTSNFDPVDPDK 941
Cdd:cd05621    316 FRNDQWNwDNIRETAAPVVPELSSDIDTSNFDDIEDDK 353
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
600-905 6.23e-82

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: 267.16  E-value: 6.23e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05581      3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthDSKYYQS 759
Cdd:cd05581     83 APNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFG---------TAKVLGP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 GDHPRQDSMDFSNEwgdpsscrcgdrlkplerraaRQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd05581    154 DSSPESTKGDADSQ---------------------IAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQML 212
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSlhIPPqaKLSPEASDLIIKLC-RGPEDRLG---KNGADEIKAHPFF 905
Cdd:cd05581    213 TGKPPFRGSNEYLTFQKIVKLEYE--FPE--NFPPDAKDLIQKLLvLDPSKRLGvneNGGYDELKAHPFF 278
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
603-958 3.90e-81

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: 266.96  E-value: 3.90e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKA---LYATKTLRKKDVLlRNQ--VAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd05584      1 LKVLGKGGYGKVFQVRKTTGSDkgkIFAMKVLKKASIV-RNQkdTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsKYY 757
Cdd:cd05584     80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLC---------KES 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDHprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05584    151 IHDGT--------------------------------------VTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYD 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVInwQTSLHIPPQakLSPEASDLIIKLC-RGPEDRLGKNGAD--EIKAHPFFKTIDFSSDL 914
Cdd:cd05584    193 MLTGAPPFTAENRKKTIDKIL--KGKLNLPPY--LTNEARDLLKKLLkRNVSSRLGSGPGDaeEIKAHPFFRHINWDDLL 268
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  915 -RQQSASYIPKITHPTDTSNFD-------PVD-PDklwsDDNEEENVNDTLNG 958
Cdd:cd05584    269 aKKVEPPFKPLLQSEEDVSQFDskftkqtPVDsPD----DSTLSESANQVFQG 317
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
600-910 1.71e-80

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: 263.50  E-value: 1.71e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05609      2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYQs 759
Cdd:cd05609     82 VEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTNLYE- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gDHPRQDSMDFSNEwgdpsscrcgdrlkplerraarqhQRClahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd05609    161 -GHIEKDTREFLDK------------------------QVC------GTPEYIAPEVILRQGYGKPVDWWAMGIILYEFL 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  840 VGQPPFLAQTPLETQMKVIN----WQTSLHIPPqaklsPEASDLIIKLCR-GPEDRLGKNGADEIKAHPFFKTIDF 910
Cdd:cd05609    210 VGCVPFFGDTPEELFGQVISdeieWPEGDDALP-----DDAQDLITRLLQqNPLERLGTGGAEEVKQHPFFQDLDW 280
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
604-975 1.08e-79

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: 263.02  E-value: 1.08e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAeaDN---EWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd05575      1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLL--KNvkhPFLVGLHYSFQTKDKLYFVLDYV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsg 760
Cdd:cd05575     79 NGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLC--------------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 dhprQDSMdfsnEWGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 840
Cdd:cd05575    144 ----KEGI----EPSDTTSTFC------------------------GTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLY 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  841 GQPPFLAQTPLETQMKVINWQtsLHIPPQakLSPEASDLIIKLC-RGPEDRLG-KNGADEIKAHPFFKTIDFsSDL--RQ 916
Cdd:cd05575    192 GLPPFYSRDTAEMYDNILHKP--LRLRTN--VSPSARDLLEGLLqKDRTKRLGsGNDFLEIKNHSFFRPINW-DDLeaKK 266
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  917 QSASYIPKITHPTDTSNFD------PVDPDKLWSDDneeenvndtLNGWYKNGKHPEHAFYEFTF 975
Cdd:cd05575    267 IPPPFNPNVSGPLDLRNIDpeftrePVPASVGKSAD---------SVAVSASVQEADNAFDGFSY 322
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
604-936 6.67e-77

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: 255.02  E-value: 6.67e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKV---DTKALYATKTLRKKDVLLRNQVaHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd05582      1 KVLGQGSFGKVFLVRKItgpDAGTLYAMKVLKKATLKVRDRV-RTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyQSG 760
Cdd:cd05582     80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSK-----------ESI 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 DHPRQdsmdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 840
Cdd:cd05582    149 DHEKK------------------------------------AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  841 GQPPFLAQTPLETQMKVINWQTSLhipPQAkLSPEASDLIIKLC-RGPEDRLG--KNGADEIKAHPFFKTIDFSSDLRQQ 917
Cdd:cd05582    193 GSLPFQGKDRKETMTMILKAKLGM---PQF-LSPEAQSLLRALFkRNPANRLGagPDGVEEIKRHPFFATIDWNKLYRKE 268
                          330       340
                   ....*....|....*....|
gi 1178431733  918 -SASYIPKITHPTDTSNFDP 936
Cdd:cd05582    269 iKPPFKPAVSRPDDTFYFDP 288
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
606-959 7.97e-75

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: 249.41  E-value: 7.97e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd05585      2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdhprq 765
Cdd:cd05585     82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLC-------------------- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  766 dSMDFSNEwgDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd05585    142 -KLNMKDD--DKTNTFC------------------------GTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPF 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  846 LAQTPLETQMKVInwQTSLHIPpqAKLSPEASDLIIKLC-RGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQ-SASYIP 923
Cdd:cd05585    195 YDENTNEMYRKIL--QEPLRFP--DGFDRDAKDLLIGLLnRDPTKRLGYNGAQEIKNHPFFDQIDWKRLLMKKiQPPFKP 270
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1178431733  924 KITHPTDTSNFDP-----VDPDKLWSDDNEEENVNDTLNGW 959
Cdd:cd05585    271 AVENAIDTSNFDEeftreKPIDSVVDDSHLSESVQQQFEGW 311
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
600-935 8.21e-74

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: 245.39  E-value: 8.21e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd14209      3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT---GFRWThdsky 756
Cdd:cd14209     83 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKrvkGRTWT----- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd14209    158 ------------------------------------------------LCGTPEYLAPEIILSKGYNKAVDWWALGVLIY 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVInwQTSLHIPpqAKLSPEASDLIIKLCR-GPEDRLG--KNGADEIKAHPFFKTIDFSSD 913
Cdd:cd14209    190 EMAAGYPPFFADQPIQIYEKIV--SGKVRFP--SHFSSDLKDLLRNLLQvDLTKRFGnlKNGVNDIKNHKWFATTDWIAI 265
                          330       340
                   ....*....|....*....|...
gi 1178431733  914 LRQQ-SASYIPKITHPTDTSNFD 935
Cdd:cd14209    266 YQRKvEAPFIPKLKGPGDTSNFD 288
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
600-935 1.70e-73

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: 244.65  E-value: 1.70e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05612      3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqs 759
Cdd:cd05612     83 VPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFG---------------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdFSNEWGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd05612    147 ----------FAKKLRDRTWTLC------------------------GTPEYLAPEVIQSKGHNKAVDWWALGILIYEML 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  840 VGQPPFLAQTPLETQMKVInwQTSLHIPPQakLSPEASDLIIKLCRGPE-DRLG--KNGADEIKAHPFFKTIDFSSDL-R 915
Cdd:cd05612    193 VGYPPFFDDNPFGIYEKIL--AGKLEFPRH--LDLYAKDLIKKLLVVDRtRRLGnmKNGADDVKNHRWFKSVDWDDVPqR 268
                          330       340
                   ....*....|....*....|
gi 1178431733  916 QQSASYIPKITHPTDTSNFD 935
Cdd:cd05612    269 KLKPPIVPKVSHDGDTSNFD 288
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
604-948 5.75e-72

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: 241.52  E-value: 5.75e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEA-DNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd05592      1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALAsQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdh 762
Cdd:cd05592     81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMC----------------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prQDSMdfsnewgdpsscrCGDRlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd05592    144 --KENI-------------YGEN---------------KASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQ 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  843 PPFLAQTPLETQMKVINwqTSLHIPpqAKLSPEASDLIIKLC-RGPEDRLG--KNGADEIKAHPFFKTIDFSS-DLRQQS 918
Cdd:cd05592    194 SPFHGEDEDELFWSICN--DTPHYP--RWLTKEAASCLSLLLeRNPEKRLGvpECPAGDIRDHPFFKTIDWDKlERREID 269
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1178431733  919 ASYIPKITHPTDTSNFD-----------PVDPDKLWSDDNE 948
Cdd:cd05592    270 PPFKPKVKSANDVSNFDpdftmekpvltPVDKKLLASMDQE 310
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
606-905 6.05e-72

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: 239.43  E-value: 6.05e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd05572      1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQSGdhprq 765
Cdd:cd05572     81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGF---------AKKLGSG----- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  766 dsmdfsnewgdpsscrcgdrlkplerraarqhQRclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd05572    147 --------------------------------RK--TWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPF 192
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  846 --LAQTPLETqMKVINWQTS-LHIPPqaKLSPEASDLIIKLC-RGPEDRLG--KNGADEIKAHPFF 905
Cdd:cd05572    193 ggDDEDPMKI-YNIILKGIDkIEFPK--YIDKNAKNLIKQLLrRNPEERLGylKGGIRDIKKHKWF 255
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
604-950 5.81e-70

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: 236.10  E-value: 5.81e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd05571      1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdhp 763
Cdd:cd05571     81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLC------------------ 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rQDSMDFsnewGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQP 843
Cdd:cd05571    143 -KEEISY----GATTKTFC------------------------GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  844 PFLAQTPlETQMKVInWQTSLHIPPqaKLSPEASDLIIKLC-RGPEDRLG--KNGADEIKAHPFFKTIDFsSDL--RQQS 918
Cdd:cd05571    194 PFYNRDH-EVLFELI-LMEEVRFPS--TLSPEAKSLLAGLLkKDPKKRLGggPRDAKEIMEHPFFASINW-DDLyqKKIP 268
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1178431733  919 ASYIPKITHPTDTSNFD-----------PVDPDKLWSDDNEEE 950
Cdd:cd05571    269 PPFKPQVTSETDTRYFDeeftaesveltPPDRGDLLGLEEEER 311
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
606-908 7.79e-69

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: 231.13  E-value: 7.79e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKV---DTKALYATKTLRKKDVLLRNQVA-HVKAERDILaEA--DNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05583      2 LGTGAYGKVFLVRKVgghDAGKLYAMKVLKKATIVQKAKTAeHTMTERQVL-EAvrQSPFLVTLHYAFQTDAKLHLILDY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQS 759
Cdd:cd05583     81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGL---------SKEFLP 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 GDHPRqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLR--TGYTQLCDWWSVGVILFE 837
Cdd:cd05583    152 GENDR-------------------------------------AYSFCGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYE 194
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLG--KNGADEIKAHPFFKTI 908
Cdd:cd05583    195 LLTGASPFTVDGERNSQSEISKRILKSHPPIPKTFSAEAKDFILKlLEKDPKKRLGagPRGAHEIKEHPFFKGL 268
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
600-935 1.40e-68

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: 233.23  E-value: 1.40e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05610      6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEY 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL---------CTGFRW 750
Cdd:cd05610     86 LIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLskvtlnrelNMMDIL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 THDSKYYQSGDHPRQD----SMDFSNEWGDPSSCRCGdrlKPLERRAAR-QHQRCLahslvGTPNYIAPEVLLRTGYTQL 825
Cdd:cd05610    166 TTPSMAKPKNDYSRTPgqvlSLISSLGFNTPTPYRTP---KSVRRGAARvEGERIL-----GTPDYLAPELLLGKPHGPA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 CDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINwqtsLHIP-PQA--KLSPEASDLI-IKLCRGPEDRlgkNGADEIKA 901
Cdd:cd05610    238 VDWWALGVCLFEFLTGIPPFNDETPQQVFQNILN----RDIPwPEGeeELSVNAQNAIeILLTMDPTKR---AGLKELKQ 310
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1178431733  902 HPFFKTIDFsSDLRQQSASYIPKITHPTDTSNFD 935
Cdd:cd05610    311 HPLFHGVDW-ENLQNQTMPFIPQPDDETDTSYFE 343
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
600-905 5.68e-68

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: 228.29  E-value: 5.68e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05578      2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqs 759
Cdd:cd05578     82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNI--------------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdrlkplerrAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd05578    147 ---------------------------------ATKLTDGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEML 193
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  840 VGQPPF--LAQTPLE--TQMKVinwQTSLHIPPQakLSPEASDLIIK-LCRGPEDRLGknGADEIKAHPFF 905
Cdd:cd05578    194 RGKRPYeiHSRTSIEeiRAKFE---TASVLYPAG--WSEEAIDLINKlLERDPQKRLG--DLSDLKNHPYF 257
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
600-936 4.31e-67

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: 228.34  E-value: 4.31e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILA---EADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd05589      1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFEtvnSARHPFLVNLFACFQTPEHVCFV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMsLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsky 756
Cdd:cd05589     81 MEYAAGGDLM-MHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC----------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprQDSMDFsnewGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd05589    149 --------KEGMGF----GDRTSTFC------------------------GTPEFLAPEVLTDTSYTRAVDWWGLGVLIY 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPFlaqtPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLG--KNGADEIKAHPFFKTIDFSSD 913
Cdd:cd05589    193 EMLVGESPF----PGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRkNPERRLGasERDAEDVKKQPFFRNIDWEAL 268
                          330       340
                   ....*....|....*....|....
gi 1178431733  914 L-RQQSASYIPKITHPTDTSNFDP 936
Cdd:cd05589    269 LaRKIKPPFVPTIKSPEDVSNFDE 292
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
603-936 1.16e-65

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: 224.19  E-value: 1.16e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLrKKDVLLRNQ-VAHVKAERDILAEADN-EWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd05587      1 LMVLGKGSFGKVMLAERKGTDELYAIKIL-KKDVIIQDDdVECTMVEKRVLALSGKpPFLTQLHSCFQTMDRLYFVMEYV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqsg 760
Cdd:cd05587     80 NGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCK-------------- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 dhprqdsmdfSNEWGDPSScrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 840
Cdd:cd05587    146 ----------EGIFGGKTT-----------------------RTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLA 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  841 GQPPFLAQTPLETQMKVINWQTSLhipPQAkLSPEAsdliIKLCRG-----PEDRLG--KNGADEIKAHPFFKTIDFSS- 912
Cdd:cd05587    193 GQPPFDGEDEDELFQSIMEHNVSY---PKS-LSKEA----VSICKGlltkhPAKRLGcgPTGERDIKEHPFFRRIDWEKl 264
                          330       340
                   ....*....|....*....|....
gi 1178431733  913 DLRQQSASYIPKITHPTDTSNFDP 936
Cdd:cd05587    265 ERREIQPPFKPKIKSPRDAENFDK 288
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
605-941 3.11e-65

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 223.16  E-value: 3.11e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  605 TLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:PTZ00263    25 TLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgdhpr 764
Cdd:PTZ00263   105 LFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGF-------------------- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  765 qdsmdfsnewgdpsscrcgdrlkplerrAARQHQRclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPP 844
Cdd:PTZ00263   165 ----------------------------AKKVPDR--TFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPP 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  845 FLAQTPLETQMKVI-------NWqtslhippqakLSPEASDLIIKLCR-GPEDRLG--KNGADEIKAHPFFKTIDFSSDL 914
Cdd:PTZ00263   215 FFDDTPFRIYEKILagrlkfpNW-----------FDGRARDLVKGLLQtDHTKRLGtlKGGVADVKNHPYFHGANWDKLY 283
                          330       340       350
                   ....*....|....*....|....*....|
gi 1178431733  915 RQQSASYIP-KITHPTDTSNFD--PVDPDK 941
Cdd:PTZ00263   284 ARYYPAPIPvRVKSPGDTSNFEkyPDSPVD 313
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
603-904 3.24e-65

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: 220.47  E-value: 3.24e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14003      5 GKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSK-LKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqsgdh 762
Cdd:cd14003     84 GELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSN---------------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsSCRCGDRLkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGY-TQLCDWWSVGVILFEMLVG 841
Cdd:cd14003    148 ----------------EFRGGSLL----------------KTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTG 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  842 QPPFLAQTPLETQMKVINwqTSLHIPPQakLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:cd14003    196 YLPFDDDNDSKLFRKILK--GKYPIPSH--LSPDARDLIRRmLVVDPSKRI---TIEEILNHPW 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
600-904 1.24e-63

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: 216.19  E-value: 1.24e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLlRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05117      2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLK-SEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLctgfrwthdSKY 756
Cdd:cd05117     81 CTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGL---------AKI 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 YQSGDHprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd05117    152 FEEGEK---------------------------------------LKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILY 192
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:cd05117    193 ILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRlLVVDPKKRL---TAAEALNHPW 258
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
600-934 1.47e-62

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: 215.94  E-value: 1.47e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKV---DTKALYATKTLRKKDVLLRNQVA-HVKAERDILAEA-DNEWVVRLYYSFQDKDNLY 674
Cdd:cd05614      2 FELLKVLGTGAYGKVFLVRKVsghDANKLYAMKVLRKAALVQKAKTVeHTRTERNVLEHVrQSPFLVTLHYAFQTDAKLH 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdS 754
Cdd:cd05614     82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGL---------S 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 KYYQSGDHPRqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLL-RTGYTQLCDWWSVGV 833
Cdd:cd05614    153 KEFLTEEKER-------------------------------------TYSFCGTIEYMAPEIIRgKSGHGKAVDWWSLGI 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  834 ILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKL-CRGPEDRLGK--NGADEIKAHPFFKTIDF 910
Cdd:cd05614    196 LMFELLTGASPFTLEGEKNTQSEVSRRILKCDPPFPSFIGPVARDLLQKLlCKDPKKRLGAgpQGAQEIKEHPFFKGLDW 275
                          330       340
                   ....*....|....*....|....*
gi 1178431733  911 SS-DLRQQSASYIPKITHPTDTSNF 934
Cdd:cd05614    276 EAlALRKVNPPFRPSIRSELDVGNF 300
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
594-935 7.25e-62

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: 214.02  E-value: 7.25e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  594 KMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEA-DNEWVVRLYYSFQDKDN 672
Cdd:cd05619      1 KLTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKEN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwth 752
Cdd:cd05619     81 LFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCK------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfSNEWGDPSSCrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd05619    155 ------------------ENMLGDAKTS-----------------------TFCGTPDYIAPEILLGQKYNTSVDWWSFG 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  833 VILFEMLVGQPPFLAQTPlETQMKVINWQTSLHipPQAkLSPEASDLIIKL-CRGPEDRLGKNGadEIKAHPFFKTIDFS 911
Cdd:cd05619    194 VLLYEMLIGQSPFHGQDE-EELFQSIRMDNPFY--PRW-LEKEAKDILVKLfVREPERRLGVRG--DIRQHPFFREINWE 267
                          330       340
                   ....*....|....*....|....*
gi 1178431733  912 S-DLRQQSASYIPKITHPTDTSNFD 935
Cdd:cd05619    268 AlEEREIEPPFKPKVKSPFDCSNFD 292
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
600-906 8.60e-62

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: 210.79  E-value: 8.60e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd14007      2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqs 759
Cdd:cd14007     82 APNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSV------------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewGDPSScrcgdrlkpleRRaarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14007    149 ---------------HAPSN-----------RR----------KTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELL 192
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQtsLHIPPqaKLSPEASDLIIKLCRG-PEDRLgknGADEIKAHPFFK 906
Cdd:cd14007    193 VGKPPFESKSHQETYKRIQNVD--IKFPS--SVSPEAKDLISKLLQKdPSKRL---SLEQVLNHPWIK 253
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
604-949 3.06e-61

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: 211.58  E-value: 3.06e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILA-EADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd05591      1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdh 762
Cdd:cd05591     81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC----------------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 pRQDSMDfsnewGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd05591    144 -KEGILN-----GKTTTTFC------------------------GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQ 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  843 PPFLAQTplETQMkvinWQTSLH--IPPQAKLSPEASDlIIK--LCRGPEDRLG----KNGADEIKAHPFFKTIDFSS-D 913
Cdd:cd05591    194 PPFEADN--EDDL----FESILHddVLYPVWLSKEAVS-ILKafMTKNPAKRLGcvasQGGEDAIRQHPFFREIDWEAlE 266
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1178431733  914 LRQQSASYIPKITHPTDTSNFD-----------PVDPDKLWSDDNEE 949
Cdd:cd05591    267 QRKVKPPFKPKIKTKRDANNFDqdftkeepvltPVDPAVIKQINQEE 313
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
604-935 4.07e-60

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: 208.26  E-value: 4.07e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEA-DNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd05620      1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqsgdh 762
Cdd:cd05620     81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCK---------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfSNEWGDPSscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd05620    145 --------ENVFGDNR-----------------------ASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQ 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  843 PPFLAQTPLETqMKVINWQTSlHIPPQakLSPEASDLIIKLC-RGPEDRLGKNGadEIKAHPFFKTIDFSS-DLRQQSAS 920
Cdd:cd05620    194 SPFHGDDEDEL-FESIRVDTP-HYPRW--ITKESKDILEKLFeRDPTRRLGVVG--NIRGHPFFKTINWTAlEKRELDPP 267
                          330
                   ....*....|....*
gi 1178431733  921 YIPKITHPTDTSNFD 935
Cdd:cd05620    268 FKPKVKSPSDYSNFD 282
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
606-936 7.61e-60

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: 208.19  E-value: 7.61e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDIL---AEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd05586      1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILvrtALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKyyqsgdh 762
Cdd:cd05586     81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGL---------SK------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLL-RTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd05586    145 -------------------------------ADLTDNKTTNTFCGTTEYLAPEVLLdEKGYTKMVDFWSLGVLVFEMCCG 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  842 QPPFLAQTPLETQMKVINWQTSLhipPQAKLSPEASDLIIKLC-RGPEDRLGK-NGADEIKAHPFFKTIDFSSDLRQQ-S 918
Cdd:cd05586    194 WSPFYAEDTQQMYRNIAFGKVRF---PKDVLSDEGRSFVKGLLnRNPKHRLGAhDDAVELKEHPFFADIDWDLLSKKKiT 270
                          330
                   ....*....|....*...
gi 1178431733  919 ASYIPKITHPTDTSNFDP 936
Cdd:cd05586    271 PPFKPIVDSDTDVSNFDP 288
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
603-937 1.21e-59

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: 207.51  E-value: 1.21e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAE-ADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd05604      1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgd 761
Cdd:cd05604     81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLC---------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprQDSMDFSnewgDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd05604    145 ---KEGISNS----DTTTTFC------------------------GTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYG 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  842 QPPFLAQTPLETQMKVINwqTSLHIPPQAKLsPEASDLIIKLCRGPEDRLG-KNGADEIKAHPFFKTIDFsSDLRQQSAS 920
Cdd:cd05604    194 LPPFYCRDTAEMYENILH--KPLVLRPGISL-TAWSILEELLEKDRQLRLGaKEDFLEIKNHPFFESINW-TDLVQKKIP 269
                          330
                   ....*....|....*....
gi 1178431733  921 --YIPKITHPTDTSNFDPV 937
Cdd:cd05604    270 ppFNPNVNGPDDISNFDAE 288
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
604-936 4.41e-59

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: 205.59  E-value: 4.41e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEA-DNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd05603      1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNlKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyQSGDH 762
Cdd:cd05603     81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLC------------KEGME 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 PRQDSMDFsnewgdpssCrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd05603    149 PEETTSTF---------C--------------------------GTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  843 PPFLAQTPleTQMKVINWQTSLHIPPQAKLSpeASDLIIKLCRGPEDRLGKNGAD--EIKAHPFFKTIDFsSDL--RQQS 918
Cdd:cd05603    194 PPFYSRDV--SQMYDNILHKPLHLPGGKTVA--ACDLLQGLLHKDQRRRLGAKADflEIKNHVFFSPINW-DDLyhKRIT 268
                          330
                   ....*....|....*...
gi 1178431733  919 ASYIPKITHPTDTSNFDP 936
Cdd:cd05603    269 PPYNPNVAGPADLRHFDP 286
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
604-936 1.03e-57

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: 202.06  E-value: 1.03e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLrKKDVLLR-NQVAHVKAERDILAEADNE-WVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd05590      1 RVLGKGSFGKVMLARLKESGRLYAVKVL-KKDVILQdDDVECTMTEKRILSLARNHpFLTQLYCCFQTPDRLFFVMEFVN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqsgd 761
Cdd:cd05590     80 GGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCK--------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd05590    145 --------------------------------EGIFNGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCG 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  842 QPPFLAQTPLETQMKVINWQTslhIPPqAKLSPEASDlIIK--LCRGPEDRLG---KNGADEIKAHPFFKTIDFSS-DLR 915
Cdd:cd05590    193 HAPFEAENEDDLFEAILNDEV---VYP-TWLSQDAVD-ILKafMTKNPTMRLGsltLGGEEAILRHPFFKELDWEKlNRR 267
                          330       340
                   ....*....|....*....|.
gi 1178431733  916 QQSASYIPKITHPTDTSNFDP 936
Cdd:cd05590    268 QIEPPFRPRIKSREDVSNFDP 288
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
604-949 1.16e-56

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: 199.08  E-value: 1.16e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd05595      1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyQSGdhp 763
Cdd:cd05595     81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLC------------KEG--- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rqdsmdFSNEWGDPSSCrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQP 843
Cdd:cd05595    146 ------ITDGATMKTFC--------------------------GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  844 PFLAQTPlETQMKVINWQtSLHIPpqAKLSPEASDLIIKLCR-GPEDRL--GKNGADEIKAHPFFKTIDFSSDLRQQ-SA 919
Cdd:cd05595    194 PFYNQDH-ERLFELILME-EIRFP--RTLSPEAKSLLAGLLKkDPKQRLggGPSDAKEVMEHRFFLSINWQDVVQKKlLP 269
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1178431733  920 SYIPKITHPTDTSNFDP---------VDPDKLWSDDNEE 949
Cdd:cd05595    270 PFKPQVTSEVDTRYFDDeftaqsitiTPPDRYDSLDLLE 308
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
606-910 1.78e-54

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: 191.20  E-value: 1.78e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd05577      1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMG--IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgdhp 763
Cdd:cd05577     81 KYHIYNVGtrGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGL------------------- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rqdSMDFSNEwgdpsscrcgdrlKPLERRaarqhqrclahslVGTPNYIAPEVLLR-TGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd05577    142 ---AVEFKGG-------------KKIKGR-------------VGTHGYMAPEVLQKeVAYDFSVDWFALGCMLYEMIAGR 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  843 PPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLI-IKLCRGPEDRLG--KNGADEIKAHPFFKTIDF 910
Cdd:cd05577    193 SPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCeGLLQKDPERRLGcrGGSADEVKEHPFFRSLNW 263
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
604-946 1.91e-54

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: 192.64  E-value: 1.91e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNE-WVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd05588      1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNHpFLVGLHSCFQTESRLFFVIEFVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyQSGDH 762
Cdd:cd05588     81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMC------------KEGLR 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 PrqdsmdfsnewGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd05588    149 P-----------GDTTSTFC------------------------GTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGR 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  843 PPF----------------LAQTPLETQMKVinwqtslhipPQAkLSPEASDlIIK--LCRGPEDRLG---KNGADEIKA 901
Cdd:cd05588    194 SPFdivgssdnpdqntedyLFQVILEKPIRI----------PRS-LSVKAAS-VLKgfLNKNPAERLGchpQTGFADIQS 261
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1178431733  902 HPFFKTIDFSS-DLRQQSASYIPKITHPTDTSNFDPV---DPDKLWSDD 946
Cdd:cd05588    262 HPFFRTIDWEQlEQKQVTPPYKPRIESERDLENFDPQftnEPVQLTPDD 310
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
600-928 6.19e-53

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: 187.13  E-value: 6.19e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKV---DTKALYATKTLRKKDVLLRNQVA-HVKAERDILAEA-DNEWVVRLYYSFQDKDNLY 674
Cdd:cd05613      2 FELLKVLGTGAYGKVFLVRKVsghDAGKLYAMKVLKKATIVQKAKTAeHTRTERQVLEHIrQSPFLVTLHYAFQTDTKLH 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthds 754
Cdd:cd05613     82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEF------ 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerrAARQHQRclAHSLVGTPNYIAPEVLL--RTGYTQLCDWWSVG 832
Cdd:cd05613    156 --------------------------------------LLDENER--AYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLG 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRL--GKNGADEIKAHPFFKTID 909
Cdd:cd05613    196 VLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDIIQRlLMKDPKKRLgcGPNGADEIKKHPFFQKIN 275
                          330
                   ....*....|....*....
gi 1178431733  910 FsSDLrqqSASYIPKITHP 928
Cdd:cd05613    276 W-DDL---AAKKVPAPFKP 290
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
598-936 3.04e-52

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: 186.76  E-value: 3.04e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAE-ADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd05602      7 SDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKnVKHPFLVGLHFSFQTTDKLYFV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsky 756
Cdd:cd05602     87 LDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLC----------- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprqdsmdfsNEWGDPSSCrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd05602    156 ---------------KENIEPNGT---------------------TSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLY 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVINwqTSLHIPPQakLSPEASDLIIKLCRgpEDRLGKNGAD----EIKAHPFFKTIDFsS 912
Cdd:cd05602    200 EMLYGLPPFYSRNTAEMYDNILN--KPLQLKPN--ITNSARHLLEGLLQ--KDRTKRLGAKddftEIKNHIFFSPINW-D 272
                          330       340
                   ....*....|....*....|....*.
gi 1178431733  913 DL--RQQSASYIPKITHPTDTSNFDP 936
Cdd:cd05602    273 DLinKKITPPFNPNVSGPNDLRHFDP 298
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
600-905 5.38e-52

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: 183.11  E-value: 5.38e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRnQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd06606      2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEE-ELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYQS 759
Cdd:cd06606     81 VPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCA---KRLAEIATGEG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 GdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd06606    158 T------------------------------------------KSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMA 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  840 VGQPPFLAQT-PLETQMKVINWQTSLHIPPqaKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd06606    196 TGKPPWSELGnPVAALFKIGSSGEPPPIPE--HLSEEAKDFLRKcLQRDPKKRP---TADELLQHPFL 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
603-890 1.76e-51

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: 182.02  E-value: 1.76e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14014      5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYQSGdh 762
Cdd:cd14014     85 GSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIA---RALGDSGLTQTG-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14014    160 -----------------------------------------SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGR 198
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1178431733  843 PPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDR 890
Cdd:cd14014    199 PPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRaLAKDPEER 247
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
600-905 2.13e-51

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: 181.60  E-value: 2.13e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd14099      3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfRWTHDskyyqs 759
Cdd:cd14099     83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAA--RLEYD------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcGDRLKPLerraarqhqrClahslvGTPNYIAPEVLLRT-GYTQLCDWWSVGVILFEM 838
Cdd:cd14099    155 -----------------------GERKKTL----------C------GTPNYIAPEVLEKKkGHSFEVDIWSLGVILYTL 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  839 LVGQPPFLAQTPLETQMKVINWQTSlhIPPQAKLSPEASDLIIKLCRG-PEDRLgknGADEIKAHPFF 905
Cdd:cd14099    196 LVGKPPFETSDVKETYKRIKKNEYS--FPSHLSISDEAKDLIRSMLQPdPTKRP---SLDEILSHPFF 258
MobB_LATS1 cd21778
Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; ...
524-599 9.91e-51

Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; LATS1, also called WARTS protein kinase, is a serine/threonine-protein kinase that 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. LATS1 belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. LATS proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of LATS1 serine/threonine protein kinase and similar proteins.


Pssm-ID: 439273  Cd Length: 76  Bit Score: 172.68  E-value: 9.91e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  524 SRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMDKSM 599
Cdd:cd21778      1 SRVQSYSPQAFKFFMEQHVENVLKSHQQRLHRRKQLENEMAKVGLSEEAQDQMRKMLCQKESNYIRLKRAKMDKSM 76
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
600-935 1.61e-50

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: 181.35  E-value: 1.61e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILA-EADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd05616      2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyq 758
Cdd:cd05616     82 YVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK------------ 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqdsmdfSNEWGDPSScrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd05616    150 ------------ENIWDGVTT-----------------------KTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEM 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  839 LVGQPPFLAQTPLETQMKVINWQTSLhipPQAkLSPEAsdliIKLCRG-----PEDRL--GKNGADEIKAHPFFKTIDFS 911
Cdd:cd05616    195 LAGQAPFEGEDEDELFQSIMEHNVAY---PKS-MSKEA----VAICKGlmtkhPGKRLgcGPEGERDIKEHAFFRYIDWE 266
                          330       340
                   ....*....|....*....|....*
gi 1178431733  912 S-DLRQQSASYIPKITHpTDTSNFD 935
Cdd:cd05616    267 KlERKEIQPPYKPKACG-RNAENFD 290
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
600-910 2.41e-50

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: 179.47  E-value: 2.41e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05605      2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGI--FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskYY 757
Cdd:cd05605     82 MNGGDLKFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAV---------EI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05605    153 PEGE---------------------------------------TIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYE 193
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  838 MLVGQPPFLAQTPLETQMKV---INWQTslhIPPQAKLSPEASDLIIK-LCRGPEDRLG--KNGADEIKAHPFFKTIDF 910
Cdd:cd05605    194 MIEGQAPFRARKEKVKREEVdrrVKEDQ---EEYSEKFSEEAKSICSQlLQKDPKTRLGcrGEGAEDVKSHPFFKSINF 269
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
603-890 4.06e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 184.83  E-value: 4.06e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:COG0515     12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdh 762
Cdd:COG0515     92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIA----------------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:COG0515    155 -----------------------------RALGGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGR 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1178431733  843 PPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDR 890
Cdd:COG0515    206 PPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRaLAKDPEER 254
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
606-904 1.94e-49

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: 175.49  E-value: 1.94e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14009      1 IGRGSFATVWKGRHKQTGEVVAIKEISRKK-LNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH---IKLTDFGLctgfrwthdSKYYQSGDh 762
Cdd:cd14009     80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGF---------ARSLQPAS- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14009    150 --------------------------------------MAETLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGK 191
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  843 PPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKL-CRGPEDRLgknGADEIKAHPF 904
Cdd:cd14009    192 PPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLlRRDPAERI---SFEEFFAHPF 251
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
606-905 2.50e-49

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: 175.82  E-value: 2.50e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKT-----LRKKDVL------LRNQVAHVKAERDILAEADNEWVVRLYYSFQD--KDN 672
Cdd:cd14008      1 LGRGSFGKVKLALDTETGQLYAIKIfnksrLRKRREGkndrgkIKNALDDVRREIAIMKKLDHPNIVRLYEVIDDpeSDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSL--LIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrw 750
Cdd:cd14008     81 LYLVLEYCEGGPVMELdsGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGV------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdSKYYQSGDhprqdsmdfsnewgdpsscrcgDRLKPLErraarqhqrclahslvGTPNYIAPEvLLRTGYTQLC---- 826
Cdd:cd14008    155 ---SEMFEDGN----------------------DTLQKTA----------------GTPAFLAPE-LCDGDSKTYSgkaa 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  827 DWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQakLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14008    193 DIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPPE--LSPELKDLLRRmLEKDPEKRI---TLKEIKEHPWV 267
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
600-910 2.98e-49

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: 176.37  E-value: 2.98e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05630      2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGI--FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyy 757
Cdd:cd05630     82 MNGGDLKFHIYHMGQagFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAV----------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qsgdHPRQDsmdfsnewgdpsscrcgdrlKPLERRaarqhqrclahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05630    151 ----HVPEG--------------------QTIKGR-------------VGTVGYMAPEVVKNERYTFSPDWWALGCLLYE 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPF------LAQTPLETQMKVINWQTSlhippqAKLSPEASDLI-IKLCRGPEDRLG--KNGADEIKAHPFFKTI 908
Cdd:cd05630    194 MIAGQSPFqqrkkkIKREEVERLVKEVPEEYS------EKFSPQARSLCsMLLCKDPAERLGcrGGGAREVKEHPLFKKL 267

                   ..
gi 1178431733  909 DF 910
Cdd:cd05630    268 NF 269
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
591-951 4.73e-49

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 177.86  E-value: 4.73e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  591 KRAKMDKSMFVKIKTLGIGAFGEVCLAR-KVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQD 669
Cdd:PTZ00426    23 RKNKMKYEDFNFIRTLGTGSFGRVILATyKNEDFPPVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKD 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  670 KDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfr 749
Cdd:PTZ00426   103 ESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFA---- 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 wthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlKPLERRaarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWW 829
Cdd:PTZ00426   179 -------------------------------------KVVDTR---------TYTLCGTPEYIAPEILLNVGHGKAADWW 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  830 SVGVILFEMLVGQPPFLAQTPLETQMKVInwQTSLHIPpqAKLSPEASDLIIK-LCRGPEDRLG--KNGADEIKAHPFFK 906
Cdd:PTZ00426   213 TLGIFIYEILVGCPPFYANEPLLIYQKIL--EGIIYFP--KFLDNNCKHLMKKlLSHDLTKRYGnlKKGAQNVKEHPWFG 288
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1178431733  907 TIDFSSDLRQQ-SASYIPKITHPTDTSNFDPVDPDKLWSDDNEEEN 951
Cdd:PTZ00426   289 NIDWVSLLHKNvEVPYKPKYKNVFDSSNFERVQEDLTIADKITNEN 334
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
599-905 5.09e-49

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: 174.70  E-value: 5.09e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATK-----TLRKKDVLLRnqvahvkaERDILAEADNEWVVRLYYSFQDKDNL 673
Cdd:cd05122      1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKkinleSKEKKESILN--------EIAILKKCKHPNIVKYYGSYLKKDEL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDYIPGGDMMSLL-IRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwth 752
Cdd:cd05122     73 WIVMEFCSGGSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSA------ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfsnewgdpsscrcgdRLKPLERRaarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd05122    147 --------------------------------QLSDGKTR----------NTFVGTPYWMAPEVIQGKPYGFKADIWSLG 184
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETqMKVI--NWQTSLHIPPqaKLSPEASDlIIKLC--RGPEDRLgknGADEIKAHPFF 905
Cdd:cd05122    185 ITAIEMAEGKPPYSELPPMKA-LFLIatNGPPGLRNPK--KWSKEFKD-FLKKClqKDPEKRP---TAEQLLKHPFI 254
Pkinase pfam00069
Protein kinase domain;
600-905 5.33e-49

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 173.20  E-value: 5.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQvAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMgfihrdikpdnilidrdghikltdfglctgfrwthdskyyqs 759
Cdd:pfam00069   80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLESGSSL------------------------------------------ 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:pfam00069  118 -------------------------------------------TTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELL 154
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  840 VGQPPFLAQTPLETQMKVINwQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:pfam00069  155 TGKPPFPGINGNEIYELIID-QPYAFPELPSNLSEEAKDLLKKlLKKDPSKRL---TATQALQHPWF 217
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
592-935 1.01e-47

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: 174.45  E-value: 1.01e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  592 RAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKD 671
Cdd:cd05594     19 KHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHD 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVH-KMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrw 750
Cdd:cd05594     99 RLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCK---- 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpSSCRCGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd05594    175 ---------------------------EGIKDGATMK----------------TFCGTPEYLAPEVLEDNDYGRAVDWWG 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  831 VGVILFEMLVGQPPFLAQTPlETQMKVInWQTSLHIPpqAKLSPEASDLIIKLC-RGPEDRL--GKNGADEIKAHPFFKT 907
Cdd:cd05594    212 LGVVMYEMMCGRLPFYNQDH-EKLFELI-LMEEIRFP--RTLSPEAKSLLSGLLkKDPKQRLggGPDDAKEIMQHKFFAG 287
                          330       340
                   ....*....|....*....|....*....
gi 1178431733  908 IDFSSDLRQQ-SASYIPKITHPTDTSNFD 935
Cdd:cd05594    288 IVWQDVYEKKlVPPFKPQVTSETDTRYFD 316
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
591-946 1.25e-47

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: 173.73  E-value: 1.25e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  591 KRAKMDKsmFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDK 670
Cdd:cd05593     10 KRKTMND--FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrw 750
Cdd:cd05593     88 DRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC----- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhpRQDSMDfsnewgdpsscrcgdrlkplerrAARQHQRClahslvGTPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd05593    163 -------------KEGITD-----------------------AATMKTFC------GTPEYLAPEVLEDNDYGRAVDWWG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  831 VGVILFEMLVGQPPFLAQtpleTQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRL--GKNGADEIKAHPFFKT 907
Cdd:cd05593    201 LGVVMYEMMCGRLPFYNQ----DHEKLFELILMEDIKFPRTLSADAKSLLSGlLIKDPNKRLggGPDDAKEIMRHSFFTG 276
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1178431733  908 IDFSSDL-RQQSASYIPKITHPTDTSNFD--------PVDPDKLWSDD 946
Cdd:cd05593    277 VNWQDVYdKKLVPPFKPQVTSETDTRYFDeeftaqtiTITPPEKYDED 324
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
606-928 1.71e-47

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: 171.08  E-value: 1.71e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILA----EADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd05606      2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSlvstGGDCPFIVCMTYAFQTPDKLCFILDLMN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgd 761
Cdd:cd05606     82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGL----------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdSMDFSNEwgdpsscrcgdrlKPlerraarqhqrclaHSLVGTPNYIAPEVLLR-TGYTQLCDWWSVGVILFEMLV 840
Cdd:cd05606    145 -----ACDFSKK-------------KP--------------HASVGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLK 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  841 GQPPFLAQ-TPLETQMKVINWQTSLHIPpqAKLSPEASDLIIKLC-RGPEDRLG--KNGADEIKAHPFFKTIDFSSDLRQ 916
Cdd:cd05606    193 GHSPFRQHkTKDKHEIDRMTLTMNVELP--DSFSPELKSLLEGLLqRDVSKRLGclGRGATEVKEHPFFKGVDWQQVYLQ 270
                          330
                   ....*....|..
gi 1178431733  917 QsasYIPKITHP 928
Cdd:cd05606    271 K---YPPPLIPP 279
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
600-948 4.48e-47

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: 172.51  E-value: 4.48e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEAD-NEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd05617     17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASsNPFLVGLHSCFQTTSRLFLVIE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyQ 758
Cdd:cd05617     97 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMC------------K 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SGDHPrqdsmdfsnewGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd05617    165 EGLGP-----------GDTTSTFC------------------------GTPNYIAPEILRGEEYGFSVDWWALGVLMFEM 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  839 LVGQPPF--LAQTP---LETQMKVINWQTSLHIPpqAKLSPEASDLIIK-LCRGPEDRLG---KNGADEIKAHPFFKTID 909
Cdd:cd05617    210 MAGRSPFdiITDNPdmnTEDYLFQVILEKPIRIP--RFLSVKASHVLKGfLNKDPKERLGcqpQTGFSDIKSHTFFRSID 287
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1178431733  910 FSS-DLRQQSASYIPKITHPTDTSNFD---PVDPDKLWSDDNE 948
Cdd:cd05617    288 WDLlEKKQVTPPFKPQITDDYGLENFDtqfTSEPVQLTPDDED 330
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
600-935 1.29e-46

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: 170.56  E-value: 1.29e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNE-WVVRLYYSFQDKDNLYFVMD 678
Cdd:cd05615     12 FNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPpFLTQLHSCFQTVDRLYFVME 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyq 758
Cdd:cd05615     92 YVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMC------------- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhpRQDSMDfsnewGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd05615    159 -----KEHMVE-----GVTTRTFC------------------------GTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEM 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  839 LVGQPPFLAQTPLETQMKVINWQTSLhipPQAkLSPEAsdliIKLCRG-----PEDRL--GKNGADEIKAHPFFKTIDFS 911
Cdd:cd05615    205 LAGQPPFDGEDEDELFQSIMEHNVSY---PKS-LSKEA----VSICKGlmtkhPAKRLgcGPEGERDIREHAFFRRIDWD 276
                          330       340
                   ....*....|....*....|....*
gi 1178431733  912 S-DLRQQSASYIPKITHpTDTSNFD 935
Cdd:cd05615    277 KlENREIQPPFKPKVCG-KGAENFD 300
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
600-910 1.40e-45

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: 165.94  E-value: 1.40e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05631      2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGI--FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdskyy 757
Cdd:cd05631     82 MNGGDLKFHIYNMGNpgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQI--------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qsgdhPRqdsmdfsnewgdpsscrcGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05631    153 -----PE------------------GETVR----------------GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYE 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPL----ETQMKVINWQTSLhippQAKLSPEASDLI-IKLCRGPEDRLG--KNGADEIKAHPFFKTIDF 910
Cdd:cd05631    194 MIQGQSPFRKRKERvkreEVDRRVKEDQEEY----SEKFSEDAKSICrMLLTKNPKERLGcrGNGAAGVKQHPIFKNINF 269
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
600-905 1.56e-45

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: 164.56  E-value: 1.56e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAhVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd08215      2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREE-ALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRM----GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSK 755
Cdd:cd08215     81 ADGGDLAQKIKKQkkkgQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGI---------SK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSgdhprqdSMDFsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd08215    152 VLES-------TTDL-------------------------------AKTVVGTPYYLSPELCENKPYNYKSDIWALGCVL 193
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  836 FEMLVGQPPFLAQTPLETQMKVINWQTSlHIPPQakLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd08215    194 YELCTLKHPFEANNLPALVYKIVKGQYP-PIPSQ--YSSELRDLVNSmLQKDPEKRP---SANEILSSPFI 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
606-903 2.18e-45

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: 162.82  E-value: 2.18e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLlrNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd00180      1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLK--KLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLI-RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsKYYQSGDhpr 764
Cdd:cd00180     79 KDLLKeNKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLA---------KDLDSDD--- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  765 qdsmdfsnewgDPSSCRCGDrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMlvgqpp 844
Cdd:cd00180    147 -----------SLLKTTGGT----------------------TPPYYAPPELLGGRYYGPKVDIWSLGVILYEL------ 187
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  845 flaqtpletqmkvinwqtslhippqaklsPEASDLIIK-LCRGPEDRLgknGADEIKAHP 903
Cdd:cd00180    188 -----------------------------EELKDLIRRmLQYDPKKRP---SAKELLEHL 215
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
600-948 3.44e-45

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: 167.13  E-value: 3.44e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADN-EWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd05618     22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNhPFLVGLHSCFQTESRLFFVIE 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyQ 758
Cdd:cd05618    102 YVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMC------------K 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SGDHPrqdsmdfsnewGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd05618    170 EGLRP-----------GDTTSTFC------------------------GTPNYIAPEILRGEDYGFSVDWWALGVLMFEM 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  839 LVGQPPF----------------LAQTPLETQMKVinwqtslhipPQAKLSPEASDLIIKLCRGPEDRLG---KNGADEI 899
Cdd:cd05618    215 MAGRSPFdivgssdnpdqntedyLFQVILEKQIRI----------PRSLSVKAASVLKSFLNKDPKERLGchpQTGFADI 284
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  900 KAHPFFKTIDFS-SDLRQQSASYIPKITHPTDTSNFDPV---DPDKLWSDDNE 948
Cdd:cd05618    285 QGHPFFRNVDWDlMEQKQVVPPFKPNISGEFGLDNFDSQftnEPVQLTPDDDD 337
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
597-910 6.88e-45

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: 164.76  E-value: 6.88e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd05632      1 KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGI--FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthds 754
Cdd:cd05632     81 LTIMNGGDLKFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKI------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhPRQDSMdfsnewgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 834
Cdd:cd05632    155 --------PEGESI----------------------------------RGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCL 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  835 LFEMLVGQPPFLAQTPL----ETQMKVINWQTSLhippQAKLSPEASDLI-IKLCRGPEDRLG--KNGADEIKAHPFFKT 907
Cdd:cd05632    193 IYEMIEGQSPFRGRKEKvkreEVDRRVLETEEVY----SAKFSEEAKSICkMLLTKDPKQRLGcqEEGAGEVKRHPFFRN 268

                   ...
gi 1178431733  908 IDF 910
Cdd:cd05632    269 MNF 271
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
604-904 2.64e-43

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: 158.34  E-value: 2.64e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14663      6 RTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwTHDSkyyqsgDHP 763
Cdd:cd14663     86 ELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGL------SALS------EQF 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 RQDSMdfsnewgdpsscrcgdrlkplerraarQHQRClahslvGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVGQ 842
Cdd:cd14663    154 RQDGL---------------------------LHTTC------GTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGY 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  843 PPFLAQTPLETQMKVINWQtsLHIPPQakLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:cd14663    201 LPFDDENLMALYRKIMKGE--FEYPRW--FSPGAKSLIKRiLDPNPSTRI---TVEQIMASPW 256
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
603-904 3.13e-42

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: 155.33  E-value: 3.13e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAH-VKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd14098      5 IDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQlFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG--HIKLTDFGLctgfrwthdskyyqs 759
Cdd:cd14098     85 GGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGL--------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdrlkplerrAARQHQRCLAHSLVGTPNYIAPEVLLRT------GYTQLCDWWSVGV 833
Cdd:cd14098    150 ---------------------------------AKVIHTGTFLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGC 196
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  834 ILFEMLVGQPPF--LAQTPLETQMKvinwQTSLHIPP--QAKLSPEASDLIIKLCR-GPEDRLgknGADEIKAHPF 904
Cdd:cd14098    197 LVYVMLTGALPFdgSSQLPVEKRIR----KGRYTQPPlvDFNISEEAIDFILRLLDvDPEKRM---TAAQALDHPW 265
MobB_LATS2 cd21777
Mob-binding domain found in large tumor suppressor homolog 2 (LATS2); LATS2, also called ...
517-599 1.25e-41

Mob-binding domain found in large tumor suppressor homolog 2 (LATS2); LATS2, also called kinase phosphorylated during mitosis protein, serine/threonine-protein kinase kpm, or Warts-like kinase, is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and for governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. LATS2 belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. LATS proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of LATS2 serine/threonine protein kinase.


Pssm-ID: 439272  Cd Length: 83  Bit Score: 147.14  E-value: 1.25e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  517 KDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMD 596
Cdd:cd21777      1 RDEEKRESRIKSYSPFAFKFYMEQHVENVMKTYQQKLNRRLQLEQEMAKAGLSEAEQEQMRKILYQKESNYNRLKRAKMD 80

                   ...
gi 1178431733  597 KSM 599
Cdd:cd21777     81 KSM 83
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
606-905 1.42e-40

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: 150.45  E-value: 1.42e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd06627      8 IGRGAFGSVYKGLNLNTGEFVAIKQISLEK-IPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqsgdhprq 765
Cdd:cd06627     87 ASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAT------------------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  766 dsmdfsnewgdpsscrcgdRLKPLERRaarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd06627    148 -------------------KLNEVEKD---------ENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPY 199
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  846 LAQTPLETQMKVINWQtslHIPPQAKLSPEASDLIIKlC--RGPEDRLgknGADEIKAHPFF 905
Cdd:cd06627    200 YDLQPMAALFRIVQDD---HPPLPENISPELRDFLLQ-CfqKDPTLRP---SAKELLKHPWL 254
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
600-906 2.22e-40

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: 149.67  E-value: 2.22e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIktlGIGAFGEVCLARKVDTKALYATKTLR---KKDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd06614      5 LEKI---GEGASGEVYKATDRATGKEVAIKKMRlrkQNKELIINEIL-------IMKECKHPNIVDYYDSYLVGDELWVV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIR-MGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdsk 755
Cdd:cd06614     75 MEYMDGGSLTDIITQnPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAA--------- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyqsgdhprqdsmdfsnewgdpsscrcgdRLKPlerraaRQHQRclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd06614    146 -----------------------------QLTK------EKSKR---NSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMC 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  836 FEMLVGQPPFLAQTPLETqMKVInwqTSLHIPP---QAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFK 906
Cdd:cd06614    188 IEMAEGEPPYLEEPPLRA-LFLI---TTKGIPPlknPEKWSPEFKDFLNKcLVKDPEKRP---SAEELLQHPFLK 255
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
600-910 1.02e-39

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: 148.90  E-value: 1.02e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05607      4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLAR--FYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRwthdskyy 757
Cdd:cd05607     84 MNGGDLKYHIYNVGERGIEMERviFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVK-------- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qSGdhprqdsmdfsnewgdpsscrcgdrlKPLERRAarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05607    156 -EG--------------------------KPITQRA-------------GTNGYMAPEILKEESYSYPVDWFAMGCSIYE 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPF-----------LAQTPLETQMKVinwqtslhipPQAKLSPEASDLI-IKLCRGPEDRLGKNG-ADEIKAHPF 904
Cdd:cd05607    196 MVAGRTPFrdhkekvskeeLKRRTLEDEVKF----------EHQNFTEEAKDICrLFLAKKPENRLGSRTnDDDPRKHEF 265

                   ....*.
gi 1178431733  905 FKTIDF 910
Cdd:cd05607    266 FKSINF 271
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
602-904 1.96e-39

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: 147.16  E-value: 1.96e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLR--KKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd06632      4 KGQLLGSGSFGSVYEGFNGDTGDFFAVKEVSlvDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQS 759
Cdd:cd06632     84 VPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGM---------AKHVEA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 GDHPRqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLR--TGYTQLCDWWSVGVILFE 837
Cdd:cd06632    155 FSFAK---------------------------------------SFKGSPYWMAPEVIMQknSGYGLAVDIWSLGCTVLE 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQakLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPF 904
Cdd:cd06632    196 MATGKPPWSQYEGVAAIFKIGNSGELPPIPDH--LSPDAKDFIRLcLQRDPEDR---PTASQLLEHPF 258
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
604-903 4.58e-39

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: 146.77  E-value: 4.58e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEA------DNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd14084     12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRK-FTIGSRREINKPRNIETEIeilkklSHPCIIKIEDFFDAEDDYYIVL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLctgfrwthdS 754
Cdd:cd14084     91 ELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGL---------S 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 KYYQsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhQRCLAHSLVGTPNYIAPEVLL---RTGYTQLCDWWSV 831
Cdd:cd14084    162 KILG---------------------------------------ETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSL 202
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  832 GVILFEMLVGQPPF---LAQTPLETQmkVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHP 903
Cdd:cd14084    203 GVILFICLSGYPPFseeYTQMSLKEQ--ILSGKYTFIPKAWKNVSEEAKDLVKKmLVVDPSRRP---SIEEALEHP 273
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
600-909 1.69e-38

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: 144.66  E-value: 1.69e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLR-KKDVLLRNQVAhvkAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd06623      3 LERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHvDGDEEFRKQLL---RELKTLRSCESPYVVKCYGAFYKEGEISIVLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPESlarfYIAELTCAV-------ESVHKMgfIHRDIKPDNILIDRDGHIKLTDFGLCTGfrwt 751
Cdd:cd06623     80 YMDGGSLADLLKKVGKIPEP----VLAYIARQIlkgldylHTKRHI--IHRDIKPSNLLINSKGEVKIADFGISKV---- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 hdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkpLERRAARqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSV 831
Cdd:cd06623    150 -------------------------------------LENTLDQ------CNTFVGTVTYMSPERIQGESYSYAADIWSL 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  832 GVILFEMLVGQPPFLA--QTPLETQMKVINWQTSLHIPPQAKlSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTI 908
Cdd:cd06623    187 GLTLLECALGKFPFLPpgQPSFFELMQAICDGPPPSLPAEEF-SPEFRDFISAcLQKDPKKRP---SAAELLQHPFIKKA 262

                   .
gi 1178431733  909 D 909
Cdd:cd06623    263 D 263
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
603-905 1.73e-38

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: 144.61  E-value: 1.73e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLA-RKVDTKAL------YATKTLRKKDVLLrnqvahvkAERDILAEADNEWVVRLYYSFQDKDN--L 673
Cdd:cd08217      5 LETIGKGSFGTVRKVrRKSDGKILvwkeidYGKMSEKEKQQLV--------SEVNILRELKHPNIVRYYDRIVDRANttL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDYIPGGDMmSLLIRM-----GIFPESLARFYIAELTCAVESVH-----KMGFIHRDIKPDNILIDRDGHIKLTDFG 743
Cdd:cd08217     77 YIVMEYCEGGDL-AQLIKKckkenQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LCtgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlKPLErraarqHQRCLAHSLVGTPNYIAPEVLLRTGYT 823
Cdd:cd08217    156 LA-----------------------------------------RVLS------HDSSFAKTYVGTPYYMSPELLNEQSYD 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  824 QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKvINWQTSLHIPPQakLSPEASDLI-IKLCRGPEDRlgkNGADEIKAH 902
Cdd:cd08217    189 EKSDIWSLGCLIYELCALHPPFQAANQLELAKK-IKEGKFPRIPSR--YSSELNEVIkSMLNVDPDKR---PSVEELLQL 262

                   ...
gi 1178431733  903 PFF 905
Cdd:cd08217    263 PLI 265
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
604-950 3.51e-38

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: 145.58  E-value: 3.51e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAER---DILAEADNEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd14223      6 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERimlSLVSTGDCPFIVCMSYAFHTPDKLSFILDLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsg 760
Cdd:cd14223     86 NGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGL---------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 dhprqdSMDFSNEwgdpsscrcgdrlKPlerraarqhqrclaHSLVGTPNYIAPEVLLR-TGYTQLCDWWSVGVILFEML 839
Cdd:cd14223    150 ------ACDFSKK-------------KP--------------HASVGTHGYMAPEVLQKgVAYDSSADWFSLGCMLFKLL 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  840 VGQPPFlAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRLG--KNGADEIKAHPFFKTIDFSSDLRQ 916
Cdd:cd14223    197 RGHSPF-RQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLqRDVNRRLGcmGRGAQEVKEEPFFRGLDWQMVFLQ 275
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1178431733  917 QsasYIPKITHPT---------DTSNFDPVDPDKLWSDDNEEE 950
Cdd:cd14223    276 K---YPPPLIPPRgevnaadafDIGSFDEEDTKGIKLLESDQE 315
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
604-962 1.09e-37

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: 144.82  E-value: 1.09e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAER---DILAEADNEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd05633     11 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERimlSLVSTGDCPFIVCMTYAFHTPDKLCFILDLM 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsg 760
Cdd:cd05633     91 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGL---------------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 dhprqdSMDFSNEwgdpsscrcgdrlKPlerraarqhqrclaHSLVGTPNYIAPEVLLR-TGYTQLCDWWSVGVILFEML 839
Cdd:cd05633    155 ------ACDFSKK-------------KP--------------HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  840 VGQPPFlAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRLG--KNGADEIKAHPFFKTIDFSSDLRQ 916
Cdd:cd05633    202 RGHSPF-RQHKTKDKHEIDRMTLTVNVELPDSFSPELKSLLEGLLqRDVSKRLGchGRGAQEVKEHSFFKGIDWQQVYLQ 280
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1178431733  917 QsasYIPKITHPTDTSN-FDPVDPDKLWSDDNEEENVNDTLNGWYKN 962
Cdd:cd05633    281 K---YPPPLIPPRGEVNaADAFDIGSFDEEDTKGIKLLDSDQELYKN 324
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
604-905 1.31e-37

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: 141.62  E-value: 1.31e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14081      7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyYQSGDHP 763
Cdd:cd14081     87 ELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS----------LQPEGSL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 RQdsmdfsnewgdpSSCrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVGQ 842
Cdd:cd14081    157 LE------------TSC--------------------------GSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGA 198
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  843 PPFLAQTPLETQMKVINWQtsLHIPPqaKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14081    199 LPFDDDNLRQLLEKVKRGV--FHIPH--FISPDAQDLLRRmLEVNPEKRI---TIEEIKKHPWF 255
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
600-905 1.59e-37

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: 141.70  E-value: 1.59e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTL---RKKDVLLRNqvahVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd14069      3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVdmkRAPGDCPEN----IKKEVCIQKMLSHKNVVRFYGHRREGEFQYLF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDmmsLLIRM----GIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRwtH 752
Cdd:cd14069     79 LEYASGGE---LFDKIepdvGM-PEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFR--Y 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 DSKyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplERraarqhqrcLAHSLVGTPNYIAPEVLLRTGY-TQLCDWWSV 831
Cdd:cd14069    153 KGK----------------------------------ER---------LLNKMCGTLPYVAPELLAKKKYrAEPVDVWSC 189
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  832 GVILFEMLVGQPPFlaQTPLETQMKVINWQT--SLHIPPQAKLSPEASDLIIKLCR-GPEDRLgknGADEIKAHPFF 905
Cdd:cd14069    190 GIVLFAMLAGELPW--DQPSDSCQEYSDWKEnkKTYLTPWKKIDTAALSLLRKILTeNPNKRI---TIEDIKKHPWY 261
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
600-923 1.60e-37

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: 142.71  E-value: 1.60e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05608      3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDmmsllIRMGI---------FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrw 750
Cdd:cd05608     83 MNGGD-----LRYHIynvdeenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLA----- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkpLERRAARQHQRCLAhslvGTPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd05608    153 --------------------------------------VELKDGQTKTKGYA----GTPGFMAPELLLGEEYDYSVDYFT 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  831 VGVILFEMLVGQPPFLAQTPletqmKVINWQTSLHIPPQA-----KLSPEASDLIIKLC-RGPEDRLG-KNGA-DEIKAH 902
Cdd:cd05608    191 LGVTLYEMIAARGPFRARGE-----KVENKELKQRILNDSvtyseKFSPASKSICEALLaKDPEKRLGfRDGNcDGLRTH 265
                          330       340
                   ....*....|....*....|.
gi 1178431733  903 PFFKTIDFssdlRQQSASYIP 923
Cdd:cd05608    266 PFFRDINW----RKLEAGILP 282
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
606-904 3.82e-36

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: 137.42  E-value: 3.82e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLA-RKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14121      3 LGSGTYATVYKAyRKSGAREVVAVKCVSKSS-LNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MmSLLIRM-GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG--HIKLTDFGLctgfrwthdSKYYQSGD 761
Cdd:cd14121     82 L-SRFIRSrRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGF---------AQHLKPND 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 HprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd14121    152 E---------------------------------------AHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFG 192
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  842 QPPFLAQTPLETQMKVINwQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRLgknGADEIKAHPF 904
Cdd:cd14121    193 RAPFASRSFEELEEKIRS-SKPIEIPTRPELSADCRDLLLRLLqRDPDRRI---SFEEFFAHPF 252
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
602-905 5.48e-36

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: 136.98  E-value: 5.48e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDK--DNLYFVMDY 679
Cdd:cd05118      3 VLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLNDVEGHPNIVKLLDVFEHRggNHLCLVFEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPggdmMSL--LIRMGI--FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID-RDGHIKLTDFGLCtgfRWTHDS 754
Cdd:cd05118     83 MG----MNLyeLIKDYPrgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLA---RSFTSP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 KYYQSgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLR-TGYTQLCDWWSVGV 833
Cdd:cd05118    156 PYTPY----------------------------------------------VATRWYRAPEVLLGaKPYGSSIDIWSLGC 189
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  834 ILFEMLVGQPPFLAQTPLETQMKVInwqtslhippqAKL-SPEASDLIIKLCR-GPEDRLgknGADEIKAHPFF 905
Cdd:cd05118    190 ILAELLTGRPLFPGDSEVDQLAKIV-----------RLLgTPEALDLLSKMLKyDPAKRI---TASQALAHPYF 249
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
592-906 1.60e-35

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: 136.03  E-value: 1.60e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  592 RAKMDKsmFVKIktlGIGAFGEVCLARKVDTKALYATKT--LRKKD--VLLRNQVAhvkaerdILAEADNEWVVRLYYSF 667
Cdd:cd06648      6 RSDLDN--FVKI---GEGSTGIVCIATDKSTGRQVAVKKmdLRKQQrrELLFNEVV-------IMRDYQHPNIVEMYSSY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  668 QDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTcAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTG 747
Cdd:cd06648     74 LVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCRAVLK-ALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 FrwthdskyyqSGDHPRqdsmdfsnewgdpsscrcgdrlkpleRRaarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCD 827
Cdd:cd06648    153 V----------SKEVPR--------------------------RK-----------SLVGTPYWMAPEVISRLPYGTEVD 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  828 WWSVGVILFEMLVGQPPFLAQTPLETqMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFK 906
Cdd:cd06648    186 IWSLGIMVIEMVDGEPPYFNEPPLQA-MKRIRDNEPPKLKNLHKVSPRLRSFLDRmLVRDPAQRA---TAAELLNHPFLA 261
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
603-905 2.89e-35

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: 135.39  E-value: 2.89e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLA--RKVDTKALYATKTLRKKdvllrnqvahvKAERD-----------ILAEADNEWVVRLYYSFQD 669
Cdd:cd14080      5 GKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKK-----------KAPKDflekflpreleILRKLRHPNIIQVYSIFER 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  670 KDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfr 749
Cdd:cd14080     74 GSKVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGF----- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 wthdSKYyqsgdHPRQDSMDFSNEWgdpsscrCGDrlkplerrAArqhqrclahslvgtpnYIAPEVLLRTGYT-QLCDW 828
Cdd:cd14080    149 ----ARL-----CPDDDGDVLSKTF-------CGS--------AA----------------YAAPEILQGIPYDpKKYDI 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  829 WSVGVILFEMLVGQPPF----LAQTPLETQMKVINWQTSLHippqaKLSPEASDLIIKLCR-GPEDRLgknGADEIKAHP 903
Cdd:cd14080    189 WSLGVILYIMLCGSMPFddsnIKKMLKDQQNRKVRFPSSVK-----KLSPECKDLIDQLLEpDPTKRA---TIEEILNHP 260

                   ..
gi 1178431733  904 FF 905
Cdd:cd14080    261 WL 262
MobB_LATS cd21774
Mob-binding domain found in the large tumor suppressor (LATS) subfamily; LATS was originally ...
534-595 7.66e-35

Mob-binding domain found in the large tumor suppressor (LATS) subfamily; 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. This subfamily belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. LATS proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of LATS subfamily serine/threonine protein kinases.


Pssm-ID: 439269  Cd Length: 62  Bit Score: 126.60  E-value: 7.66e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  534 FKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKM 595
Cdd:cd21774      1 FKFYMEQHVENLLKSHKEREKRRRQLEKEMSKVGLSEEAREQMRKLLSQKESNYIRLKRAKM 62
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
604-904 8.34e-35

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: 133.93  E-value: 8.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAH-VKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14116     11 RPLGKGKFGNVYLAREKQSKFILALKVLFKAQ-LEKAGVEHqLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrWTHDSkyyqsgdh 762
Cdd:cd14116     90 GTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG------WSVHA-------- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdPSScrcgdrlkpleRRAarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14116    156 --------------PSS-----------RRT----------TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGK 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  843 PPFLAQTPLETQMKV--INWQTSLHIppqaklSPEASDLIIKLCR-GPEDRLGKNGADEikaHPF 904
Cdd:cd14116    201 PPFEANTYQETYKRIsrVEFTFPDFV------TEGARDLISRLLKhNPSQRPMLREVLE---HPW 256
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
606-904 1.69e-34

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: 132.88  E-value: 1.69e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLAR-KVDTKALYATKTLRKKDvLLRNQVAHVKaERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14120      1 IGHGAFAVVFKGRhRKKPDLPVAIKCITKKN-LSKSQNLLGK-EIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG---------HIKLTDFGLctgfrwthdSK 755
Cdd:cd14120     79 LADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGF---------AR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSGDhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd14120    150 FLQDGM---------------------------------------MAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIV 190
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  836 FEMLVGQPPFLAQTPLETQ---MKVINWQTSlhIPPQAklSPEASDLIIKLC-RGPEDRLgknGADEIKAHPF 904
Cdd:cd14120    191 YQCLTGKAPFQAQTPQELKafyEKNANLRPN--IPSGT--SPALKDLLLGLLkRNPKDRI---DFEDFFSHPF 256
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
602-905 2.95e-34

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: 132.09  E-value: 2.95e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLR--KKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd06625      4 QGKLLGQGAFGQVYLCYDADTGRELAVKQVEidPINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthDSKYYQs 759
Cdd:cd06625     84 MPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFG---------ASKRLQ- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdrlkplerrAARQHQRClaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd06625    154 ---------------------------------TICSSTGM--KSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEML 198
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSLHIPPQakLSPEASDLiIKLC--RGPEDRlgkNGADEIKAHPFF 905
Cdd:cd06625    199 TTKPPWAEFEPMAAIFKIATQPTNPQLPPH--VSEDARDF-LSLIfvRNKKQR---PSAEELLSHSFV 260
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
606-905 6.76e-34

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: 131.23  E-value: 6.76e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTlrkkdVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG-- 683
Cdd:cd06612     11 LGEGSYGSVYKAIHKETGQVVAIKV-----VPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAGsv 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 -DMMSllIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdskyyqsgdh 762
Cdd:cd06612     86 sDIMK--ITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQL-------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prQDSMDFSNewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd06612    150 --TDTMAKRN-------------------------------TVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGK 196
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  843 PPFLAQTPLETQMKVINWqtslhiPPQA-----KLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPFF 905
Cdd:cd06612    197 PPYSDIHPMRAIFMIPNK------PPPTlsdpeKWSPEFNDFVKKcLVKDPEER---PSAIQLLQHPFI 256
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
606-903 1.24e-33

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: 130.08  E-value: 1.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAhVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14006      1 LGRGRFGVVKRCIEKATGREFAAKFIPKRD---KKKEA-VLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID--RDGHIKLTDFGLCTgfrwthdskyyqsgdhp 763
Cdd:cd14006     77 LDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLAR----------------- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rqdsmdfsnewgdpsscrcgdRLKPLErraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQP 843
Cdd:cd14006    140 ---------------------KLNPGE----------ELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLS 188
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  844 PFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHP 903
Cdd:cd14006    189 PFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKlLVKEPRKRP---TAQEALQHP 246
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
600-914 1.75e-33

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 130.44  E-value: 1.75e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKT--LRKKDvllrNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd06609      3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVidLEEAE----DEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLiRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyy 757
Cdd:cd06609     79 EYCGGGSVLDLL-KPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGV------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qSGDhprqdsmdfsnewgdpsscrcgdrlkpLERRAARqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd06609    145 -SGQ---------------------------LTSTMSK------RNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIE 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPletqMKVInWQTSLHIPPQ---AKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTIDFSSD 913
Cdd:cd06609    191 LAKGEPPLSDLHP----MRVL-FLIPKNNPPSlegNKFSKPFKDFVELcLNKDPKERP---SAKELLKHKFIKKAKKTSY 262

                   .
gi 1178431733  914 L 914
Cdd:cd06609    263 L 263
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
606-904 2.98e-33

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: 129.38  E-value: 2.98e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKdvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14167     11 LGTGAFSEVVLAEEKRTQKLVAIKCIAKK--ALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL---IDRDGHIKLTDFGLctgfrwthdSKYYQSGDh 762
Cdd:cd14167     89 FDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL---------SKIEGSGS- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14167    159 --------------------------------------VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGY 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  843 PPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRlgkNGADEIKAHPF 904
Cdd:cd14167    201 PPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIQHLMeKDPEKR---FTCEQALQHPW 260
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
603-905 3.29e-33

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: 129.96  E-value: 3.29e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKK-----DVLlrnQVAHVKAERDILAeadNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd07830      4 IKQLGDGTFGSVYLARNKETGELVAIKKMKKKfysweECM---NLREVKSLRKLNE---HPNIVKLKEVFRENDELYFVF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGG--DMMSLliRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDS 754
Cdd:cd07830     78 EYMEGNlyQLMKD--RKGKpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLA---REIRSR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 KYYQsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLR-TGYTQLCDWWSVGV 833
Cdd:cd07830    153 PPYT---------------------------------------------DYVSTRWYRAPEILLRsTSYSSPVDIWALGC 187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  834 ILFEMLVGQPPFLAQTPLETQMKVI---------NW------------------QTSLH-IPPQAklSPEASDLIIKLCR 885
Cdd:cd07830    188 IMAELYTLRPLFPGSSEIDQLYKICsvlgtptkqDWpegyklasklgfrfpqfaPTSLHqLIPNA--SPEAIDLIKDMLR 265
                          330       340
                   ....*....|....*....|.
gi 1178431733  886 -GPEDRLgknGADEIKAHPFF 905
Cdd:cd07830    266 wDPKKRP---TASQALQHPYF 283
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
597-904 5.36e-33

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: 129.34  E-value: 5.36e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKK----DVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDN 672
Cdd:cd14166      2 RETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSplsrDSSLENEIA-------VLKRIKHENIVTLEDIYESTTH 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLctgfr 749
Cdd:cd14166     75 YYLVMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGL----- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 wthdSKYYQSGdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWW 829
Cdd:cd14166    150 ----SKMEQNG----------------------------------------IMSTACGTPGYVAPEVLAQKPYSKAVDCW 185
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  830 SVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRLgknGADEIKAHPF 904
Cdd:cd14166    186 SIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRHLLeKNPSKRY---TCEKALSHPW 258
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
600-890 5.89e-33

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: 128.95  E-value: 5.89e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvlLRN-QVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd13996      8 FEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIR-----LTEkSSASEKVLREVkaLAKLNHPNIVRYYTAWVEEPPLYIQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGIFP---ESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID-RDGHIKLTDFGLCTGFRWTH 752
Cdd:cd13996     83 MELCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATSIGNQK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 DSKYYQSGDHPRQDSMDFSNewgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd13996    163 RELNNLNNNNNGNTSNNSVG---------------------------------IGTPLYASPEQLDGENYNEKADIYSLG 209
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  833 VILFEMLVgqppflaqtPLETQMKVINWQTSLH---IPPQAKLS-PEASDLIIKLC-RGPEDR 890
Cdd:cd13996    210 IILFEMLH---------PFKTAMERSTILTDLRngiLPESFKAKhPKEADLIQSLLsKNPEER 263
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
607-904 7.09e-33

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: 128.57  E-value: 7.09e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  607 GIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRlYYSFQ-DKDNLYFVMDYIPGGDM 685
Cdd:cd06626      9 GEGTFGKVYTAVNLDTGELMAMKEIRFQD-NDPKTIKEIADEMKVLEGLDHPNLVR-YYGVEvHREEVYIFMEYCQEGTL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthDSKYYQSGdhprq 765
Cdd:cd06626     87 EELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG---------SAVKLKNN----- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  766 dsmdfsnewgdpsscrcGDRLKPLErraarqhqrclAHSLVGTPNYIAPEVLL---RTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd06626    153 -----------------TTTMAPGE-----------VNSLVGTPAYMAPEVITgnkGEGHGRAADIWSLGCVVLEMATGK 204
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  843 PPFlaqTPLETqmkviNWQTSLH--------IPPQAKLSPEASDLiIKLC--RGPEDRLgknGADEIKAHPF 904
Cdd:cd06626    205 RPW---SELDN-----EWAIMYHvgmghkppIPDSLQLSPEGKDF-LSRCleSDPKKRP---TASELLDHPF 264
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
603-905 1.14e-32

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: 127.86  E-value: 1.14e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKT--LRKKDVLLRNQVAHVKAerdiLAEADNEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd06610      6 IEVIGSGATAVVYAAYCLPKKEKVAIKRidLEKCQTSMDELRKEIQA----MSQCNHPNVVSYYTSFVVGDELWLVMPLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGG---DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdskyY 757
Cdd:cd06610     82 SGGsllDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASL--------A 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDhprqdsmdfsnewgdpsscrcgdrlkplERRAARqhqrclaHSLVGTPNYIAPEVLLR-TGYTQLCDWWSVGVILF 836
Cdd:cd06610    154 TGGD----------------------------RTRKVR-------KTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAI 198
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVINwqtslHIPPQ-------AKLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPFF 905
Cdd:cd06610    199 ELATGAAPYSKYPPMKVLMLTLQ-----NDPPSletgadyKKYSKSFRKMISLcLQKDPSKR---PTAEELLKHKFF 267
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
600-904 1.76e-32

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: 127.50  E-value: 1.76e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLR-------KKDVLLRNQVAHVKAERDILAEADNEWVVRlYYSFQDKDN 672
Cdd:cd06629      3 WVKGELIGKGTYGRVYLAMNATTGEMLAVKQVElpktssdRADSRQKTVVDALKSEIDTLKDLDHPNIVQ-YLGFEETED 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFV-MDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwt 751
Cdd:cd06629     82 YFSIfLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFG-------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 hdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkpLERRAARQHQRCLAHSLVGTPNYIAPEVL--LRTGYTQLCDWW 829
Cdd:cd06629    154 -------------------------------------ISKKSDDIYGNNGATSMQGSVFWMAPEVIhsQGQGYSAKVDIW 196
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  830 SVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRlgkNGADEIKAHPF 904
Cdd:cd06629    197 SLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPVPEDVNLSPEALDFLNACFAiDPRDR---PTAAELLSHPF 269
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
604-905 2.05e-32

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: 127.00  E-value: 2.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14079      8 KTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQSGDHP 763
Cdd:cd14079     88 ELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGL---------SNIMRDGEFL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 RqdsmdfsnewgdpSSCrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVGQ 842
Cdd:cd14079    159 K-------------TSC--------------------------GSPNYAAPEVISGKLYAgPEVDVWSCGVILYALLCGS 199
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  843 PPFLAQTpLETQMKVINwQTSLHIPpqAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14079    200 LPFDDEH-IPNLFKKIK-SGIYTIP--SHLSPGARDLIKRmLVVDPLKRI---TIPEIRQHPWF 256
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
597-890 2.33e-32

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: 126.72  E-value: 2.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd14083      2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKK--ALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLctgfrwthd 753
Cdd:cd14083     80 MELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGL--------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 SKYYQSGDhprqdsMDfsnewgdpSSCrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGV 833
Cdd:cd14083    151 SKMEDSGV------MS--------TAC--------------------------GTPGYVAPEVLAQKPYGKAVDCWSIGV 190
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  834 ILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKL-CRGPEDR 890
Cdd:cd14083    191 ISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDFIRHLmEKDPNKR 248
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
604-903 1.22e-31

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: 124.75  E-value: 1.22e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRK-----KDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd14095      6 RVIGDGNFAVVKECRDKATDKEYALKIIDKakckgKEHMIENEVA-------ILRRVKHPNIVQLIEEYDTDTELYLVME 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG----HIKLTDFGLCTgfrwthds 754
Cdd:cd14095     79 LVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLAT-------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprqdsmdfsnEWGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVI 834
Cdd:cd14095    151 ------------------EVKEPLFTVC------------------------GTPTYVAPEILAETGYGLKVDIWAAGVI 188
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  835 LFEMLVGQPPFLAQTPLETQM--KVINWQTSLHIPPQAKLSPEASDLIIKLCRG-PEDRLgknGADEIKAHP 903
Cdd:cd14095    189 TYILLCGFPPFRSPDRDQEELfdLILAGEFEFLSPYWDNISDSAKDLISRMLVVdPEKRY---SAGQVLDHP 257
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
606-845 1.73e-31

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: 124.34  E-value: 1.73e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEV--CLARKVDTKALYATKTLRKKD--VLLRNQVAHVKAERDILAEADNEWVVRLYYSFQD-KDNLYFVMDYI 680
Cdd:cd13994      1 IGKGATSVVriVTKKNPRSGVLYAVKEYRRRDdeSKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEYC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSkyyqsg 760
Cdd:cd13994     81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEK------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 dhprqdsmdfsnewgdpsscrcgdrLKPLERRaarqhqrclahsLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEML 839
Cdd:cd13994    155 -------------------------ESPMSAG------------LCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALF 197

                   ....*.
gi 1178431733  840 VGQPPF 845
Cdd:cd13994    198 TGRFPW 203
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
600-890 1.96e-31

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: 124.06  E-value: 1.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATK--TLRKKDVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd08529      2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKqiDISRMSRKMREEAID---EARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIR-MG-IFPESLA-RFYIaELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthds 754
Cdd:cd08529     79 EYAENGDLHSLIKSqRGrPLPEDQIwKFFI-QTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKIL------ 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprQDSMDFsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 834
Cdd:cd08529    152 ----------SDTTNF-------------------------------AQTIVGTPYYLSPELCEDKPYNEKSDVWALGCV 190
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  835 LFEMLVGQPPFLAQTPLETQMKVINwqtSLHIPPQAKLSPEASDLIIK-LCRGPEDR 890
Cdd:cd08529    191 LYELCTGKHPFEAQNQGALILKIVR---GKYPPISASYSQDLSQLIDScLTKDYRQR 244
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
603-845 3.26e-31

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: 123.27  E-value: 3.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14073      6 LETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQSGDh 762
Cdd:cd14073     86 GELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGL---------SNLYSKDK- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVG 841
Cdd:cd14073    156 --------------------------------------LLQTFCGSPLYASPEIVNGTPYQgPEVDCWSLGVLLYTLVYG 197

                   ....
gi 1178431733  842 QPPF 845
Cdd:cd14073    198 TMPF 201
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
606-882 4.49e-31

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: 122.65  E-value: 4.49e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKAlyATKTLRKKDVLLRNQVAhVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd13999      1 IGSGSFGEVYKGKWRGTDV--AIKKLKVEDDNDELLKE-FRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqsgdhpr 764
Cdd:cd13999     78 YDLLHKKKIpLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSR------------------ 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  765 qdsmdFSNEWGDPSScrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPP 844
Cdd:cd13999    140 -----IKNSTTEKMT------------------------GVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVP 190
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1178431733  845 FLAQTPLetQMKVINWQTSLHIPPQAKLSPEASDLIIK 882
Cdd:cd13999    191 FKELSPI--QIAAAVVQKGLRPPIPPDCPPELSKLIKR 226
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
599-904 5.12e-31

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: 123.03  E-value: 5.12e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKTLR------KKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDN 672
Cdd:cd06628      1 KWIKGALIGSGSFGSVYLGMNASSGELMAVKQVElpsvsaENKDRKKSMLDALQREIALLRELQHENIVQYLGSSSDANH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwth 752
Cdd:cd06628     81 LNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGI-------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dSKYYQSgdhprqDSMDFSNEWGDPsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd06628    153 -SKKLEA------NSLSTKNNGARP--------------------------SLQGSVFWMAPEVVKQTSYTRKADIWSLG 199
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  833 VILFEMLVGQPPFlaqtPLETQMKVI---NWQTSLHIPPQAklSPEASDLIIKLCRgpEDRLGKNGADEIKAHPF 904
Cdd:cd06628    200 CLVVEMLTGTHPF----PDCTQMQAIfkiGENASPTIPSNI--SSEARDFLEKTFE--IDHNKRPTADELLKHPF 266
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
603-904 6.45e-31

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: 123.70  E-value: 6.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVclARKVDTKALY---ATKTLRKKDV----LLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYF 675
Cdd:cd14096      6 INKIGEGAFSNV--YKAVPLRNTGkpvAIKVVRKADLssdnLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRdghikltdfglcTGFRWTHDSK 755
Cdd:cd14096     84 VLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEP------------IPFIPSIVKL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSGDHPRQDSMDFSNEWGdpsSCRCGdRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd14096    152 RKADDDETKVDEGEFIPGVG---GGGIG-IVKLADFGLSKQVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVL 227
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  836 FEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:cd14096    228 YTLLCGFPPFYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHlLTVDPAKRY---DIDEFLAHPW 294
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
606-909 1.03e-30

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: 122.92  E-value: 1.03e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRnqvAHVKAER--DILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14086      9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSAR---DHQKLEReaRICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCTGFrwthdskyyqSG 760
Cdd:cd14086     86 ELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEV----------QG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 DHPRqdsmdfsneWgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 840
Cdd:cd14086    156 DQQA---------W----------------------------FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLV 198
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  841 GQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTID 909
Cdd:cd14086    199 GYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQmLTVNPAKRI---TAAEALKHPWICQRD 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
600-903 1.49e-30

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: 121.34  E-value: 1.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYAtktLRKKDVLLRNQvahvkAERD-------ILAEADNEWVVRLYYSFQDKDN 672
Cdd:cd08530      2 FKVLKKLGKGSYGSVYKVKRLSDNQVYA---LKEVNLGSLSQ-----KEREdsvneirLLASVNHPNIIRYKEAFLDGNR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMG----IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgf 748
Cdd:cd08530     74 LCIVMEYAPFGDLSKLISKRKkkrrLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGI---- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdSKYYQSGdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDW 828
Cdd:cd08530    150 -----SKVLKKN----------------------------------------LAKTQIGTPLYAAPEVWKGRPYDYKSDI 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  829 WSVGVILFEMLVGQPPFLAQTPLETQMKVINWQtslhIPPqakLSPEASDLIIKLCR-----GPEDRLgknGADEIKAHP 903
Cdd:cd08530    185 WSLGCLLYEMATFRPPFEARTMQELRYKVCRGK----FPP---IPPVYSQDLQQIIRsllqvNPKKRP---SCDKLLQSP 254
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
600-905 2.21e-30

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: 122.02  E-value: 2.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIktlGIGAFGEVCLARKVDTKALYATKT--LRKKD--VLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYF 675
Cdd:cd06659     26 YVKI---GEGSTGVVCIAREKHSGRQVAVKMmdLRKQQrrELLFNEVV-------IMRDYQHPNVVEMYKSYLVGEELWV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIFPESLARFYIAELTcAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdsk 755
Cdd:cd06659     96 LMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQ-ALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQI------- 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyqSGDHPRQdsmdfsnewgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd06659    168 ---SKDVPKR-------------------------------------KSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMV 207
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  836 FEMLVGQPPFLAQTPLETqMKVINWQTslhiPPQA----KLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPFF 905
Cdd:cd06659    208 IEMVDGEPPYFSDSPVQA-MKRLRDSP----PPKLknshKASPVLRDFLERmLVRDPQER---ATAQELLDHPFL 274
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
597-891 3.75e-30

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: 120.77  E-value: 3.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIK-TLGIGAFGEVCLARKVDTKALYATKTLRKKdvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYF 675
Cdd:cd14169      1 INSVYELKeKLGEGAFSEVVLAQERGSQRLVALKCIPKK--ALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID---RDGHIKLTDFGLctgfrwth 752
Cdd:cd14169     79 AMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGL-------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dSKYYQSGdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd14169    151 -SKIEAQG----------------------------------------MLSTACGTPGYVAPELLEQKPYGKAVDVWAIG 189
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRL 891
Cdd:cd14169    190 VISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIRHLLeRDPEKRF 249
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
606-903 3.98e-30

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: 120.93  E-value: 3.98e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVL--------------------LRNQVAHVKAERDILAEADNEWVVRLYY 665
Cdd:cd14118      2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLkqagffrrppprrkpgalgkPLDPLDRVYREIAILKKLDHPNVVKLVE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  666 SFQD--KDNLYFVMDYIPGGDMMSLlIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG 743
Cdd:cd14118     82 VLDDpnEDNLYMVFELVDKGAVMEV-PTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LCTGFrwthdskyyqSGDhprqdsmDFSNEwgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYT 823
Cdd:cd14118    161 VSNEF----------EGD-------DALLS------------------------------STAGTPAFMAPEALSESRKK 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  824 Q---LCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINwqTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEI 899
Cdd:cd14118    194 FsgkALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKT--DPVVFPDDPVVSEQLKDLILRmLDKNPSERI---TLPEI 268

                   ....
gi 1178431733  900 KAHP 903
Cdd:cd14118    269 KEHP 272
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
606-849 5.71e-30

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: 119.96  E-value: 5.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLlRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14097      9 LGQGSFGVVIEATHKETQTKWAIKKINREKAG-SSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGEL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG-------HIKLTDFGLCTgfrwthdSKYYQ 758
Cdd:cd14097     88 KELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSV-------QKYGL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SGDHPRqdsmdfsnewgdpSSCrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd14097    161 GEDMLQ-------------ETC--------------------------GTPIYMAPEVISAHGYSQQCDIWSIGVIMYML 201
                          250
                   ....*....|.
gi 1178431733  839 LVGQPPFLAQT 849
Cdd:cd14097    202 LCGEPPFVAKS 212
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
605-905 5.92e-30

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: 119.89  E-value: 5.92e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  605 TLGIGAFGEVCLARKVDTKALYATKTLRKK----DVLLRnqvaHVKAERDILAEADNEWVVRLYYSFQDKDN-LYFVMDY 679
Cdd:cd14165      8 NLGEGSYAKVKSAYSERLKCNVAIKIIDKKkapdDFVEK----FLPRELEILARLNHKSIIKTYEIFETSDGkVYIVMEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqs 759
Cdd:cd14165     84 GVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFG---------------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdFSnewgdpsscrcgdrlKPLERRAarQHQRCLAHSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEM 838
Cdd:cd14165    148 ----------FS---------------KRCLRDE--NGRIVLSKTFCGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIM 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  839 LVGQPPFLAQTPLEtqMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14165    201 VCGSMPYDDSNVKK--MLKIQKEHRVRFPRSKNLTSECKDLIYRlLQPDVSQRL---CIDEVLSHPWL 263
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
599-906 6.80e-30

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: 120.69  E-value: 6.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKtlrkKdVLlrnQVAHVKA-ERDILAEADNEWVVRLYYSF------QDKD 671
Cdd:cd14137      5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIK----K-VL---QDKRYKNrELQIMRRLKHPNIVKLKYFFyssgekKDEV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPG--GDMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD-GHIKLTDFGlctg 747
Cdd:cd14137     77 YLNLVMEYMPEtlYRVIRHYSKNKqTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDFG---- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 frwthDSKyyqsgdhprqdsmdfsnewgdpsscrcgdRLKPlerraarqhqrclahslvGTPN--YI------APEVLLR 819
Cdd:cd14137    153 -----SAK-----------------------------RLVP------------------GEPNvsYIcsryyrAPELIFG 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  820 -TGYTQLCDWWSVGVILFEMLVGQPPFLAQ--------------TPLETQMKVINWQTSLHIPPQ-----------AKLS 873
Cdd:cd14137    181 aTDYTTAIDIWSAGCVLAELLLGQPLFPGEssvdqlveiikvlgTPTREQIKAMNPNYTEFKFPQikphpwekvfpKRTP 260
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1178431733  874 PEASDLIIKLCR-GPEDRLgknGADEIKAHPFFK 906
Cdd:cd14137    261 PDAIDLLSKILVyNPSKRL---TALEALAHPFFD 291
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
591-904 1.15e-29

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: 120.15  E-value: 1.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  591 KRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDK 670
Cdd:cd14168      3 KQVEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKK--ALKGKESSIENEIAVLRKIKHENIVALEDIYESP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLctg 747
Cdd:cd14168     81 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGL--- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 frwthdSKYYQSGDhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCD 827
Cdd:cd14168    158 ------SKMEGKGD---------------------------------------VMSTACGTPGYVAPEVLAQKPYSKAVD 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  828 WWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIikLCRGPEDRLGKNGADEIKAHPF 904
Cdd:cd14168    193 CWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDSAKDFI--RNLMEKDPNKRYTCEQALRHPW 267
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
604-905 1.89e-29

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: 118.17  E-value: 1.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKK----DVLLRnqvaHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd14162      6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKkapeDYLQK----FLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqs 759
Cdd:cd14162     82 AENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGF--------------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsSCRCgdrLKPLERRaarqhqRCLAHSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEM 838
Cdd:cd14162    147 -------------------ARGV---MKTKDGK------PKLSETYCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTM 198
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  839 LVGQPPFlAQTPLETQMKVInwQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14162    199 VYGRLPF-DDSNLKVLLKQV--QRRVVFPKNPTVSEECKDLILRMLSPVKKRI---TIEEIKRDPWF 259
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
604-905 2.35e-29

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 118.22  E-value: 2.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRK----KDVllRNQVAHvkaERDILAEA-DNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd14106     14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKrrrgQDC--RNEILH---EIAVLELCkDCPRVVNLHEVYETRSELILILE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL---IDRDGHIKLTDFGLctgfrwthdSK 755
Cdd:cd14106     89 LAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILltsEFPLGDIKLCDFGI---------SR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSGDHPRQdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd14106    160 VIGEGEEIRE---------------------------------------ILGTPDYVAPEILSYEPISLATDMWSIGVLT 200
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  836 FEMLVGQPPFLAQTPLETQMKVInwQTSLHIPPQ--AKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14106    201 YVLLTGHSPFGGDDKQETFLNIS--QCNLDFPEElfKDVSPLAIDFIKRlLVKDPEKRL---TAKECLEHPWL 268
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
606-904 2.40e-29

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: 118.04  E-value: 2.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14186      9 LGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEM 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLI-RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYyqsgdhpr 764
Cdd:cd14186     89 SRYLKnRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHF-------- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  765 qdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPP 844
Cdd:cd14186    161 ---------------------------------------TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPP 201
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  845 FLAQTPLETQMKVInwqTSLHIPPqAKLSPEASDLIIKLCR-GPEDRLgknGADEIKAHPF 904
Cdd:cd14186    202 FDTDTVKNTLNKVV---LADYEMP-AFLSREAQDLIHQLLRkNPADRL---SLSSVLDHPF 255
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
587-919 2.51e-29

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: 118.98  E-value: 2.51e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  587 YIRLKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYS 666
Cdd:cd06644      1 YEHVRRDLDPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKS---EEELEDYMVEIEILATCNHPYIVKLLGA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  667 FQDKDNLYFVMDYIPGG--DMMSLLIRMGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd06644     78 FYWDGKLWIMIEFCPGGavDAIMLELDRGL-TEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  745 ctgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrCGDRLKPLERRaarqhqrclaHSLVGTPNYIAPEVLL-----R 819
Cdd:cd06644    157 -------------------------------------SAKNVKTLQRR----------DSFIGTPYWMAPEVVMcetmkD 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  820 TGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPqAKLSPEASDLI-IKLCRGPEDRlgkNGADE 898
Cdd:cd06644    190 TPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQP-SKWSMEFRDFLkTALDKHPETR---PSAAQ 265
                          330       340
                   ....*....|....*....|.
gi 1178431733  899 IKAHPFFKTIDFSSDLRQQSA 919
Cdd:cd06644    266 LLEHPFVSSVTSNRPLRELVA 286
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
604-845 3.14e-29

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: 117.48  E-value: 3.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDvlLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14078      9 ETIGSGGFAKVKLATHILTGEKVAIKIMDKKA--LGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqsgdhp 763
Cdd:cd14078     87 ELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCA----------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rqdsmdfsnewgdpsscrcgdrlKPlerRAARQHQrclAHSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVGQ 842
Cdd:cd14078    150 -----------------------KP---KGGMDHH---LETCCGSPAYAAPELIQGKPYIgSEADVWSMGVLLYALLCGF 200

                   ...
gi 1178431733  843 PPF 845
Cdd:cd14078    201 LPF 203
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
604-906 3.16e-29

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: 118.04  E-value: 3.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14117     12 RPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrWTHDSkyyqsgdhp 763
Cdd:cd14117     92 ELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFG------WSVHA--------- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rqdsmdfsnewgdPSscrcgdrlkpLERRaarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQP 843
Cdd:cd14117    157 -------------PS----------LRRR-----------TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMP 202
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  844 PFLAQTPLETQMKVINwqTSLHIPPQakLSPEASDLIIKLCR-GPEDRLGKNGadeIKAHPFFK 906
Cdd:cd14117    203 PFESASHTETYRRIVK--VDLKFPPF--LSDGSRDLISKLLRyHPSERLPLKG---VMEHPWVK 259
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
604-904 3.38e-29

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: 117.74  E-value: 3.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDvlLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14185      6 RTIGDGNFAVVKECRHWNENQEYAMKIIDKSK--LKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI----DRDGHIKLTDFGLctgfrwthdSKYYqs 759
Cdd:cd14185     84 DLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGL---------AKYV-- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdrLKPLerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14185    153 --------------------------TGPI-------------FTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILL 193
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  840 VGQPPFlaQTPLETQMKVINWQTSLH---IPPQ-AKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:cd14185    194 CGFPPF--RSPERDQEELFQIIQLGHyefLPPYwDNISEAAKDLISRlLVVDPEKRY---TAKQVLQHPW 258
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
606-904 4.12e-29

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: 117.78  E-value: 4.12e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKdvllrnQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14010      8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKS------KRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgdhprq 765
Cdd:cd14010     82 ETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGL--------------------- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  766 dsmdfsnewgdpsSCRCGDRLKPLERRAA---RQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14010    141 -------------ARREGEILKELFGQFSdegNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGK 207
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  843 PPFLAQTPLETQMKVINWQTSLHIPPQ-AKLSPEASDLIIKLC-RGPEDRLgknGADEIKAHPF 904
Cdd:cd14010    208 PPFVAESFTELVEKILNEDPPPPPPKVsSKPSPDFKSLLKGLLeKDPAKRL---SWDELVKHPF 268
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
597-905 6.59e-29

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: 117.03  E-value: 6.59e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKAL-YATKTLRKKDvLLRNQVAHVKaERDILAEADNEWVVRLYySFQDKDN-LY 674
Cdd:cd14202      1 KFEFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKN-LAKSQTLLGK-EIKILKELKHENIVALY-DFQEIANsVY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG---------HIKLTDFGLc 745
Cdd:cd14202     78 LVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGF- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  746 tgfrwthdSKYYQSGdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrCLAHSLVGTPNYIAPEVLLRTGYTQL 825
Cdd:cd14202    157 --------ARYLQNN---------------------------------------MMAATLCGSPMYMAPEVIMSQHYDAK 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 CDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14202    190 ADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETSSHLRQLLLGLLQRNQKDRM---DFDEFFHHPFL 266
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
600-905 7.60e-29

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: 116.65  E-value: 7.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd14188      3 YCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqs 759
Cdd:cd14188     83 CSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAA------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdRLKPLERRaarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14188    150 -------------------------RLEPLEHR---------RRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTML 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSLhipPQAKLSPEASDLIIKLCRGPEDRlgkNGADEIKAHPFF 905
Cdd:cd14188    196 LGRPPFETTNLKETYRCIREARYSL---PSSLLAPAKHLIASMLSKNPEDR---PSLDEIIRHDFF 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
607-904 1.48e-28

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: 115.43  E-value: 1.48e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  607 GIGAFGEVCLARKVDTKALYATKTLRKK---DVLLRNqvahVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGg 683
Cdd:cd14002     10 GEGSFGKVYKGRRKYTGQVVALKFIPKRgksEKELRN----LRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQG- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdhp 763
Cdd:cd14002     85 ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFA------------------ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rqdsmdfsnewgdpsscrcgdrlkplerRAARQHQRCLaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQP 843
Cdd:cd14002    147 ----------------------------RAMSCNTLVL-TSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQP 197
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  844 PFLAQTPLE-TQMKV---INWQTSlhippqakLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:cd14002    198 PFYTNSIYQlVQMIVkdpVKWPSN--------MSPEFKSFLQGlLNKDPSKRL---SWPDLLEHPF 252
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
599-905 1.56e-28

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: 115.48  E-value: 1.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd06613      1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEP---GDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWThdskyyq 758
Cdd:cd06613     78 YCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTAT------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqdsmdfsnewgdpsscrcgdrlkpLERRaarqhqrclaHSLVGTPNYIAPEVLL---RTGYTQLCDWWSVGVIL 835
Cdd:cd06613    151 ------------------------------IAKR----------KSFIGTPYWMAPEVAAverKGGYDGKCDIWALGITA 190
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  836 FEMLVGQPPFLAQTPletqMKVINWQTSLHIPP-----QAKLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPFF 905
Cdd:cd06613    191 IELAELQPPMFDLHP----MRALFLIPKSNFDPpklkdKEKWSPDFHDFIKKcLTKNPKKR---PTATKLLQHPFV 259
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
600-907 2.80e-28

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: 115.03  E-value: 2.80e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd14187      9 YVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWThdskyyqs 759
Cdd:cd14187     89 CRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYD-------- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14187    161 -----------------------GERKK----------------TLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLL 201
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSlhIPPQakLSPEASDLIIKLCRGpeDRLGKNGADEIKAHPFFKT 907
Cdd:cd14187    202 VGKPPFETSCLKETYLRIKKNEYS--IPKH--INPVAASLIQKMLQT--DPTARPTINELLNDEFFTS 263
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
605-933 3.19e-28

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: 115.81  E-value: 3.19e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  605 TLGIGAFGEVCLARKVDTKALYATKTLRKkdvLLRNqvahVKAERDILAEADN-EWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14091      7 EIGKGSYSVCKRCIHKATGKEYAVKIIDK---SKRD----PSEEIEILLRYGQhPNIITLRDVYDDGNSVYLVTELLRGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILidrdghikltdfglctgfrwthdskyyqsgdhp 763
Cdd:cd14091     80 ELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNIL--------------------------------- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rqdsmdFSNEWGDPSSCRCGDR--LKPLerRAarqhqrclAHSLVGTP----NYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd14091    127 ------YADESGDPESLRICDFgfAKQL--RA--------ENGLLMTPcytaNFVAPEVLKKQGYDAACDIWSLGVLLYT 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLA---QTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFfktidfssd 913
Cdd:cd14091    191 MLAGYTPFASgpnDTPEVILARIGSGKIDLSGGNWDHVSDSAKDLVRKmLHVDPSQRP---TAAQVLQHPW--------- 258
                          330       340
                   ....*....|....*....|
gi 1178431733  914 LRQQSASYIPKITHPTDTSN 933
Cdd:cd14091    259 IRNRDSLPQRQLTDPQDAAL 278
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
606-906 3.88e-28

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: 115.11  E-value: 3.88e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLAR-KVDTKALYATKTLRKKDvLLRNQVAHVKaERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14201     14 VGHGAFAVVFKGRhRKKTDWEVAIKSINKKN-LSKSQILLGK-EIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGD 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG---------HIKLTDFGLctgfrwthdSK 755
Cdd:cd14201     92 LADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGF---------AR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSGdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd14201    163 YLQSN---------------------------------------MMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVI 203
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  836 FEMLVGQPPFLAQTPLETQM---KVINWQTSlhIPPQAklSPEASDLIIKLC-RGPEDRLgknGADEIKAHPFFK 906
Cdd:cd14201    204 YQCLVGKPPFQANSPQDLRMfyeKNKNLQPS--IPRET--SPYLADLLLGLLqRNQKDRM---DFEAFFSHPFLE 271
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
602-906 3.93e-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: 114.75  E-value: 3.93e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLRKK-DVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd06605      5 YLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEiDEALQKQILR---ELDVLHKCNSPYIVGFYGAFYSEGDISICMEYM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPES-LARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqS 759
Cdd:cd06605     82 DGGSLDKILKEVGRIPERiLGKIAVAVVKGLIYLHEKHKIIHRDVKPSNILVNSRGQVKLCDFGV--------------S 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 GDhpRQDSMdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd06605    148 GQ--LVDSL---------------------------------AKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELA 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  840 VGQPPF------LAQTPLETQMKVINWQTSLHipPQAKLSPEASDLiIKLC--RGPEDRlgkNGADEIKAHPFFK 906
Cdd:cd06605    193 TGRFPYpppnakPSMMIFELLSYIVDEPPPLL--PSGKFSPDFQDF-VSQClqKDPTER---PSYKELMEHPFIK 261
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
603-905 4.07e-28

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: 114.41  E-value: 4.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLrKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14071      5 ERTIGKGNFAVVKLARHRITKTEVAIKII-DKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQSGDH 762
Cdd:cd14071     84 GEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGF---------SNFFKPGEL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfSNEWgdpssCrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYT--QLcDWWSVGVILFEMLV 840
Cdd:cd14071    155 --------LKTW-----C--------------------------GSPPYAAPEVFEGKEYEgpQL-DIWSLGVVLYVLVC 194
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  841 GQPPFLAQTPLETQMKVINWQtsLHIPpqAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14071    195 GALPFDGSTLQTLRDRVLSGR--FRIP--FFMSTDCEHLIRRmLVLDPSKRL---TIEQIKKHKWM 253
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
600-905 4.33e-28

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: 114.25  E-value: 4.33e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd14189      3 YCKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqs 759
Cdd:cd14189     83 CSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAA------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdRLKPLERRAArqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14189    150 -------------------------RLEPPEQRKK---------TICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLL 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  840 VGQPPFlAQTPLETQMKVINwQTSLHIPpqAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14189    196 CGNPPF-ETLDLKETYRCIK-QVKYTLP--ASLSLPARHLLAGiLKRNPGDRL---TLDQILEHEFF 255
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
597-906 4.76e-28

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: 114.25  E-value: 4.76e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTL----RKKDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDN 672
Cdd:cd06647      6 KKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMnlqqQPKKELIINEIL-------VMRENKNPNIVNYLDSYLVGDE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFyIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwth 752
Cdd:cd06647     79 LWVVMEYLAGGSLTDVVTETCMDEGQIAAV-CRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA------ 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfsnewgdpsscrcgdRLKPLERRAArqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd06647    152 --------------------------------QITPEQSKRS---------TMVGTPYWMAPEVVTRKAYGPKVDIWSLG 190
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETqMKVINWQTSLHIPPQAKLSPEASDLiikLCRGPEDRLGKNG-ADEIKAHPFFK 906
Cdd:cd06647    191 IMAIEMVEGEPPYLNENPLRA-LYLIATNGTPELQNPEKLSAIFRDF---LNRCLEMDVEKRGsAKELLQHPFLK 261
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
601-907 6.03e-28

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: 115.48  E-value: 6.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  601 VKIKTLGIGAFgEVClaRK---VDTKALYATKTL-RKKDV-----LLRNQVAHvkaerdilaeadnEWVVRLYYSFQDKD 671
Cdd:cd14092      9 LREEALGDGSF-SVC--RKcvhKKTGQEFAVKIVsRRLDTsrevqLLRLCQGH-------------PNIVKLHEVFQDEL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL---IDRDGHIKLTDFGlctgf 748
Cdd:cd14092     73 HTYLVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLftdEDDDAEIKIVDFG----- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdskyyqsgdhprqdsmdFSnewgdpsscrcgdRLKPlerRAARQHQRCLahslvgTPNYIAPEVLLRT----GYTQ 824
Cdd:cd14092    148 ---------------------FA-------------RLKP---ENQPLKTPCF------TLPYAAPEVLKQAlstqGYDE 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  825 LCDWWSVGVILFEMLVGQPPFLA---QTPLETQMKVI----------NWQTslhippqakLSPEASDLIiklcRG----- 886
Cdd:cd14092    185 SCDLWSLGVILYTMLSGQVPFQSpsrNESAAEIMKRIksgdfsfdgeEWKN---------VSSEAKSLI----QGlltvd 251
                          330       340
                   ....*....|....*....|.
gi 1178431733  887 PEDRLgknGADEIKAHPFFKT 907
Cdd:cd14092    252 PSKRL---TMSELRNHPWLQG 269
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
600-905 6.20e-28

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: 114.97  E-value: 6.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllrnqvahvkaERD-----------ILAEADNEWVVRLY---- 664
Cdd:cd07840      1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN------------EKEgfpitaireikLLQKLDHPNVVRLKeivt 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  665 --YSFQDKDNLYFVMDYIPGgDMMSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTD 741
Cdd:cd07840     69 skGSAKYKGSIYMVFEYMDH-DLTGLLDNPEVkFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLAD 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  742 FGLCtgfRWTHDSKyyqsgdhprqdSMDFSNewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLL-RT 820
Cdd:cd07840    148 FGLA---RPYTKEN-----------NADYTN--------------------------------RVITLWYRPPELLLgAT 181
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  821 GYTQLCDWWSVGVILFEMLVGQPPFLAQTPLEtQMKVI----------NWQTSLHIP------PQ------------AKL 872
Cdd:cd07840    182 RYGPEVDMWSVGCILAELFTGKPIFQGKTELE-QLEKIfelcgspteeNWPGVSDLPwfenlkPKkpykrrlrevfkNVI 260
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1178431733  873 SPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd07840    261 DPSALDLLDKlLTLDPKKRI---SADQALQHEYF 291
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
604-904 7.36e-28

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: 113.66  E-value: 7.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKK--DVLLRnqvAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd14074      9 ETLGRGHFAVVKLARHVFTGEKVAVKVIDKTklDDVSK---AHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI-DRDGHIKLTDFGlctgfrwthdskyyqs 759
Cdd:cd14074     86 GGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFG---------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdFSNEW--GDPSSCRCGDrlkplerraarqhqrcLAHSlvgtpnyiAPEVLLRTGY-TQLCDWWSVGVILF 836
Cdd:cd14074    150 ----------FSNKFqpGEKLETSCGS----------------LAYS--------APEILLGDEYdAPAVDIWSLGVILY 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVINWQtsLHIPPQakLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:cd14074    196 MLVCGQPPFQEANDSETLTMIMDCK--YTVPAH--VSPECKDLIRRmLIRDPKKRA---SLEEIENHPW 257
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
606-904 8.74e-28

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: 113.69  E-value: 8.74e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARkVDTKALYATK--TLRKKDVLL-RNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd06631      9 LGKGAYGTVYCGL-TSTGQLIAVKqvELDTSDKEKaEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsgdh 762
Cdd:cd06631     88 GSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFG------------------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrCGDRLkpLERRAARQHQRCLaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd06631    149 -------------------CAKRL--CINLSSGSQSQLL-KSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGK 206
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  843 PPfLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLiIKLC--RGPEDRLgknGADEIKAHPF 904
Cdd:cd06631    207 PP-WADMNPMAAIFAIGSGRKPVPRLPDKFSPEARDF-VHACltRDQDERP---SAEQLLKHPF 265
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
606-904 1.41e-27

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: 113.52  E-value: 1.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLL-----------------------RNQVAHVKAERDILAEADNEWVVR 662
Cdd:cd14199     10 IGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRqagfprrppprgaraapegctqpRGPIERVYQEIAILKKLDHPNVVK 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  663 LYYSFQD--KDNLYFVMDYIPGGDMMSLLIrMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLT 740
Cdd:cd14199     90 LVEVLDDpsEDHLYMVFELVKQGPVMEVPT-LKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIA 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  741 DFGLctgfrwthdskyyqsgdhprqdsmdfSNEWgdpsscrcgdrlkplerraarQHQRCLAHSLVGTPNYIAPEVLLRT 820
Cdd:cd14199    169 DFGV--------------------------SNEF---------------------EGSDALLTNTVGTPAFMAPETLSET 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  821 GYT---QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINwqTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGA 896
Cdd:cd14199    202 RKIfsgKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIKT--QPLEFPDQPDISDDLKDLLFRmLDKNPESRI---SV 276

                   ....*...
gi 1178431733  897 DEIKAHPF 904
Cdd:cd14199    277 PEIKLHPW 284
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
598-907 1.57e-27

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: 113.34  E-value: 1.57e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATK--TLRKKDvllrNQVAHVKAERDILAE---ADNEWVVRLYYSFQDKDN 672
Cdd:cd06917      1 SLYRRLELVGRGSYGAVYRGYHVKTGRVVALKvlNLDTDD----DDVSDIQKEVALLSQlklGQPKNIIKYYGSYLKGPS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLiRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwth 752
Cdd:cd06917     77 LWIIMDYCEGGSIRTLM-RAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASL---- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyQSGDHPRQdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLR-TGYTQLCDWWSV 831
Cdd:cd06917    152 -----NQNSSKRS--------------------------------------TFVGTPYWMAPEVITEgKYYDTKADIWSL 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  832 GVILFEMLVGQPPFLAQTPLETQMKVINWQtslhiPPQAKL---SPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKT 907
Cdd:cd06917    189 GITTYEMATGNPPYSDVDALRAVMLIPKSK-----PPRLEGngySPLLKEFVAAcLDEEPKDRL---SADELLKSKWIKQ 260
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
645-905 2.01e-27

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: 112.83  E-value: 2.01e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  645 VKAERDILAE-ADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRD 723
Cdd:cd14093     55 TRREIEILRQvSGHPNIIELHDVFESPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRD 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  724 IKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsgdhprqdsmdFSNEWGDpsscrcGDRLKplerraarqhqrclah 803
Cdd:cd14093    135 LKPENILLDDNLNVKISDFG--------------------------FATRLDE------GEKLR---------------- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  804 SLVGTPNYIAPEVLLRT------GYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEAS 877
Cdd:cd14093    167 ELCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSPEWDDISDTAK 246
                          250       260
                   ....*....|....*....|....*....
gi 1178431733  878 DLIIKLCR-GPEDRLgknGADEIKAHPFF 905
Cdd:cd14093    247 DLISKLLVvDPKKRL---TAEEALEHPFF 272
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
600-838 3.37e-27

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: 112.46  E-value: 3.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLAR-KVDTKaLYATK--TLRKKDVLLRNqvahVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd14046      8 FEELQVLGKGAFGQVVKVRnKLDGR-YYAIKkiKLRSESKNNSR----ILREVMLLSRLNHQHVVRYYQAWIERANLYIQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGgDMMSLLIRMGIFPES--LARFY--IAEltcAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwth 752
Cdd:cd14046     83 MEYCEK-STLRDLIDSGLFQDTdrLWRLFrqILE---GLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAT------ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 DSKyyQSGDHPRQD---SMDFSNEWGDPSScrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTG--YTQLCD 827
Cdd:cd14046    153 SNK--LNVELATQDinkSTSAALGSSGDLT------------------------GNVGTALYVAPEVQSGTKstYNEKVD 206
                          250
                   ....*....|.
gi 1178431733  828 WWSVGVILFEM 838
Cdd:cd14046    207 MYSLGIIFFEM 217
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
603-909 3.80e-27

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: 112.14  E-value: 3.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd06611     10 IGELGDGAFGKVYKAQHKETGLFAAAKIIQIES---EEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgd 761
Cdd:cd06611     87 GALDSIMLELErGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGV----------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsmdfsnewgdpsscrCGDRLKPLERRaarqhqrclaHSLVGTPNYIAPEVLL-----RTGYTQLCDWWSVGVILF 836
Cdd:cd06611    150 --------------------SAKNKSTLQKR----------DTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLI 199
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVINWQtslhiPPQ----AKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTID 909
Cdd:cd06611    200 ELAQMEPPHHELNPMRVLLKILKSE-----PPTldqpSKWSSSFNDFLKScLVKDPDDRP---TAAELLKHPFVSDQS 269
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
594-906 5.06e-27

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 111.49  E-value: 5.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  594 KMDKSM---------FVKIKTLGI--GAFGEVCLARKVDTKALYATKTLRKKDV-LLRNQVAHVKAerdilaeaDNEWVV 661
Cdd:PHA03390     1 NMDKSLselvqflknCEIVKKLKLidGKFGKVSVLKHKPTQKLFVQKIIKAKNFnAIEPMVHQLMK--------DNPNFI 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  662 RLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR-DGHIKLT 740
Cdd:PHA03390    73 KLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRaKDRIYLC 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  741 DFGLCtgfrwthdskyyqsgdHPRqdsmdfsnewGDPSscrCGDrlkplerraarqhqrclahslvGTPNYIAPEVLLRT 820
Cdd:PHA03390   153 DYGLC----------------KII----------GTPS---CYD----------------------GTLDYFSPEKIKGH 181
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  821 GYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgkNGADEI 899
Cdd:PHA03390   182 NYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQQKKLPFIKNVSKNANDFVQSmLKYNINYRL--TNYNEI 259

                   ....*..
gi 1178431733  900 KAHPFFK 906
Cdd:PHA03390   260 IKHPFLK 266
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
600-906 7.38e-27

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: 111.67  E-value: 7.38e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIktlGIGAFGEVCLARKVDTKALYATKTL----RKKDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYF 675
Cdd:cd06658     27 FIKI---GEGSTGIVCIATEKHTGKQVAVKKMdlrkQQRRELLFNEVV-------IMRDYHHENVVDMYNSYLVGDELWV 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIFPESLARFYIAELTcAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdsk 755
Cdd:cd06658     97 VMEFLEGGALTDIVTHTRMNEEQIATVCLSVLR-ALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV------- 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyqSGDHPRQDsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd06658    169 ---SKEVPKRK-------------------------------------SLVGTPYWMAPEVISRLPYGTEVDIWSLGIMV 208
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  836 FEMLVGQPPFLAQTPLETQMKVINwqtslHIPPQAKLSPEASDLI-----IKLCRGPEDRLgknGADEIKAHPFFK 906
Cdd:cd06658    209 IEMIDGEPPYFNEPPLQAMRRIRD-----NLPPRVKDSHKVSSVLrgfldLMLVREPSQRA---TAQELLQHPFLK 276
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
603-891 1.40e-26

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: 109.93  E-value: 1.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTL-GIGAFGEVCLARKVDTKALYATKTLRKKdvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd14087      5 IKALiGRGSFSRVVRVEHRVTRQPYAIKMIETK----CRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELAT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH---IKLTDFGLCTgfrwthdskyyq 758
Cdd:cd14087     81 GGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLAS------------ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqdsmdfsnewgdpsscrcgdrlkplerrAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd14087    149 ----------------------------------TRKKGPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYIL 194
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  839 LVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRL 891
Cdd:cd14087    195 LSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRLLTvNPGERL 248
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
600-905 5.01e-26

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: 109.11  E-value: 5.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVL-------LRnqvahvkaERDILAEADNEWVVRLYYSFQDKDN 672
Cdd:cd07829      1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegipstaLR--------EISLLKELKHPNIVKLLDVIHTENK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPggdmMSL--LIRM--GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGF 748
Cdd:cd07829     73 LYLVFEYCD----QDLkkYLDKrpGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAF 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwTHDSKYYqsgdhprqdsmdfSNEwgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLR-TGYTQLCD 827
Cdd:cd07829    149 --GIPLRTY-------------THE--------------------------------VVTLWYRAPEILLGsKHYSTAVD 181
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  828 WWSVGVILFEMLVGQPPF-----LAQ---------TPLETQ----MKVINWQTSL-HIPPQ------AKLSPEASDLIIK 882
Cdd:cd07829    182 IWSVGCIFAELITGKPLFpgdseIDQlfkifqilgTPTEESwpgvTKLPDYKPTFpKWPKNdlekvlPRLDPEGIDLLSK 261
                          330       340
                   ....*....|....*....|....
gi 1178431733  883 LCR-GPEDRLgknGADEIKAHPFF 905
Cdd:cd07829    262 MLQyNPAKRI---SAKEALKHPYF 282
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
604-883 7.52e-26

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: 107.88  E-value: 7.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEV------CLARKVDTKALYATKTLRKKDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd14082      9 EVLGSGQFGIVyggkhrKTGRDVAIKVIDKLRFPTKQESQLRNEVA-------ILQQLSHPGVVNLECMFETPERVFVVM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIpGGDMMSLLI--RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG---HIKLTDFGlctgfrwth 752
Cdd:cd14082     82 EKL-HGDMLEMILssEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFG--------- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdFSNEWGDPSScrcgdrlkpleRRaarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd14082    152 -----------------FARIIGEKSF-----------RR-----------SVVGTPAYLAPEVLRNKGYNRSLDMWSVG 192
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETQMKvinwQTSLHIPPQ--AKLSPEASDLIIKL 883
Cdd:cd14082    193 VIIYVSLSGTFPFNEDEDINDQIQ----NAAFMYPPNpwKEISPDAIDLINNL 241
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
603-916 8.50e-26

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: 108.58  E-value: 8.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd06643     10 VGELGDGAFGKVYKAQNKETGILAAAKVIDTKS---EEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgd 761
Cdd:cd06643     87 GAVDAVMLELErPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGV----------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsmdfsnewgdpsscrCGDRLKPLERRaarqhqrclaHSLVGTPNYIAPEVLL-----RTGYTQLCDWWSVGVILF 836
Cdd:cd06643    150 --------------------SAKNTRTLQRR----------DSFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGVTLI 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVINWQTSLHIPPqAKLSPEASDLIIKLCRGPEDrlGKNGADEIKAHPFFKTIDFSSDLRQ 916
Cdd:cd06643    200 EMAQIEPPHHELNPMRVLLKIAKSEPPTLAQP-SRWSPEFKDFLRKCLEKNVD--ARWTTSQLLQHPFVSVLVSNKPLRE 276
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
603-941 1.12e-25

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: 109.15  E-value: 1.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRK--KDVL-----LRnqvahvkaERDILAEADNEWVVRL--------YYSF 667
Cdd:cd07834      5 LKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfDDLIdakriLR--------EIKILRHLKHENIIGLldilrppsPEEF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  668 QDkdnLYFVMDYIPGgDMMSLlIRMgifPESLA----RFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG 743
Cdd:cd07834     77 ND---VYIVTELMET-DLHKV-IKS---PQPLTddhiQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LCTGFrwthdskyyqsGDHPRQDSM-DFsnewgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLR-TG 821
Cdd:cd07834    149 LARGV-----------DPDEDKGFLtEY-----------------------------------VVTRWYRAPELLLSsKK 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  822 YTQLCDWWSVGVILFEMLVGQPPF--------------LAQTP------LETQMKVINWQTSL---------HIPPQAkl 872
Cdd:cd07834    183 YTKAIDIWSVGCIFAELLTRKPLFpgrdyidqlnliveVLGTPseedlkFISSEKARNYLKSLpkkpkkplsEVFPGA-- 260
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  873 SPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTIDFSSDLrqqsasyiPKITHPTDTSNFDPVDPDK 941
Cdd:cd07834    261 SPEAIDLLEKmLVFNPKKRI---TADEALAHPYLAQLHDPEDE--------PVAKPPFDFPFFDDEELTI 319
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
600-906 1.14e-25

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: 107.52  E-value: 1.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQ---VAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd06630      2 WLKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQeevVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG-HIKLTDFGlcTGFRWThdSK 755
Cdd:cd06630     82 VEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFG--AAARLA--SK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSGDHPRQdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd06630    158 GTGAGEFQGQ---------------------------------------LLGTIAFMAPEVLRGEQYGRSCDVWSVGCVI 198
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  836 FEMLVGQPPFLA---QTPLETQMKVINWQTSLHIPPQakLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPFFK 906
Cdd:cd06630    199 IEMATAKPPWNAekiSNHLALIFKIASATTPPPIPEH--LSPGLRDVTLRcLELQPEDR---PPARELLKHPVFT 268
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
601-890 1.19e-25

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: 107.25  E-value: 1.19e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   601 VKIKTLGIGAFGEVCLAR----KVDTKALYATKTLRKkdvllrnqVAHVKAERDILAEA------DNEWVVRLYYSFQDK 670
Cdd:smart00221    2 TLGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKE--------DASEQQIEEFLREArimrklDHPNIVKLLGVCTEE 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   671 DNLYFVMDYIPGGDMMSLLIRMGIFPESLARF--YIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgf 748
Cdd:smart00221   74 EPLMIVMEYMPGGDLLDYLRKNRPKELSLSDLlsFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS--- 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   749 RWTHDSKYYqsgdhprqdsmdfsnewgDPSSCRCgdrlkPLerraarqhqrclahslvgtpNYIAPEVLLRTGYTQLCDW 828
Cdd:smart00221  151 RDLYDDDYY------------------KVKGGKL-----PI--------------------RWMAPESLKEGKFTSKSDV 187
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733   829 WSVGVILFEML-VGQPPFLAQTPLEtqmkVINWQTSLHIPPQAKLSPEASDLIIKLC--RGPEDR 890
Cdd:smart00221  188 WSFGVLLWEIFtLGEEPYPGMSNAE----VLEYLKKGYRLPKPPNCPPELYKLMLQCwaEDPEDR 248
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
601-890 1.39e-25

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 106.85  E-value: 1.39e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   601 VKIKTLGIGAFGEVCLAR----KVDTKALYATKTLRKkdvllrnqVAHVKAERDILAEA------DNEWVVRLYYSFQDK 670
Cdd:smart00219    2 TLGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKE--------DASEQQIEEFLREArimrklDHPNVVKLLGVCTEE 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   671 DNLYFVMDYIPGGDMMSLLIRM-GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfR 749
Cdd:smart00219   74 EPLYIVMEYMEGGDLLSYLRKNrPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS---R 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733   750 WTHDSKYYqsgdhpRQDSMDFSNEWgdpsscrcgdrlkplerraarqhqrclahslvgtpnyIAPEVLLRTGYTQLCDWW 829
Cdd:smart00219  151 DLYDDDYY------RKRGGKLPIRW-------------------------------------MAPESLKEGKFTSKSDVW 187
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733   830 SVGVILFEML-VGQPPFLAQTPLEtqmkVINWQTSLHIPPQAKLSPEASDLIIKLC--RGPEDR 890
Cdd:smart00219  188 SFGVLLWEIFtLGEQPYPGMSNEE----VLEYLKNGYRLPQPPNCPPELYDLMLQCwaEDPEDR 247
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
606-846 1.72e-25

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 106.77  E-value: 1.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAhVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd13978      1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKA-LLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLL-IRMGIFPESLaRFYIA-ELTCAVESVHKM--GFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHdskyyqsgd 761
Cdd:cd13978     80 KSLLeREIQDVPWSL-RFRIIhEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSI--------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdSMDFSNEwgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEvLLRTGY---TQLCDWWSVGVILFEM 838
Cdd:cd13978    150 -----SANRRRG----------------------------TENLGGTPIYMAPE-AFDDFNkkpTSKSDVYSFAIVIWAV 195

                   ....*...
gi 1178431733  839 LVGQPPFL 846
Cdd:cd13978    196 LTRKEPFE 203
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
600-905 2.39e-25

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: 107.42  E-value: 2.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIktlGIGAFGEVCLARKVDTKALYATKTL----RKKDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYF 675
Cdd:cd06657     25 FIKI---GEGSTGIVCIATVKSSGKLVAVKKMdlrkQQRRELLFNEVV-------IMRDYQHENVVEMYNSYLVGDELWV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIFPESLARFYIAELTcAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRwthdsk 755
Cdd:cd06657     95 VMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLK-ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS------ 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyqsgdhprqdsmdfsnewgdpsscrcgdrlKPLERRaarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd06657    168 -------------------------------KEVPRR----------KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMV 206
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  836 FEMLVGQPPFLAQTPLETqMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd06657    207 IEMVDGEPPYFNEPPLKA-MKMIRDNLPPKLKNLHKVSPSLKGFLDRlLVRDPAQRA---TAAELLKHPFL 273
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
599-905 2.73e-25

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: 106.36  E-value: 2.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd08221      1 HYIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSR-LSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMG--IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsky 756
Cdd:cd08221     80 YCNGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGIS----------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprqdsmdfsnewgdpsscrcgdrlKPLERRAArqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd08221    149 ------------------------------KVLDSESS------MAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLY 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVI--NWQTSLhippqAKLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPFF 905
Cdd:cd08221    193 ELLTLKRTFDATNPLRLAVKIVqgEYEDID-----EQYSEEIIQLVHDcLHQDPEDR---PTAEELLERPLL 256
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
606-905 4.89e-25

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: 106.26  E-value: 4.89e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATK--TLRKKDVLLRNQvahvkAERDI--LAEA-DNEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd07832      8 IGEGAHGIVFKAKDRETGETVALKkvALRKLEGGIPNQ-----ALREIkaLQACqGHPYVVKLRDVFPHGTGFVLVFEYM 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGdmMSLLIRMGI--FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdskyyq 758
Cdd:cd07832     83 LSS--LSEVLRDEErpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLF---------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SGDHPRQDSmdfsnewgdpsscrcgdrlkplerraarqHQrclahslVGTPNYIAPEVLL--RTgYTQLCDWWSVGVILF 836
Cdd:cd07832    151 SEEDPRLYS-----------------------------HQ-------VATRWYRAPELLYgsRK-YDEGVDLWAVGCIFA 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPF-----LAQ---------TPLETQ-----------------MKVINWQTslHIPpqaKLSPEASDLIIKLCR 885
Cdd:cd07832    194 ELLNGSPLFpgendIEQlaivlrtlgTPNEKTwpeltslpdynkitfpeSKGIRLEE--IFP---DCSPEAIDLLKGLLV 268
                          330       340
                   ....*....|....*....|
gi 1178431733  886 GPEDRlgKNGADEIKAHPFF 905
Cdd:cd07832    269 YNPKK--RLSAEEALRHPYF 286
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
606-904 5.88e-25

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 106.19  E-value: 5.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLR-----------------------NQVAHVKAERDILAEADNEWVVR 662
Cdd:cd14200      8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgeqakplAPLERVYQEIAILKKLDHVNIVK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  663 LYYSFQD--KDNLYFVMDYIPGGDMMSLLIRMGiFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLT 740
Cdd:cd14200     88 LIEVLDDpaEDNLYMVFDLLRKGPVMEVPSDKP-FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  741 DFGLctgfrwthdSKYYQSGDhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrCLAHSLVGTPNYIAPEVLLRT 820
Cdd:cd14200    167 DFGV---------SNQFEGND--------------------------------------ALLSSTAGTPAFMAPETLSDS 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  821 GYT---QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINwqTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGA 896
Cdd:cd14200    200 GQSfsgKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKN--KPVEFPEEPEISEELKDLILKmLDKNPETRI---TV 274

                   ....*...
gi 1178431733  897 DEIKAHPF 904
Cdd:cd14200    275 PEIKVHPW 282
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
600-907 6.03e-25

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: 106.12  E-value: 6.03e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd07841      2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDGINFTALREIklLQELKHPNIIGLLDVFGHKSNINLVF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGgDMmSLLIRMGIFPESLA--RFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdsk 755
Cdd:cd07841     82 EFMET-DL-EKVIKDKSIVLTPAdiKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSF------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyqsgdhprqdsmdfsnewGDPSscrcgdrlkplerraarqhqRCLAHSLVgTPNYIAPEVLL-RTGYTQLCDWWSVGVI 834
Cdd:cd07841    153 -------------------GSPN--------------------RKMTHQVV-TRWYRAPELLFgARHYGVGVDMWSVGCI 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  835 LFEMLVGQPPFLAQTPLEtQMKVI----------NWQ--TSL-------HIPPQA--KLSPEASDLIIKLCRG-----PE 888
Cdd:cd07841    193 FAELLLRVPFLPGDSDID-QLGKIfealgtpteeNWPgvTSLpdyvefkPFPPTPlkQIFPAASDDALDLLQRlltlnPN 271
                          330
                   ....*....|....*....
gi 1178431733  889 DRLgknGADEIKAHPFFKT 907
Cdd:cd07841    272 KRI---TARQALEHPYFSN 287
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
599-845 6.60e-25

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: 105.05  E-value: 6.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd08224      1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMG----IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdS 754
Cdd:cd08224     81 LADAGDLSRLIKHFKkqkrLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL---------G 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 KYYQSgdhprqdsmdfsnewgdpsscrcgdrlKPLErraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 834
Cdd:cd08224    152 RFFSS---------------------------KTTA-----------AHSLVGTPYYMSPERIREQGYDFKSDIWSLGCL 193
                          250
                   ....*....|.
gi 1178431733  835 LFEMLVGQPPF 845
Cdd:cd08224    194 LYEMAALQSPF 204
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
606-903 7.11e-25

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: 104.62  E-value: 7.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATK---TLRKKDVllrnqvAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14103      1 LGRGKFGTVYRCVEKATGKELAAKfikCRKAKDR------EDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDGH-IKLTDFGLCtgfrwthdSKYyqs 759
Cdd:cd14103     75 GELFERVVDDDfELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLA--------RKY--- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgDPSScrcgdRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14103    144 ----------------DPDK-----KLK----------------VLFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLL 186
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKL-CRGPEDRLgknGADEIKAHP 903
Cdd:cd14103    187 SGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLlVKDPRKRM---SAAQCLQHP 248
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
603-858 1.07e-24

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: 104.52  E-value: 1.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14072      5 LKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQ-LNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsgdh 762
Cdd:cd14072     84 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFG------------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdFSNEWgdpsscRCGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVG 841
Cdd:cd14072    145 -------FSNEF------TPGNKLD----------------TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSG 195
                          250
                   ....*....|....*..
gi 1178431733  842 QPPFLAQTPLETQMKVI 858
Cdd:cd14072    196 SLPFDGQNLKELRERVL 212
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
602-846 1.38e-24

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: 104.35  E-value: 1.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLRKK----DVLLRNQVAHVKAERDILAEA-DNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd13993      4 LISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnsKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIYIV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGIFPES--LARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD-GHIKLTDFGLCTgfrwthD 753
Cdd:cd13993     84 LEYCPNGDLFEAITENRIYVGKteLIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLAT------T 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 SKYyqsgdhprqdSMDFSnewgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVL-----LRTGY-TQLCD 827
Cdd:cd13993    158 EKI----------SMDFG----------------------------------VGSEFYMAPECFdevgrSLKGYpCAAGD 193
                          250
                   ....*....|....*....
gi 1178431733  828 WWSVGVILFEMLVGQPPFL 846
Cdd:cd13993    194 IWSLGIILLNLTFGRNPWK 212
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
608-905 1.82e-24

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: 104.17  E-value: 1.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  608 IGAFGEVCLARKVDTKALYATKTLRKKdvllrnqvAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMS 687
Cdd:cd05576      9 LGVIDKVLLVMDTRTQETFILKGLRKS--------SEYSRERKTIIPRCVPNMVCLRKYIISEESVFLVLQHAEGGKLWS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  688 LLIRM----------------------GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlc 745
Cdd:cd05576     81 YLSKFlndkeihqlfadlderlaaasrFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFS-- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  746 tgfRWThdskyyqsgdhprqdsmdfsnEWGDpsSCrCGDRLKPLerraarqhqrclahslvgtpnYIAPEVLLRTGYTQL 825
Cdd:cd05576    159 ---RWS---------------------EVED--SC-DSDAIENM---------------------YCAPEVGGISEETEA 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 CDWWSVGVILFEMLVGQPpflaqtPLETQMKVINWQTSLHIPPQakLSPEASDLIIKLCR-GPEDRLGKNGA--DEIKAH 902
Cdd:cd05576    191 CDWWSLGALLFELLTGKA------LVECHPAGINTHTTLNIPEW--VSEEARSLLQQLLQfNPTERLGAGVAgvEDIKSH 262

                   ...
gi 1178431733  903 PFF 905
Cdd:cd05576    263 PFF 265
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
606-890 1.89e-24

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: 104.12  E-value: 1.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKA-LYATK-----------TLRKKDVLLRNQVAHVKAERDILAEADnewVVRLYYSFQDKDNL 673
Cdd:cd08528      8 LGSGAFGCVYKVRKKSNGQtLLALKeinmtnpafgrTEQERDKSVGDIISEVNIIKEQLRHPN---IVRYYKTFLENDRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDYIPGGDMMSLLIRM----GIFPESLARFYIAELTCAVESVHK-MGFIHRDIKPDNILIDRDGHIKLTDFGLCtgf 748
Cdd:cd08528     85 YIVMELIEGAPLGEHFSSLkeknEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDFGLA--- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdskyyqsgdhpRQDSMDFSnewgdpsscrcgdRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDW 828
Cdd:cd08528    162 ---------------KQKGPESS-------------KMT----------------SVVGTILYSCPEIVQNEPYGEKADI 197
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  829 WSVGVILFEMLVGQPPFLAQTPLETQMKVINWQtslHIP-PQAKLSPEASDLIIK-LCRGPEDR 890
Cdd:cd08528    198 WALGCILYQMCTLQPPFYSTNMLTLATKIVEAE---YEPlPEGMYSDDITFVIRScLTPDPEAR 258
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
603-904 1.98e-24

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: 103.70  E-value: 1.98e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvllRNQVAHVKAERDILAEAD--NEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd14662      5 VKDIGSGNFGVARLMRNKETKELVAVKYIE------RGLKIDENVQREIINHRSlrHPNIIRFKEVVLTPTHLAIVMEYA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD--GHIKLTDFGlctgfrwthdskYYQ 758
Cdd:cd14662     79 AGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFG------------YSK 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRclAHSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFE 837
Cdd:cd14662    147 S----------------------------------SVLHSQ--PKSTVGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYV 190
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLH--IPPQAKLSPEASDLIIKLCRG-PEDRLgknGADEIKAHPF 904
Cdd:cd14662    191 MLVGAYPFEDPDDPKNFRKTIQRIMSVQykIPDYVRVSQDCRHLLSRIFVAnPAKRI---TIPEIKNHPW 257
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
600-908 2.02e-24

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: 103.73  E-value: 2.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLAR----KVDTKALYATKTLRKKdvllrnqvAHVKAERDILAEA------DNEWVVRLYYSFQD 669
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTLKEG--------ADEEEREDFLEEAsimkklDHPNIVKLLGVCTQ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  670 KDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIA-ELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgf 748
Cdd:pfam07714   73 GEPLYIVTEYMPGGDLLDFLRKHKRKLTLKDLLSMAlQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLS--- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 RWTHDSKYYQSGDHprqdsmdfsnewgdpsscrCGDRLKplerraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDW 828
Cdd:pfam07714  150 RDIYDDDYYRKRGG-------------------GKLPIK-----------------------WMAPESLKDGKFTSKSDV 187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  829 WSVGVILFEML-VGQPPFLAQTPLEtqmkVINWQTSLHIPPQAKLSPEASDLIIKLC--RGPEDRlgkngadeikahPFF 905
Cdd:pfam07714  188 WSFGVLLWEIFtLGEQPYPGMSNEE----VLEFLEDGYRLPQPENCPDELYDLMKQCwaYDPEDR------------PTF 251

                   ...
gi 1178431733  906 KTI 908
Cdd:pfam07714  252 SEL 254
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
600-890 3.06e-24

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: 102.97  E-value: 3.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQvAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd08218      2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKER-EESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLL-IRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDskyy 757
Cdd:cd08218     81 CDGGDLYKRInAQRGVlFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVE---- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd08218    157 -------------------------------------------LARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYE 193
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQtslHIPPQAKLSPEASDLIIKLC-RGPEDR 890
Cdd:cd08218    194 MCTLKHAFEAGNMKNLVLKIIRGS---YPPVPSRYSYDLRSLVSQLFkRNPRDR 244
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
597-906 3.83e-24

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: 104.04  E-value: 3.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFG------EVCLARKVDTKALYATKTLRKKdvLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDK 670
Cdd:cd06655     18 KKKYTRYEKIGQGASGtvftaiDVATGQEVAIKQINLQKQPKKE--LIINEIL-------VMKELKNPNIVNFLDSFLVG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DNLYFVMDYIPGGDMMSLLIRMGIFPESLARFyIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrw 750
Cdd:cd06655     89 DELFVVMEYLAGGSLTDVVTETCMDEAQIAAV-CRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCA---- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpsscrcgdRLKPLERRAArqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd06655    164 ----------------------------------QITPEQSKRS---------TMVGTPYWMAPEVVTRKAYGPKVDIWS 200
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  831 VGVILFEMLVGQPPFLAQTPLETqMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKngADEIKAHPFFK 906
Cdd:cd06655    201 LGIMAIEMVEGEPPYLNENPLRA-LYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGS--AKELLQHPFLK 273
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
603-904 4.29e-24

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: 102.76  E-value: 4.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNqvahvkAERDILAEAD--NEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd14665      5 VKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDEN------VQREIINHRSlrHPNIVRFKEVILTPTHLAIVMEYA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG--HIKLTDFGLctgfrwthdSKYYQ 758
Cdd:cd14665     79 AGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGY---------SKSSV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SGDHPRqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFE 837
Cdd:cd14665    150 LHSQPK---------------------------------------STVGTPAYIAPEVLLKKEYDgKIADVWSCGVTLYV 190
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  838 MLVGQPPFlaQTPLE------TQMKVINWQTSlhIPPQAKLSPEASDLIIKL-CRGPEDRLgknGADEIKAHPF 904
Cdd:cd14665    191 MLVGAYPF--EDPEEprnfrkTIQRILSVQYS--IPDYVHISPECRHLISRIfVADPATRI---TIPEIRNHEW 257
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
602-905 4.31e-24

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: 103.55  E-value: 4.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd07833      5 VLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESE---DDEDVKKTALREVkvLRQLRHENIVNLKEAFRRKGRLYLVFEY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGgDMMSLLIRM-GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyq 758
Cdd:cd07833     82 VER-TLLELLEASpGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFG--------------- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqdsmdFSNEWGDPSSCRCGDrlkplerraarqhqrclahsLVGTPNYIAPEVLLR-TGYTQLCDWWSVGVILFE 837
Cdd:cd07833    146 -----------FARALTARPASPLTD--------------------YVATRWYRAPELLVGdTNYGKPVDVWAIGCIMAE 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPF--------------------------LAQTPLETQMKVINWQT--SLHIPPQAKLSPEASDLIIK-LCRGPE 888
Cdd:cd07833    195 LLDGEPLFpgdsdidqlyliqkclgplppshqelFSSNPRFAGVAFPEPSQpeSLERRYPGKVSSPALDFLKAcLRMDPK 274
                          330
                   ....*....|....*..
gi 1178431733  889 DRLgknGADEIKAHPFF 905
Cdd:cd07833    275 ERL---TCDELLQHPYF 288
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
599-883 5.11e-24

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: 103.97  E-value: 5.11e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFG--EVCLARKVDTKalYATKTLRKK-DVLLRNQVAHVKaerdiLAEADNEwVVRLYYSFQDKDNLYF 675
Cdd:cd14179      8 LDLKDKPLGEGSFSicRKCLHKKTNQE--YAVKIVSKRmEANTQREIAALK-----LCEGHPN-IVKLHEVYHDQLHTFL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCtgfrwth 752
Cdd:cd14179     80 VMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFA------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfsnewgdpsscrcgdRLKPLERRAARqhQRCLahslvgTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd14179    153 --------------------------------RLKPPDNQPLK--TPCF------TLHYAAPELLNYNGYDESCDLWSLG 192
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  833 VILFEMLVGQPPF------LAQTPLETQMKVINwQTSLHIPPQA--KLSPEASDLIIKL 883
Cdd:cd14179    193 VILYTMLSGQVPFqchdksLTCTSAEEIMKKIK-QGDFSFEGEAwkNVSQEAKDLIQGL 250
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
597-906 5.92e-24

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: 103.26  E-value: 5.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTL----RKKDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDN 672
Cdd:cd06656     18 KKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMnlqqQPKKELIINEIL-------VMRENKNPNIVNYLDSYLVGDE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFyIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwth 752
Cdd:cd06656     91 LWVVMEYLAGGSLTDVVTETCMDEGQIAAV-CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA------ 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfsnewgdpsscrcgdRLKPLERRAArqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd06656    164 --------------------------------QITPEQSKRS---------TMVGTPYWMAPEVVTRKAYGPKVDIWSLG 202
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETqMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKngADEIKAHPFFK 906
Cdd:cd06656    203 IMAIEMVEGEPPYLNENPLRA-LYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGS--AKELLQHPFLK 273
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
604-880 7.30e-24

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: 102.43  E-value: 7.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLR--KKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQD--KDNLYFVMDY 679
Cdd:cd06652      8 KLLGQGAFGRVYLCYDADTGRELAVKQVQfdPESPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDpqERTLSIFMEY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQs 759
Cdd:cd06652     88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGA---------SKRLQ- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpSSCRCGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd06652    158 ------------------TICLSGTGMK----------------SVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEML 203
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSLHIPP---------------QAKLSPEASDLI 880
Cdd:cd06652    204 TEKPPWAEFEAMAAIFKIATQPTNPQLPAhvsdhcrdflkrifvEAKLRPSADELL 259
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
600-922 7.60e-24

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: 102.80  E-value: 7.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEV--CLARKVDTKalYATKTLRKK--------DVLLR-NQVAHVKAERDIlaeadnewvvrlyysFQ 668
Cdd:cd14175      3 YVVKETIGVGSYSVCkrCVHKATNME--YAVKVIDKSkrdpseeiEILLRyGQHPNIITLKDV---------------YD 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  669 DKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILidrdghikltdfglctgf 748
Cdd:cd14175     66 DGKHVYLVTELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNIL------------------ 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdskyyqsgdhprqdsmdFSNEWGDPSSCRCGDRLKPLERRAarqhQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDW 828
Cdd:cd14175    128 ---------------------YVDESGNPESLRICDFGFAKQLRA----ENGLLMTPCYTANFVAPEVLKRQGYDEGCDI 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  829 WSVGVILFEMLVGQPPF---LAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLgknGADEIKAHPF 904
Cdd:cd14175    183 WSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDLVSKMLHvDPHQRL---TAKQVLQHPW 259
                          330       340
                   ....*....|....*....|
gi 1178431733  905 FKTIDF--SSDLRQQSASYI 922
Cdd:cd14175    260 ITQKDKlpQSQLNHQDVQLV 279
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
660-905 8.71e-24

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: 102.36  E-value: 8.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  660 VVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKL 739
Cdd:cd14181     78 IITLIDSYESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKL 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  740 TDFGLctgfrwthdskyyqsgdhprqdsmdfsnewgdpsSCRcgdrLKPLERraarqhqrclAHSLVGTPNYIAPEVL-- 817
Cdd:cd14181    158 SDFGF----------------------------------SCH----LEPGEK----------LRELCGTPGYLAPEILkc 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  818 ----LRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLg 892
Cdd:cd14181    190 smdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSPEWDDRSSTVKDLISRLLVvDPEIRL- 268
                          250
                   ....*....|...
gi 1178431733  893 knGADEIKAHPFF 905
Cdd:cd14181    269 --TAEQALQHPFF 279
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
603-904 9.37e-24

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: 102.38  E-value: 9.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLrkkDVLLRNQVAhVKAERDILAE-ADNEWVVRLYYSFQDK------DNLYF 675
Cdd:cd06608     11 VEVIGEGTYGKVYKARHKKTGQLAAIKIM---DIIEDEEEE-IKLEINILRKfSNHPNIATFYGAFIKKdppggdDQLWL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGG---DMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwt 751
Cdd:cd06608     87 VMEYCGGGsvtDLVKGLRKKGkRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS------ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 hdskyyqsgdhpRQdsMDfsnewgdpsscrcgdrlKPLERRaarqhqrclaHSLVGTPNYIAPEVL-----LRTGYTQLC 826
Cdd:cd06608    161 ------------AQ--LD-----------------STLGRR----------NTFIGTPYWMAPEVIacdqqPDASYDARC 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  827 DWWSVGVILFEMLVGQPPFLAQTPLETQMKVINwqtslHIPPQ----AKLSPEASDLIIK-LCRGPEDRlgkNGADEIKA 901
Cdd:cd06608    200 DVWSLGITAIELADGKPPLCDMHPMRALFKIPR-----NPPPTlkspEKWSKEFNDFISEcLIKNYEQR---PFTEELLE 271

                   ...
gi 1178431733  902 HPF 904
Cdd:cd06608    272 HPF 274
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
600-905 9.82e-24

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: 101.69  E-value: 9.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAH-----VKAERDILA---EADNEWVVRLYYSFQDKD 671
Cdd:cd14004      2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDrklgtVPLEIHILDtlnKRSHPNIVKLLDFFEDDE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMD-YIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrw 750
Cdd:cd14004     82 FYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thDSKYYQSGdhprqdsmDFSnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYT-QLCDWW 829
Cdd:cd14004    155 --SAAYIKSG--------PFD--------------------------------TFVGTIDYAAPEVLRGNPYGgKEQDIW 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  830 SVGVILFEMLVGQPPFLAqtpLETQMKvinwqTSLHIPpqAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14004    193 ALGVLLYTLVFKENPFYN---IEEILE-----ADLRIP--YAVSEDLIDLISRmLNRDVGDRP---TIEELLTDPWL 256
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
606-890 2.52e-23

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: 101.24  E-value: 2.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATK----TLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQ-DKDNLYFVMDYI 680
Cdd:cd13990      8 LGKGGFSEVYKAFDLVEQRYVACKihqlNKDWSEEKKQNYIKHALREYEIHKSLDHPRIVKLYDVFEiDTDSFCTVLEYC 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVE--SVHKMGFIHRDIKPDNILIDRD---GHIKLTDFGLctgfrwthdSK 755
Cdd:cd13990     88 DGNDLDFYLKQHKSIPEREARSIIMQVVSALKylNEIKPPIIHYDLKPGNILLHSGnvsGEIKITDFGL---------SK 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSgDHPRQDSMDfsnewgdpsscrcgdrlkpLERRAArqhqrclahslvGTPNYIAPEVLLRTG----YTQLCDWWSV 831
Cdd:cd13990    159 IMDD-ESYNSDGME-------------------LTSQGA------------GTYWYLPPECFVVGKtppkISSKVDVWSV 206
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  832 GVILFEMLVGQPPF---LAQTPLETQMKVINwQTSLHIPPQAKLSPEASDLIIKLCR-GPEDR 890
Cdd:cd13990    207 GVIFYQMLYGRKPFghnQSQEAILEENTILK-ATEVEFPSKPVVSSEAKDFIRRCLTyRKEDR 268
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
603-845 2.56e-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: 100.41  E-value: 2.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALyATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14161      8 LETLGKGTYGRVKKARDSSGRLV-AIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYqsgdh 762
Cdd:cd14161     87 GDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGL---------SNLY----- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerraarqHQRCLAHSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVG 841
Cdd:cd14161    153 ----------------------------------NQDKFLQTYCGSPLYASPEIVNGRPYIgPEVDSWSLGVLLYILVHG 198

                   ....
gi 1178431733  842 QPPF 845
Cdd:cd14161    199 TMPF 202
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
606-905 4.59e-23

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: 99.58  E-value: 4.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRkkdvlLRNQV-AHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14107     10 IGRGTFGFVKRVTHKGNGECCAAKFIP-----LRSSTrARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCSSEE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDgHIKLTDFGLCtgfrwthdskyyqsgd 761
Cdd:cd14107     85 LLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvspTRE-DIKICDFGFA---------------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsmdfsnewgdpsscrcgDRLKPLErraarqHQrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd14107    148 ----------------------QEITPSE------HQ----FSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTC 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  842 QPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPFF 905
Cdd:cd14107    196 HSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRvLQPDPEKR---PSASECLSHEWF 257
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
604-904 4.76e-23

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: 99.71  E-value: 4.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTL--RKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKD--NLYFVMDY 679
Cdd:cd06653      8 KLLGRGAFGEVYLCYDADTGRELAVKQVpfDPDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEekKLSIFVEY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQs 759
Cdd:cd06653     88 MPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA---------SKRIQ- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpSSCRCGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd06653    158 ------------------TICMSGTGIK----------------SVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEML 203
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSLHIPPQAklSPEASDLIIKLCRGPEDRlgkNGADEIKAHPF 904
Cdd:cd06653    204 TEKPPWAEYEAMAAIFKIATQPTKPQLPDGV--SDACRDFLRQIFVEEKRR---PTAEFLLRHPF 263
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
648-906 5.45e-23

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: 99.99  E-value: 5.45e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  648 ERDILAE-ADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKP 726
Cdd:cd14182     59 EIDILRKvSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKP 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  727 DNILIDRDGHIKLTDFGLctgfrwthdskyyqsgdhprqdsmdfsnewgdpsSCRC--GDRLKplerraarqhqrclahS 804
Cdd:cd14182    139 ENILLDDDMNIKLTDFGF----------------------------------SCQLdpGEKLR----------------E 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  805 LVGTPNYIAPEVLL------RTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASD 878
Cdd:cd14182    169 VCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDRSDTVKD 248
                          250       260
                   ....*....|....*....|....*....
gi 1178431733  879 LIIK-LCRGPEDRLgknGADEIKAHPFFK 906
Cdd:cd14182    249 LISRfLVVQPQKRY---TAEEALAHPFFQ 274
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
603-905 6.15e-23

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: 99.22  E-value: 6.15e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLR--KKDVLLRNQVAHVKAERDILAEA---DNewVVRLYYSFQDKDNLYFVM 677
Cdd:cd14019      6 IEKIGEGTFSSVYKAEDKLHDLYDRNKGRLvaLKHIYPTSSPSRILNELECLERLggsNN--VSGLITAFRNEDQVVAVL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGiFPEslARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD-GHIKLTDFGLCtgfRWTHDSKy 756
Cdd:cd14019     84 PYIEHDDFRDFYRKMS-LTD--IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNREtGKGVLVDFGLA---QREEDRP- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprqdsmdfsnewgdpsscrcgdrlkplERRAARqhqrclahslVGTPNYIAPEVLLR-TGYTQLCDWWSVGVIL 835
Cdd:cd14019    157 ---------------------------------EQRAPR----------AGTRGFRAPEVLFKcPHQTTAIDIWSAGVIL 193
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  836 FEMLVGQ-PPFLAQTPLETQMKVinwqtslhippqAKL--SPEASDLIIKLCR-GPEDRLgknGADEIKAHPFF 905
Cdd:cd14019    194 LSILSGRfPFFFSSDDIDALAEI------------ATIfgSDEAYDLLDKLLElDPSKRI---TAEEALKHPFF 252
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
600-837 8.74e-23

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: 99.42  E-value: 8.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLAR-KVDTKALYATKTLRKKDVLLRNQVAHVKaERDILAEADNE---WVVRLYYSFQDKDNLYF 675
Cdd:cd14052      2 FANVELIGSGEFSQVYKVSeRVPTGKVYAVKKLKPNYAGAKDRLRRLE-EVSILRELTLDghdNIVQLIDSWEYHGHLYI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIfpesLARF-------YIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgf 748
Cdd:cd14052     81 QTELCENGSLDVFLSELGL----LGRLdefrvwkILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAT-- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 RWThdskyyqsgdhprqDSMDFSNEwgdpsscrcGDRlkplerraarqhqrclahslvgtpNYIAPEVLLRTGYTQLCDW 828
Cdd:cd14052    155 VWP--------------LIRGIERE---------GDR------------------------EYIAPEILSEHMYDKPADI 187

                   ....*....
gi 1178431733  829 WSVGVILFE 837
Cdd:cd14052    188 FSLGLILLE 196
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
600-904 1.10e-22

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: 98.56  E-value: 1.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKI-KTLGIGAFGEVCLA------RKVDTKALYATKTLRKKDVLLRNQVAHvkaerdiLAEADNEWVVRLYYSFQDKDN 672
Cdd:cd14075      3 FYRIrGELGSGNFSQVKLGihqltkEKVAIKILDKTKLDQKTQRLLSREISS-------MEKLHHPNIIRLYEVVETLSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwth 752
Cdd:cd14075     76 LHLVMEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFG--------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdFSnewgdpSSCRCGDRLkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYT-QLCDWWSV 831
Cdd:cd14075    147 -----------------FS------THAKRGETL----------------NTFCGSPPYAAPELFKDEHYIgIYVDIWAL 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  832 GVILFEMLVGQPPFLAQTPleTQMKVINWQTSLHIPPQakLSPEASDLIIKLCR-GPEDRLgknGADEIKAHPF 904
Cdd:cd14075    188 GVLLYFMVTGVMPFRAETV--AKLKKCILEGTYTIPSY--VSEPCQELIRGILQpVPSDRY---SIDEIKNSEW 254
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
606-904 1.28e-22

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: 99.33  E-value: 1.28e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHvkaERDILAEADNEW-VVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14173     10 LGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFR---EVEMLYQCQGHRnVLELIEFFEEEDKFYLVFEKMRGGS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCTGFRWThdskyyqsgd 761
Cdd:cd14173     87 ILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLGSGIKLN---------- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsmdfsnewGDPSSCRCGDRLKPlerraarqhqrclahslVGTPNYIAPEVL-----LRTGYTQLCDWWSVGVILF 836
Cdd:cd14173    157 -------------SDCSPISTPELLTP-----------------CGSAEYMAPEVVeafneEASIYDKRCDLWSLGVILY 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPFLAQ------------TPLETQMKVINWQTSLHIPPQ---AKLSPEASDLIIK-LCRGPEDRLgknGADEIK 900
Cdd:cd14173    207 IMLSGYPPFVGRcgsdcgwdrgeaCPACQNMLFESIQEGKYEFPEkdwAHISCAAKDLISKlLVRDAKQRL---SAAQVL 283

                   ....
gi 1178431733  901 AHPF 904
Cdd:cd14173    284 QHPW 287
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
604-845 1.29e-22

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: 98.74  E-value: 1.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVA-HVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14070      8 RKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTkNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRwthdskyyqsgdh 762
Cdd:cd14070     88 GNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAG------------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfSNEWGDPSSCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14070    155 --------ILGYSDPFSTQC------------------------GSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGT 202

                   ...
gi 1178431733  843 PPF 845
Cdd:cd14070    203 LPF 205
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
600-903 1.49e-22

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: 98.22  E-value: 1.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLAR-KVDTKaLYATKTLRKK---DVLLRNQVAHVKAERdILAEADNewVVRLYYSFQDKDNLYF 675
Cdd:cd13997      2 FHELEQIGSGSFSEVFKVRsKVDGC-LYAVKKSKKPfrgPKERARALREVEAHA-ALGQHPN--IVRYYSSWEEGGHLYI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGG---DMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfRWTh 752
Cdd:cd13997     78 QMELCENGslqDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLAT--RLE- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyQSGDhprqdsmdfsNEWGDpsscrcgdrlkplerraarqhqrclahslvgtPNYIAPEVL-LRTGYTQLCDWWSV 831
Cdd:cd13997    155 -----TSGD----------VEEGD--------------------------------SRYLAPELLnENYTHLPKADIFSL 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  832 GVILFEMLVGQpPFLAQTPLETQMKvinwQTSLHIPPQAKLSPEASDLiIKLCRGPEDRLgKNGADEIKAHP 903
Cdd:cd13997    188 GVTVYEAATGE-PLPRNGQQWQQLR----QGKLPLPPGLVLSQELTRL-LKVMLDPDPTR-RPTADQLLAHD 252
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
597-906 1.68e-22

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: 99.03  E-value: 1.68e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTL----RKKDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDN 672
Cdd:cd06654     19 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMnlqqQPKKELIINEIL-------VMRENKNPNIVNYLDSYLVGDE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFyIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwth 752
Cdd:cd06654     92 LWVVMEYLAGGSLTDVVTETCMDEGQIAAV-CRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA------ 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfsnewgdpsscrcgdRLKPLERRAArqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd06654    165 --------------------------------QITPEQSKRS---------TMVGTPYWMAPEVVTRKAYGPKVDIWSLG 203
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETqMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKngADEIKAHPFFK 906
Cdd:cd06654    204 IMAIEMIEGEPPYLNENPLRA-LYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGS--AKELLQHQFLK 274
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
604-903 2.42e-22

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: 97.74  E-value: 2.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEV--CLARKvdTKALYATKTLRKKDvllrnqvahvKAERdilaEADNEW-------VVRLY--Y--SFQDK 670
Cdd:cd14089      7 QVLGLGINGKVleCFHKK--TGEKFALKVLRDNP----------KARR----EVELHWrasgcphIVRIIdvYenTYQGR 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DNLYFVMDYIPGGDMMSLLIRMGI--FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLC 745
Cdd:cd14089     71 KCLLVVMECMEGGELFSRIQERADsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYsskGPNAILKLTDFGFA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  746 tgfRWTHDSKYYQSgdhprqdsmdfsnewgdpsscrcgdrlkPlerraarqhqrCLahslvgTPNYIAPEVLLRTGYTQL 825
Cdd:cd14089    151 ---KETTTKKSLQT----------------------------P-----------CY------TPYYVAPEVLGPEKYDKS 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 CDWWSVGVILFEMLVGQPPFLAQT--PLETQMK--VINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLgknGADEIK 900
Cdd:cd14089    183 CDMWSLGVIMYILLCGYPPFYSNHglAISPGMKkrIRNGQYEFPNPEWSNVSEEAKDLIRGLLKtDPSERL---TIEEVM 259

                   ...
gi 1178431733  901 AHP 903
Cdd:cd14089    260 NHP 262
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
603-890 2.51e-22

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: 97.72  E-value: 2.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLAR-KVDTKALyATKTLRKKDVLLRNQVAHvKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd08225      5 IKKIGEGSFGKIYLAKaKSDSEHC-VIKEIDLTKMPVKEKEAS-KKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMG--IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHI-KLTDFGLCTGFrwthdskyyq 758
Cdd:cd08225     83 GGDLMKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQL---------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprQDSMDFsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd08225    153 ------NDSMEL-------------------------------AYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYEL 195
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  839 LVGQPPFLAQTPLETQMKVInwQTSLHiPPQAKLSPEASDLIIKLCR-GPEDR 890
Cdd:cd08225    196 CTLKHPFEGNNLHQLVLKIC--QGYFA-PISPNFSRDLRSLISQLFKvSPRDR 245
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
600-906 3.25e-22

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: 98.38  E-value: 3.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKkdvllrnqVAHVKAERDI-----LAEADNewVVRLYYSFQDKDNLY 674
Cdd:cd14132     20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKP--------VKKKKIKREIkilqnLRGGPN--IVKLLDVVKDPQSKT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 --FVMDYIPGGDMMSLLIRMGIFPeslARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH-IKLTDFGLctgfrwt 751
Cdd:cd14132     90 psLIFEYVNNTDFKTLYPTLTDYD---IRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGL------- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 hdSKYYqsgdHPRQDsmdfsnewgdpSSCRcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLRTG-YTQLCDWWS 830
Cdd:cd14132    160 --AEFY----HPGQE-----------YNVR------------------------VASRYYKGPELLVDYQyYDYSLDMWS 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  831 VGVILFEMLVGQPPF----------------LAQTPL------------------ETQMKVINWQTSLHIPPQAKLSPEA 876
Cdd:cd14132    199 LGCMLASMIFRKEPFfhghdnydqlvkiakvLGTDDLyayldkygielpprlndiLGRHSKKPWERFVNSENQHLVTPEA 278
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1178431733  877 SDLIIKLCR-GPEDRLgknGADEIKAHPFFK 906
Cdd:cd14132    279 LDLLDKLLRyDHQERI---TAKEAMQHPYFD 306
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
600-904 3.84e-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: 97.28  E-value: 3.84e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDtKALYATKTLRKKDVllRNQVAH-VKAERDILAE-ADNEWVVRLY-YSFQD-KDNLYF 675
Cdd:cd14131      3 YEILKQLGKGGSSKVYKVLNPK-KKIYALKRVDLEGA--DEQTLQsYKNEIELLKKlKGSDRIIQLYdYEVTDeDDYLYM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYiPGGDMMSLLI--RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIdRDGHIKLTDFGLCTGFRWTHD 753
Cdd:cd14131     80 VMEC-GEIDLATILKkkRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIAKAIQNDTT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 SKYyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraaRQHQrclahslVGTPNYIAPEVLLRTGYTQL-------- 825
Cdd:cd14131    158 SIV--------------------------------------RDSQ-------VGTLNYMSPEAIKDTSASGEgkpkskig 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 --CDWWSVGVILFEMLVGQPPFLA-QTPLETQMKVINWQTSLHIPPQAklSPEASDlIIKLC--RGPEDRLgknGADEIK 900
Cdd:cd14131    193 rpSDVWSLGCILYQMVYGKTPFQHiTNPIAKLQAIIDPNHEIEFPDIP--NPDLID-VMKRClqRDPKKRP---SIPELL 266

                   ....
gi 1178431733  901 AHPF 904
Cdd:cd14131    267 NHPF 270
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
603-905 3.91e-22

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: 97.73  E-value: 3.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRK--KDVLLRNQVAHVKAERDIlaeADNEWVVRLYYSFQDKDN--LYFV-- 676
Cdd:cd07831      4 LGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKhfKSLEQVNNLREIQALRRL---SPHPNILRLIEVLFDRKTgrLALVfe 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 -MDyipggdmMSL--LI--RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDgHIKLTDFGLCTGFRWT 751
Cdd:cd07831     81 lMD-------MNLyeLIkgRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSCRGIYSK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 HDSKYYqsgdhprqdsmdFSNEWgdpsscrcgdrlkplerraarqhqrclahslvgtpnYIAPEVLLRTG-YTQLCDWWS 830
Cdd:cd07831    153 PPYTEY------------ISTRW------------------------------------YRAPECLLTDGyYGPKMDIWA 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  831 VGVILFEMLVGQPPF-----LAQ---------TPLET--QMKVINWQTSLHIPPQ-----AKLSPEAS----DLIIKLCR 885
Cdd:cd07831    185 VGCVFFEILSLFPLFpgtneLDQiakihdvlgTPDAEvlKKFRKSRHMNYNFPSKkgtglRKLLPNASaeglDLLKKLLA 264
                          330       340
                   ....*....|....*....|.
gi 1178431733  886 -GPEDRLgknGADEIKAHPFF 905
Cdd:cd07831    265 yDPDERI---TAKQALRHPYF 282
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
598-852 5.46e-22

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: 97.89  E-value: 5.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLR---KKDVllRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLY 674
Cdd:cd06615      1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHleiKPAI--RNQIIR---ELKVLHECNSPYIVGFYGAFYSDGEIS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLIRMGIFPES-LARFYIAELT--CAVESVHKMgfIHRDIKPDNILIDRDGHIKLTDFGLctgfrwt 751
Cdd:cd06615     76 ICMEHMDGGSLDQVLKKAGRIPENiLGKISIAVLRglTYLREKHKI--MHRDVKPSNILVNSRGEIKLCDFGV------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 hdskyyqSGDhpRQDSMdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSV 831
Cdd:cd06615    147 -------SGQ--LIDSM---------------------------------ANSFVGTRSYMSPERLQGTHYTVQSDIWSL 184
                          250       260
                   ....*....|....*....|.
gi 1178431733  832 GVILFEMLVGQPPFLAQTPLE 852
Cdd:cd06615    185 GLSLVEMAIGRYPIPPPDAKE 205
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
600-858 5.81e-22

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: 96.72  E-value: 5.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDV--LLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd08222      2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVgeLQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDM----MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIdRDGHIKLTDFGLCTGFRWTHD 753
Cdd:cd08222     82 EYCEGGDLddkiSEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILMGTSD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 skyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGV 833
Cdd:cd08222    161 -----------------------------------------------LATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGC 193
                          250       260
                   ....*....|....*....|....*
gi 1178431733  834 ILFEMLVGQPPFLAQTPLETQMKVI 858
Cdd:cd08222    194 ILYEMCCLKHAFDGQNLLSVMYKIV 218
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
603-886 6.59e-22

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: 96.20  E-value: 6.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLlrNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd08219      5 LRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSS--SAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSL--LIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsg 760
Cdd:cd08219     83 GDLMQKikLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFG----------------- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 dhprqdsmdfsnewgdpsscrcgdrlkplerrAAR--QHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd08219    146 --------------------------------SARllTSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYEL 193
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1178431733  839 LVGQPPFLAQTpletqmkvinWQtslhippqaklspeasDLIIKLCRG 886
Cdd:cd08219    194 CTLKHPFQANS----------WK----------------NLILKVCQG 215
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
604-883 6.98e-22

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: 96.57  E-value: 6.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVahvKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14192     10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEV---KNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDGH-IKLTDFGLctgfrwthdskyyqsg 760
Cdd:cd14192     87 ELFDRITDESYqLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGL---------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 dhprqdsmdfsnewgdpsscrcGDRLKPLERRAARqhqrclahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 840
Cdd:cd14192    151 ----------------------ARRYKPREKLKVN----------FGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLS 198
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1178431733  841 GQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKL 883
Cdd:cd14192    199 GLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRL 241
MobB_NDR_LATS-like cd21742
Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear ...
535-595 8.70e-22

Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear Dbf2-related (NDR)/large tumor suppressor (LATS) family includes NDR, LATS, CBK1, and Sid2p. They are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. NDR/LATS kinases bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. These kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR/LATS family serine/threonine protein kinases.


Pssm-ID: 439267  Cd Length: 62  Bit Score: 89.57  E-value: 8.70e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  535 KFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKM 595
Cdd:cd21742      2 KQYIENHYTNLLQQLKERRERRKQLEEKLENLNLSEEEKEQLRKELLKKESEYLRLQRQKL 62
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
598-857 8.72e-22

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: 96.20  E-value: 8.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd14113      7 SFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKK-LMKRDQVTH---ELGVLQSLQHPQLVGLLDTFETPTSYILVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH---IKLTDFGLCTGFrwthDS 754
Cdd:cd14113     83 EMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQL----NT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 KYYqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 834
Cdd:cd14113    159 TYY--------------------------------------------IHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVL 194
                          250       260
                   ....*....|....*....|...
gi 1178431733  835 LFEMLVGQPPFLAQTPLETQMKV 857
Cdd:cd14113    195 TYVLLSGVSPFLDESVEETCLNI 217
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
606-912 1.10e-21

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: 96.62  E-value: 1.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFG--EVCLARKVDTKalYATKTLRKK--------DVLLR-NQVAHVKAERDIlaeadnewvvrlyysFQDKDNLY 674
Cdd:cd14178     11 IGIGSYSvcKRCVHKATSTE--YAVKIIDKSkrdpseeiEILLRyGQHPNIITLKDV---------------YDDGKFVY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILidrdghikltdfglctgfrwthds 754
Cdd:cd14178     74 LVMELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNIL------------------------ 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprqdsmdFSNEWGDPSSCRCGDRLKPLERRAarqhQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 834
Cdd:cd14178    130 ---------------YMDESGNPESIRICDFGFAKQLRA----ENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGIL 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  835 LFEMLVGQPPFL---AQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLgknGADEIKAHPFFKTIDF 910
Cdd:cd14178    191 LYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGGNWDSISDAAKDIVSKMLHvDPHQRL---TAPQVLRHPWIVNREY 267

                   ..
gi 1178431733  911 SS 912
Cdd:cd14178    268 LS 269
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
602-903 1.17e-21

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: 95.57  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAhVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd08220      4 KIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQA-ALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMG--IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHI-KLTDFGLctgfrwthdSKYYQ 758
Cdd:cd08220     83 GGTLFEYIQQRKgsLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGI---------SKILS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd08220    154 S---------------------------------------KSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYEL 194
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  839 LVGQPPFLAQTPLETQMKVINwqtSLHIPPQAKLSPEASDLIIKLCRGPEDRlgKNGADEIKAHP 903
Cdd:cd08220    195 ASLKRAFEAANLPALVLKIMR---GTFAPISDRYSEELRHLILSMLHLDPNK--RPTLSEIMAQP 254
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
604-904 1.70e-21

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: 95.10  E-value: 1.70e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEV--CLARKvdTKALYATKTLRK-----KDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd14184      7 KVIGDGNFAVVkeCVERS--TGKEFALKIIDKakccgKEHLIENEVS-------ILRRVKHPNIIMLIEEMDTPAELYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI----DRDGHIKLTDFGLCTGFRwth 752
Cdd:cd14184     78 MELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVE--- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfsnewgdpsscrcgdrlKPLerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd14184    155 ----------------------------------GPL-------------YTVCGTPTYVAPEIIAETGYGLKVDIWAAG 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETQM--KVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLgknGADEIKAHPF 904
Cdd:cd14184    188 VITYILLCGFPPFRSENNLQEDLfdQILLGKLEFPSPYWDNITDSAKELISHMLQvNVEARY---TAEQILSHPW 259
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
604-904 2.48e-21

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: 95.15  E-value: 2.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLR--KKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDK--DNLYFVMDY 679
Cdd:cd06651     13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQfdPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEY 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQs 759
Cdd:cd06651     93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA---------SKRLQ- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpSSCRCGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd06651    163 ------------------TICMSGTGIR----------------SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 208
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  840 VGQPPFLAQTPLETQMKVINWQTSLHIPpqAKLSPEASDLIIKLCRGPEDRlgkNGADEIKAHPF 904
Cdd:cd06651    209 TEKPPWAEYEAMAAIFKIATQPTNPQLP--SHISEHARDFLGCIFVEARHR---PSAEELLRHPF 268
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
597-844 3.21e-21

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: 94.73  E-value: 3.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd06640      3 EELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEA--EDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLiRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKy 756
Cdd:cd06640     81 MEYLGGGSALDLL-RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd06640    159 ----------------------------------------------NTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAI 192

                   ....*...
gi 1178431733  837 EMLVGQPP 844
Cdd:cd06640    193 ELAKGEPP 200
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
604-845 3.55e-21

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: 94.47  E-value: 3.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALY-----ATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd14076      7 RTLGEGEFGKVKLGWPLPKANHRsgvqvAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdskyyq 758
Cdd:cd14076     87 FVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTF---------- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgDHPRQDSMDfsnewgdpSSCrcgdrlkplerraarqhqrclahslvGTPNYIAPE-VLLRTGYT-QLCDWWSVGVILF 836
Cdd:cd14076    157 --DHFNGDLMS--------TSC--------------------------GSPCYAAPElVVSDSMYAgRKADIWSCGVILY 200

                   ....*....
gi 1178431733  837 EMLVGQPPF 845
Cdd:cd14076    201 AMLAGYLPF 209
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
603-907 5.70e-21

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: 95.51  E-value: 5.70e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLAR------KVDTKAL--------YATKTLRKKDVLLRNQVAHVKAERDILaeadnewvvRLYYSFQ 668
Cdd:cd07855     10 IETIGSGAYGVVCSAIdtksgqKVAIKKIpnafdvvtTAKRTLRELKILRHFKHDNIIAIRDIL---------RPKVPYA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  669 DKDNLYFVMDYIPGgDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgf 748
Cdd:cd07855     81 DFKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGM---- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdskyyqsgdhprqdsmdfsnewgdpssCRCGDRlKPLErraarqHQRCLAhSLVGTPNYIAPEVLLRTG-YTQLCD 827
Cdd:cd07855    156 -------------------------------ARGLCT-SPEE------HKYFMT-EYVATRWYRAPELMLSLPeYTQAID 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  828 WWSVGVILFEMLVGQPPFLAQTPLEtQMKVInwQTSLHIPPQA------------------------------KLSPEAS 877
Cdd:cd07855    197 MWSVGCIFAEMLGRRQLFPGKNYVH-QLQLI--LTVLGTPSQAvinaigadrvrryiqnlpnkqpvpwetlypKADQQAL 273
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1178431733  878 DLIIKLCR-GPEDRLGKNGADEikaHPFFKT 907
Cdd:cd07855    274 DLLSQMLRfDPSERITVAEALQ---HPFLAK 301
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
602-883 5.87e-21

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 93.82  E-value: 5.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd14193      8 KEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARS---QKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDGH-IKLTDFGLctgfrwthdskyyq 758
Cdd:cd14193     85 GGELFDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGL-------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqdsmdfsnewgdpsscrcGDRLKPLERRAARqhqrclahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd14193    151 ------------------------ARRYKPREKLRVN----------FGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYML 196
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1178431733  839 LVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKL 883
Cdd:cd14193    197 LSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISKL 241
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
606-905 7.55e-21

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: 93.88  E-value: 7.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATK--------------TLRKKDVLLR-NQVAH---VKAeRDILA--EADNEWVVRLYY 665
Cdd:cd07838      7 IGEGAYGTVYKARDLQDGRFVALKkvrvplseegiplsTIREIALLKQlESFEHpnvVRL-LDVCHgpRTDRELKLTLVF 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  666 SFQDKDNLYFVMDYIPGGdmmsllirmgiFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLc 745
Cdd:cd07838     86 EHVDQDLATYLDKCPKPG-----------LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGL- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  746 tgfrwthdSKYYqsgdhprQDSMDFSnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQL 825
Cdd:cd07838    154 --------ARIY-------SFEMALT--------------------------------SVVVTLWYRAPEVLLQSSYATP 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 CDWWSVGVILFEMLVGQPPFLAQT--------------------PLETQMKVINWQTSLHIPPQA---KLSPEASDLIIK 882
Cdd:cd07838    187 VDMWSVGCIFAELFNRRPLFRGSSeadqlgkifdviglpseeewPRNSALPRSSFPSYTPRPFKSfvpEIDEEGLDLLKK 266
                          330       340
                   ....*....|....*....|....
gi 1178431733  883 -LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd07838    267 mLTFNPHKRI---SAFEALQHPYF 287
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
604-904 9.23e-21

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: 93.14  E-value: 9.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEV--CLARKVDTKalYATKTLRK-----KDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd14183     12 RTIGDGNFAVVkeCVERSTGRE--YALKIINKskcrgKEHMIQNEVS-------ILRRVKHPNIVLLIEEMDMPTELYLV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI----DRDGHIKLTDFGLCTGFrwth 752
Cdd:cd14183     83 MELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVV---- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgDHPrqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd14183    159 --------DGP--------------------------------------LYTVCGTPTYVAPEIIAETGYGLKVDIWAAG 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETQM--KVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRlgKNGADEIKAHPF 904
Cdd:cd14183    193 VITYILLCGFPPFRGSGDDQEVLfdQILMGQVDFPSPYWDNVSDSAKELITMMLQVDVDQ--RYSALQVLEHPW 264
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
606-905 1.11e-20

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: 92.68  E-value: 1.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRnqvAHVKAERDILAE---------ADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd14005      8 LGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEW---AMINGPVPVPLEialllkaskPGVPGVIRLLDWYERPDGFLLI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDY-IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID-RDGHIKLTDFGlctgfrwthds 754
Cdd:cd14005     85 MERpEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFG----------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprqdsmdfsnewgdpsscrCGDRLKpleRRAARQHQrclahslvGTPNYIAPEVLLRTGY-----TQlcdwW 829
Cdd:cd14005    154 ---------------------------CGALLK---DSVYTDFD--------GTRVYSPPEWIRHGRYhgrpaTV----W 191
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  830 SVGVILFEMLVGQPPFlaqtplETQMKVINWQtsLHIPPqaKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14005    192 SLGILLYDMLCGDIPF------ENDEQILRGN--VLFRP--RLSKECCDLISRcLQFDPSKRP---SLEQILSHPWF 255
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
606-904 1.15e-20

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: 93.63  E-value: 1.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHvkaERDILAE-ADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14090     10 LGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFR---EVETLHQcQGHPNILQLIEYFEDDERFYLVFEKMRGGP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHI---KLTDFGLCTGfrwthdskyyqsgd 761
Cdd:cd14090     87 LLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLGSG-------------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsMDFSNEWGDPSSCRcgDRLKPlerraarqhqrclahslVGTPNYIAPEVL-----LRTGYTQLCDWWSVGVILF 836
Cdd:cd14090    153 ------IKLSSTSMTPVTTP--ELLTP-----------------VGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILY 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPFLA--------------QTPLETQMKVInwQTSLHIPPQAK---LSPEASDLIIKL-CRGPEDRLgknGADE 898
Cdd:cd14090    208 IMLCGYPPFYGrcgedcgwdrgeacQDCQELLFHSI--QEGEYEFPEKEwshISAEAKDLISHLlVRDASQRY---TAEQ 282

                   ....*.
gi 1178431733  899 IKAHPF 904
Cdd:cd14090    283 VLQHPW 288
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
606-898 1.28e-20

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: 93.78  E-value: 1.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTL-RKKDVLLRNQVAHVKaerdiLAEADNEwVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14180     14 LGEGSFSVCRKCRHRQSGQEYAVKIIsRRMEANTQREVAALR-----LCQSHPN-IVALHEVLHDQYHTYLVMELLRGGE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH---IKLTDFGLCtgfrwthdskyyqsgd 761
Cdd:cd14180     88 LLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFA---------------- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsmdfsnewgdpsscrcgdRLKPleRRAARQHQRCLahslvgTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd14180    152 -----------------------RLRP--QGSRPLQTPCF------TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSG 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  842 QPPFLAQTPLETQ-------MKVINWQTSLHIPPQAKLSPEASDLIiklcRG-----PEDRLGKNGADE 898
Cdd:cd14180    201 QVPFQSKRGKMFHnhaadimHKIKEGDFSLEGEAWKGVSEEAKDLV----RGlltvdPAKRLKLSELRE 265
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
606-905 2.04e-20

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 91.93  E-value: 2.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDvlLR---NQVAHVKAERDILAEADNEWVVRLYYSFQD--KDNLYFVMDYI 680
Cdd:cd14119      1 LGEGSYGKVKEVLDTETLCRRAVKILKKRK--LRripNGEANVKREIQILRRLNHRNVIKLVDVLYNeeKQKLYMVMEYC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGdMMSLLIR--MGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwTHDSKYYQ 758
Cdd:cd14119     79 VGG-LQEMLDSapDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGV------AEALDLFA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SGDhprqdsmdfsnewgdpsscRCgdrlkplerraarqhqrclaHSLVGTPNYIAPEVL--LRTGYTQLCDWWSVGVILF 836
Cdd:cd14119    152 EDD-------------------TC--------------------TTSQGSPAFQPPEIAngQDSFSGFKVDIWSAGVTLY 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  837 EMLVGQPPFLAqtplETQMKVIN--WQTSLHIPPQakLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14119    193 NMTTGKYPFEG----DNIYKLFEniGKGEYTIPDD--VDPDLQDLLRGmLEKDPEKRF---TIEQIRQHPWF 255
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
606-905 2.47e-20

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: 91.90  E-value: 2.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14190     12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLL---EIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDGH-IKLTDFGLctgfrwthdskyyqsgdh 762
Cdd:cd14190     89 FERIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILcVNRTGHqVKIIDFGL------------------ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcGDRLKPLERRAARqhqrclahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14190    151 --------------------ARRYNPREKLKVN----------FGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGL 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  843 PPFLAQTPLETQMKVI--NW----QTSLHIPPQAKlsPEASDLIIKlcrgpeDRLGKNGADEIKAHPFF 905
Cdd:cd14190    201 SPFLGDDDTETLNNVLmgNWyfdeETFEHVSDEAK--DFVSNLIIK------ERSARMSATQCLKHPWL 261
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
604-905 2.97e-20

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 91.92  E-value: 2.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRK--KDVLLRNQVAHVKAERDIlaEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd14197     15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKrrKGQDCRMEIIHEIAVLEL--AQANPWVINLHEVYETASEMILVLEYAA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLI--RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD---GHIKLTDFGLctgfrwthdSKY 756
Cdd:cd14197     93 GGEIFNQCVadREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGL---------SRI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 YQSGDHPRQdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd14197    164 LKNSEELRE---------------------------------------IMGTPEYVAPEILSYEPISTATDMWSIGVLAY 204
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14197    205 VMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAIDFIKTlLIKKPENRA---TAEDCLKHPWL 271
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
600-849 3.22e-20

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


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 93.01  E-value: 3.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkDVLLRNQVAhvKAERDIL---AEADNE---WVVRLYYSFQDKDNL 673
Cdd:cd14134     14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIR--NVEKYREAA--KIEIDVLetlAEKDPNgksHCVQLRDWFDYRGHM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDyIPGgdmMSLLIRM-----GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID---------------- 732
Cdd:cd14134     90 CIVFE-LLG---PSLYDFLkknnyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVdsdyvkvynpkkkrqi 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  733 ---RDGHIKLTDFGLCTgFRWTHDSkyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTP 809
Cdd:cd14134    166 rvpKSTDIKLIDFGSAT-FDDEYHS-------------------------------------------------SIVSTR 195
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1178431733  810 NYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFlaQT 849
Cdd:cd14134    196 HYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLF--QT 233
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
606-866 3.44e-20

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: 92.13  E-value: 3.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRL-----YYSFQDKDNLYFV-MDY 679
Cdd:cd13989      1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSArdvppELEKLSPNDLPLLaMEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRM----GIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNI-LIDRDGHI--KLTDFGlctgfrwth 752
Cdd:cd13989     81 CSGGDLRKVLNQPenccGL-KESEVRTLLSDISSAISYLHENRIIHRDLKPENIvLQQGGGRViyKLIDLG--------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdFSNEWGDPSSCRcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd13989    151 -----------------YAKELDQGSLCT----------------------SFVGTLQYLAPELFESKKYTCTVDYWSFG 191
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETQMKVINWQTSLHI 866
Cdd:cd13989    192 TLAFECITGYRPFLPNWQPVQWHGKVKQKKPEHI 225
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
603-845 5.49e-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: 90.97  E-value: 5.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTL--RKKDVLLRNQVAHVKAE--RDI--LAEADNEWVVRLYYSFQDKDNL--- 673
Cdd:cd14077      6 VKTIGAGSMGKVKLAKHIRTGEKCAIKIIprASNAGLKKEREKRLEKEisRDIrtIREAALSSLLNHPHICRLRDFLrtp 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 ---YFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrw 750
Cdd:cd14077     86 nhyYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL------ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdSKYYQSGDHPRQ--DSMDFSnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVllrtgytqlcDW 828
Cdd:cd14077    160 ---SNLYDPRRLLRTfcGSLYFA------------------------------APELLQAQPYTGPEV----------DV 196
                          250
                   ....*....|....*..
gi 1178431733  829 WSVGVILFEMLVGQPPF 845
Cdd:cd14077    197 WSFGVVLYVLVCGKVPF 213
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
597-851 5.69e-20

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: 91.27  E-value: 5.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd06642      3 EELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEA--EDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLiRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKy 756
Cdd:cd06642     81 MEYLGGGSALDLL-KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd06642    159 ----------------------------------------------NTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAI 192
                          250
                   ....*....|....*
gi 1178431733  837 EMLVGQPPFLAQTPL 851
Cdd:cd06642    193 ELAKGEPPNSDLHPM 207
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
600-904 6.74e-20

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 90.87  E-value: 6.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd06645     13 FELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEP---GEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWThdskyyqs 759
Cdd:cd06645     90 CGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITAT-------- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdrlkpLERRaarqhqrclaHSLVGTPNYIAPEVLL---RTGYTQLCDWWSVGVILF 836
Cdd:cd06645    162 -----------------------------IAKR----------KSFIGTPYWMAPEVAAverKGGYNQLCDIWAVGITAI 202
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  837 EMLVGQPPFLAQTPLET--QMKVINWQtslhiPPQAKLSPEASD-----LIIKLCRGPEDRlgkNGADEIKAHPF 904
Cdd:cd06645    203 ELAELQPPMFDLHPMRAlfLMTKSNFQ-----PPKLKDKMKWSNsfhhfVKMALTKNPKKR---PTAEKLLQHPF 269
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
603-906 7.90e-20

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: 91.85  E-value: 7.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTK---ALyatktlrKK--DVLlRNQVAHVKAERDI--LAE-ADNEWVVRLYYSFQ---DKD 671
Cdd:cd07852     12 LKKLGKGAYGIVWKAIDKKTGevvAL-------KKifDAF-RNATDAQRTFREImfLQElNDHPNIIKLLNVIRaenDKD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 nLYFVMDYipggdMMSLL---IRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgf 748
Cdd:cd07852     84 -IYLVFEY-----METDLhavIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLA--- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 RwthdSKYYQSGDHPRQDSMDFsnewgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLL-RTGYTQLCD 827
Cdd:cd07852    155 R----SLSQLEEDDENPVLTDY-----------------------------------VATRWYRAPEILLgSTRYTKGVD 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  828 WWSVGVILFEMLVGQPPF------------LAQTPLETQMKVINWQT--------SLHIPPQ-------AKLSPEASDLI 880
Cdd:cd07852    196 MWSVGCILGEMLLGKPLFpgtstlnqlekiIEVIGRPSAEDIESIQSpfaatmleSLPPSRPksldelfPKASPDALDLL 275
                          330       340
                   ....*....|....*....|....*..
gi 1178431733  881 IK-LCRGPEDRLgknGADEIKAHPFFK 906
Cdd:cd07852    276 KKlLVFNPNKRL---TAEEALRHPYVA 299
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
597-852 8.06e-20

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: 90.90  E-value: 8.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd06641      3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEA--EDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLiRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKy 756
Cdd:cd06641     81 MEYLGGGSALDLL-EPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKR- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd06641    159 ----------------------------------------------N*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAI 192
                          250
                   ....*....|....*.
gi 1178431733  837 EMLVGQPPFLAQTPLE 852
Cdd:cd06641    193 ELARGEPPHSELHPMK 208
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
606-924 9.57e-20

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: 92.01  E-value: 9.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAerdILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14176     27 IGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEI---LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILidrdghikltdfglctgfrwthdskyyqsgdhprq 765
Cdd:cd14176    101 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIL----------------------------------- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  766 dsmdFSNEWGDPSSCRCGDRLKPLERRAarqhQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd14176    146 ----YVDESGNPESIRICDFGFAKQLRA----ENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPF 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  846 L---AQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLgknGADEIKAHPFFKTIDF--SSDLRQQSA 919
Cdd:cd14176    218 AngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHvDPHQRL---TAALVLRHPWIVHWDQlpQYQLNRQDA 294

                   ....*
gi 1178431733  920 SYIPK 924
Cdd:cd14176    295 PHLVK 299
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
604-845 1.25e-19

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: 89.91  E-value: 1.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLAR---KVDTKALYATKTLRKKDVLlrnqvahvKAERDILAEA------DNEWVVRLY-YSFqDKDNL 673
Cdd:cd00192      1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDASE--------SERKDFLKEArvmkklGHPNVVRLLgVCT-EEEPL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDYIPGGDMMS-LLIRMGIFPE------SLARF--YIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd00192     72 YLVMEYMEGGDLLDfLRKSRPVFPSpepstlSLKDLlsFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  745 CtgfRWTHDSKYYQSgdhprqdsmdfsnewgdpsscrcgDRLKPLERRaarqhqrclahslvgtpnYIAPEVLLRTGYTQ 824
Cdd:cd00192    152 S---RDIYDDDYYRK------------------------KTGGKLPIR------------------WMAPESLKDGIFTS 186
                          250       260
                   ....*....|....*....|..
gi 1178431733  825 LCDWWSVGVILFEMLV-GQPPF 845
Cdd:cd00192    187 KSDVWSFGVLLWEIFTlGATPY 208
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
600-890 1.51e-19

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: 89.93  E-value: 1.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKD-VLLRNQVA-HVKAerdiLAEADNEWVVRLYYS--------FQD 669
Cdd:cd14048      8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNnELAREKVLrEVRA----LAKLDHPGIVRYFNAwlerppegWQE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  670 KDN---LYFVMDYIPG---GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG 743
Cdd:cd14048     84 KMDevyLYIQMQLCRKenlKDWMNRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LCTgfrwthdskyyqsgdHPRQDSMDFSNEWGDPSScrcgdrlkplerraARQHQRclahslVGTPNYIAPEVLLRTGYT 823
Cdd:cd14048    164 LVT---------------AMDQGEPEQTVLTPMPAY--------------AKHTGQ------VGTRLYMSPEQIHGNQYS 208
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  824 QLCDWWSVGVILFEMLVgqppflaqtPLETQMKVINWQT---SLHIPPQ-AKLSPEASDLIIK-LCRGPEDR 890
Cdd:cd14048    209 EKVDIFALGLILFELIY---------SFSTQMERIRTLTdvrKLKFPALfTNKYPEERDMVQQmLSPSPSER 271
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
606-853 1.84e-19

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 89.63  E-value: 1.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDV-LLRNQVAHVKAER--DILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14196     13 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrASRRGVSREEIERevSILRQVLHPNIITLHDVYENRTDVVLILELVSG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNI-LIDRDG---HIKLTDFGLCtgfrwthdskyyq 758
Cdd:cd14196     93 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLA------------- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdHPRQDSMDFSNewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd14196    160 ---HEIEDGVEFKN--------------------------------IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYIL 204
                          250
                   ....*....|....*
gi 1178431733  839 LVGQPPFLAQTPLET 853
Cdd:cd14196    205 LSGASPFLGDTKQET 219
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
599-749 1.87e-19

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: 89.44  E-value: 1.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKtLRKKDvLLRNQVAHvkaERDILAE-ADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd14016      1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIK-IEKKD-SKHPQLEY---EAKVYKLlQGGPGIPRLYWFGQEGDYNVMVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIpGGDMMSLLIRMGifpeslARF------YIA-ELTCAVESVHKMGFIHRDIKPDNILIDRDGHIK---LTDFGLCTG 747
Cdd:cd14016     76 DLL-GPSLEDLFNKCG------RKFslktvlMLAdQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAKK 148

                   ..
gi 1178431733  748 FR 749
Cdd:cd14016    149 YR 150
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
606-890 1.90e-19

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: 89.31  E-value: 1.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVahvkaeRDI---LAEADNEWVVRLY-YSFQDKDNLYFVMDYIP 681
Cdd:cd13987      1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFL------REYnisLELSVHPHIIKTYdVAFETEDYYVFAQEYAP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLI-RMGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI-DRD-GHIKLTDFGLCTgfrwthdskyyq 758
Cdd:cd13987     75 YGDLFSIIPpQVGL-PEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLTR------------ 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhpRQDSmdfsnewgdpsscrcgdrlkpLERRAArqhqrclahslvGTPNYIAPEVL---LRTGYT--QLCDWWSVGV 833
Cdd:cd13987    142 -----RVGS---------------------TVKRVS------------GTIPYTAPEVCeakKNEGFVvdPSIDVWAFGV 183
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  834 ILFEMLVGQPPFLAQTPLETQM-KVINWQTSLH--IPPQAK-LSPEASDLIIK-LCRGPEDR 890
Cdd:cd13987    184 LLFCCLTGNFPWEKADSDDQFYeEFVRWQKRKNtaVPSQWRrFTPKALRMFKKlLAPEPERR 245
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
604-845 2.28e-19

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: 89.32  E-value: 2.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEV----CLARKvDTKALYATKTLRKKDVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd08228      8 KKIGRGQFSEVyratCLLDR-KPVALKKVQIFEMMDAKARQDCVK---EIDLLKQLNHPNVIKYLDSFIEDNELNIVLEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLI----RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSK 755
Cdd:cd08228     84 ADAGDLSQMIKyfkkQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL---------GR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd08228    155 FFSS--------------------------------------KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLL 196
                          250
                   ....*....|
gi 1178431733  836 FEMLVGQPPF 845
Cdd:cd08228    197 YEMAALQSPF 206
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
660-880 3.33e-19

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: 89.30  E-value: 3.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  660 VVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDGH-- 736
Cdd:cd14177     60 IITLKDVYDDGRYVYLVTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANad 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  737 -IKLTDFGLCTGFRwthdskyyqsGDHprqdsmdfsnewgdpsscrcGDRLKPlerraarqhqrCLahslvgTPNYIAPE 815
Cdd:cd14177    140 sIRICDFGFAKQLR----------GEN--------------------GLLLTP-----------CY------TANFVAPE 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  816 VLLRTGYTQLCDWWSVGVILFEMLVGQPPFL---AQTPLETQMKVINWQTSLHIPPQAKLSPEASDLI 880
Cdd:cd14177    173 VLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWDTVSDAAKDLL 240
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
606-891 3.65e-19

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: 88.54  E-value: 3.65e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLL-RNQVAHVKAERD--ILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14194     13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsRRGVSREDIEREvsILKEIQHPNVITLHEVYENKTDVILILELVAG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNI-LIDRDG---HIKLTDFGLCtgfrwthdskyyq 758
Cdd:cd14194     93 GELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVpkpRIKIIDFGLA------------- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqDSMDFSNEWgdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLlrtGYTQL---CDWWSVGVIL 835
Cdd:cd14194    160 -------HKIDFGNEF----------------------------KNIFGTPEFVAPEIV---NYEPLgleADMWSIGVIT 201
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  836 FEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRL 891
Cdd:cd14194    202 YILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFIRRlLVKDPKKRM 258
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
603-905 3.74e-19

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: 88.48  E-value: 3.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKaerdILA------EADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd14133      4 LEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIR----LLEllnkkdKADKYHIVRLKDVFYFKNHLCIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIpgGDMMSLLIRMGIFPE-SLARF-YIA-ELTCAVESVHKMGFIHRDIKPDNILI---DRDGhIKLTDFGlctgfrw 750
Cdd:cd14133     80 FELL--SQNLYEFLKQNKFQYlSLPRIrKIAqQILEALVFLHSLGLIHCDLKPENILLasySRCQ-IKIIDFG------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpSSCRCGDRLkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd14133    150 ---------------------------SSCFLTQRL----------------YSYIQSRYYRAPEVILGLPYDEKIDMWS 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  831 VGVILFEMLVGQPPFLAQTPLETQMKVInwqTSLHIPPQAKLS------PEASDLIIK-LCRGPEDRLgknGADEIKAHP 903
Cdd:cd14133    187 LGCILAELYTGEPLFPGASEVDQLARII---GTIGIPPAHMLDqgkaddELFVDFLKKlLEIDPKERP---TASQALSHP 260

                   ..
gi 1178431733  904 FF 905
Cdd:cd14133    261 WL 262
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
602-852 4.58e-19

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: 88.90  E-value: 4.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGI---GAFGEVCLARKVDTKALYATKTLRK-------KDVLLRnqvahvkaERDILAEADNEWVVRLYYSFQDKD 671
Cdd:cd07848      2 KFEVLGVvgeGAYGVVLKCRHKETKEIVAIKKFKDseeneevKETTLR--------ELKMLRTLKQENIVELKEAFRRRG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGgDMMSLLIRM--GIFPESLaRFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFR 749
Cdd:cd07848     74 KLYLVFEYVEK-NMLELLEEMpnGVPPEKV-RSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLS 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 WTHDSKYYQsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWW 829
Cdd:cd07848    152 EGSNANYTE----------------------------------------------YVATRWYRSPELLLGAPYGKAVDMW 185
                          250       260
                   ....*....|....*....|...
gi 1178431733  830 SVGVILFEMLVGQPPFLAQTPLE 852
Cdd:cd07848    186 SVGCILGELSDGQPLFPGESEID 208
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
660-890 7.44e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 91.40  E-value: 7.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  660 VVRLYYSFQDKDNLYFVMDYIPGgdmMSL--LIRMG--IFPESLARfYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG 735
Cdd:NF033483    69 IVSVYDVGEDGGIPYIVMEYVDG---RTLkdYIREHgpLSPEEAVE-IMIQILSALEHAHRNGIVHRDIKPQNILITKDG 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  736 HIKLTDFGLCtgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerRAARQHQRCLAHSLVGTPNYIAPE 815
Cdd:NF033483   145 RVKVTDFGIA----------------------------------------------RALSSTTMTQTNSVLGTVHYLSPE 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  816 ------VLLRTgytqlcDWWSVGVILFEMLVGQPPFLAQTPLETQMKvinwqtslHI-----PPQA---KLSPEASDLII 881
Cdd:NF033483   179 qarggtVDARS------DIYSLGIVLYEMLTGRPPFDGDSPVSVAYK--------HVqedppPPSElnpGIPQSLDAVVL 244
                          250
                   ....*....|
gi 1178431733  882 K-LCRGPEDR 890
Cdd:NF033483   245 KaTAKDPDDR 254
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
600-839 1.17e-18

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: 87.16  E-value: 1.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLAR-KVDTKaLYATKtlrkkdvllRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDN---- 672
Cdd:cd14047      8 FKEIELIGSGGFGQVFKAKhRIDGK-TYAIK---------RVKLNNEKAEREVkaLAKLDHPNIVRYNGCWDGFDYdpet 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 ------------LYFVMDYIPGGDMMSLLIRMGIFP----ESLARFYiaELTCAVESVHKMGFIHRDIKPDNILIDRDGH 736
Cdd:cd14047     78 sssnssrsktkcLFIQMEFCEKGTLESWIEKRNGEKldkvLALEIFE--QITKGVEYIHSKKLIHRDLKPSNIFLVDTGK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  737 IKLTDFGLCTGfrwthdskyyQSGDHPRQDSMdfsnewgdpsscrcgdrlkplerraarqhqrclahslvGTPNYIAPEV 816
Cdd:cd14047    156 VKIGDFGLVTS----------LKNDGKRTKSK--------------------------------------GTLSYMSPEQ 187
                          250       260
                   ....*....|....*....|...
gi 1178431733  817 LLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14047    188 ISSQDYGKEVDIYALGLILFELL 210
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
603-904 1.26e-18

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: 88.23  E-value: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDT----------------KALYATKTLRKKDvLLRnqvaHVKAERDI--LAEADNEWvvrlY 664
Cdd:cd07857      5 IKELGQGAYGIVCSARNAETseeetvaikkitnvfsKKILAKRALRELK-LLR----HFRGHKNItcLYDMDIVF----P 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  665 YSFqdkDNLYFVMDYIPGGdmMSLLIRMGIfPESLARF--YIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDF 742
Cdd:cd07857     76 GNF---NELYLYEELMEAD--LHQIIRSGQ-PLTDAHFqsFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDF 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  743 GLCTGFrwtHDSKYYQSGdhprqdsmdFSNEWgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLR-TG 821
Cdd:cd07857    150 GLARGF---SENPGENAG---------FMTEY-------------------------------VATRWYRAPEIMLSfQS 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  822 YTQLCDWWSVGVILFEMLVGQPPFLAQ--------------TPLETQM------KVINWQTSLHIPPQAKL-------SP 874
Cdd:cd07857    187 YTKAIDVWSVGCILAELLGRKPVFKGKdyvdqlnqilqvlgTPDEETLsrigspKAQNYIRSLPNIPKKPFesifpnaNP 266
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1178431733  875 EASDLIIKLCR-GPEDRLgknGADEIKAHPF 904
Cdd:cd07857    267 LALDLLEKLLAfDPTKRI---SVEEALEHPY 294
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
604-890 1.47e-18

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: 87.00  E-value: 1.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVllrNQVAHVKAERDILAE-ADNEWVVRLYYS--FQDKDNLYF--VMD 678
Cdd:cd13985      6 KQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDE---EQLRVAIKEIEIMKRlCGHPNIVQYYDSaiLSSEGRKEVllLME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGgdmmSLLIRM-----GIFPESLARFYIAELTCAVESVHKMG--FIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwT 751
Cdd:cd13985     83 YCPG----SLVDILeksppSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSAT----T 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 HDSKYYqsgdhprqdsmdfsnewgdpSSCRCGDRLKPLERRAarqhqrclahslvgTPNYIAPEVLLRTGYTQLC---DW 828
Cdd:cd13985    155 EHYPLE--------------------RAEEVNIIEEEIQKNT--------------TPMYRAPEMIDLYSKKPIGekaDI 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  829 WSVGVILFEMLVGQPPFLAqtplETQMKVINwqTSLHIPPQAKLSPEASDLI-IKLCRGPEDR 890
Cdd:cd13985    201 WALGCLLYKLCFFKLPFDE----SSKLAIVA--GKYSIPEQPRYSPELHDLIrHMLTPDPAER 257
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
616-858 1.57e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 90.08  E-value: 1.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  616 LARKVDTKALYATK------TLRKKDVLLRN--QVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMmS 687
Cdd:PTZ00267    75 VGRNPTTAAFVATRgsdpkeKVVAKFVMLNDerQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDL-N 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  688 LLIRMGI-----FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsgdh 762
Cdd:PTZ00267   154 KQIKQRLkehlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFG------------------- 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdFSNEWGDPSSCRcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:PTZ00267   215 -------FSKQYSDSVSLD-------------------VASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLH 268
                          250
                   ....*....|....*.
gi 1178431733  843 PPFLAQTPLETQMKVI 858
Cdd:PTZ00267   269 RPFKGPSQREIMQQVL 284
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
606-891 1.62e-18

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: 86.77  E-value: 1.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLL-RNQVAHVKAERD--ILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14105     13 LGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKAsRRGVSREDIEREvsILRQVLHPNIITLHDVFENKTDVVLILELVAG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNI-LIDRD---GHIKLTDFGLCtgfrwthdskyyq 758
Cdd:cd14105     93 GELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENImLLDKNvpiPRIKLIDFGLA------------- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdHPRQDSMDFSNewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLlrtGYTQL---CDWWSVGVIL 835
Cdd:cd14105    160 ---HKIEDGNEFKN--------------------------------IFGTPEFVAPEIV---NYEPLgleADMWSIGVIT 201
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  836 FEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRL 891
Cdd:cd14105    202 YILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSELAKDFIRQlLVKDPRKRM 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
604-904 1.93e-18

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: 87.13  E-value: 1.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKtlrkkdVLLRNQVAHVKAERDILAeADNEWVVRLYYSFQD----------KDNL 673
Cdd:cd14171     12 QKLGTGISGPVRVCVKKSTGERFALK------ILLDRPKARTEVRLHMMC-SGHPNIVQIYDVYANsvqfpgesspRARL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLC---TG 747
Cdd:cd14171     85 LIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGFAkvdQG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 FRWT-HDSKYYQSgdhprqdsmdfsnewgdpsscrcgdrlkPLERRAARQHQRCLAHSL-VGTPNYiapevllrtgYTQL 825
Cdd:cd14171    165 DLMTpQFTPYYVA----------------------------PQVLEAQRRHRKERSGIPtSPTPYT----------YDKS 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 CDWWSVGVILFEMLVGQPPFLAQTP---LETQMKVINWQTSLHIPPQ--AKLSPEASDLIIK-LCRGPEDRLgknGADEI 899
Cdd:cd14171    207 CDMWSLGVIIYIMLCGYPPFYSEHPsrtITKDMKRKIMTGSYEFPEEewSQISEMAKDIVRKlLCVDPEERM---TIEEV 283

                   ....*
gi 1178431733  900 KAHPF 904
Cdd:cd14171    284 LHHPW 288
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
603-904 2.03e-18

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 86.62  E-value: 2.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd06646     14 IQRVGSGTYGDVYKARNLHTGELAAVKIIKLEP---GDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGG 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWThdskyyqsgdh 762
Cdd:cd06646     91 GSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITAT----------- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerRAARQhqrclahSLVGTPNYIAPEVLL---RTGYTQLCDWWSVGVILFEML 839
Cdd:cd06646    160 -----------------------------IAKRK-------SFIGTPYWMAPEVAAvekNGGYNQLCDIWAVGITAIELA 203
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  840 VGQPPFLAQTPLET--QMKVINWQtslhiPP----QAKLSPEASDLI-IKLCRGPEDRlgkNGADEIKAHPF 904
Cdd:cd06646    204 ELQPPMFDLHPMRAlfLMSKSNFQ-----PPklkdKTKWSSTFHNFVkISLTKNPKKR---PTAERLLTHLF 267
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
606-904 3.35e-18

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 85.92  E-value: 3.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVllrNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd06624     16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDS---REVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLI-RMG--IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR-DGHIKLTDFGlctgfrwthDSKyyqsgd 761
Cdd:cd06624     93 SALLRsKWGplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFG---------TSK------ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsmdfsnewgdpsscrcgdRLKPLerraarqhQRClAHSLVGTPNYIAPEVL---LRtGYTQLCDWWSVGVILFEM 838
Cdd:cd06624    158 -----------------------RLAGI--------NPC-TETFTGTLQYMAPEVIdkgQR-GYGPPADIWSLGCTIIEM 204
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  839 LVGQPPFLAQTPLETQM-KVINWQTSLHIPPQakLSPEASDLIIKlCRGPeDRLGKNGADEIKAHPF 904
Cdd:cd06624    205 ATGKPPFIELGEPQAAMfKVGMFKIHPEIPES--LSEEAKSFILR-CFEP-DPDKRATASDLLQDPF 267
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
600-905 4.69e-18

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: 85.80  E-value: 4.69e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvlLRNQVAHV--KAERDI--LAEADNEWVVRLYYSFQDKDNLYF 675
Cdd:cd07835      1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIR-----LETEDEGVpsTAIREIslLKELNHPNIVRLLDVVHSENKLYL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIpggDM-----MSLLIRMGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrw 750
Cdd:cd07835     76 VFEFL---DLdlkkyMDSSPLTGL-DPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAF-- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewGDPsscrcgdrlkplerraarqhQRCLAHSLVgTPNYIAPEVLL-RTGYTQLCDWW 829
Cdd:cd07835    150 ------------------------GVP--------------------VRTYTHEVV-TLWYRAPEILLgSKHYSTPVDIW 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  830 SVGVILFEMLVGQPPF--------------LAQTPLETQMKVI-----------NWQT---SLHIPPqakLSPEASDLII 881
Cdd:cd07835    185 SVGCIFAEMVTRRPLFpgdseidqlfrifrTLGTPDEDVWPGVtslpdykptfpKWARqdlSKVVPS---LDEDGLDLLS 261
                          330       340
                   ....*....|....*....|....*
gi 1178431733  882 K-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd07835    262 QmLVYDPAKRI---SAKAALQHPYF 283
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
594-845 5.12e-18

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: 85.57  E-value: 5.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  594 KMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLR-KKDVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDN 672
Cdd:cd06620      1 DLKNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHiDAKSSVRKQILR---ELQILHECHSPYIVSFYGAFLNENN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 -LYFVMDYIPGGDMMSLLIRMGIFPEslarFYIAELTCAVES-------VHKMgfIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd06620     78 nIIICMEYMDCGSLDKILKKKGPFPE----EVLGKIAVAVLEgltylynVHRI--IHRDIKPSNILVNSKGQIKLCDFGV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  745 ctgfrwthdskyyqsgdhprqdSMDFSNEwgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQ 824
Cdd:cd06620    152 ----------------------SGELINS---------------------------IADTFVGTSTYMSPERIQGGKYSV 182
                          250       260
                   ....*....|....*....|.
gi 1178431733  825 LCDWWSVGVILFEMLVGQPPF 845
Cdd:cd06620    183 KSDVWSLGLSIIELALGEFPF 203
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
606-906 5.24e-18

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: 85.85  E-value: 5.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHvkaERDILAEAD-NEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14174     10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFR---EVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCTGFRWThdskyyqsgd 761
Cdd:cd14174     87 ILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLGSGVKLN---------- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprqdsmdfsnewgdpSSCrcgdrlKPLErrAARQHQRClahslvGTPNYIAPEVL-----LRTGYTQLCDWWSVGVILF 836
Cdd:cd14174    157 ----------------SAC------TPIT--TPELTTPC------GSAEYMAPEVVevftdEATFYDKRCDLWSLGVILY 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  837 EMLVGQPPFL-----------AQTPLETQMKVIN--WQTSLHIPPQ--AKLSPEASDLIIK-LCRGPEDRLgknGADEIK 900
Cdd:cd14174    207 IMLSGYPPFVghcgtdcgwdrGEVCRVCQNKLFEsiQEGKYEFPDKdwSHISSEAKDLISKlLVRDAKERL---SAAQVL 283

                   ....*.
gi 1178431733  901 AHPFFK 906
Cdd:cd14174    284 QHPWVQ 289
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
604-906 6.49e-18

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: 85.65  E-value: 6.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRK---KDVllrnqvahVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd14085      9 SELGRGATSVVYRCRQKGTQKPYAVKKLKKtvdKKI--------VRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR---DGHIKLTDFGLctgfrwthdSKYY 757
Cdd:cd14085     81 TGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpapDAPLKIADFGL---------SKIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qsgdhPRQDSMDfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd14085    152 -----DQQVTMK----------------------------------TVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYI 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  838 MLVGQPPFLAQTPlETQM--KVINWQTSLHIPPQAKLSPEASDLIIKLCRG-PEDRLGKNGADEikaHPFFK 906
Cdd:cd14085    193 LLCGFEPFYDERG-DQYMfkRILNCDYDFVSPWWDDVSLNAKDLVKKLIVLdPKKRLTTQQALQ---HPWVT 260
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
606-906 8.95e-18

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 84.47  E-value: 8.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKvDTKALYATKTLRKKDVLLRNQVAHVKaERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14027      1 LDSGGFGKVSLCFH-RTQGLVVLKTVYTGPNCIEHNEALLE-EGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWThdskyyqsgdhprq 765
Cdd:cd14027     79 MHVLKKVSV-PLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWS-------------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  766 dsmdfsnewgdpsscrcgdRLKPLERRAARQHQRCLAHSlVGTPNYIAPEVL--LRTGYTQLCDWWSVGVILFEMLVGQP 843
Cdd:cd14027    144 -------------------KLTKEEHNEQREVDGTAKKN-AGTLYYMAPEHLndVNAKPTEKSDVYSFAIVLWAIFANKE 203
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  844 PF---LAQTPLETQMKVINWQTSLHIPPqaKLSPEASDLiIKLC--RGPEDRLGKNGADEiKAHPFFK 906
Cdd:cd14027    204 PYenaINEDQIIMCIKSGNRPDVDDITE--YCPREIIDL-MKLCweANPEARPTFPGIEE-KFRPFYL 267
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
603-882 1.32e-17

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: 84.29  E-value: 1.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEV--CLARKVDTKAlyATKTLRKkdvlLRNQVAHVKAERDIL-AEADNEWVVRLYYSFQDKD-----NLY 674
Cdd:cd06638     23 IETIGKGTYGKVfkVLNKKNGSKA--AVKILDP----IHDIDEEIEAEYNILkALSDHPNVVKFYGMYYKKDvkngdQLW 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSL----LIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrw 750
Cdd:cd06638     97 LVLELCNGGSVTDLvkgfLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGV------ 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdSKYYQSGDHPRQDSmdfsnewgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVL-----LRTGYTQL 825
Cdd:cd06638    171 ---SAQLTSTRLRRNTS--------------------------------------VGTPFWMAPEVIaceqqLDSTYDAR 209
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  826 CDWWSVGVILFEMLVGQPPFLAQTPLETQMKVI-NWQTSLHIPPQakLSPEASDLIIK 882
Cdd:cd06638    210 CDVWSLGITAIELGDGDPPLADLHPMRALFKIPrNPPPTLHQPEL--WSNEFNDFIRK 265
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
597-936 1.36e-17

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: 85.39  E-value: 1.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvlLRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNL- 673
Cdd:cd07880     14 PDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRP---FQSELFAKRAYRELrlLKHMKHENVIGLLDVFTPDLSLd 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 -----YFVMDYIpgGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgf 748
Cdd:cd07880     91 rfhdfYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGL---- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVgTPNYIAPEVLLR-TGYTQLCD 827
Cdd:cd07880    165 ---------------------------------------------ARQTDSEMTGYVV-TRWYRAPEVILNwMHYTQTVD 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  828 WWSVGVILFEMLVGQPPFLAQTPLETQMKVI--------------------NWQTSLhipPQ------AKLSPEASDLII 881
Cdd:cd07880    199 IWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMkvtgtpskefvqklqsedakNYVKKL---PRfrkkdfRSLLPNANPLAV 275
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  882 KLCRG-----PEDRLgknGADEIKAHPFFKTI------------DFSSDLRQQSASYIPKITHpTDTSNFDP 936
Cdd:cd07880    276 NVLEKmlvldAESRI---TAAEALAHPYFEEFhdpedeteappyDDSFDEVDQSLEEWKRLTF-TEILSFQP 343
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
604-845 1.82e-17

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: 84.31  E-value: 1.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd08229     30 KKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAG 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMG----IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQS 759
Cdd:cd08229    110 DLSRMIKHFKkqkrLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL---------GRFFSS 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd08229    181 --------------------------------------KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMA 222

                   ....*.
gi 1178431733  840 VGQPPF 845
Cdd:cd08229    223 ALQSPF 228
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
593-884 1.85e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 84.81  E-value: 1.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  593 AKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLR----KKDVLLRNQVA-----HVKAERD--ILAEADNEWVV 661
Cdd:PTZ00024     4 FSISERYIQKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKiieiSNDVTKDRQLVgmcgiHFTTLRElkIMNEIKHENIM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  662 RLYYSFQDKDNLYFVMDYIpGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTD 741
Cdd:PTZ00024    84 GLVDVYVEGDFINLVMDIM-ASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIAD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  742 FGLCTGFRWthdskyyqsgdhprqdsmdfsnewgDPSSCRCGDRLKPLERRaarqhqrcLAHSLVGTPNYIAPEVLL-RT 820
Cdd:PTZ00024   163 FGLARRYGY-------------------------PPYSDTLSKDETMQRRE--------EMTSKVVTLWYRAPELLMgAE 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  821 GYTQLCDWWSVGVILFEMLVGQPPF--------------LAQTPLETqmkviNWQTSLHIP---PQAKLSPEASDLIIKL 883
Cdd:PTZ00024   210 KYHFAVDMWSVGCIFAELLTGKPLFpgeneidqlgrifeLLGTPNED-----NWPQAKKLPlytEFTPRKPKDLKTIFPN 284

                   .
gi 1178431733  884 C 884
Cdd:PTZ00024   285 A 285
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
642-906 2.27e-17

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: 84.13  E-value: 2.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  642 VAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMG----IFPESLARFYIAELTCAVESVHKM 717
Cdd:cd14094     49 TEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDN 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  718 GFIHRDIKPDNILI---DRDGHIKLTDFGLCTgfrwthdskyyqsgDHPRQDSMdfsnewgdpsscrcgdrlkplerraa 794
Cdd:cd14094    129 NIIHRDVKPHCVLLaskENSAPVKLGGFGVAI--------------QLGESGLV-------------------------- 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  795 rqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAqTPLETQMKVINWQTSLHIPPQAKLSP 874
Cdd:cd14094    169 -------AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISE 240
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1178431733  875 EASDLIIK-LCRGPEDRLgknGADEIKAHPFFK 906
Cdd:cd14094    241 SAKDLVRRmLMLDPAERI---TVYEALNHPWIK 270
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
599-905 3.51e-17

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: 82.94  E-value: 3.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvlLRNQVAHV--KAERDI--LAEADNEWVVRLYYSFQDKDNLY 674
Cdd:cd07860      1 NFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIR-----LDTETEGVpsTAIREIslLKELNHPNIVKLLDVIHTENKLY 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIpGGDM---MSLLIRMGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwt 751
Cdd:cd07860     76 LVFEFL-HQDLkkfMDASALTGI-PLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAF--- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 hdskyyqsgdhprqdsmdfsnewGDPSscrcgdrlkplerraarqhqRCLAHSLVgTPNYIAPEVLLRTG-YTQLCDWWS 830
Cdd:cd07860    151 -----------------------GVPV--------------------RTYTHEVV-TLWYRAPEILLGCKyYSTAVDIWS 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  831 VGVILFEMLVGQPPFLAQ--------------TPLE------TQMKviNWQTSL-HIPPQA------KLSPEASDLIIK- 882
Cdd:cd07860    187 LGCIFAEMVTRRALFPGDseidqlfrifrtlgTPDEvvwpgvTSMP--DYKPSFpKWARQDfskvvpPLDEDGRDLLSQm 264
                          330       340
                   ....*....|....*....|...
gi 1178431733  883 LCRGPEDRLGKNGAdeiKAHPFF 905
Cdd:cd07860    265 LHYDPNKRISAKAA---LAHPFF 284
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
604-890 3.61e-17

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: 82.66  E-value: 3.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEV--CLARKvdTKALYATKTLRKKDvllRNQ--VAHVKAERDILAEA-DNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd14198     14 KELGRGKFAVVrqCISKS--TGQEYAAKFLKKRR---RGQdcRAEILHEIAVLELAkSNPRVVNLHEVYETTSEIILILE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLI--RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL---IDRDGHIKLTDFGLctgfrwthd 753
Cdd:cd14198     89 YAAGGEIFNLCVpdLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILlssIYPLGDIKIVDFGM--------- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 skyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerrAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGV 833
Cdd:cd14198    160 ---------------------------------------SRKIGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGV 200
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  834 ILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDR 890
Cdd:cd14198    201 IAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQLATDFIQKlLVKNPEKR 258
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
603-905 5.62e-17

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: 83.13  E-value: 5.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYAtktLRKKDVLLRNQVAHVKAERDI--LAEADNEWVVRL---YYSFQDKDN----- 672
Cdd:cd07866     13 LGKLGEGTFGEVYKARQIKTGRVVA---LKKILMHNEKDGFPITALREIkiLKKLKHPNVVPLidmAVERPDKSKrkrgs 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIpGGDMMSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwt 751
Cdd:cd07866     90 VYMVTPYM-DHDLSGLLENPSVkLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPY--- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 HDSKYyqsgdhprqdsmdfsnEWGDPSScrcgdrlkPLERRAArqhqrclahSLVGTPNYIAPEVLL-RTGYTQLCDWWS 830
Cdd:cd07866    166 DGPPP----------------NPKGGGG--------GGTRKYT---------NLVVTRWYRPPELLLgERRYTTAVDIWG 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  831 VGVILFEMLVGQPPF--------------LAQTPLETQMKVI-------NWQTSLHIPPQ-----AKLSPEASDLIIKLC 884
Cdd:cd07866    213 IGCVFAEMFTRRPILqgksdidqlhlifkLCGTPTEETWPGWrslpgceGVHSFTNYPRTleerfGKLGPEGLDLLSKLL 292
                          330       340
                   ....*....|....*....|..
gi 1178431733  885 R-GPEDRLGKNGAdeiKAHPFF 905
Cdd:cd07866    293 SlDPYKRLTASDA---LEHPYF 311
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
600-910 5.70e-17

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: 83.18  E-value: 5.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKK-DVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd06650      7 FEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEiKPAIRNQIIR---ELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPES-LARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyy 757
Cdd:cd06650     84 HMDGGSLDQVLKKAGRIPEQiLGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGV------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qSGDhpRQDSMdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd06650    151 -SGQ--LIDSM---------------------------------ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVE 194
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  838 MLVGQPPFlaQTPLETQMKVINWQTSLHIPPQAKLSPeasdliiklcRGPEDRLGKNGADEIKAHPFFKTIDF 910
Cdd:cd06650    195 MAVGRYPI--PPPDAKELELMFGCQVEGDAAETPPRP----------RTPGRPLSSYGMDSRPPMAIFELLDY 255
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
600-905 7.09e-17

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: 83.41  E-value: 7.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvlLRNQVAHVKAERDI--LAEADNEWVVRLY------YSFQDKD 671
Cdd:cd07879     17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRP---FQSEIFAKRAYRELtlLKHMQHENVIGLLdvftsaVSGDEFQ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIpggdMMSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrw 750
Cdd:cd07879     94 DFYLVMPYM----QTDLQKIMGHpLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGL------ 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARqHQRCLAHSLVGTPNYIAPEVLLR-TGYTQLCDWW 829
Cdd:cd07879    164 -------------------------------------------AR-HADAEMTGYVVTRWYRAPEVILNwMHYNQTVDIW 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  830 SVGVILFEMLVGQPPFLAQTPLE--TQ-MKVI-----------------NWQTSLHIPPQAKLS-------PEASDLIIK 882
Cdd:cd07879    200 SVGCIMAEMLTGKTLFKGKDYLDqlTQiLKVTgvpgpefvqkledkaakSYIKSLPKYPRKDFStlfpkasPQAVDLLEK 279
                          330       340
                   ....*....|....*....|....
gi 1178431733  883 LCR-GPEDRLgknGADEIKAHPFF 905
Cdd:cd07879    280 MLElDVDKRL---TATEALEHPYF 300
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
606-905 7.47e-17

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: 81.59  E-value: 7.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVllrNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14191     10 LGSGKFGQVFRLVEKKTKKVWAGKFFKAYSA---KEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGEL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDG-HIKLTDFGLctgfrwthdskyyqsgdh 762
Cdd:cd14191     87 FERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGL------------------ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdrlkplerrAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14191    149 ------------------------------ARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGL 198
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  843 PPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRgpEDRLGKNGADEIKAHPFF 905
Cdd:cd14191    199 SPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLK--KDMKARLTCTQCLQHPWL 259
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
604-891 7.61e-17

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: 81.96  E-value: 7.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEV--CLARKVDTKAlyATKTLRKKDVLLRNQVAHVKAerdilaeADNEWVVRLYYSFQD----KDNLYFVM 677
Cdd:cd14172     10 QVLGLGVNGKVleCFHRRTGQKC--ALKLLYDSPKARREVEHHWRA-------SGGPHIVHILDVYENmhhgKRCLLIIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMG--IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLctgfrwth 752
Cdd:cd14172     81 ECMEGGELFSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGF-------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqSGDHPRQDSMDfsnewgdpSSCRcgdrlkplerraarqhqrclahslvgTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd14172    153 ------AKETTVQNALQ--------TPCY--------------------------TPYYVAPEVLGPEKYDKSCDMWSLG 192
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  833 VILFEMLVGQPPFLAQT--PLETQMK--VINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRL 891
Cdd:cd14172    193 VIMYILLCGFPPFYSNTgqAISPGMKrrIRMGQYGFPNPEWAEVSEEAKQLIRHLLKtDPTERM 256
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
600-890 8.47e-17

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: 81.33  E-value: 8.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLAR-KVDTKAlYATKTLRKKDVLLRNQVAhVKAERDILAEADNEWVVRLYYSFQDKDN-LYFVM 677
Cdd:cd08223      2 YQFLRVIGKGSYGEVWLVRhKRDRKQ-YVIKKLNLKNASKRERKA-AEQEAKLLSKLKHPNIVSYKESFEGEDGfLYIVM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLL-IRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsk 755
Cdd:cd08223     80 GFCEGGDLYTRLkEQKGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIA---------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyqsgdhprqdsmdfsnewgdpsscrcgdrlKPLErraarqHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd08223    150 -------------------------------RVLE------SSSDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCV 192
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  836 FEMLVGQPPFLAQTPLETQMKVINWQtslhIPPQAK-LSPEASDLI-IKLCRGPEDR 890
Cdd:cd08223    193 YEMATLKHAFNAKDMNSLVYKILEGK----LPPMPKqYSPELGELIkAMLHQDPEKR 245
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
604-905 1.12e-16

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 81.02  E-value: 1.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRnqvahvkaERDILAEADNEWVVRLYYSFQD-KDNLYFVMDYIPG 682
Cdd:cd14109     10 EDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPFLMR--------EVDIHNSLDHPNIVQMHDAYDDeKLAVTVIDNLAST 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMS--LLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDgHIKLTDFGLctgfrwthdskyyqsg 760
Cdd:cd14109     82 IELVRdnLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQ---------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 dhprqdsmdfsnewgdpsscrcgdrlkplERRAARQHqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 840
Cdd:cd14109    145 -----------------------------SRRLLRGK---LTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLG 192
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  841 GQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14109    193 GISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFIKKlLVYIPESRL---TVDEALNHPWF 255
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
600-905 1.18e-16

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: 81.37  E-value: 1.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvLLRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd07836      2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIH----LDAEEGTPSTAIREIslMKELKHENIVRLHDVIHTENKLMLVF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGgDM---MSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDS 754
Cdd:cd07836     78 EYMDK-DLkkyMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprqdsmdFSNEwgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLL--RTgYTQLCDWWSVG 832
Cdd:cd07836    157 ---------------FSNE--------------------------------VVTLWYRAPDVLLgsRT-YSTSIDIWSVG 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  833 VILFEMLVGQPPFLAQTPlETQMKVI----------NWQTSLHIP------------PQAKLSPEASDLIIKLCRG---- 886
Cdd:cd07836    189 CIMAEMITGRPLFPGTNN-EDQLLKIfrimgtptesTWPGISQLPeykptfpryppqDLQQLFPHADPLGIDLLHRllql 267
                          330       340
                   ....*....|....*....|
gi 1178431733  887 -PEDRLgknGADEIKAHPFF 905
Cdd:cd07836    268 nPELRI---SAHDALQHPWF 284
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
606-906 1.23e-16

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: 81.20  E-value: 1.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLL-RNQVAHVKAER--DILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14195     13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSsRRGVSREEIERevNILREIQHPNIITLHDIFENKTDVVLILELVSG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNI-LIDRDG---HIKLTDFGLCtgfrwthdskyyq 758
Cdd:cd14195     93 GELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImLLDKNVpnpRIKLIDFGIA------------- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdHPRQDSMDFSNewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd14195    160 ---HKIEAGNEFKN--------------------------------IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYIL 204
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  839 LVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFK 906
Cdd:cd14195    205 LSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRlLVKDPKKRM---TIAQSLEHSWIK 270
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
606-905 1.85e-16

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: 80.32  E-value: 1.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVahvKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14114     10 LGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETV---RKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGEL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID--RDGHIKLTDFGLCTgfrwthdskyyqsgdh 762
Cdd:cd14114     87 FERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLAT---------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdRLKPLErraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14114    151 ----------------------HLDPKE----------SVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGL 198
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  843 PPFLAQTPLET--QMKVINWQTSLHipPQAKLSPEASDLIIKLC-RGPEDRLGKNGADEikaHPFF 905
Cdd:cd14114    199 SPFAGENDDETlrNVKSCDWNFDDS--AFSGISEEAKDFIRKLLlADPNKRMTIHQALE---HPWL 259
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
600-850 2.26e-16

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: 80.93  E-value: 2.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKT-LRKKDVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDK--DNLYFV 676
Cdd:cd06621      3 IVELSSLGEGAGGSVTKCRLRNTKTIFALKTiTTDPNPDVQKQILR---ELEINKSCASPYIVKYYGAFLDEqdSSIGIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMG-----IFPESLARfyIAE-LTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrw 750
Cdd:cd06621     80 MEYCEGGSLDSIYKKVKkkggrIGEKVLGK--IAEsVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGV------ 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfSNEWGDPsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd06621    152 --------------------SGELVNS-----------------------LAGTFTGTSYYMAPERIQGGPYSITSDVWS 188
                          250       260
                   ....*....|....*....|
gi 1178431733  831 VGVILFEMLVGQPPFLAQTP 850
Cdd:cd06621    189 LGLTLLEVAQNRFPFPPEGE 208
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
600-906 3.05e-16

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: 81.19  E-value: 3.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvllRNQVAHVKA---ERDILAEADNEWVVRLYYSF------QDK 670
Cdd:cd07851     17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRP----FQSAIHAKRtyrELRLLKHMKHENVIGLLDVFtpasslEDF 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DNLYFVMDYIpGGDMmSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrw 750
Cdd:cd07851     93 QDVYLVTHLM-GADL-NNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGL------ 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQhqrcLAHSL---VGTPNYIAPEVLL-RTGYTQLC 826
Cdd:cd07851    165 -------------------------------------------ARH----TDDEMtgyVATRWYRAPEIMLnWMHYNQTV 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  827 DWWSVGVILFEMLVGQPPF--------------LAQTPLETQMKVI------NWQTSLHIPPQAKL-------SPEASDL 879
Cdd:cd07851    198 DIWSVGCIMAELLTGKTLFpgsdhidqlkrimnLVGTPDEELLKKIssesarNYIQSLPQMPKKDFkevfsgaNPLAIDL 277
                          330       340
                   ....*....|....*....|....*...
gi 1178431733  880 IIK-LCRGPEDRLgknGADEIKAHPFFK 906
Cdd:cd07851    278 LEKmLVLDPDKRI---TAAEALAHPYLA 302
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
606-906 3.72e-16

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 79.90  E-value: 3.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVllrNQVAhVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd14104      8 LGRGQFGIVHRCVETSSKKTYMAKFVKVKGA---DQVL-VKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVDI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLirmgifpeSLARFYIAELTC---------AVESVHKMGFIHRDIKPDNIL--IDRDGHIKLTDFGlctgfrwthDS 754
Cdd:cd14104     84 FERI--------TTARFELNEREIvsyvrqvceALEFLHSKNIGHFDIRPENIIycTRRGSYIKIIEFG---------QS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 KYYQSGDHPRqdsMDFSnewgdpsscrcgdrlkplerraarqhqrclahslvgTPNYIAPEVLLRTGYTQLCDWWSVGVI 834
Cdd:cd14104    147 RQLKPGDKFR---LQYT------------------------------------SAEFYAPEVHQHESVSTATDMWSLGCL 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  835 LFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRgpEDRLGKNGADEIKAHPFFK 906
Cdd:cd14104    188 VYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLV--KERKSRMTAQEALNHPWLK 257
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
600-837 4.58e-16

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: 78.89  E-value: 4.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLR---KKDVLLRNQVAHVKaERDILAEADNewVVRLYYSFQDKDNLYFV 676
Cdd:cd14050      3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRsrfRGEKDRKRKLEEVE-RHEKLGEHPN--CVRFIKAWEEKGILYIQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPggdmMSL---LIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRwTHD 753
Cdd:cd14050     80 TELCD----TSLqqyCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELD-KED 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 SKYYQSGDhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahslvgtPNYIAPEvLLRTGYTQLCDWWSVGV 833
Cdd:cd14050    155 IHDAQEGD-----------------------------------------------PRYMAPE-LLQGSFTKAADIFSLGI 186

                   ....
gi 1178431733  834 ILFE 837
Cdd:cd14050    187 TILE 190
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
604-905 5.50e-16

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: 78.88  E-value: 5.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVclarkvdtKALYATKTLRKKDVLLRNQVA--------HVKAERDILAEADNEWVVRLYYSFQDKD-NLY 674
Cdd:cd14163      6 KTIGEGTYSKV--------KEAFSKKHQRKVAIKIIDKSGgpeefiqrFLPRELQIVERLDHKNIIHVYEMLESADgKIY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIdRDGHIKLTDFGLCtgfrwthds 754
Cdd:cd14163     78 LVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFA--------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprqdsmdfsnewgdpsscrcgdRLKPLERRAarqhqrcLAHSLVGTPNYIAPEVLLRTGY-TQLCDWWSVGV 833
Cdd:cd14163    148 ------------------------------KQLPKGGRE-------LSQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGV 190
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  834 ILFEMLVGQPPFlaqtpLETQMKVINW--QTSLHIPPQAKLSPEASDLIIKLCRgpEDRLGKNGADEIKAHPFF 905
Cdd:cd14163    191 VLYVMLCAQLPF-----DDTDIPKMLCqqQKGVSLPGHLGVSRTCQDLLKRLLE--PDMVLRPSIEEVSWHPWL 257
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
604-845 5.70e-16

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: 78.75  E-value: 5.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKK--------DVLLRnqvahvkaERDILAEADNEWVVRLYYSFQDKDN-LY 674
Cdd:cd14164      6 TTIGEGSFSKVKLATSQKYCCKVAIKIVDRRraspdfvqKFLPR--------ELSILRRVNHPNIVQMFECIEVANGrLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDyIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG-HIKLTDFGlctgfrwthd 753
Cdd:cd14164     78 IVME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFG---------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 skyyqsgdhprqdsmdFSNEWGDPSScrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGY-TQLCDWWSVG 832
Cdd:cd14164    147 ----------------FARFVEDYPE---------------------LSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLG 189
                          250
                   ....*....|...
gi 1178431733  833 VILFEMLVGQPPF 845
Cdd:cd14164    190 VVLYVMVTGTMPF 202
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
603-749 8.35e-16

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: 78.45  E-value: 8.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRK---KDVLlrnqvahvKAERDILAEADN-EWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd14017      5 VKKIGGGGFGEIYKVRDVVDGEEVAMKVESKsqpKQVL--------KMEVAVLKKLQGkPHFCRLIGCGRTERYNYIVMT 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  679 YIpGGDMMSLLIRM--GIFPESLA-RFYIAELtCAVESVHKMGFIHRDIKPDNILIDRDGH----IKLTDFGLCTGFR 749
Cdd:cd14017     77 LL-GPNLAELRRSQprGKFSVSTTlRLGIQIL-KAIEDIHEVGFLHRDVKPSNFAIGRGPSdertVYILDFGLARQYT 152
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
598-928 9.52e-16

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: 79.82  E-value: 9.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLArkVDTKAlyaTKTLRKKDVLLRN--QVAHVKAERDILAEADNEWVVRLYYSFQDK----- 670
Cdd:cd07854      5 SRYMDLRPLGCGSNGLVFSA--VDSDC---DKRVAVKKIVLTDpqSVKHALREIKIIRRLDHDNIVKVYEVLGPSgsdlt 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 ---------DNLYFVMDYIPGGdmMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHI-KLT 740
Cdd:cd07854     80 edvgsltelNSVYIVQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  741 DFGLCTgfrwTHDSKYYQSGdhprQDSMDFSNEWgdpsscrcgdrlkplerraarqhqrclahslvgtpnYIAPEVLLR- 819
Cdd:cd07854    158 DFGLAR----IVDPHYSHKG----YLSEGLVTKW------------------------------------YRSPRLLLSp 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  820 TGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLEtQMKVI---------------------NWQTSLHIP--PQAKL---- 872
Cdd:cd07854    194 NNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELE-QMQLIlesvpvvreedrnellnvipsFVRNDGGEPrrPLRDLlpgv 272
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  873 SPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTIDFSSDLrqqsasyiPKITHP 928
Cdd:cd07854    273 NPEALDFLEQiLTFNPMDRL---TAEEALMHPYMSCYSCPFDE--------PVSLHP 318
pknD PRK13184
serine/threonine-protein kinase PknD;
603-845 1.31e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 81.74  E-value: 1.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRK---KDVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:PRK13184     7 IRLIGKGGMGEVYLAYDPVCSRRVALKKIREdlsENPLLKKRFLR---EAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRM---GIFPESLA---------RFYIaELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTg 747
Cdd:PRK13184    84 IEGYTLKSLLKSVwqkESLSKELAektsvgaflSIFH-KICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAI- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 frwthdskyYQSGDHPRQDSMDFsnewGDPSSCrcgdrlkplerraarQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCD 827
Cdd:PRK13184   162 ---------FKKLEEEDLLDIDV----DERNIC---------------YSSMTIPGKIVGTPDYMAPERLLGVPASESTD 213
                          250
                   ....*....|....*...
gi 1178431733  828 WWSVGVILFEMLVGQPPF 845
Cdd:PRK13184   214 IYALGVILYQMLTLSFPY 231
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
600-904 1.83e-15

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: 78.89  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLA------RKVDTK-------ALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEwvvrlyyS 666
Cdd:cd07849      7 YQNLSYIGEGAYGMVCSAvhkptgQKVAIKkispfehQTYCLRTLREIKILLRFKHENIIGILDIQRPPTFE-------S 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  667 FQDkdnLYFVMDYIPGgDMMSLlIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT 746
Cdd:cd07849     80 FKD---VYIVQELMET-DLYKL-IKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  747 gfrwTHDskyyQSGDHPRqdsmdFSNEWgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLRT-GYTQL 825
Cdd:cd07849    155 ----IAD----PEHDHTG-----FLTEY-------------------------------VATRWYRAPEIMLNSkGYTKA 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 CDWWSVGVILFEMLVGQPPF-----LAQ---------TP----LETQ--MKVINWQTSL-HIP--PQAKLSPEAS----D 878
Cdd:cd07849    191 IDIWSVGCILAEMLSNRPLFpgkdyLHQlnlilgilgTPsqedLNCIisLKARNYIKSLpFKPkvPWNKLFPNADpkalD 270
                          330       340
                   ....*....|....*....|....*..
gi 1178431733  879 LIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:cd07849    271 LLDKmLTFNPHKRI---TVEEALAHPY 294
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
604-905 1.88e-15

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: 77.25  E-value: 1.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTL----RKKDVLLRnqvahvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd14108      8 KEIGRGAFSYLRRVKEKSSDLSFAAKFIpvraKKKTSARR--------ELALLAELDHKSIVRFHDAFEKRRVVIIVTEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFpESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG--HIKLTDFGlctgfrwthdskyy 757
Cdd:cd14108     80 CHEELLERITKRPTVC-ESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFG-------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qsgdhprqdsmdfsnewgdpsscrCGDRLKPLERraarqhQRCLahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd14108    145 ------------------------NAQELTPNEP------QYCK----YGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYL 190
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCrgPEDRLGKNgADEIKAHPFF 905
Cdd:cd14108    191 CLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVL--VSDRLRPD-AEETLEHPWF 255
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
602-959 2.18e-15

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: 78.94  E-value: 2.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTL-RKKDVLLRNQVAHvkAERDILAEADNEWVVRLY------YSFQDKDNLY 674
Cdd:cd07878     19 NLTPVGSGAYGSVCSAYDTRLRQKVAVKKLsRPFQSLIHARRTY--RELRLLKHMKHENVIGLLdvftpaTSIENFNEVY 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIpGGDMMSLlIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthds 754
Cdd:cd07878     97 LVTNLM-GADLNNI-VKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGL---------- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAhSLVGTPNYIAPEVLLR-TGYTQLCDWWSVGV 833
Cdd:cd07878    165 ---------------------------------------ARQADDEMT-GYVATRWYRAPEIMLNwMHYNQTVDIWSVGC 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  834 ILFEMLVGQPPFLAQ---TPLETQMKVINWQTSLHIppqAKLSPE-ASDLIIKLCRGPEDRLGK--NGADEIKAHPFFKT 907
Cdd:cd07878    205 IMAELLKGKALFPGNdyiDQLKRIMEVVGTPSPEVL---KKISSEhARKYIQSLPHMPQQDLKKifRGANPLAIDLLEKM 281
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  908 IDFSSDLRQQSASyipKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTLNGW 959
Cdd:cd07878    282 LVLDSDKRISASE---ALAHPYFSQYHDPEDEPEAEPYDESPENKERTIEEW 330
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
609-853 2.22e-15

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: 78.03  E-value: 2.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  609 GAFGEVCLARKVDTKALYATK--------------TLRKKDVLLRNQ---VAHVKaerdilaeadnEWVVRlyysfQDKD 671
Cdd:cd07843     16 GTYGVVYRARDKKTGEIVALKklkmekekegfpitSLREINILLKLQhpnIVTVK-----------EVVVG-----SNLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGgDMMSLLIRMgifPESlarFYIAELTC-------AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd07843     80 KIYMVMEYVEH-DLKSLMETM---KQP---FLQSEVKClmlqllsGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  745 ctgfrwthdskyyqsgdhprqdsmdfSNEWGDPsscrcgdrLKPLERraarqhqrclahsLVGTPNYIAPEVLLRTG-YT 823
Cdd:cd07843    153 --------------------------AREYGSP--------LKPYTQ-------------LVVTLWYRAPELLLGAKeYS 185
                          250       260       270
                   ....*....|....*....|....*....|
gi 1178431733  824 QLCDWWSVGVILFEMLVGQPPFLAQTPLET 853
Cdd:cd07843    186 TAIDMWSVGCIFAELLTKKPLFPGKSEIDQ 215
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
594-859 2.40e-15

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: 77.92  E-value: 2.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  594 KMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLR---KKDVLLRNQVAHVKaerdILAEADNEWVVRLY------ 664
Cdd:cd07864      3 KRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIK----ILRQLNHRSVVNLKeivtdk 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  665 ---YSF-QDKDNLYFVMDYIpGGDMMSLL-IRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKL 739
Cdd:cd07864     79 qdaLDFkKDKGAFYLVFEYM-DHDLMGLLeSGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  740 TDFGLctgfrwthdSKYYQSgdhprQDSMDFSNEwgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLL- 818
Cdd:cd07864    158 ADFGL---------ARLYNS-----EESRPYTNK--------------------------------VITLWYRPPELLLg 191
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1178431733  819 RTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLeTQMKVIN 859
Cdd:cd07864    192 EERYGPAIDVWSCGCILGELFTKKPIFQANQEL-AQLELIS 231
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
603-886 3.14e-15

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: 77.34  E-value: 3.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKkdvlLRNQVAHVKAERDILAEADNEW-VVRLYYSFQDKDN-----LYFV 676
Cdd:cd06639     27 IETIGKGTYGKVYKVTNKKDGSLAAVKILDP----ISDVDEEIEAEYNILRSLPNHPnVVKFYGMFYKADQyvggqLWLV 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMM----SLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwth 752
Cdd:cd06639    103 LELCNGGSVTelvkGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL---- 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfsnewgdpSSCRcgdrlkpLERRAArqhqrclahslVGTPNYIAPEVL-----LRTGYTQLCD 827
Cdd:cd06639    179 -------------------------TSAR-------LRRNTS-----------VGTPFWMAPEVIaceqqYDYSYDARCD 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  828 WWSVGVILFEMLVGQPPFLAQTPLETQMKVInwqtslHIPPQAKLSPEasdliiKLCRG 886
Cdd:cd06639    216 VWSLGITAIELADGDPPLFDMHPVKALFKIP------RNPPPTLLNPE------KWCRG 262
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
600-845 3.27e-15

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: 77.46  E-value: 3.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvlLRNQVAHV--KAERDI--LAEADNEWVVRLYYSFQDKDNLYF 675
Cdd:cd07861      2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIR-----LESEEEGVpsTAIREIslLKELQHPNIVCLEDVLMQENRLYL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 V-----------MDYIPGGDMMsllirmgifPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd07861     77 VfeflsmdlkkyLDSLPKGKYM---------DAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  745 CTGFrwthdskyyqsgdhprqdsmdfsnewGDPSscrcgdrlkplerraarqhqRCLAHSLVgTPNYIAPEVLL-RTGYT 823
Cdd:cd07861    148 ARAF--------------------------GIPV--------------------RVYTHEVV-TLWYRAPEVLLgSPRYS 180
                          250       260
                   ....*....|....*....|..
gi 1178431733  824 QLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd07861    181 TPVDIWSIGTIFAEMATKKPLF 202
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
602-906 4.27e-15

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: 76.81  E-value: 4.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd06622      5 VLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLE--LDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLL---IRMGIFPESLARFYIAELTCAVESV-HKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyy 757
Cdd:cd06622     83 AGSLDKLYaggVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGV------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qSGdhprqdsmdfsnewgdpsscrcgdrlkplerraarQHQRCLAHSLVGTPNYIAPEVLLRTG------YTQLCDWWSV 831
Cdd:cd06622    150 -SG-----------------------------------NLVASLAKTNIGCQSYMAPERIKSGGpnqnptYTVQSDVWSL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  832 GVILFEMLVGQPPFlaqtPLET------QMKVINWQTSLHIPPQakLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPF 904
Cdd:cd06622    194 GLSILEMALGRYPY----PPETyanifaQLSAIVDGDPPTLPSG--YSDDAQDFVAKcLNKIPNRR---PTYAQLLEHPW 264

                   ..
gi 1178431733  905 FK 906
Cdd:cd06622    265 LV 266
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
603-905 4.76e-15

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: 76.92  E-value: 4.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLR-------------KKDVLLR--NQVAHVKAER--DILAEA--DNEWVVRL 663
Cdd:cd07863      5 VAEIGVGAYGTVYKARDPHSGHFVALKSVRvqtnedglplstvREVALLKrlEAFDHPNIVRlmDVCATSrtDRETKVTL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  664 YYSFQDKDnLYFVMDYIPGGDMmsllirmgifPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG 743
Cdd:cd07863     85 VFEHVDQD-LRTYLDKVPPPGL----------PAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LctgfrwthdSKYYqsgdhprqdsmdfsnewgdpsSCRCGdrLKPlerraarqhqrclahsLVGTPNYIAPEVLLRTGYT 823
Cdd:cd07863    154 L---------ARIY---------------------SCQMA--LTP----------------VVVTLWYRAPEVLLQSTYA 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  824 QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVIN---------WQTSLHIP----------PQAKLSPE----ASDLI 880
Cdd:cd07863    186 TPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDliglppeddWPRDVTLPrgafsprgprPVQSVVPEieesGAQLL 265
                          330       340
                   ....*....|....*....|....*.
gi 1178431733  881 IK-LCRGPEDRLGKNGADEikaHPFF 905
Cdd:cd07863    266 LEmLTFNPHKRISAFRALQ---HPFF 288
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
602-905 4.91e-15

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: 76.70  E-value: 4.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd07839      4 KLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDD---DDEGVPSSALREIclLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IpGGDMMSLLIRMGIFPE-SLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdskyyq 758
Cdd:cd07839     81 C-DQDLKKYFDSCNGDIDpEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAF---------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqdsmdfsnewGDPSscrcgdrlkplerraarqhqRCLAHSLVgTPNYIAPEVLL-RTGYTQLCDWWSVGVILFE 837
Cdd:cd07839    150 ----------------GIPV--------------------RCYSAEVV-TLWYRPPDVLFgAKLYSTSIDMWSAGCIFAE 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVI----------NWQTSLHIP-----PQ-----------AKLSPEASDLIIKLCR-GPEDR 890
Cdd:cd07839    193 LANAGRPLFPGNDVDDQLKRIfrllgtpteeSWPGVSKLPdykpyPMypattslvnvvPKLNSTGRDLLQNLLVcNPVQR 272
                          330
                   ....*....|....*
gi 1178431733  891 LgknGADEIKAHPFF 905
Cdd:cd07839    273 I---SAEEALQHPYF 284
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
606-904 5.10e-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: 5.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEV--CL--ARKVDTKALYATKTLRKKDvllrnQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd14115      1 IGRGRFSIVkkCLhkATRKDVAVKFVSKKMKKKE-----QAAH---EAALLQHLQHPQYITLHDTYESPTSYILVLELMD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD---GHIKLTDFGlctgfrwthdskyyq 758
Cdd:cd14115     73 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLE--------------- 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqDSMDFSNewgdpsscrcgdrlkplerraarqHQRclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd14115    138 -------DAVQISG------------------------HRH--VHHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVM 184
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  839 LVGQPPFLAQTPLETQMKVInwQTSLHIPPQ--AKLSPEASDLIIKLCRgpEDRLGKNGADEIKAHPF 904
Cdd:cd14115    185 LSGVSPFLDESKEETCINVC--RVDFSFPDEyfGDVSQAARDFINVILQ--EDPRRRPTAATCLQHPW 248
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
604-890 7.38e-15

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 78.37  E-value: 7.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDN--------LYF 675
Cdd:PTZ00283    38 RVLGSGATGTVLCAKRVSDGEPFAVKVVDMEG-MSEADKNRAQAEVCCLLNCDFFSIVKCHEDFAKKDPrnpenvlmIAL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMmslliRMGI---------FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLct 746
Cdd:PTZ00283   117 VLDYANAGDL-----RQEIksraktnrtFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGF-- 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  747 gfrwthdSKYYqsgdhprqdSMDFSNEWGdpsscrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLC 826
Cdd:PTZ00283   190 -------SKMY---------AATVSDDVG---------------------------RTFCGTPYYVAPEIWRRKPYSKKA 226
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  827 DWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSlHIPPQakLSPEASDLIIKLCRG-PEDR 890
Cdd:PTZ00283   227 DMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYD-PLPPS--ISPEMQEIVTALLSSdPKRR 288
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
600-852 7.94e-15

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: 76.64  E-value: 7.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLR---KKDVL----LRnqvahvkaERDILAEADNEWVVRLYYSFQDK-- 670
Cdd:cd07845      9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRmdnERDGIpissLR--------EITLLLNLRHPNIVELKEVVVGKhl 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DNLYFVMDYIPGgDMMSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfr 749
Cdd:cd07845     81 DSIFLVMEYCEQ-DLASLLDNMPTpFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGL----- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 wthdSKYYQSGDHPRqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahslvgTPN-----YIAPEVLL-RTGYT 823
Cdd:cd07845    155 ----ARTYGLPAKPM-------------------------------------------TPKvvtlwYRAPELLLgCTTYT 187
                          250       260
                   ....*....|....*....|....*....
gi 1178431733  824 QLCDWWSVGVILFEMLVGQPPFLAQTPLE 852
Cdd:cd07845    188 TAIDMWAVGCILAELLAHKPLLPGKSEIE 216
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
638-904 1.09e-14

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: 75.09  E-value: 1.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  638 LRNQ-VAHVKAERDILAEADNEWVVRLyysfqdkdnlyfVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHK 716
Cdd:cd14012     55 LRHPnLVSYLAFSIERRGRSDGWKVYL------------LTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHR 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  717 MGFIHRDIKPDNILIDRDGH---IKLTDFGLCTGFRwthdskyyqsgDHPRQDSMDFSNEwgdpsscrcgdrlkplerra 793
Cdd:cd14012    123 NGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLL-----------DMCSRGSLDEFKQ-------------------- 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  794 arqhqrclahslvgtPNYIAPEVLLRTG-YTQLCDWWSVGVILFEMLVGQPPFlaqtpletqmkviNWQTSLH-IPPQAK 871
Cdd:cd14012    172 ---------------TYWLPPELAQGSKsPTRKTDVWDLGLLFLQMLFGLDVL-------------EKYTSPNpVLVSLD 223
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1178431733  872 LSPEASDLIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:cd14012    224 LSASLQDFLSKcLSLDPKKRP---TALELLPHEF 254
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
591-906 1.48e-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: 75.49  E-value: 1.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  591 KRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRK-------KDVLLRNQVahvkaerdILAEADNEWVVRL 663
Cdd:cd06618      8 KKYKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRsgnkeenKRILMDLDV--------VLKSHDCPYIVKC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  664 YYSFQDKDNLYFVMDyipggdMMS-----LLIRM-GIFPEslarFYIAELTCA-VESVH----KMGFIHRDIKPDNILID 732
Cdd:cd06618     80 YGYFITDSDVFICME------LMStcldkLLKRIqGPIPE----DILGKMTVSiVKALHylkeKHGVIHRDVKPSNILLD 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  733 RDGHIKLTDFGLcTGFrwthdskyyqsgdhpRQDSMDFSnewgdpsscrcgdrlkplerRAArqhqrclahslvGTPNYI 812
Cdd:cd06618    150 ESGNVKLCDFGI-SGR---------------LVDSKAKT--------------------RSA------------GCAAYM 181
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  813 APEVL---LRTGYTQLCDWWSVGVILFEMLVGQPPF-LAQTPLETQMKVINWQTSLhIPPQAKLSPEASDLIIKLCRGPE 888
Cdd:cd06618    182 APERIdppDNPKYDIRADVWSLGISLVELATGQFPYrNCKTEFEVLTKILNEEPPS-LPPNEGFSPDFCSFVDLCLTKDH 260
                          330
                   ....*....|....*...
gi 1178431733  889 DRLGKngADEIKAHPFFK 906
Cdd:cd06618    261 RYRPK--YRELLQHPFIR 276
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
606-906 2.11e-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: 74.50  E-value: 2.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVL----------LRNQVAHVKAerdILAEADNEWVVRLYYSFQDKDNLYF 675
Cdd:cd14101      8 LGKGGFGTVYAGHRISDGLQVAIKQISRNRVQqwsklpgvnpVPNEVALLQS---VGGGPGHRGVIRLLDWFEIPEGFLL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDY-IPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID-RDGHIKLTDFGLCTGFrwtHD 753
Cdd:cd14101     85 VLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFGSGATL---KD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 SKYyqsgdhprqdsMDFSnewgdpsscrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQL-CDWWSVG 832
Cdd:cd14101    162 SMY-----------TDFD-----------------------------------GTRVYSPPEWILYHQYHALpATVWSLG 195
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  833 VILFEMLVGQPPFlaqtplETQMKVInwQTSLHIPpqAKLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPFFK 906
Cdd:cd14101    196 ILLYDMVCGDIPF------ERDTDIL--KAKPSFN--KRVSNDCRSLIRScLAYNPSDR---PSLEQILLHPWMM 257
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
606-845 4.54e-14

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: 73.46  E-value: 4.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARkVDTKALYATKTLRKKDvllrNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd14066      1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMN----CAASKKEFLTELemLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 dmmSLLIRM----GIFPESL-ARFYIA-ELTCAVESVHKMGF---IHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthds 754
Cdd:cd14066     76 ---SLEDRLhchkGSPPLPWpQRLKIAkGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLA--------- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprqdsmdfsnewgdpsscrcgdRLKPLERRAARQhqrclaHSLVGTPNYIAPEvLLRTG-YTQLCDWWSVGV 833
Cdd:cd14066    144 ------------------------------RLIPPSESVSKT------SAVKGTIGYLAPE-YIRTGrVSTKSDVYSFGV 186
                          250
                   ....*....|..
gi 1178431733  834 ILFEMLVGQPPF 845
Cdd:cd14066    187 VLLELLTGKPAV 198
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
602-905 4.76e-14

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: 74.10  E-value: 4.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYAtktLRKKDVLLRNQVAHVKAERDI---LAEADNEWVVRL----YYSFQDKDNLY 674
Cdd:cd07837      5 KLEKIGEGTYGKVYKARDKNTGKLVA---LKKTRLEMEEEGVPSTALREVsllQMLSQSIYIVRLldveHVEENGKPLLY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIpGGDMMSLLIRMG-----IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD-GHIKLTDFGLCTGF 748
Cdd:cd07837     82 LVFEYL-DTDLKKFIDSYGrgphnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGLGRAF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwTHDSKYYqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVgTPNYIAPEVLL-RTGYTQLCD 827
Cdd:cd07837    161 --TIPIKSY--------------------------------------------THEIV-TLWYRAPEVLLgSTHYSTPVD 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  828 WWSVGVILFEMLVGQPPF--------------LAQTPLETQ----MKVINWqtslHIPPQAK----------LSPEASDL 879
Cdd:cd07837    194 MWSVGCIFAEMSRKQPLFpgdselqqllhifrLLGTPNEEVwpgvSKLRDW----HEYPQWKpqdlsravpdLEPEGVDL 269
                          330       340
                   ....*....|....*....|....*..
gi 1178431733  880 IIKLCR-GPEDRLGKNGADEikaHPFF 905
Cdd:cd07837    270 LTKMLAyDPAKRISAKAALQ---HPYF 293
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
611-890 5.98e-14

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: 73.14  E-value: 5.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  611 FGEVCLARKVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLI 690
Cdd:cd14088     14 FCEIFRAKDKTTGKLYTCKKFLKRDG--RKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWIL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  691 RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILidrdghikltdfglctgfrwthdskYYQSGDHPRQDSMDF 770
Cdd:cd14088     92 DQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLV-------------------------YYNRLKNSKIVISDF 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  771 snewgdpsscrcgdRLKPLERRaarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTP 850
Cdd:cd14088    147 --------------HLAKLENG--------LIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAE 204
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1178431733  851 LETQ--------MKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDR 890
Cdd:cd14088    205 EDDYenhdknlfRKILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQ 252
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
606-890 6.02e-14

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: 72.86  E-value: 6.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd05041      3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLP--PDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMGifpeslARFYIAELT-CAVESVHKMGF------IHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYQ 758
Cdd:cd05041     81 LTFLRKKG------ARLTVKQLLqMCLDAAAGMEYleskncIHRDLAARNCLVGENNVLKISDFGMS---REEEDGEYTV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SGdhprqdsmdfsnewgdpsscrcGDRLKPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd05041    152 SD----------------------GLKQIPIK--------------------WTAPEALNYGRYTSESDVWSFGILLWEI 189
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  839 L-VGQPPFLAQTPLETQMKVinwQTSLHIPPqAKLSPEASDLIIKLC--RGPEDR 890
Cdd:cd05041    190 FsLGATPYPGMSNQQTREQI---ESGYRMPA-PELCPEAVYRLMLQCwaYDPENR 240
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
599-851 6.32e-14

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: 73.50  E-value: 6.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKTLrkkDVLlRNQVAHVKAERDILAEADNEWVVRLYY-SFQDK------D 671
Cdd:cd06636     17 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM---DVT-EDEEEEIKLEINMLKKYSHHRNIATYYgAFIKKsppghdD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGDMMSLL--IRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfr 749
Cdd:cd06636     93 QLWLVMEFCGAGSVTDLVknTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA--- 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 wthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkPLERRAARQhqrclaHSLVGTPNYIAPEVLL-----RTGYTQ 824
Cdd:cd06636    170 --------------------------------------QLDRTVGRR------NTFIGTPYWMAPEVIAcdenpDATYDY 205
                          250       260
                   ....*....|....*....|....*..
gi 1178431733  825 LCDWWSVGVILFEMLVGQPPFLAQTPL 851
Cdd:cd06636    206 RSDIWSLGITAIEMAEGAPPLCDMHPM 232
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
697-883 6.42e-14

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: 73.59  E-value: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  697 ESLARFYiaELTCAVESVHKMGFIHRDIKPDNILIDRDGH-IKLTDFGLctgfrwthdskyyqsGDHprqdsmdFSNEwg 775
Cdd:cd13974    133 EALVIFY--DVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCL---------------GKH-------LVSE-- 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  776 dpsscrcGDRLKplerraarqHQRclahslvGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVGQPPFLAQTPLETQ 854
Cdd:cd13974    187 -------DDLLK---------DQR-------GSPAYISPDVLSGKPYLgKPSDMWALGVVLFTMLYGQFPFYDSIPQELF 243
                          170       180
                   ....*....|....*....|....*....
gi 1178431733  855 MKVInwQTSLHIPPQAKLSPEASDLIIKL 883
Cdd:cd13974    244 RKIK--AAEYTIPEDGRVSENTVCLIRKL 270
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
547-957 7.07e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 75.07  E-value: 7.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  547 KSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMDKsmfvkikTLGIGAFGEVCLARKVDTKALY 626
Cdd:PTZ00036    22 KGGSGKFEMNDKKLDEEERSHNNNAGEDEDEEKMIDNDINRSPNKSYKLGN-------IIGNGSFGVVYEAICIDTSEKV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  627 ATKTL------RKKDVLLRNQVAHVkaerDILAEADnewvvrLYYSFQDKDN-----LYFVMDYIPGG--DMMSLLIRMG 693
Cdd:PTZ00036    95 AIKKVlqdpqyKNRELLIMKNLNHI----NIIFLKD------YYYTECFKKNeknifLNVVMEFIPQTvhKYMKHYARNN 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  694 -IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH-IKLTDFGlctgfrwthDSKYYQSGdhprqdsmdfs 771
Cdd:PTZ00036   165 hALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFG---------SAKNLLAG----------- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  772 newgdpsscrcgdrlkplerraarqhQRCLahSLVGTPNYIAPEVLL-RTGYTQLCDWWSVGVILFEMLVGQPPFLAQ-- 848
Cdd:PTZ00036   225 --------------------------QRSV--SYICSRFYRAPELMLgATNYTTHIDLWSLGCIIAEMILGYPIFSGQss 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  849 ------------TPLETQMKVINWQ-TSLHIP---PQ--AKLSP-----EASDLIIKLCR-GPEDRLgknGADEIKAHPF 904
Cdd:PTZ00036   277 vdqlvriiqvlgTPTEDQLKEMNPNyADIKFPdvkPKdlKKVFPkgtpdDAINFISQFLKyEPLKRL---NPIEALADPF 353
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  905 F-----------KTIDFSSDL--------RQQSASYIPKIThptdTSNFDPVDPDKLWSDDNEEENVNDTLN 957
Cdd:PTZ00036   354 FddlrdpciklpKYIDKLPDLfnfcdaeiKEMSDACRRKII----PKCTYEAYKEFLMSDENDANIIADKIS 421
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
720-905 7.20e-14

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 72.64  E-value: 7.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  720 IHRDIKPDNILID-RDGHIKLTDFGLCTgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerrAARQHQ 798
Cdd:cd13983    126 IHRDLKCDNIFINgNTGEVKIGDLGLAT----------------------------------------------LLRQSF 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  799 rclAHSLVGTPNYIAPEvLLRTGYTQLCDWWSVGVILFEMLVGQPPFL-AQTPLETQMKVINwqtslHIPPQA--KL-SP 874
Cdd:cd13983    160 ---AKSVIGTPEFMAPE-MYEEHYDEKVDIYAFGMCLLEMATGEYPYSeCTNAAQIYKKVTS-----GIKPESlsKVkDP 230
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1178431733  875 EASDLIIKLCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd13983    231 ELKDFIEKCLKPPDERP---SARELLEHPFF 258
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
606-846 8.19e-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: 73.03  E-value: 8.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKK-DVLLRNQVAHvkaERDILAEADNEWVVRL-----YYSFQDKDNLYFVMDY 679
Cdd:cd14039      1 LGTGGFGNVCLYQNQETGEKIAIKSCRLElSVKNKDRWCH---EIQIMKKLNHPNVVKAcdvpeEMNFLVNDVPLLAMEY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIR----MGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI-DRDGHI--KLTDFGlctgfrwth 752
Cdd:cd14039     78 CSGGDLRKLLNKpencCGL-KESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIvhKIIDLG--------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskYYQSGDhprqdsmdfsnewgdpsscrcgdrlkplerraarqhQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd14039    148 ---YAKDLD------------------------------------QGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFG 188
                          250
                   ....*....|....
gi 1178431733  833 VILFEMLVGQPPFL 846
Cdd:cd14039    189 TMVFECIAGFRPFL 202
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
602-845 1.06e-13

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: 72.84  E-value: 1.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGI---GAFGEVCLARKVDTKALYATKTLrkkdvLLRNQVAHVK--AERDI--LAEADNEWVVRLYYSFQDKDNLY 674
Cdd:cd07846      2 KYENLGLvgeGSYGMVMKCRHKETGQIVAIKKF-----LESEDDKMVKkiAMREIkmLKQLRHENLVNLIEVFRRKKRWY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPggdmMSLLIRMGIFP----ESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFglctGFRW 750
Cdd:cd07846     77 LVFEFVD----HTVLDDLEKYPngldESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDF----GFAR 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 THDSkyyqsgdhPRQDSMDFsnewgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLR-TGYTQLCDWW 829
Cdd:cd07846    149 TLAA--------PGEVYTDY-----------------------------------VATRWYRAPELLVGdTKYGKAVDVW 185
                          250
                   ....*....|....*.
gi 1178431733  830 SVGVILFEMLVGQPPF 845
Cdd:cd07846    186 AVGCLVTEMLTGEPLF 201
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
606-890 1.25e-13

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: 72.08  E-value: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARkvdtkalyatktlrkkdvlLRNQVAHVK----------AERDI--LAEADNEWVVRLYYSFQDKDNL 673
Cdd:cd14058      1 VGRGSFGVVCKAR-------------------WRNQIVAVKiiesesekkaFEVEVrqLSRVDHPNIIKLYGACSNQKPV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDYIPGGDMMSLLIRMGIFPEslarfYIAE------LTCA--VESVHKMG---FIHRDIKPDNILIDRDGH-IKLTD 741
Cdd:cd14058     62 CLVMEYAEGGSLYNVLHGKEPKPI-----YTAAhamswaLQCAkgVAYLHSMKpkaLIHRDLKPPNLLLTNGGTvLKICD 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  742 FGLCTgfrwthdskyyqsgdhprqdsmDFSNEWGDPSscrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTG 821
Cdd:cd14058    137 FGTAC----------------------DISTHMTNNK----------------------------GSAAWMAPEVFEGSK 166
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  822 YTQLCDWWSVGVILFEMLVGQPPF-LAQTPLETQMKVINWQTSlhiPPQAKLSPEASDLIIKLC--RGPEDR 890
Cdd:cd14058    167 YSEKCDVFSWGIILWEVITRRKPFdHIGGPAFRIMWAVHNGER---PPLIKNCPKPIESLMTRCwsKDPEKR 235
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
606-904 1.30e-13

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: 71.92  E-value: 1.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQV---AHVKAERDILAEADNEW--VVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd14100      8 LGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELpngTRVPMEIVLLKKVGSGFrgVIRLLDWFERPDSFVLVLERP 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 -PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID-RDGHIKLTDFGLCTGFRWThdskYYQ 758
Cdd:cd14100     88 ePVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLKDT----VYT 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 SGDHPRQDSmdfSNEWgdpsscrcgdrlkpleRRAARQHQRCLAhslvgtpnyiapevllrtgytqlcdWWSVGVILFEM 838
Cdd:cd14100    164 DFDGTRVYS---PPEW----------------IRFHRYHGRSAA-------------------------VWSLGILLYDM 199
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  839 LVGQPPFlaqtplETQMKVINWQTSLhippQAKLSPEASDLiIKLCRG--PEDRlgkNGADEIKAHPF 904
Cdd:cd14100    200 VCGDIPF------EHDEEIIRGQVFF----RQRVSSECQHL-IKWCLAlrPSDR---PSFEDIQNHPW 253
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
592-905 2.43e-13

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: 72.77  E-value: 2.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  592 RAKMDKSM------FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvllRNQVAHVKA---ERDILAEADNEWVVR 662
Cdd:cd07877      5 RQELNKTIwevperYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRP----FQSIIHAKRtyrELRLLKHMKHENVIG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  663 LY------YSFQDKDNLYFVMdYIPGGDMMSLlIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH 736
Cdd:cd07877     81 LLdvftpaRSLEEFNDVYLVT-HLMGADLNNI-VKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  737 IKLTDFGLCtgfRWTHDSkyyQSGdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEV 816
Cdd:cd07877    159 LKILDFGLA---RHTDDE---MTG--------------------------------------------YVATRWYRAPEI 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  817 LLR-TGYTQLCDWWSVGVILFEMLVGQPPF--------------LAQTPLETQMKVI------NWQTSLHIPPQAKLS-- 873
Cdd:cd07877    189 MLNwMHYNQTVDIWSVGCIMAELLTGRTLFpgtdhidqlklilrLVGTPGAELLKKIssesarNYIQSLTQMPKMNFAnv 268
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1178431733  874 -----PEASDLIIKLCRGPEDRlgKNGADEIKAHPFF 905
Cdd:cd07877    269 figanPLAVDLLEKMLVLDSDK--RITAAQALAHAYF 303
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
594-888 3.01e-13

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: 71.23  E-value: 3.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  594 KMDKSMFVKIKTLGIGAFGEVclARKVDTKALYATKTLRKK-DVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDN 672
Cdd:cd14145      2 EIDFSELVLEEIIGIGGFGKV--YRAIWIGDEVAVKAARHDpDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFYIaELTCAVESVHKMGF---IHRDIKPDNILI-------DRDGHI-KLTD 741
Cdd:cd14145     80 LCLVMEFARGGPLNRVLSGKRIPPDILVNWAV-QIARGMNYLHCEAIvpvIHRDLKSSNILIlekvengDLSNKIlKITD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  742 FGLctgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLLRTG 821
Cdd:cd14145    159 FGL-------------------------------------------------AREWHRTTKMSAAGTYAWMAPEVIRSSM 189
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  822 YTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAklsPEASDLIIKLCRGPE 888
Cdd:cd14145    190 FSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSLPIPSTC---PEPFARLMEDCWNPD 253
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
603-886 4.01e-13

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: 71.97  E-value: 4.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKdVLLRNQVahvKAERDILA------EADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd14226     18 DSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNK-KAFLNQA---QIEVRLLElmnkhdTENKYYIVRLKRHFMFRNHLCLV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPggdmMSL--LIR----MGIFPeSLARFYIAELTCAVE--SVHKMGFIHRDIKPDNILI--DRDGHIKLTDFGlct 746
Cdd:cd14226     94 FELLS----YNLydLLRntnfRGVSL-NLTRKFAQQLCTALLflSTPELSIIHCDLKPENILLcnPKRSAIKIIDFG--- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  747 gfrwthdskyyqsgdhprqdsmdfsnewgdpSSCRCGDRLkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLC 826
Cdd:cd14226    166 -------------------------------SSCQLGQRI----------------YQYIQSRFYRSPEVLLGLPYDLAI 198
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  827 DWWSVGVILFEMLVGQPPFLAQTPLETQMKVINwqtSLHIPPQAKL--SPEASDLIIKLCRG 886
Cdd:cd14226    199 DMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE---VLGMPPVHMLdqAPKARKFFEKLPDG 257
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
600-891 4.13e-13

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: 71.24  E-value: 4.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATK--TLRK--KDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQ-DKDNLY 674
Cdd:cd14041      8 YLLLHLLGRGGFSEVYKAFDLTEQRYVAVKihQLNKnwRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDSFC 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMG--FIHRDIKPDNILIDRD---GHIKLTDFGLCTgfr 749
Cdd:cd14041     88 TVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGtacGEIKITDFGLSK--- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 wTHDSKYYQSGDHPRQDSMDFSNEWGDPSSCrcgdrlkplerraarqhqrclahSLVGT-PNYIAPEVllrtgytqlcDW 828
Cdd:cd14041    165 -IMDDDSYNSVDGMELTSQGAGTYWYLPPEC-----------------------FVVGKePPKISNKV----------DV 210
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  829 WSVGVILFEMLVGQPPFLAQTPLET--QMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRL 891
Cdd:cd14041    211 WSVGVIFYQCLYGRKPFGHNQSQQDilQENTILKATEVQFPPKPVVTPEAKAFIRRcLAYRKEDRI 276
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
603-883 5.29e-13

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


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 72.34  E-value: 5.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVD--------TKALY----ATKTlRKKDVLLRNQvahvKAER-DILAEADNewVVRLYYSFQD 669
Cdd:COG5752     37 IKPLGQGGFGRTFLAVDEDipshphcvIKQFYfpeqGPSS-FQKAVELFRQ----EAVRlDELGKHPQ--IPELLAYFEQ 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  670 KDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI-DRDGHIKLTDFGlctgf 748
Cdd:COG5752    110 DQRLYLVQEFIEGQTLAQELEKKGVFSESQIWQLLKDLLPVLQFIHSRNVIHRDIKPANIIRrRSDGKLVLIDFG----- 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerrAARQ-HQRCLAHS--LVGTPNYIAPEvLLRTGYTQL 825
Cdd:COG5752    185 --------------------------------------------VAKLlTITALLQTgtIIGTPEYMAPE-QLRGKVFPA 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  826 CDWWSVGVILFEMLVGQPPF-LAQTPLETQMkvinWQTslHIPPQAKLSPEASDLIIKL 883
Cdd:COG5752    220 SDLYSLGVTCIYLLTGVSPFdLFDVSEDRWV----WRD--FLPPGTKVSDRLGQILDKL 272
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
606-845 7.26e-13

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: 69.72  E-value: 7.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVclarkvdTKALY-----ATKTLRK-KDVLLRNQVAHvkAERDILA-EADNewVVRLYYSFQ--DKDNLYFV 676
Cdd:cd13979     11 LGSGGFGSV-------YKATYkgetvAVKIVRRrRKNRASRQSFW--AELNAARlRHEN--IVRVLAAETgtDFASLGLI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 -MDYiPGGDMMSLLIRMGIFPESLAR--FYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlCTgfrwthd 753
Cdd:cd13979     80 iMEY-CGNGTLQQLIYEGSEPLPLAHriLISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFG-CS------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 skyyqsgdhprqDSMDFSNEWGDPSScrcgdrlkplerraarqHQRclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGV 833
Cdd:cd13979    151 ------------VKLGEGNEVGTPRS-----------------HIG-------GTYTYRAPELLKGERVTPKADIYSFGI 194
                          250
                   ....*....|..
gi 1178431733  834 ILFEMLVGQPPF 845
Cdd:cd13979    195 TLWQMLTRELPY 206
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
600-844 7.82e-13

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: 70.85  E-value: 7.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKK-DVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd06649      7 FERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEiKPAIRNQIIR---ELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGIFPES-LARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyy 757
Cdd:cd06649     84 HMDGGSLDQVLKEAKRIPEEiLGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGV------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qSGDhpRQDSMdfsnewgdpsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd06649    151 -SGQ--LIDSM---------------------------------ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVE 194

                   ....*..
gi 1178431733  838 MLVGQPP 844
Cdd:cd06649    195 LAIGRYP 201
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
600-845 9.47e-13

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: 70.52  E-value: 9.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvlLRNQVAHVKAERD-ILAEADN-EWVVRLYYSF------QDKD 671
Cdd:cd07850      2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRP---FQNVTHAKRAYRElVLMKLVNhKNIIGLLNVFtpqkslEEFQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGdmMSLLIRMGIFPESLArFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwt 751
Cdd:cd07850     79 DVYLVMELMDAN--LCQVIQMDLDHERMS-YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA------ 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  752 hdskyyqsgdhpRQDSMDFsnewgdpsscrcgdRLKPlerraarqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSV 831
Cdd:cd07850    150 ------------RTAGTSF--------------MMTP----------------YVVTRYYRAPEVILGMGYKENVDIWSV 187
                          250
                   ....*....|....
gi 1178431733  832 GVILFEMLVGQPPF 845
Cdd:cd07850    188 GCIMGEMIRGTVLF 201
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
647-905 1.37e-12

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: 69.22  E-value: 1.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  647 AERDI--LAEADN-EWVVRLYYSFQDKDNLYFVM--------DYIPGGDMMSLLIRMGIFPESLARfyiaELTCAVESVH 715
Cdd:cd13982     41 ADREVqlLRESDEhPNVIRYFCTEKDRQFLYIALelcaaslqDLVESPRESKLFLRPGLEPVRLLR----QIASGLAHLH 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  716 KMGFIHRDIKPDNILIDRD---GHIK--LTDFGLCtgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlKPLE 790
Cdd:cd13982    117 SLNIVHRDLKPQNILISTPnahGNVRamISDFGLC-----------------------------------------KKLD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  791 RraARQHQRCLAHSlVGTPNYIAPEVL---LRTGYTQLCDWWSVGVILFEMLV-GQPPFlaQTPLETQMKVINWQTSL-H 865
Cdd:cd13982    156 V--GRSSFSRRSGV-AGTSGWIAPEMLsgsTKRRQTRAVDIFSLGCVFYYVLSgGSHPF--GDKLEREANILKGKYSLdK 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1178431733  866 IPPQAKLSPEASDLIIKLCR-GPEDRlgkNGADEIKAHPFF 905
Cdd:cd13982    231 LLSLGEHGPEAQDLIERMIDfDPEKR---PSAEEVLNHPFF 268
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
603-845 1.39e-12

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: 69.88  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEV--CLARKvdTKALYATKTLRKKDVLLRnqvaHVKAERDILA------EADNEWVVRLYYSFQDKDNLY 674
Cdd:cd14210     18 LSVLGKGSFGQVvkCLDHK--TGQLVAIKIIRNKKRFHQ----QALVEVKILKhlndndPDDKHNIVRYKDSFIFRGHLC 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDyipggdMMSL----LIRM----GiFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGhIKLTDFG 743
Cdd:cd14210     92 IVFE------LLSInlyeLLKSnnfqG-LSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLkqpSKSS-IKVIDFG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 lctgfrwthdskyyqsgdhprqdsmdfsnewgdpSScrcgdrlkplerraarqhqrCLAHSLVGTpnYI------APEVL 817
Cdd:cd14210    164 ----------------------------------SS--------------------CFEGEKVYT--YIqsrfyrAPEVI 187
                          250       260
                   ....*....|....*....|....*...
gi 1178431733  818 LRTGYTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd14210    188 LGLPYDTAIDMWSLGCILAELYTGYPLF 215
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
660-905 1.46e-12

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: 69.22  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  660 VVRLYYSFQDKDNLYFVMDYIPGgDMMSLLIRM--GIFPESLaRFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHI 737
Cdd:cd07870     60 IVLLHDIIHTKETLTFVFEYMHT-DLAQYMIQHpgGLHPYNV-RLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGEL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  738 KLTDFGLCtgfrwthdskyyQSGDHPRQdsmDFSNEwgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVL 817
Cdd:cd07870    138 KLADFGLA------------RAKSIPSQ---TYSSE--------------------------------VVTLWYRPPDVL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  818 L-RTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVI-------------------NWQTSLHIPPQAKL----- 872
Cdd:cd07870    171 LgATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEKIwtvlgvptedtwpgvsklpNYKPEWFLPCKPQQlrvvw 250
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1178431733  873 -----SPEASDLIIKLCRG-PEDRLgknGADEIKAHPFF 905
Cdd:cd07870    251 krlsrPPKAEDLASQMLMMfPKDRI---SAQDALLHPYF 286
UBA_LATS1 cd14397
UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large ...
11-38 1.50e-12

UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large tumor suppressor homolog 1 or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. It plays a crucial role in the prevention of tumor formation by controlling mitosis progression. Human LATS1 is the mammalian homologs of Drosophila lats/warts gene that could suppress tumor growth and rescue all developmental defects in flies, including embryonic lethality. It forms a regulatory complex with zyxin, a regulator of actin filament assembly. The LATS1/zyxin complex plays a role in controlling mitosis progression on mitotic apparatus. LATS1 is phosphorylated in a cell-cycle-dependent manner and complexes with CDC2 in early mitosis. It can negatively modulates tumor cell growth by inducing G(2)/M cell cycle transition or apoptosis. It also functions as a mitotic exit network kinase interacting with MOB1A, a protein whose homolog in budding yeast associates with kinases involved in mitotic exit. Moreover, LATS1 acts as a novel cytoskeleton regulator that affects cytokinesis by regulating actin polymerization through inhibiting LIMK1. LATS1 can also inhibit transcription regulation and transformation functions of oncogene YAP by inhibiting its nuclear translocation through phosphorylation. In addition, LATS1 can regulate the transcriptional activity of forkhead L2 (FOXL2) via phosphorylation. It also acts as an acting-binding protein that can negatively regulate the actin polymerization. LATS1 contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


Pssm-ID: 270580  Cd Length: 41  Bit Score: 62.74  E-value: 1.50e-12
                           10        20
                   ....*....|....*....|....*...
gi 1178431733   11 QDMVIQALQKTNNRSIEAAIEFISKMSY 38
Cdd:cd14397     14 EDMVIQALQQTNNRSIEAAIEFISKMSY 41
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
603-845 1.65e-12

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: 69.97  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRN---QVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDy 679
Cdd:cd14212      4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQamlEIAILTLLNTKYDPEDKHHIVRLLDHFMHHGHLCIVFE- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 ipggdMMSL----LIRMGIF---PESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD--GHIKLTDFGlctgfrw 750
Cdd:cd14212     83 -----LLGVnlyeLLKQNQFrglSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFG------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpSSCrcgdrlkplerraarqHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd14212    151 ---------------------------SAC----------------FENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWS 187
                          250
                   ....*....|....*
gi 1178431733  831 VGVILFEMLVGQPPF 845
Cdd:cd14212    188 LGCIAAELFLGLPLF 202
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
606-842 1.65e-12

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 68.82  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGE-VCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDIlaeaDNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14222      1 LGKGFFGQaIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSL----DHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYQSGDHPr 764
Cdd:cd14222     77 LKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLS---RLIVEEKKKPPPDKP- 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  765 qdsmdfsnewgdpsscrcgdrlkPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEmLVGQ 842
Cdd:cd14222    153 -----------------------TTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCE-IIGQ 206
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
606-867 1.77e-12

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: 68.57  E-value: 1.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLAR-KVDTKALYATKTLRKKDVLLrnQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14061      2 IGVGGFGKVYRGIwRGEEVAVKAARQDPDEDISV--TLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGIFPESLARF--YIAELTCAVESVHKMGFIHRDIKPDNILIDR--------DGHIKLTDFGLctgfrwthds 754
Cdd:cd14061     80 LNRVLAGRKIPPHVLVDWaiQIARGMNYLHNEAPVPIIHRDLKSSNILILEaienedleNKTLKITDFGL---------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 834
Cdd:cd14061    150 ---------------------------------------AREWHKTTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVL 190
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1178431733  835 LFEMLVGQPPFLAQTPLETQMKVINWQTSLHIP 867
Cdd:cd14061    191 LWELLTGEVPYKGIDGLAVAYGVAVNKLTLPIP 223
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
602-843 1.91e-12

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: 68.94  E-value: 1.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLARKVDTKALYATK--TLRKKDVLLRNqvahvKAERDI--LAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd07847      5 KLSKIGEGSYGVVFKCRNRETGQIVAIKkfVESEDDPVIKK-----IALREIrmLKQLKHPNLVNLIEVFRRKRKLHLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG---LCTGfrwthds 754
Cdd:cd07847     80 EYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGfarILTG------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 kyyqsgdhPRQDSMDFsnewgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLL-RTGYTQLCDWWSVGV 833
Cdd:cd07847    153 --------PGDDYTDY-----------------------------------VATRWYRAPELLVgDTQYGPPVDVWAIGC 189
                          250
                   ....*....|
gi 1178431733  834 ILFEMLVGQP 843
Cdd:cd07847    190 VFAELLTGQP 199
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
584-858 1.95e-12

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 70.06  E-value: 1.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  584 ESNYIRLKRakmdksmFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvlLRNQVAHVKAERDI--LAEADNEWVV 661
Cdd:cd07876     14 DSTFTVLKR-------YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRP---FQNQTHAKRAYRELvlLKCVNHKNII 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  662 RLYYSF------QDKDNLYFVMDYIPGGdmMSLLIRMGIFPESLArFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG 735
Cdd:cd07876     84 SLLNVFtpqkslEEFQDVYLVMELMDAN--LCQVIHMELDHERMS-YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  736 HIKLTDFGL----CTGFRWThdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNY 811
Cdd:cd07876    161 TLKILDFGLartaCTNFMMT----------------------------------------------------PYVVTRYY 188
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1178431733  812 IAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVI 858
Cdd:cd07876    189 RAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVI 235
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
606-845 2.41e-12

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: 69.06  E-value: 2.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKT------LRKKDVLLRnqvahvkaERDILAEADNEWVVRLYYSFQDKD--NLYFVM 677
Cdd:cd13988      1 LGQGATANVFRGRHKKTGDLYAVKVfnnlsfMRPLDVQMR--------EFEVLKKLNHKNIVKLFAIEEELTtrHKVLVM 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLIR----MGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNIL--IDRDGH--IKLTDFGLCtgfR 749
Cdd:cd13988     73 ELCPCGSLYTVLEEpsnaYGL-PESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAA---R 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 WTHDSKYYQsgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEV----LLRTG---- 821
Cdd:cd13988    149 ELEDDEQFV---------------------------------------------SLYGTEEYLHPDMyeraVLRKDhqkk 183
                          250       260
                   ....*....|....*....|....
gi 1178431733  822 YTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd13988    184 YGATVDLWSIGVTFYHAATGSLPF 207
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
604-891 2.72e-12

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 68.21  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVC--LARKVDTKALY----ATKTLRKKdvllrnqvAHVKAERDILAEA------DNEWVVRLYYSFQDKD 671
Cdd:cd05044      1 KFLGSGAFGEVFegTAKDILGDGSGetkvAVKTLRKG--------ATDQEKAEFLKEAhlmsnfKHPNILKLLGVCLDND 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGDMMSLL--IRMGIFPESLARFY--------IAELTCAVESVHkmgFIHRDIKPDNILI-DRDGH---I 737
Cdd:cd05044     73 PQYIILELMEGGDLLSYLraARPTAFTPPLLTLKdllsicvdVAKGCVYLEDMH---FVHRDLAARNCLVsSKDYRervV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  738 KLTDFGLCtgfRWTHDSKYYQsgdhprqdsmdfsnewgdpsscRCGDRLKPLErraarqhqrclahslvgtpnYIAPEVL 817
Cdd:cd05044    150 KIGDFGLA---RDIYKNDYYR----------------------KEGEGLLPVR--------------------WMAPESL 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  818 LRTGYTQLCDWWSVGVILFEML-VGQPPFLAQTPLEtqmkVINWQTS---LHIPPQAklsPEASDLIIKLC--RGPEDRL 891
Cdd:cd05044    185 VDGVFTTQSDVWAFGVLMWEILtLGQQPYPARNNLE----VLHFVRAggrLDQPDNC---PDDLYELMLRCwsTDPEERP 257
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
603-880 2.74e-12

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 68.48  E-value: 2.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTlrkkdVLLRNQVAHVKAERdilaEADN------EWVVRLY-YSF----QDKD 671
Cdd:cd13986      5 QRLLGEGGFSFVYLVEDLSTGRLYALKK-----ILCHSKEDVKEAMR----EIENyrlfnhPNILRLLdSQIvkeaGGKK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGDMMSLLIRMGI----FPESLARFYIAELTCAVESVHKM---GFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd13986     76 EVYLLLPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  745 CTGFRWTHDSkyyqsgdhpRQDSMdfsnEWGDPSSCRCgdrlkplerraarqhqrclahslvgTPNYIAPEVL-LRTGYT 823
Cdd:cd13986    156 MNPARIEIEG---------RREAL----ALQDWAAEHC-------------------------TMPYRAPELFdVKSHCT 197
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  824 --QLCDWWSVGVILFEMLVGQPPFLA--QTPLETQMKVINWQTSlhIPPQAKLSPEASDLI 880
Cdd:cd13986    198 idEKTDIWSLGCTLYALMYGESPFERifQKGDSLALAVLSGNYS--FPDNSRYSEELHQLV 256
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
715-905 2.98e-12

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: 68.56  E-value: 2.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  715 HKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdhpRQDSM---DFSNEwgdpsscrcgdrlkpler 791
Cdd:cd07844    115 HQRRVLHRDLKPQNLLISERGELKLADFGLA------------------RAKSVpskTYSNE------------------ 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  792 raarqhqrclahslVGTPNYIAPEVLL-RTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVI----------NW 860
Cdd:cd07844    159 --------------VVTLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVEDQLHKIfrvlgtpteeTW 224
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  861 QTSLHIP-------------------PQAKLSPEASDLIIKLCRG-PEDRLgknGADEIKAHPFF 905
Cdd:cd07844    225 PGVSSNPefkpysfpfypprplinhaPRLDRIPHGEELALKFLQYePKKRI---SAAEAMKHPYF 286
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
600-852 3.98e-12

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: 68.11  E-value: 3.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvLLRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd07871      7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIR----LEHEEGAPCTAIREVslLKNLKHANIVTLHDIIHTERCLTLVF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGgDMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsky 756
Cdd:cd07871     83 EYLDS-DLKQYLDNCGnLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLA----------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yQSGDHPRQdsmDFSNEwgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLL-RTGYTQLCDWWSVGVIL 835
Cdd:cd07871    151 -RAKSVPTK---TYSNE--------------------------------VVTLWYRPPDVLLgSTEYSTPIDMWGVGCIL 194
                          250
                   ....*....|....*..
gi 1178431733  836 FEMLVGQPPFLAQTPLE 852
Cdd:cd07871    195 YEMATGRPMFPGSTVKE 211
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
606-845 4.84e-12

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 67.91  E-value: 4.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDT----KALYATKTLRKKDvlLRNQVahvKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd14158     23 LGEGGFGVVFKGYINDKnvavKKLAAMVDISTED--LTKQF---EQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMP 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGdmmSLLIRMGIFPESLA-----RFYIAELTC-AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsk 755
Cdd:cd14158     98 NG---SLLDRLACLNDTPPlswhmRCKIAQGTAnGINYLHENNHIHRDIKSANILLDETFVPKISDFGLA---------- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyqsgdhprqdsmdfsnewgdpsscrcgdrlkpleRRAARQHQRCLAHSLVGTPNYIAPEVlLRTGYTQLCDWWSVGVIL 835
Cdd:cd14158    165 -----------------------------------RASEKFSQTIMTERIVGTTAYMAPEA-LRGEITPKSDIFSFGVVL 208
                          250
                   ....*....|
gi 1178431733  836 FEMLVGQPPF 845
Cdd:cd14158    209 LEIITGLPPV 218
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
605-904 6.13e-12

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: 67.21  E-value: 6.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  605 TLGIGAFGEVCLARKVDTKALYATKTLrKKDVLLRNQvAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGd 684
Cdd:cd06619      8 ILGHGNGGTVYKAYHLLTRRILAVKVI-PLDITVELQ-KQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGG- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 mmSLLIRMGIFPESLARFYIAELTcAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgdhpr 764
Cdd:cd06619     85 --SLDVYRKIPEHVLGRIAVAVVK-GLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGV-------------------- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  765 qdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPP 844
Cdd:cd06619    142 -----------------------------STQLVNSIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFP 192
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  845 FL-------AQTPLETQMKVINWQTSlhIPPQAKLSPEASDLIIKLCR-GPEDRLGKNgadEIKAHPF 904
Cdd:cd06619    193 YPqiqknqgSLMPLQLLQCIVDEDPP--VLPVGQFSEKFVHFITQCMRkQPKERPAPE---NLMDHPF 255
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
606-861 6.19e-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: 67.68  E-value: 6.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKK-----------DVLLRNQVAH--VKAERDILAEADNewvvrlyysFQDKDN 672
Cdd:cd14038      2 LGTGGFGNVLRWINQETGEQVAIKQCRQElspknrerwclEIQIMKRLNHpnVVAARDVPEGLQK---------LAPNDL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRM----GIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID----RDGHiKLTDFGl 744
Cdd:cd14038     73 PLLAMEYCQGGDLRKYLNQFenccGL-REGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQqgeqRLIH-KIIDLG- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  745 ctgfrwthdskYYQSGDhprqdsmdfsnewgdpsscrcgdrlkplerraarqhQRCLAHSLVGTPNYIAPEVLLRTGYTQ 824
Cdd:cd14038    150 -----------YAKELD------------------------------------QGSLCTSFVGTLQYLAPELLEQQKYTV 182
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1178431733  825 LCDWWSVGVILFEMLVGQPPFLAqtpletqmkviNWQ 861
Cdd:cd14038    183 TVDYWSFGTLAFECITGFRPFLP-----------NWQ 208
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
600-905 6.19e-12

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: 68.17  E-value: 6.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATK--------------TLRKKDVLLRNQVAHVKAERDILAEADNEwvvrlyy 665
Cdd:cd07858      7 YVPIKPIGRGAYGIVCSAKNSETNEKVAIKkianafdnridakrTLREIKLLRHLDHENVIAIKDIMPPPHRE------- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  666 SFQDKDNLYFVMDyipgGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC 745
Cdd:cd07858     80 AFNDVYIVYELMD----TDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  746 tgfrwthdskyyqsgdHPRQDSMDFSNEWgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLR-TGYTQ 824
Cdd:cd07858    156 ----------------RTTSEKGDFMTEY-------------------------------VVTRWYRAPELLLNcSEYTT 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  825 LCDWWSVGVILFEMLVGQPPF--------------LAQTPLETQMKVINWQTSL----HIPPQAKLS---------PEAS 877
Cdd:cd07858    189 AIDVWSVGCIFAELLGRKPLFpgkdyvhqlkliteLLGSPSEEDLGFIRNEKARryirSLPYTPRQSfarlfphanPLAI 268
                          330       340
                   ....*....|....*....|....*....
gi 1178431733  878 DLIIK-LCRGPEDRLgknGADEIKAHPFF 905
Cdd:cd07858    269 DLLEKmLVFDPSKRI---TVEEALAHPYL 294
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
667-949 6.26e-12

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 67.75  E-value: 6.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  667 FQDKDNLYFVMDYIPGGDMMSLLIRMG--IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR---DGHIKLTD 741
Cdd:cd14170     68 YAGRKCLLIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTD 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  742 FGLCTGFRwTHDSKyyqsgdhprqdsmdfsnewgdPSSCRcgdrlkplerraarqhqrclahslvgTPNYIAPEVLLRTG 821
Cdd:cd14170    148 FGFAKETT-SHNSL---------------------TTPCY--------------------------TPYYVAPEVLGPEK 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  822 YTQLCDWWSVGVILFEMLVGQPPF-----LAQTPlETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLgknG 895
Cdd:cd14170    180 YDKSCDMWSLGVIMYILLCGYPPFysnhgLAISP-GMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKtEPTQRM---T 255
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  896 ADEIKAHPFFktidfssdlrQQSASyIPKIthPTDTSNFDPVDPDkLWSDDNEE 949
Cdd:cd14170    256 ITEFMNHPWI----------MQSTK-VPQT--PLHTSRVLKEDKE-RWEDVKEE 295
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
609-744 7.62e-12

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 67.25  E-value: 7.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  609 GAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSL 688
Cdd:cd14026      8 GAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSLNEL 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  689 LIRMGIFPESL--ARFYIA-ELTCAVESVHKMG--FIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd14026     88 LHEKDIYPDVAwpLRLRILyEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGL 148
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
614-913 9.03e-12

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: 67.32  E-value: 9.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  614 VCLARKVDTKALYATK--TLRKKD----VLLRNQVAHVKaerdilaEADNEWVVRLYYSFQDKDNLYFV---MDYIPGGD 684
Cdd:cd08216     16 VHLAKHKPTNTLVAVKkiNLESDSkedlKFLQQEILTSR-------QLQHPNILPYVTSFVVDNDLYVVtplMAYGSCRD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGiFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrWTHDSKYYQSGDHPR 764
Cdd:cd08216     89 LLKTHFPEG-LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSM-VKHGKRQRVVHDFPK 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  765 QDSMDFsnewgdpsscrcgdrlkplerraarqhqrclahslvgtpNYIAPEVL---LRtGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd08216    167 SSEKNL---------------------------------------PWLSPEVLqqnLL-GYNEKSDIYSVGITACELANG 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  842 QPPFlAQTPLeTQM---KV------------------------------INWQTSLHIPPQAKLSPEASDLiIKLC--RG 886
Cdd:cd08216    207 VVPF-SDMPA-TQMlleKVrgttpqlldcstypleedsmsqsedsstehPNNRDTRDIPYQRTFSEAFHQF-VELClqRD 283
                          330       340
                   ....*....|....*....|....*..
gi 1178431733  887 PEDRlgkNGADEIKAHPFFKTIDFSSD 913
Cdd:cd08216    284 PELR---PSASQLLAHSFFKQCRRSNT 307
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
648-858 9.73e-12

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 66.38  E-value: 9.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  648 ERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPD 727
Cdd:cd14111     49 EYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPD 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  728 NILIDRDGHIKLTDFGLCTGFrwthdskyyqsgdhprqdsmdfsnewgDPSScrcgdrLKPLERRaarqhqrclahslVG 807
Cdd:cd14111    129 NIMVTNLNAIKIVDFGSAQSF---------------------------NPLS------LRQLGRR-------------TG 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  808 TPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVI 858
Cdd:cd14111    163 TLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKIL 213
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
597-763 1.28e-11

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 66.46  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLAR----KVDTKALYATKTLrKKDVLLRNQVAHvKAERDILAEADNEWVVRLY--YSFQDK 670
Cdd:cd05080      3 KRYLKKIRDLGEGHFGKVSLYCydptNDGTGEMVAVKAL-KADCGPQHRSGW-KQEIDILKTLYHENIVKYKgcCSEQGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DNLYFVMDYIPGGDMMSLLIRMGIfpeSLARFYI-AELTC-AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGF 748
Cdd:cd05080     81 KSLQLIMEYVPLGSLRDYLPKHSI---GLAQLLLfAQQICeGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAV 157
                          170
                   ....*....|....*...
gi 1178431733  749 RWTHDskYY---QSGDHP 763
Cdd:cd05080    158 PEGHE--YYrvrEDGDSP 173
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
606-890 1.33e-11

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: 66.16  E-value: 1.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVclarkvdTKALYatktlRKKDVLLRnqVAHVKAERDILAEADN-EWVVRLYYSFQDKD------------N 672
Cdd:cd14148      2 IGVGGFGKV-------YKGLW-----RGEEVAVK--AARQDPDEDIAVTAENvRQEARLFWMLQHPNiialrgvclnppH 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFYIaELTCAVESVHKMGF---IHRDIKPDNILI----DRDG----HIKLTD 741
Cdd:cd14148     68 LCLVMEYARGGALNRALAGKKVPPHVLVNWAV-QIARGMNYLHNEAIvpiIHRDLKSSNILIlepiENDDlsgkTLKITD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  742 FGLctgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLLRTG 821
Cdd:cd14148    147 FGL-------------------------------------------------AREWHKTTKMSAAGTYAWMAPEVIRLSL 177
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  822 YTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAklsPEASDLIIKLCRGPEDR 890
Cdd:cd14148    178 FSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTC---PEPFARLLEECWDPDPH 243
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
598-904 1.49e-11

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: 66.83  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRK---KDVLLRnqvaHVKAERDILAEADNEWVVRLYYSF-QDKDNL 673
Cdd:cd07856     10 TRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKpfsTPVLAK----RTYRELKLLKHLRHENIISLSDIFiSPLEDI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDYIpGGDMMSLLIRMGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthd 753
Cdd:cd07856     86 YFVTELL-GTDLHRLLTSRPL-EKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGL--------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 skyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQhQRCLAHSLVGTPNYIAPEVLLR-TGYTQLCDWWSVG 832
Cdd:cd07856    155 ----------------------------------------ARI-QDPQMTGYVSTRYYRAPEIMLTwQKYDVEVDIWSAG 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  833 VILFEMLVGQPPF--------------LAQTPLETQMKVINWQTSLH----IPPQAKL---------SPEASDLIIK-LC 884
Cdd:cd07856    194 CIFAEMLEGKPLFpgkdhvnqfsiiteLLGTPPDDVINTICSENTLRfvqsLPKRERVpfsekfknaDPDAIDLLEKmLV 273
                          330       340
                   ....*....|....*....|
gi 1178431733  885 RGPEDRLgknGADEIKAHPF 904
Cdd:cd07856    274 FDPKKRI---SAAEALAHPY 290
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
600-906 1.57e-11

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: 66.29  E-value: 1.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLR-------KKDVLLrnqvahvkaERDI-LAEADNEWVVRLYYS-FQDK 670
Cdd:cd06617      3 LEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRatvnsqeQKRLLM---------DLDIsMRSVDCPYTVTFYGAlFREG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DnlyfvmdyipggdmmsLLIRMGIFPESLARFY--------------IAELTC----AVESVH-KMGFIHRDIKPDNILI 731
Cdd:cd06617     74 D----------------VWICMEVMDTSLDKFYkkvydkgltipediLGKIAVsivkALEYLHsKLSVIHRDVKPSNVLI 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  732 DRDGHIKLTDFGLctgfrwthdskyyqSGDhpRQDSMDFSNEWGdpssCrcgdrlKPlerraarqhqrclahslvgtpnY 811
Cdd:cd06617    138 NRNGQVKLCDFGI--------------SGY--LVDSVAKTIDAG----C------KP----------------------Y 169
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  812 IAPE----VLLRTGYTQLCDWWSVGVILFEMLVGQPPFLA-QTPLEtQMKVINWQTSLHIpPQAKLSPEASDLIIKLCRg 886
Cdd:cd06617    170 MAPErinpELNQKGYDVKSDVWSLGITMIELATGRFPYDSwKTPFQ-QLKQVVEEPSPQL-PAEKFSPEFQDFVNKCLK- 246
                          330       340
                   ....*....|....*....|
gi 1178431733  887 pEDRLGKNGADEIKAHPFFK 906
Cdd:cd06617    247 -KNYKERPNYPELLQHPFFE 265
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
603-845 1.61e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 68.61  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQvAHVKAERDILAEADNEWVVRLYYSFQDKDN--LYFVMDYI 680
Cdd:PTZ00266    18 IKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREK-SQLVIEVNVMRELKHKNIVRYIDRFLNKANqkLYILMEFC 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIR----MGIFPESLARFYIAELTCAVESVHKMG-------FIHRDIKPDNILidrdghikltdfgLCTGFR 749
Cdd:PTZ00266    97 DAGDLSRNIQKcykmFGKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIF-------------LSTGIR 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 wthdskyyqsgdHPRQDSMDFSNEWGDPSScRCGDRlkPLERRAARQhqrCLAHSLVGTPNYIAPEVLLR--TGYTQLCD 827
Cdd:PTZ00266   164 ------------HIGKITAQANNLNGRPIA-KIGDF--GLSKNIGIE---SMAHSCVGTPYYWSPELLLHetKSYDDKSD 225
                          250
                   ....*....|....*...
gi 1178431733  828 WWSVGVILFEMLVGQPPF 845
Cdd:PTZ00266   226 MWALGCIIYELCSGKTPF 243
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
600-858 1.72e-11

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: 66.18  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvLLRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd07873      4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIR----LEHEEGAPCTAIREVslLKDLKHANIVTLHDIIHTEKSLTLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIpGGDMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsky 756
Cdd:cd07873     80 EYL-DKDLKQYLDDCGnSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA----------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhpRQDSM---DFSNEwgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLL-RTGYTQLCDWWSVG 832
Cdd:cd07873    148 -------RAKSIptkTYSNE--------------------------------VVTLWYRPPDILLgSTDYSTQIDMWGVG 188
                          250       260
                   ....*....|....*....|....*.
gi 1178431733  833 VILFEMLVGQPPFLAQTpLETQMKVI 858
Cdd:cd07873    189 CIFYEMSTGRPLFPGST-VEEQLHFI 213
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
599-851 1.82e-11

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: 66.28  E-value: 1.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvLLRNQVAHVKAERDILAEADNEWVVRLYY-SFQDK------D 671
Cdd:cd06637      7 IFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKKYSHHRNIATYYgAFIKKnppgmdD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGDMMSLL--IRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfr 749
Cdd:cd06637     83 QLWLVMEFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSA--- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 wthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkPLERRAARQhqrclaHSLVGTPNYIAPEVLL-----RTGYTQ 824
Cdd:cd06637    160 --------------------------------------QLDRTVGRR------NTFIGTPYWMAPEVIAcdenpDATYDF 195
                          250       260
                   ....*....|....*....|....*..
gi 1178431733  825 LCDWWSVGVILFEMLVGQPPFLAQTPL 851
Cdd:cd06637    196 KSDLWSLGITAIEMAEGAPPLCDMHPM 222
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
720-909 1.86e-11

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: 66.23  E-value: 1.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  720 IHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdskyyqsgdhprQDSMDFSNEWGdpssCRcgdrlkPlerraarqhqr 799
Cdd:cd06616    132 IHRDVKPSNILLDRNGNIKLCDFGISGQL----------------VDSIAKTRDAG----CR------P----------- 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  800 clahslvgtpnYIAPEVLL----RTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQM-KVINWQtslhiPPQAKLSP 874
Cdd:cd06616    175 -----------YMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLtQVVKGD-----PPILSNSE 238
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1178431733  875 EAS---DLI--IKLCRgPEDRLGKNGADEIKAHPFFKTID 909
Cdd:cd06616    239 EREfspSFVnfVNLCL-IKDESKRPKYKELLKHPFIKMYE 277
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
667-849 3.76e-11

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 64.84  E-value: 3.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  667 FQDKdNLYFVMDYIPGGDMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC 745
Cdd:cd14154     60 YKDK-KLNLITEYIPGGTLKDVLKDMArPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLA 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  746 tgfrwthdskyyQSGDHPRQDSmdfsnewgdpsscrcGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQL 825
Cdd:cd14154    139 ------------RLIVEERLPS---------------GNMSPSETLRHLKSPDRKKRYTVVGNPYWMAPEMLNGRSYDEK 191
                          170       180
                   ....*....|....*....|....*...
gi 1178431733  826 CDWWSVGVILFEmLVGQ----PPFLAQT 849
Cdd:cd14154    192 VDIFSFGIVLCE-IIGRveadPDYLPRT 218
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
606-904 4.01e-11

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: 64.59  E-value: 4.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDIL----AEADNEWVVRLYYSFQDKDNLYFVMDYI- 680
Cdd:cd14102      8 LGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVllkkVGSGFRGVIKLLDWYERPDGFLIVMERPe 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILID-RDGHIKLTDFGLCTGFRwthDSKYyqs 759
Cdd:cd14102     88 PVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLK---DTVY--- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsMDFSnewgdpsscrcgdrlkplerraarqhqrclahslvGTPNYIAPE-VLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd14102    162 --------TDFD-----------------------------------GTRVYSPPEwIRYHRYHGRSATVWSLGVLLYDM 198
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  839 LVGQPPFlaqtplETQMKVInwQTSLHIppQAKLSPEASDLiIKLCRG--PEDRlgkNGADEIKAHPF 904
Cdd:cd14102    199 VCGDIPF------EQDEEIL--RGRLYF--RRRVSPECQQL-IKWCLSlrPSDR---PTLEQIFDHPW 252
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
595-910 4.43e-11

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 64.84  E-value: 4.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  595 MDKsmFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDN 672
Cdd:PLN00009     1 MDQ--YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQ---EDEGVPSTAIREIslLKEMQHGNIVRLQDVVHSEKR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPggdmMSLLIRMGIFPE-----SLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH-IKLTDFGLCT 746
Cdd:PLN00009    76 LYLVFEYLD----LDLKKHMDSSPDfaknpRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLAR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  747 GFrwthdskyyqsgdhprqdsmdfsnewGDPSscrcgdrlkplerraarqhqRCLAHSLVgTPNYIAPEVLLRT-GYTQL 825
Cdd:PLN00009   152 AF--------------------------GIPV--------------------RTFTHEVV-TLWYRAPEILLGSrHYSTP 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 CDWWSVGVILFEMLVGQPPFLAQTPLETQMKVIN---------WQ--TSL--------HIPPQ------AKLSPEASDLI 880
Cdd:PLN00009   185 VDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRilgtpneetWPgvTSLpdyksafpKWPPKdlatvvPTLEPAGVDLL 264
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1178431733  881 IK-LCRGPEDRLGKNGADEikaHPFFKTIDF 910
Cdd:PLN00009   265 SKmLRLDPSKRITARAALE---HEYFKDLGD 292
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
706-885 4.70e-11

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: 64.84  E-value: 4.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  706 ELTCAVESVHKMGFIHRDIKPDNILID-RDGHIKLTDFGLCtgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrCGD 784
Cdd:cd14049    128 QLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLA------------------------------------CPD 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  785 RLKPLERRAARQHQRCLAH-SLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVgqppflaqtPLETQMKVINWQTS 863
Cdd:cd14049    172 ILQDGNDSTTMSRLNGLTHtSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---------PFGTEMERAEVLTQ 242
                          170       180
                   ....*....|....*....|....*.
gi 1178431733  864 L---HIPPQ-AKLSPEASDLIIKLCR 885
Cdd:cd14049    243 LrngQIPKSlCKRWPVQAKYIKLLTS 268
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
606-839 4.92e-11

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: 64.05  E-value: 4.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDvllrNQVAHVKaERDILAEADNEWVVRlYYSFQDKDN-LYFVMDYIPGGD 684
Cdd:cd14065      1 LGKGFFGEVYKVTHRETGKVMVMKELKRFD----EQRSFLK-EVKLMRRLSHPNILR-FIGVCVKDNkLNFITEYVNGGT 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMgifPESLARFYIAELTCAVES----VHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCTgfrwthdskyy 757
Cdd:cd14065     75 LEELLKSM---DEQLPWSQRVSLAKDIASgmayLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAR----------- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDHPRQDsmdfsnewgdpsscrcGDRLKPLerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd14065    141 EMPDEKTKK----------------PDRKKRL--------------TVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCE 190

                   ..
gi 1178431733  838 ML 839
Cdd:cd14065    191 II 192
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
676-884 6.50e-11

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: 63.67  E-value: 6.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdsk 755
Cdd:cd14059     59 LMEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSK--------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyqsgdhprqdsmdfsnEWGDPSScrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd14059    130 -----------------ELSEKST----------------------KMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVL 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  836 FEMLVGQPPFlaqtpLETQMKVINW---QTSLHIP-PQAklSPEASDLIIKLC 884
Cdd:cd14059    171 WELLTGEIPY-----KDVDSSAIIWgvgSNSLQLPvPST--CPDGFKLLMKQC 216
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
584-858 6.96e-11

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: 65.07  E-value: 6.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  584 ESNYIRLKRakmdksmFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvlLRNQVAHVKAERDI--LAEADNEWVV 661
Cdd:cd07875     17 DSTFTVLKR-------YQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRP---FQNQTHAKRAYRELvlMKCVNHKNII 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  662 RLY------YSFQDKDNLYFVMDYIPGGdmMSLLIRMGIFPESLArFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG 735
Cdd:cd07875     87 GLLnvftpqKSLEEFQDVYIVMELMDAN--LCQVIQMELDHERMS-YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  736 HIKLTDFGLCtgfrwthdskyyqsgdhpRQDSMDFsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPE 815
Cdd:cd07875    164 TLKILDFGLA------------------RTAGTSF------------------------------MMTPYVVTRYYRAPE 195
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1178431733  816 VLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVI 858
Cdd:cd07875    196 VILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVI 238
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
606-744 7.00e-11

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: 64.07  E-value: 7.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRkkdvllrnqVAHVKAER-DILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd13991     14 IGRGSFGEVHRMEDKQTGFQCAVKKVR---------LEVFRAEElMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGS 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  685 MMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG-HIKLTDFGL 744
Cdd:cd13991     85 LGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGH 145
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
602-858 9.48e-11

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: 63.94  E-value: 9.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  602 KIKTLGIGAFGEVCLAR----KVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRLYY--SFQDKDNLYF 675
Cdd:cd05038      8 FIKQLGEGHFGSVELCRydplGDNTGEQVAVKSLQPSGE--EQHMSDFKREIEILRTLDHEYIVKYKGvcESPGRRSLRL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLL---------IRMGIFPESLARfyiaeltcAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT 746
Cdd:cd05038     86 IMEYLPSGSLRDYLqrhrdqidlKRLLLFASQICK--------GMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  747 GFrwTHDSKYYQSGDhPRqdsmDFSNEWgdpsscrcgdrlkplerraarqhqrclahslvgtpnYiAPEVLLRTGYTQLC 826
Cdd:cd05038    158 VL--PEDKEYYYVKE-PG----ESPIFW------------------------------------Y-APECLRESRFSSAS 193
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1178431733  827 DWWSVGVILFEMLVGQPPFlaQTPLETQMKVI 858
Cdd:cd05038    194 DVWSFGVTLYELFTYGDPS--QSPPALFLRMI 223
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
596-890 1.17e-10

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: 63.79  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  596 DKSMFVKIKTLGIGAFGEVCLAR----KVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRlYYSF--QD 669
Cdd:cd05079      2 EKRFLKRIRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLKPESG--GNHIADLKKEIEILRNLYHENIVK-YKGIctED 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  670 KDN-LYFVMDYIPGGDMMSLLIR--MGIFPESLARfYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT 746
Cdd:cd05079     79 GGNgIKLIMEFLPSGSLKEYLPRnkNKINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  747 GFRwtHDSKYYQSGDhprqdsmdfsnewgdpsscrcgDRLKPLerraarqhqrclahslvgtpNYIAPEVLLRTGYTQLC 826
Cdd:cd05079    158 AIE--TDKEYYTVKD----------------------DLDSPV--------------------FWYAPECLIQSKFYIAS 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  827 DWWSVGVILFEMLV----GQPP---FLAQT-PLETQM------KVINWQTSLHIPPQAklsPEASDLIIKLC--RGPEDR 890
Cdd:cd05079    194 DVWSFGVTLYELLTycdsESSPmtlFLKMIgPTHGQMtvtrlvRVLEEGKRLPRPPNC---PEEVYQLMRKCweFQPSKR 270
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
607-867 1.22e-10

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: 63.05  E-value: 1.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  607 GIGAFGEVCLARKVDTKALYATKTLRKkdvllrnqvahVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMM 686
Cdd:cd14060      2 GGGSFGSVYRAIWVSQDKEVAVKKLLK-----------IEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  687 SLLIRmgifPESLARFYIAELTCAVESVHKMGF---------IHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyy 757
Cdd:cd14060     71 DYLNS----NESEEMDMDQIMTWATDIAKGMHYlhmeapvkvIHRDLKSRNVVIAADGVLKICDFG-------------- 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qsgdhprqdsmdfsnewgdpsscrcgdrlkplerrAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd14060    133 -----------------------------------ASRFHSHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWE 177
                          250       260       270
                   ....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFLAQTPLETQMKVINWQTSLHIP 867
Cdd:cd14060    178 MLTREVPFKGLEGLQVAWLVVEKNERPTIP 207
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
701-839 1.30e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 65.10  E-value: 1.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  701 RFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsgdhprqDSMDFSNEwgdpssc 780
Cdd:PHA03210   270 RAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFG----------------------TAMPFEKE------- 320
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  781 rcgdrlkplerRAARQhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:PHA03210   321 -----------REAFD------YGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDML 362
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
595-890 1.44e-10

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: 62.85  E-value: 1.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  595 MDKSMFVKIKTLGIGAFGEVCLAR---KVDTkalyATKTLRKKdvllrnqvahVKAERDILAEAD------NEWVVRLYY 665
Cdd:cd05059      1 IDPSELTFLKELGSGQFGVVHLGKwrgKIDV----AIKMIKEG----------SMSEDDFIEEAKvmmklsHPKLVQLYG 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  666 SFQDKDNLYFVMDYIPGGDMMSLLIRM-GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd05059     67 VCTKQRPIFIVTEYMANGCLLNYLRERrGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  745 CtgfRWTHDSKYYQSGdhprqdSMDFSNEWGdpsscrcgdrlkplerraarqhqrclahslvgtpnyiAPEVLLRTGYTQ 824
Cdd:cd05059    147 A---RYVLDDEYTSSV------GTKFPVKWS-------------------------------------PPEVFMYSKFSS 180
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  825 LCDWWSVGVILFEMLV-GQPPFLAQTPLETQMKVinwQTSLHIpPQAKLSPEASDLIIKLC--RGPEDR 890
Cdd:cd05059    181 KSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHI---SQGYRL-YRPHLAPTEVYTIMYSCwhEKPEER 245
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
603-890 1.66e-10

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: 63.14  E-value: 1.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALyATKTLRKKDVllrnQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd05072     12 VKKLGAGQFGEVWMGYYNNSTKV-AVKTLKPGTM----SVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMG----IFPESLArfYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYyq 758
Cdd:cd05072     87 GSLLDFLKSDEggkvLLPKLID--FSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLA---RVIEDNEY-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqdsmdfsnewgdpsSCRCGDRLkPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd05072    160 --------------------TAREGAKF-PIK--------------------WTAPEAINFGSFTIKSDVWSFGILLYEI 198
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  839 LV-GQPPFlaqtPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC--RGPEDR 890
Cdd:cd05072    199 VTyGKIPY----PGMSNSDVMSALQRGYRMPRMENCPDELYDIMKTCwkEKAEER 249
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
604-878 3.35e-10

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: 61.97  E-value: 3.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVclARKVDTKALYATKTLRK---KDVLLRNQvaHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd14147      9 EVIGIGGFGKV--YRGSWRGELVAVKAARQdpdEDISVTAE--SVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARF--YIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH--------IKLTDFGLctgfrw 750
Cdd:cd14147     85 AGGPLSRALAGRRVPPHVLVNWavQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIEnddmehktLKITDFGL------ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd14147    159 -------------------------------------------AREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWS 195
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  831 VGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIP-----PQAKLSPEASD 878
Cdd:cd14147    196 FGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPstcpePFAQLMADCWA 248
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
596-748 3.78e-10

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: 62.39  E-value: 3.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  596 DKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKtlrkkDVLLRNQVA--HVKAERD--ILAEADNEWVVRLY------- 664
Cdd:cd07865     10 EVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALK-----KVLMENEKEgfPITALREikILQLLKHENVVNLIeicrtka 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  665 --YSfQDKDNLYFVMDYIPGgDMMSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTD 741
Cdd:cd07865     85 tpYN-RYKGSIYLVFEFCEH-DLAGLLSNKNVkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLAD 162

                   ....*..
gi 1178431733  742 FGLCTGF 748
Cdd:cd07865    163 FGLARAF 169
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
600-891 3.82e-10

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: 62.38  E-value: 3.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATK--TLRK--KDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQ-DKDNLY 674
Cdd:cd14040      8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKihQLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFC 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMG--FIHRDIKPDNILI---DRDGHIKLTDFGLCtgfR 749
Cdd:cd14040     88 TVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLS---K 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 WTHDSKYyqsgdhpRQDSMDFSNEWGdpsscrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLL----RTGYTQL 825
Cdd:cd14040    165 IMDDDSY-------GVDGMDLTSQGA-------------------------------GTYWYLPPECFVvgkePPKISNK 206
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  826 CDWWSVGVILFEMLVGQPPFLAQTPLET--QMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRL 891
Cdd:cd14040    207 VDVWSVGVIFFQCLYGRKPFGHNQSQQDilQENTILKATEVQFPVKPVVSNEAKAFIRRcLAYRKEDRF 275
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
597-846 4.88e-10

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: 61.98  E-value: 4.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd06633     20 EEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGG--DMMSllirmgIFPESLARFYIAELT----CAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrw 750
Cdd:cd06633    100 MEYCLGSasDLLE------VHKKPLQEVEIAAIThgalQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG------- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfSNEWGDPsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTG---YTQLCD 827
Cdd:cd06633    167 --------------------SASIASP------------------------ANSFVGTPYWMAPEVILAMDegqYDGKVD 202
                          250
                   ....*....|....*....
gi 1178431733  828 WWSVGVILFEMLVGQPPFL 846
Cdd:cd06633    203 IWSLGITCIELAERKPPLF 221
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
609-850 5.58e-10

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 61.18  E-value: 5.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  609 GAFGEVCLARKVDTKALYATKTLrkkdvllrnQVAHVK-AERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMS 687
Cdd:cd13995     15 GAFGKVYLAQDTKTKKRMACKLI---------PVEQFKpSDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  688 LLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIkLTDFGLCTGFRwthDSKYYqsgdhPRqds 767
Cdd:cd13995     86 KLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMT---EDVYV-----PK--- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  768 mdfsnewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLA 847
Cdd:cd13995    154 ------------------------------------DLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVR 197

                   ...
gi 1178431733  848 QTP 850
Cdd:cd13995    198 RYP 200
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
604-845 5.62e-10

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 61.21  E-value: 5.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVclarkvdTKALYATKTLRKKDVLLR--NQVAHVKAERDILAEA------DNEWVVRLYYSFQDkDNLYF 675
Cdd:cd05060      1 KELGHGNFGSV-------RKGVYLMKSGKEVEVAVKtlKQEHEKAGKKEFLREAsvmaqlDHPCIVRLIGVCKG-EPLML 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCA---VESVHkmgFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRwtH 752
Cdd:cd05060     73 VMELAPLGPLLKYLKKRREIPVSDLKELAHQVAMGmayLESKH---FVHRDLAARNVLLVNRHQAKISDFGMSRALG--A 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 DSKYYQSGDHPRqdsmdfsneWgdpsscrcgdrlkPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd05060    148 GSDYYRATTAGR---------W-------------PLK--------------------WYAPECINYGKFSSKSDVWSYG 185
                          250
                   ....*....|....
gi 1178431733  833 VILFEML-VGQPPF 845
Cdd:cd05060    186 VTLWEAFsYGAKPY 199
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
807-905 6.82e-10

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 60.83  E-value: 6.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  807 GTPNYIAPEVLLRTG-YT-QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSlhIPPQakLSPEASDLIIKLC 884
Cdd:cd14023    148 GCPAYVSPEILNTTGtYSgKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC--IPDH--VSPKARCLIRSLL 223
                           90       100
                   ....*....|....*....|..
gi 1178431733  885 RG-PEDRLgknGADEIKAHPFF 905
Cdd:cd14023    224 RRePSERL---TAPEILLHPWF 242
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
584-858 6.90e-10

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: 62.03  E-value: 6.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  584 ESNYIRLKRakmdksmFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvlLRNQVAHVKAERDI--LAEADNEWVV 661
Cdd:cd07874     10 DSTFTVLKR-------YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRP---FQNQTHAKRAYRELvlMKCVNHKNII 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  662 RLYYSFQDKDNL------YFVMDYIPGGdmMSLLIRMGIFPESLArFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDG 735
Cdd:cd07874     80 SLLNVFTPQKSLeefqdvYLVMELMDAN--LCQVIQMELDHERMS-YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  736 HIKLTDFGLCtgfrwthdskyyqsgdhpRQDSMDFsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPE 815
Cdd:cd07874    157 TLKILDFGLA------------------RTAGTSF------------------------------MMTPYVVTRYYRAPE 188
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1178431733  816 VLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVI 858
Cdd:cd07874    189 VILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVI 231
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
673-839 7.14e-10

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: 61.80  E-value: 7.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFyIAELTCAVESVHKMGFIHRDIKPDNILI--DRDGHI-KLTDFGLctgfr 749
Cdd:cd13977    110 LWFVMEFCDGGDMNEYLLSRRPDRQTNTSF-MLQLSSALAFLHRNQIVHRDLKPDNILIshKRGEPIlKVADFGL----- 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  750 wthdSKYyqsgdhprqdsmdfsnewgdpssCRcGDRLKPLERRAARQhqrCLAHSLVGTPNYIAPEVlLRTGYTQLCDWW 829
Cdd:cd13977    184 ----SKV-----------------------CS-GSGLNPEEPANVNK---HFLSSACGSDFYMAPEV-WEGHYTAKADIF 231
                          170
                   ....*....|
gi 1178431733  830 SVGVILFEML 839
Cdd:cd13977    232 ALGIIIWAMV 241
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
667-745 7.16e-10

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 58.82  E-value: 7.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  667 FQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARF--YIAELtcavesvHKMGFIHRDIKPDNILIDrDGHIKLTDFGL 744
Cdd:COG3642     25 DVDPDDADLVMEYIEGETLADLLEEGELPPELLRELgrLLARL-------HRAGIVHGDLTTSNILVD-DGGVYLIDFGL 96

                   .
gi 1178431733  745 C 745
Cdd:COG3642     97 A 97
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
598-904 9.37e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 61.76  E-value: 9.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLR-KKDVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:PLN00034    74 SELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYgNHEDTVRRQICR---EIEILRDVNHPNVVKCHDMFDHNGEIQVL 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGIFPESLARfyiaELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWThdsky 756
Cdd:PLN00034   151 LEFMDGGSLEGTHIADEQFLADVAR----QILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQT----- 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprqdsMDFSNewgdpsscrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVL-------LRTGYTQlcDWW 829
Cdd:PLN00034   222 -----------MDPCN-------------------------------SSVGTIAYMSPERIntdlnhgAYDGYAG--DIW 257
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  830 SVGVILFEMLVGQPPFLA--QTPLETQMKVINWQTSLHIPPQAklSPEASDLIIK-LCRGPEDRLgknGADEIKAHPF 904
Cdd:PLN00034   258 SLGVSILEFYLGRFPFGVgrQGDWASLMCAICMSQPPEAPATA--SREFRHFISCcLQREPAKRW---SAMQLLQHPF 330
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
600-908 1.09e-09

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: 61.16  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvLLRNQVAHVKAERDI--LAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd07872      8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIR----LEHEEGAPCTAIREVslLKDLKHANIVTLHDIVHTDKSLTLVF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIpGGDMMSLLIRMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsky 756
Cdd:cd07872     84 EYL-DKDLKQYMDDCGnIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA----------- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yQSGDHPRQdsmDFSNEwgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLRTG-YTQLCDWWSVGVIL 835
Cdd:cd07872    152 -RAKSVPTK---TYSNE--------------------------------VVTLWYRPPDVLLGSSeYSTQIDMWGVGCIF 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  836 FEMLVGQPPFLAQTpLETQMKVI----------NWQ--------TSLHIP---PQ------AKLSPEASDLIIKLCRGPE 888
Cdd:cd07872    196 FEMASGRPLFPGST-VEDELHLIfrllgtpteeTWPgissndefKNYNFPkykPQplinhaPRLDTEGIELLTKFLQYES 274
                          330       340
                   ....*....|....*....|
gi 1178431733  889 DRlgKNGADEIKAHPFFKTI 908
Cdd:cd07872    275 KK--RISAEEAMKHAYFRSL 292
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
606-849 1.24e-09

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: 60.35  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTL-RKKDVLLRNQVAHVKAERDIlaeaDNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14221      1 LGKGCFGQAIKVTHRETGEVMVMKELiRFDEETQRTFLKEVKVMRCL----EHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLIRMGI-FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsgdhp 763
Cdd:cd14221     77 LRGIIKSMDShYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGL------------------- 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rqdsmdfsnewgdpSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML---V 840
Cdd:cd14221    138 --------------ARLMVDEKTQPEGLRSLKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIgrvN 203

                   ....*....
gi 1178431733  841 GQPPFLAQT 849
Cdd:cd14221    204 ADPDYLPRT 212
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
592-890 1.32e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 61.55  E-value: 1.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  592 RAKMDKSMFVKIKTLGIGA--FGEVCLARKVdtkalyatktlRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSF-- 667
Cdd:PHA03212    86 RAGIEKAGFSILETFTPGAegFAFACIDNKT-----------CEHVVIKAGQRGGTATEAHILRAINHPSIIQLKGTFty 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  668 ---------QDKDNLYFVMD---YIPGGDMMSLlirmgifPESLARfyiaeltcAVESVHKMGFIHRDIKPDNILIDRDG 735
Cdd:PHA03212   155 nkftclilpRYKTDLYCYLAakrNIAICDILAI-------ERSVLR--------AIQYLHENRIIHRDIKAENIFINHPG 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  736 HIKLTDFGLCTGFRWTHDSKYYQsgdhprqdsmdfsneWGdpsscrcgdrlkplerraarqhqrclahslvGTPNYIAPE 815
Cdd:PHA03212   220 DVCLGDFGAACFPVDINANKYYG---------------WA-------------------------------GTIATNAPE 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  816 VLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPL------ETQMKVINWQTSLH-----IPPQAKLSPEASDLIIKLC 884
Cdd:PHA03212   254 LLARDPYGPAVDIWSAGIVLFEMATCHDSLFEKDGLdgdcdsDRQIKLIIRRSGTHpnefpIDAQANLDEIYIGLAKKSS 333

                   ....*.
gi 1178431733  885 RGPEDR 890
Cdd:PHA03212   334 RKPGSR 339
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
603-894 1.36e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 60.43  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALY-ATKTLR---KKDVLLRNQVAHVKAERDiLAEADNEWVVRLY----YSFQDKDN-L 673
Cdd:cd07862      6 VAEIGEGAYGKVFKARDLKNGGRFvALKRVRvqtGEEGMPLSTIREVAVLRH-LETFEHPNVVRLFdvctVSRTDRETkL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDYIpGGDMMSLLIRM---GIFPESLARFyIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrw 750
Cdd:cd07862     85 TLVFEHV-DQDLTTYLDKVpepGVPTETIKDM-MFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGL------ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLA-HSLVGTPNYIAPEVLLRTGYTQLCDWW 829
Cdd:cd07862    157 -------------------------------------------ARIYSFQMAlTSVVVTLWYRAPEVLLQSSYATPVDLW 193
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  830 SVGVILFEMLVGQPPFLAQTPLETQMKVI---------NWQTSLHIpPQAKLSPEASDLIIKLCrgPE-DRLGKN 894
Cdd:cd07862    194 SVGCIFAEMFRRKPLFRGSSDVDQLGKILdviglpgeeDWPRDVAL-PRQAFHSKSAQPIEKFV--TDiDELGKD 265
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
606-875 1.58e-09

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: 60.05  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLAR-KVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 684
Cdd:cd14146      2 IGVGGFGKVYRATwKGQEVAVKAARQDPDEDI--KATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  685 MMSLLI--------RMG--IFPESLARFYIaELTCAVESVHKMGF---IHRDIKPDNIL----IDRDG----HIKLTDFG 743
Cdd:cd14146     80 LNRALAaanaapgpRRArrIPPHILVNWAV-QIARGMLYLHEEAVvpiLHRDLKSSNILllekIEHDDicnkTLKITDFG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LctgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLLRTGYT 823
Cdd:cd14146    159 L-------------------------------------------------AREWHRTTKMSAAGTYAWMAPEVIKSSLFS 189
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  824 QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIP-----PQAKLSPE 875
Cdd:cd14146    190 KGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTLPIPstcpePFAKLMKE 246
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
603-868 1.83e-09

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: 60.49  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAeRDILAEADNEwvvRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14225     48 LEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALVEVKI-LDALRRKDRD---NSHNVIHMKEYFYFRNHLCIT 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSL----LIRMGIFPE-SLA---RFYIAELTCaVESVHKMGFIHRDIKPDNILIDRDGH--IKLTDFGlctgfrwth 752
Cdd:cd14225    124 FELLGMnlyeLIKKNNFQGfSLSlirRFAISLLQC-LRLLYRERIIHCDLKPENILLRQRGQssIKVIDFG--------- 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfsnewgdpSSCrcgdrlkplerraaRQHQRclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd14225    194 -------------------------SSC--------------YEHQR--VYTYIQSRFYRSPEVILGLPYSMAIDMWSLG 232
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1178431733  833 VILFEMLVGQPPFLAQTPLEtQMKVInwQTSLHIPP 868
Cdd:cd14225    233 CILAELYTGYPLFPGENEVE-QLACI--MEVLGLPP 265
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
603-842 2.48e-09

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: 59.93  E-value: 2.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDT-KALYATKTLRkkdvllRNQVAHVKAERDI-----LAEADNE---WVVRLYYSFQDKDNL 673
Cdd:cd14135      5 YGYLGKGVFSNVVRARDLARgNQEVAIKIIR------NNELMHKAGLKELeilkkLNDADPDdkkHCIRLLRHFEHKNHL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDyipggdMMSLLIRmgifpESLARF-------------YIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH-IKL 739
Cdd:cd14135     79 CLVFE------SLSMNLR-----EVLKKYgknvglnikavrsYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  740 TDFGlctgfrwthdskyyqsgdhprqdSMDFSNEwgdpsscrcGDRLKPLERRAarqhqrclahslvgtpnYIAPEVLLR 819
Cdd:cd14135    148 CDFG-----------------------SASDIGE---------NEITPYLVSRF-----------------YRAPEIILG 178
                          250       260
                   ....*....|....*....|...
gi 1178431733  820 TGYTQLCDWWSVGVILFEMLVGQ 842
Cdd:cd14135    179 LPYDYPIDMWSVGCTLYELYTGK 201
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
664-743 2.64e-09

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: 59.68  E-value: 2.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  664 YYSFQDKDNLYFVMDYIPGGDMMSLLIRM-----GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR----- 733
Cdd:cd13981     67 HSAHLFQDESILVMDYSSQGTLLDVVNKMknktgGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLeicad 146
                           90       100
                   ....*....|....*....|
gi 1178431733  734 -----DGH-----IKLTDFG 743
Cdd:cd13981    147 wpgegENGwlskgLKLIDFG 166
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
807-905 2.76e-09

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 58.90  E-value: 2.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  807 GTPNYIAPEVLLRTG-YT-QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLhipPQAkLSPEASDLIIK-L 883
Cdd:cd14022    148 GCPAYVSPEILNTSGsYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNI---PET-LSPKAKCLIRSiL 223
                           90       100
                   ....*....|....*....|..
gi 1178431733  884 CRGPEDRLgknGADEIKAHPFF 905
Cdd:cd14022    224 RREPSERL---TSQEILDHPWF 242
MobB_NDR-like cd21775
Mob-binding domain found in the nuclear Dbf2-related kinase (NDR) subfamily; NDR kinases ...
539-595 3.94e-09

Mob-binding domain found in the nuclear Dbf2-related kinase (NDR) subfamily; 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 includes Drosophila melanogaster tricorner, which is a serine/threonine-protein kinase that plays an important role in controlling cell structure and proliferation of a variety of polarized outgrowths including epidermal hairs, bristles, arista laterals, and dendrites. It affects cellular morphogenesis by regulating the expression of target genes that encode cytoskeleton-interacting proteins and not via the direct modification of the cytoskeleton. It maintains the integrity of epidermal hairs and is an essential component of the signaling pathway regulating dendritic branching of sensory neurons. The NDR subfamily belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. NDR-like kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR-like serine/threonine protein kinases.


Pssm-ID: 439270  Cd Length: 65  Bit Score: 53.83  E-value: 3.94e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  539 EQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKM 595
Cdd:cd21775      9 ENYYSNLLTQCEERENRLKKLEQRMEEEGLSEEEKEERRKQHAAKETEFLRLKRTRL 65
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
715-858 4.60e-09

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: 59.37  E-value: 4.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  715 HKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerRAA 794
Cdd:cd07853    120 HSAGILHRDIKPGNLLVNSNCVLKICDFGLA----------------------------------------------RVE 153
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  795 RQHQRCLAHSLVGTPNYIAPEVLL-RTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLeTQMKVI 858
Cdd:cd07853    154 EPDESKHMTQEVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPI-QQLDLI 217
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
599-845 8.27e-09

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


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 57.46  E-value: 8.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  599 MFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd06607      2 IFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPG--GDMMSLLiRMGIFPESLARFYIAELTcAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdsky 756
Cdd:cd06607     82 YCLGsaSDIVEVH-KKPLQEVEIAAICHGALQ-GLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG------------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 yqsgdhprQDSMdfsnewgdpsscrcgdrlkplerraarqhqRCLAHSLVGTPNYIAPEVLLRTG---YTQLCDWWSVGV 833
Cdd:cd06607    147 --------SASL------------------------------VCPANSFVGTPYWMAPEVILAMDegqYDGKVDVWSLGI 188
                          250
                   ....*....|..
gi 1178431733  834 ILFEMLVGQPPF 845
Cdd:cd06607    189 TCIELAERKPPL 200
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
606-857 9.55e-09

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: 57.32  E-value: 9.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDtKALYATKTLrKKDVLLRNQVAHVKAERdILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 685
Cdd:cd05085      4 LGKGNFGEVYKGTLKD-KTPVAVKTC-KEDLPQELKIKFLSEAR-ILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  686 MSLLIRMG--IFPESLARFYIaELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYQSGdhp 763
Cdd:cd05085     81 LSFLRKKKdeLKTKQLVKFSL-DAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMS---RQEDDGVYSSSG--- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  764 rqdsmdfsnewgdpsscrcgdrLKPLERRaarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDWWSVGVILFEML-VGQ 842
Cdd:cd05085    154 ----------------------LKQIPIK------------------WTAPEALNYGRYSSESDVWSFGILLWETFsLGV 193
                          250
                   ....*....|....*
gi 1178431733  843 PPFLAQTPLETQMKV 857
Cdd:cd05085    194 CPYPGMTNQQAREQV 208
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
603-845 1.16e-08

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 57.47  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLAR-----KVDTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd05046     10 ITTLGRGEFGEVFLAKakgieEEGGETLVLVKALQKTKD--ENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMIL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDMMSLLI--RMGIFPE------SLARFYIAELTC-AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgf 748
Cdd:cd05046     88 EYTDLGDLKQFLRatKSKDEKLkppplsTKQKVALCTQIAlGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLS--- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 RWTHDSKYYQsgdhprqdsmdFSNEWgdpsscrcgdrlKPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDW 828
Cdd:cd05046    165 KDVYNSEYYK-----------LRNAL------------IPLR--------------------WLAPEAVQEDDFSTKSDV 201
                          250
                   ....*....|....*...
gi 1178431733  829 WSVGVILFEMLV-GQPPF 845
Cdd:cd05046    202 WSFGVLMWEVFTqGELPF 219
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
606-743 1.18e-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: 54.76  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHvkaERDILAEADNEW--VVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd13968      1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLES---EMDILRRLKGLElnIPKVLVTEDVDGPNILLMELVKGG 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARFYIAELTCaVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG 743
Cdd:cd13968     78 TLIAYTQEEELDEKDVESIMYQLAEC-MRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
604-845 1.21e-08

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 57.54  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLA--RKVDTKALY-ATKTLrKKDVLLRNQVAHVKAERDILAEADNEWVVRLY-YSFQDKDNLYF---- 675
Cdd:cd05035      5 KILGEGEFGSVMEAqlKQDDGSQLKvAVKTM-KVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIgVCFTASDLNKPpspm 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 -VMDYIPGGDMMSLLI--RMGIFPE-----SLARFyIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctg 747
Cdd:cd05035     84 vILPFMKHGDLHSYLLysRLGGLPEklplqTLLKF-MVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGL--- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 frwthdSKYYQSGDHPRQDsmdfsnewgdpsscrcgdrlkplerraarqhqrCLAHSLVgtpNYIAPEVLLRTGYTQLCD 827
Cdd:cd05035    160 ------SRKIYSGDYYRQG---------------------------------RISKMPV---KWIALESLADNVYTSKSD 197
                          250
                   ....*....|....*....
gi 1178431733  828 WWSVGVILFEMLV-GQPPF 845
Cdd:cd05035    198 VWSFGVTMWEIATrGQTPY 216
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
603-858 1.28e-08

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: 57.20  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLArKVDTKALYATKTLRKKDVllrnqvahvkAERDILAEA------DNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd05113      9 LKELGTGQFGVVKYG-KWRGQYDVAIKMIKEGSM----------SEDEFIEEAkvmmnlSHEKLVQLYGVCTKQRPIFII 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLIRMGIFPESLARFYIAELTC-AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSK 755
Cdd:cd05113     78 TEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCeAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLS---RYVLDDE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSGdhprqdSMDFSNEWGdpsscrcgdrlkplerraarqhqrclahslvgtpnyiAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd05113    155 YTSSV------GSKFPVRWS-------------------------------------PPEVLMYSKFSSKSDVWAFGVLM 191
                          250       260
                   ....*....|....*....|....
gi 1178431733  836 FEML-VGQPPFLAQTPLETQMKVI 858
Cdd:cd05113    192 WEVYsLGKMPYERFTNSETVEHVS 215
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
604-892 1.31e-08

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 56.89  E-value: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVclarkvdTKALYATKTLRKKDV--LLRNQVAHVKAERDILAEA------DNEWVVRLYySFQDKDNLYF 675
Cdd:cd05116      1 GELGSGNFGTV-------KKGYYQMKKVVKTVAvkILKNEANDPALKDELLREAnvmqqlDNPYIVRMI-GICEAESWML 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRwtHDSK 755
Cdd:cd05116     73 VMEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALR--ADEN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 YYQSGDHprqdsmdfsNEWgdpsscrcgdrlkPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDWWSVGVIL 835
Cdd:cd05116    151 YYKAQTH---------GKW-------------PVK--------------------WYAPECMNYYKFSSKSDVWSFGVLM 188
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  836 FEML-VGQPPFLAQTPLE-TQMkvINWQTSLHIPPQAklSPEASDLiIKLC--RGPEDRLG 892
Cdd:cd05116    189 WEAFsYGQKPYKGMKGNEvTQM--IEKGERMECPAGC--PPEMYDL-MKLCwtYDVDERPG 244
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
606-843 1.35e-08

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: 57.73  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQvahvKAERDILAEADNEWV-----VRLYYSFQDKDNLYFVMDYI 680
Cdd:cd14229      8 LGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQG----QIEVGILARLSNENAdefnfVRAYECFQHRNHTCLVFEML 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGgDMMSLLIRMGIFPESLA--RFYIAELTCAVESVHKMGFIHRDIKPDNI-LID---RDGHIKLTDFGLCTGFRWTHDS 754
Cdd:cd14229     84 EQ-NLYDFLKQNKFSPLPLKviRPILQQVATALKKLKSLGLIHADLKPENImLVDpvrQPYRVKVIDFGSASHVSKTVCS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  755 KYYQSgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahslvgtPNYIAPEVLLRTGYTQLCDWWSVGVI 834
Cdd:cd14229    163 TYLQS-------------------------------------------------RYYRAPEIILGLPFCEAIDMWSLGCV 193

                   ....*....
gi 1178431733  835 LFEMLVGQP 843
Cdd:cd14229    194 IAELFLGWP 202
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
807-905 1.47e-08

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 56.67  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  807 GTPNYIAPEVLLRTG-YT-QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQtsLHIPpqAKLSPEASDLIIKLC 884
Cdd:cd13976    148 GCPAYVSPEILNSGAtYSgKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQ--FAIP--ETLSPRARCLIRSLL 223
                           90       100
                   ....*....|....*....|..
gi 1178431733  885 R-GPEDRLgknGADEIKAHPFF 905
Cdd:cd13976    224 RrEPSERL---TAEDILLHPWL 242
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
718-905 2.05e-08

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 56.95  E-value: 2.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  718 GFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdhprQDSMDFSNEWgdPSSCRCGDRLKPLERRaarqh 797
Cdd:cd14011    135 KLVHGNICPESVVINSNGEWKLAGFDFC-------------------ISSEQATDQF--PYFREYDPNLPPLAQP----- 188
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  798 qrclahslvgTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV-GQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEA 876
Cdd:cd14011    189 ----------NLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNkGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEKVPEEL 258
                          170       180       190
                   ....*....|....*....|....*....|
gi 1178431733  877 SDLIIKLC-RGPEDRLgknGADEIKAHPFF 905
Cdd:cd14011    259 RDHVKTLLnVTPEVRP---DAEQLSKIPFF 285
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
604-857 2.15e-08

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: 56.48  E-value: 2.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALYATKTLRkkDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 683
Cdd:cd05084      2 ERIGRGNFGEVFSGRLRADNTPVAVKSCR--ETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGifpeslARFYIAELTCAVESVHK-MGF------IHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKY 756
Cdd:cd05084     80 DFLTFLRTEG------PRLKVKELIRMVENAAAgMEYleskhcIHRDLAARNCLVTEKNVLKISDFGMS---REEEDGVY 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  757 YQSGdhprqdsmdfsnewgdpsscrcGDRLKPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDWWSVGVILF 836
Cdd:cd05084    151 AATG----------------------GMKQIPVK--------------------WTAPEALNYGRYSSESDVWSFGILLW 188
                          250       260
                   ....*....|....*....|..
gi 1178431733  837 EML-VGQPPFLAQTPLETQMKV 857
Cdd:cd05084    189 ETFsLGAVPYANLSNQQTREAV 210
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
701-925 2.58e-08

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: 57.10  E-value: 2.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  701 RFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC-TGFRWTHDSKYyqsgdhprqdsmdfsneWGDpss 779
Cdd:cd07859    106 QFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLArVAFNDTPTAIF-----------------WTD--- 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  780 crcgdrlkplerraarqhqrclahsLVGTPNYIAPEVL--LRTGYTQLCDWWSVGVILFEMLVGQPPF------------ 845
Cdd:cd07859    166 -------------------------YVATRWYRAPELCgsFFSKYTPAIDIWSIGCIFAEVLTGKPLFpgknvvhqldli 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  846 ---LAQTPLETQMKVIN-----WQTSLHIPPQAKLS---PEASDLIIKLCR-----GPEDRlgkNGADEIKAHPFFKTId 909
Cdd:cd07859    221 tdlLGTPSPETISRVRNekarrYLSSMRKKQPVPFSqkfPNADPLALRLLErllafDPKDR---PTAEEALADPYFKGL- 296
                          250
                   ....*....|....*.
gi 1178431733  910 fSSDLRQQSASYIPKI 925
Cdd:cd07859    297 -AKVEREPSAQPITKL 311
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
601-783 2.59e-08

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: 56.20  E-value: 2.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  601 VKIKTLGIGAFGEVCLArkvdtkalyatkTLRKKDVLLRNQVAHVKAERDILAEAD------NEWVVRLYYSFQDKDNLY 674
Cdd:cd05039      9 KLGELIGKGEFGDVMLG------------DYRGQKVAVKCLKDDSTAAQAFLAEASvmttlrHPNLVQLLGVVLEGNGLY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLI---RMGIFPESLARFyiAELTC-AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrw 750
Cdd:cd05039     77 IVTEYMAKGSLVDYLRsrgRAVITRKDQLGF--ALDVCeGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGL------ 148
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1178431733  751 thdSKYYQSGdhprQDSMDFSNEWGDPSSCRCG 783
Cdd:cd05039    149 ---AKEASSN----QDGGKLPIKWTAPEALREK 174
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
604-845 2.83e-08

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 56.17  E-value: 2.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVC--LARKVDTKALYATKTLrKKDVLLRNQVAHVKAERDILAEADNEWVVRLY-YSFQDKDNLYF----- 675
Cdd:cd05075      6 KTLGEGEFGSVMegQLNQDDSVLKVAVKTM-KIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIgVCLQNTESEGYpspvv 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLI--RMGIFP-----ESLARFyIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgf 748
Cdd:cd05075     85 ILPFMKHGDLHSFLLysRLGDCPvylptQMLVKF-MTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGL---- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdSKYYQSGDHPRQDsmdfsnewgdpsscrcgdrlkplerRAARQHQRclahslvgtpnYIAPEVLLRTGYTQLCDW 828
Cdd:cd05075    160 -----SKKIYNGDYYRQG-------------------------RISKMPVK-----------WIAIESLADRVYTTKSDV 198
                          250
                   ....*....|....*...
gi 1178431733  829 WSVGVILFEMLV-GQPPF 845
Cdd:cd05075    199 WSFGVTMWEIATrGQTPY 216
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
598-733 3.02e-08

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: 56.18  E-value: 3.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  598 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdvlLRNQVAHVKAERDILAEA---DNEWVVRLYYSFQDKDNLY 674
Cdd:cd14138      5 TEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKP---LAGSVDEQNALREVYAHAvlgQHSHVVRYYSAWAEDDHML 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  675 FVMDYIPGGDMMSLLI----RMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR 733
Cdd:cd14138     82 IQNEYCNGGSLADAISenyrIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISR 144
MobB_Trc-like cd21780
Mob-binding domain found in Drosophila melanogaster tricorner and similar proteins; Drosophila ...
535-595 3.31e-08

Mob-binding domain found in Drosophila melanogaster tricorner and similar proteins; Drosophila melanogaster tricorner, also called serine/threonine-protein kinase 38-like, or NDR protein kinase, is a serine/threonine-protein kinase that plays an important role in controlling cell structure and proliferation of a variety of polarized outgrowths including epidermal hairs, bristles, arista laterals, and dendrites. It affects cellular morphogenesis by regulating the expression of target genes that encode cytoskeleton-interacting proteins and not via the direct modification of the cytoskeleton. It maintains the integrity of epidermal hairs and is an essential component of the signaling pathway regulating dendritic branching of sensory neurons. Tricorner belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. These kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of Tricorner-like serine/threonine protein kinases.


Pssm-ID: 439274  Cd Length: 65  Bit Score: 51.20  E-value: 3.31e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  535 KFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKM 595
Cdd:cd21780      5 KVTLENYYSNLIAQHKERENRLKKLEESMEEEGLTEEQKQEKRQQHALKETEFLRLKRSRL 65
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
606-845 3.91e-08

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 55.61  E-value: 3.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEV----CLARKVDTKALYATKTLRKKDV--LLRnqvahvkaERDILAEADNEWVVRLY-YSFQDKDNLYFVMD 678
Cdd:cd14064      1 IGSGSFGKVykgrCRNKIVAIKRYRANTYCSKSDVdmFCR--------EVSILCRLNHPCVIQFVgACLDDPSQFAIVTQ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLL--IRMGIFPESlarfyiaELTCAVESVHKMGF--------IHRDIKPDNILIDRDGHIKLTDFGlctgf 748
Cdd:cd14064     73 YVSGGSLFSLLheQKRVIDLQS-------KLIIAVDVAKGMEYlhnltqpiIHRDLNSHNILLYEDGHAVVADFG----- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthDSKYYQsgdhprqdSMDFSNEWGDPSSCRcgdrlkplerraarqhqrclahslvgtpnYIAPEVLLR-TGYTQLCD 827
Cdd:cd14064    141 ----ESRFLQ--------SLDEDNMTKQPGNLR-----------------------------WMAPEVFTQcTRYSIKAD 179
                          250
                   ....*....|....*...
gi 1178431733  828 WWSVGVILFEMLVGQPPF 845
Cdd:cd14064    180 VFSYALCLWELLTGEIPF 197
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
641-904 4.47e-08

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 55.27  E-value: 4.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  641 QVAHVKAERDILAEAD----NEWVVRLYYSFQDKDNLY--FVMDYipgGDMMSLLIRMGIFPESLARFYIAELTCAVESV 714
Cdd:cd14024     24 KVLSLRSYQECLAPYDrlgpHEGVCSVLEVVIGQDRAYafFSRHY---GDMHSHVRRRRRLSEDEARGLFTQMARAVAHC 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  715 HKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSkyyqsgdhprqDSMDfsnewgDPSSCrcgdrlkplerraa 794
Cdd:cd14024    101 HQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNGDD-----------DSLT------DKHGC-------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  795 rqhqrclahslvgtPNYIAPEVL-LRTGYT-QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVinWQTSLHIPpqAKL 872
Cdd:cd14024    150 --------------PAYVGPEILsSRRSYSgKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKI--RRGAFSLP--AWL 211
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1178431733  873 SPEASDLI-IKLCRGPEDRLgknGADEIKAHPF 904
Cdd:cd14024    212 SPGARCLVsCMLRRSPAERL---KASEILLHPW 241
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
604-759 5.42e-08

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 55.51  E-value: 5.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLA---RKVDTKALYATKTLRKKDVLLRNQvaHVKAERDILAEADNEWVVRLYYSFQDkDNLYFVMDYI 680
Cdd:cd05056     12 RCIGEGQFGDVYQGvymSPENEKIAVAVKTCKNCTSPSVRE--KFLQEAYIMRQFDHPHIVKLIGVITE-NPVWIVMELA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLL-IRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYQS 759
Cdd:cd05056     89 PLGELRSYLqVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLS---RYMEDESYYKA 165
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
603-843 5.93e-08

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 55.43  E-value: 5.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEV---CLAR--KVDTKALYATKTLrkkdvllrNQVAHVKAERDILAEA------DNEWVVRLYYSFQDKD 671
Cdd:cd05032     11 IRELGQGSFGMVyegLAKGvvKGEPETRVAIKTV--------NENASMRERIEFLNEAsvmkefNCHHVVRLLGVVSTGQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGDMMSLL--------IRMGIFPESLARFY--IAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTD 741
Cdd:cd05032     83 PTLVVMELMAKGDLKSYLrsrrpeaeNNPGLGPPTLQKFIqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  742 FGLCtgfRWTHDSKYYQSGdhprqdsmdfsnewgdpsscrcGDRLKPLErraarqhqrclahslvgtpnYIAPEVLLRTG 821
Cdd:cd05032    163 FGMT---RDIYETDYYRKG----------------------GKGLLPVR--------------------WMAPESLKDGV 197
                          250       260
                   ....*....|....*....|....
gi 1178431733  822 YTQLCDWWSVGVILFEM--LVGQP 843
Cdd:cd05032    198 FTTKSDVWSFGVVLWEMatLAEQP 221
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
597-846 6.43e-08

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: 55.44  E-value: 6.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd06635     24 EKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGG--DMMSllirmgIFPESLARFYIAELT----CAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrw 750
Cdd:cd06635    104 MEYCLGSasDLLE------VHKKPLQEIEIAAIThgalQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG------- 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfSNEWGDPsscrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTG---YTQLCD 827
Cdd:cd06635    171 --------------------SASIASP------------------------ANSFVGTPYWMAPEVILAMDegqYDGKVD 206
                          250
                   ....*....|....*....
gi 1178431733  828 WWSVGVILFEMLVGQPPFL 846
Cdd:cd06635    207 VWSLGITCIELAERKPPLF 225
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
606-845 6.52e-08

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: 55.19  E-value: 6.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARkVDTKALYATKTLRKkdvllRNQVAH---VKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14664      1 IGRGGAGTVYKGV-MPNGTLVAVKRLKG-----EGTQGGdhgFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESL---ARFYIAeltcaVESVHKMGF---------IHRDIKPDNILIDRDGHIKLTDFGLCTGFrw 750
Cdd:cd14664     75 GSLGELLHSRPESQPPLdweTRQRIA-----LGSARGLAYlhhdcspliIHRDVKSNNILLDEEFEAHVADFGLAKLM-- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgDPSSCRCgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd14664    148 -------------------------DDKDSHV-------------------MSSVAGSYGYIAPEYAYTGKVSEKSDVYS 183
                          250
                   ....*....|....*
gi 1178431733  831 VGVILFEMLVGQPPF 845
Cdd:cd14664    184 YGVVLLELITGKRPF 198
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
604-891 6.53e-08

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 55.40  E-value: 6.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLAR-----KVDTKALYATKTLRKKDVLLRNQVahvKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd05094     11 RELGEGAFGKVFLAEcynlsPTKDKMLVAVKTLKDPTLAARKDF---QREAELLTNLQHDHIVKFYGVCGDGDPLIMVFE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSLLIRMGifPESL-----------------ARFYIA-ELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLT 740
Cdd:cd05094     88 YMKHGDLNKFLRAHG--PDAMilvdgqprqakgelglsQMLHIAtQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  741 DFGLCtgfRWTHDSKYYQSGDHPrqdsmdfsnewgdpsscrcgdrLKPLErraarqhqrclahslvgtpnYIAPEVLLRT 820
Cdd:cd05094    166 DFGMS---RDVYSTDYYRVGGHT----------------------MLPIR--------------------WMPPESIMYR 200
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  821 GYTQLCDWWSVGVILFEMLV-GQPPFLAQTPLEtqmkVINWQTSLHIPPQAKLSPEASDLIIKLC--RGPEDRL 891
Cdd:cd05094    201 KFTTESDVWSFGVILWEIFTyGKQPWFQLSNTE----VIECITQGRVLERPRVCPKEVYDIMLGCwqREPQQRL 270
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
695-841 6.79e-08

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: 55.79  E-value: 6.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  695 FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRdghiklTDFGLCTGFRWTHDSKYYQSGDhprQDSMDFSNew 774
Cdd:cd14215    113 YPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVN------SDYELTYNLEKKRDERSVKSTA---IRVVDFGS-- 181
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  775 gdpsscrcgdrlkplerrAARQHQRclaHS-LVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd14215    182 ------------------ATFDHEH---HStIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVG 228
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
603-845 6.95e-08

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: 55.16  E-value: 6.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLAR-----KVDTKALYATKTLrkKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd05049     10 KRELGEGAFGKVFLGEcynlePEQDKMLVAVKTL--KDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGDM----------MSLLIRMGIFPESLAR---FYIA-ELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG 743
Cdd:cd05049     88 EYMEHGDLnkflrshgpdAAFLASEDSAPGELTLsqlLHIAvQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFG 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LCtgfRWTHDSKYYQSGdhprqdsmdfsnewgdpsscrcGDRLKPLErraarqhqrclahslvgtpnYIAPEVLLRTGYT 823
Cdd:cd05049    168 MS---RDIYSTDYYRVG----------------------GHTMLPIR--------------------WMPPESILYRKFT 202
                          250       260
                   ....*....|....*....|...
gi 1178431733  824 QLCDWWSVGVILFEMLV-GQPPF 845
Cdd:cd05049    203 TESDVWSFGVVLWEIFTyGKQPW 225
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
590-845 6.99e-08

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 55.31  E-value: 6.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  590 LKRAKMDKSMFVKIKTLGIGAFG---EVCLARKVDTKALYATKTLrKKDVLLRNQVAHVKAERDILAEADNEWVVRLY-- 664
Cdd:cd05074      1 LKDVLIQEQQFTLGRMLGKGEFGsvrEAQLKSEDGSFQKVAVKML-KADIFSSSDIEEFLREAACMKEFDHPNVIKLIgv 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  665 -YSFQDKDNLYFVMDYIP---GGDMMSLLI--RMGIFP-----ESLARFYIaELTCAVESVHKMGFIHRDIKPDNILIDR 733
Cdd:cd05074     80 sLRSRAKGRLPIPMVILPfmkHGDLHTFLLmsRIGEEPftlplQTLVRFMI-DIASGMEYLSSKNFIHRDLAARNCMLNE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  734 DGHIKLTDFGLctgfrwthdSKYYQSGDHPRQDsmdfsnewgdpsscrCGDRLkPLErraarqhqrclahslvgtpnYIA 813
Cdd:cd05074    159 NMTVCVADFGL---------SKKIYSGDYYRQG---------------CASKL-PVK--------------------WLA 193
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1178431733  814 PEVLLRTGYTQLCDWWSVGVILFE-MLVGQPPF 845
Cdd:cd05074    194 LESLADNVYTTHSDVWAFGVTMWEiMTRGQTPY 226
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
600-858 1.02e-07

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: 54.70  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRkkdvLLRNQVAHVKAERD--ILAEADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd07869      7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIR----LQEEEGTPFTAIREasLLKGLKHANIVLLHDIIHTKETLTLVF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIpGGDMMSLLIRM--GIFPESLaRFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsk 755
Cdd:cd07869     83 EYV-HTDLCQYMDKHpgGLHPENV-KLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLA---------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyQSGDHPrqdSMDFSNEwgdpsscrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLL-RTGYTQLCDWWSVGVI 834
Cdd:cd07869    151 --RAKSVP---SHTYSNE--------------------------------VVTLWYRPPDVLLgSTEYSTCLDMWGVGCI 193
                          250       260
                   ....*....|....*....|....
gi 1178431733  835 LFEMLVGQPPFLAQTPLETQMKVI 858
Cdd:cd07869    194 FVEMIQGVAAFPGMKDIQDQLERI 217
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
603-890 1.12e-07

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: 54.12  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALyATKTLRKKDVllrnQVAHVKAERDILAEADNEWVVRLYySFQDKDNLYFVMDYIPG 682
Cdd:cd05067     12 VERLGAGQFGEVWMGYYNGHTKV-AIKSLKQGSM----SPDAFLAEANLMKQLQHQRLVRLY-AVVTQEPIYIITEYMEN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLL-----IRMGIFPESLARFYIAELTCAVEsvhKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYY 757
Cdd:cd05067     86 GSLVDFLktpsgIKLTINKLLDMAAQIAEGMAFIE---ERNYIHRDLRAANILVSDTLSCKIADFGLA---RLIEDNEYT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QsgdhprQDSMDFSNEWgdpsscrcgdrlkplerraarqhqrclahslvgtpnyIAPEVLLRTGYTQLCDWWSVGVILFE 837
Cdd:cd05067    160 A------REGAKFPIKW-------------------------------------TAPEAINYGTFTIKSDVWSFGILLTE 196
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  838 MLV-GQPPFlaqtPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC--RGPEDR 890
Cdd:cd05067    197 IVThGRIPY----PGMTNPEVIQNLERGYRMPRPDNCPEELYQLMRLCwkERPEDR 248
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
604-849 1.14e-07

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


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 54.57  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARkvDTKALYATKTLRKKD--VLLRNQVAHVKAERDILAEADNEWVvrlYYSFQDKDNL-YFVMDYI 680
Cdd:cd13980      6 KSLGSTRFLKVARAR--HDEGLVVVKVFVKPDpaLPLRSYKQRLEEIRDRLLELPNVLP---FQKVIETDKAaYLIRQYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGgdmmSLLIRMGIFP--ESLARFYIA-ELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFglcTGFRWThdskyY 757
Cdd:cd13980     81 KY----NLYDRISTRPflNLIEKKWIAfQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDF---ASFKPT-----Y 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 QSGDHPRQDSMDFsnewgDPSScrcgdrlkpleRRaarqhqRClahslvgtpnYIAPEVLLRTGY------------TQL 825
Cdd:cd13980    149 LPEDNPADFSYFF-----DTSR-----------RR------TC----------YIAPERFVDALTldaeserrdgelTPA 196
                          250       260
                   ....*....|....*....|....*.
gi 1178431733  826 CDWWSVGVILFEM-LVGQPPF-LAQT 849
Cdd:cd13980    197 MDIFSLGCVIAELfTEGRPLFdLSQL 222
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
606-845 1.59e-07

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 54.20  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLAR-----KVDTKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd05092     13 LGEGAFGKVFLAEchnllPEQDKMLVAVKALKEAT---ESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMG----IFPESLARFY--------------IAELTCAVESVHkmgFIHRDIKPDNILIDRDGHIKLTDF 742
Cdd:cd05092     90 RHGDLNRFLRSHGpdakILDGGEGQAPgqltlgqmlqiasqIASGMVYLASLH---FVHRDLATRNCLVGQGLVVKIGDF 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  743 GLCtgfRWTHDSKYYQSGdhprqdsmdfsnewgdpsscrcGDRLKPLErraarqhqrclahslvgtpnYIAPEVLLRTGY 822
Cdd:cd05092    167 GMS---RDIYSTDYYRVG----------------------GRTMLPIR--------------------WMPPESILYRKF 201
                          250       260
                   ....*....|....*....|....
gi 1178431733  823 TQLCDWWSVGVILFEMLV-GQPPF 845
Cdd:cd05092    202 TTESDIWSFGVVLWEIFTyGKQPW 225
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
603-744 2.28e-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: 53.74  E-value: 2.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLAR----KVDTKALYATKTLRKKDVllrNQVAHVKAERDILAEADNEWVVR---LYYSfQDKDNLYF 675
Cdd:cd05081      9 ISQLGKGNFGSVELCRydplGDNTGALVAVKQLQHSGP---DQQRDFQREIQILKALHSDFIVKyrgVSYG-PGRRSLRL 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLIR-MGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd05081     85 VMEYLPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGL 154
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
706-870 2.55e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 54.51  E-value: 2.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  706 ELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYqsgdhprqdsmdfsnewgdpsscrcgdr 785
Cdd:PHA03211   268 QLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFARGSWSTPFH---------------------------- 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  786 lkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLA------QTPLETQMKVIN 859
Cdd:PHA03211   320 -----------------YGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIFEAAVHTASLFSasrgdeRRPYDAQILRII 382
                          170
                   ....*....|....
gi 1178431733  860 WQTSLHI---PPQA 870
Cdd:PHA03211   383 RQAQVHVdefPQHA 396
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
603-845 2.98e-07

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: 53.98  E-value: 2.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKtlrkkdvLLRNqvahvkaERDILAEADNEWVVRLYYSFQDKDNlyfVMDYIPG 682
Cdd:cd14224     70 LKVIGKGSFGQVVKAYDHKTHQHVALK-------MVRN-------EKRFHRQAAEEIRILEHLKKQDKDN---TMNVIHM 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GD---------MMSLLIRMGI-----------FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH--IKLT 740
Cdd:cd14224    133 LEsftfrnhicMTFELLSMNLyelikknkfqgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVI 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  741 DFGlctgfrwthdskyyqsgdhprqdsmdfsnewgdpSSCRcgdrlkplerraarQHQRclAHSLVGTPNYIAPEVLLRT 820
Cdd:cd14224    213 DFG----------------------------------SSCY--------------EHQR--IYTYIQSRFYRAPEVILGA 242
                          250       260
                   ....*....|....*....|....*
gi 1178431733  821 GYTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd14224    243 RYGMPIDMWSFGCILAELLTGYPLF 267
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
607-905 3.44e-07

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 53.44  E-value: 3.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  607 GIGAFGEVCLAR--KVDTKALYATKTLrKKDVLLRNQVAhVKAERDI--LAEADNEWVVRLYYSFQDKDN--LYFVMDYI 680
Cdd:cd07842      9 GRGTYGRVYKAKrkNGKDGKEYAIKKF-KGDKEQYTGIS-QSACREIalLRELKHENVVSLVEVFLEHADksVYLLFDYA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGgDMMSLL------IRMGIfPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH----IKLTDFGLctgfrw 750
Cdd:cd07842     87 EH-DLWQIIkfhrqaKRVSI-PPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPergvVKIGDLGL------ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdSKYYQSgdhPRQDSMDfsnewGDPsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLLrtG---YTQLCD 827
Cdd:cd07842    159 ---ARLFNA---PLKPLAD-----LDP---------------------------VVVTIWYRAPELLL--GarhYTKAID 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  828 WWSVGVILFEMLVGQPPF-------LAQTPLE-TQMKVI----------NWQTSLHIPPQAKL----------------- 872
Cdd:cd07842    199 IWAIGCIFAELLTLEPIFkgreakiKKSNPFQrDQLERIfevlgtptekDWPDIKKMPEYDTLksdtkastypnsllakw 278
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1178431733  873 -------SPEASDLIIKLCR-GPEDRLgknGADEIKAHPFF 905
Cdd:cd07842    279 mhkhkkpDSQGFDLLRKLLEyDPTKRI---TAEEALEHPYF 316
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
675-845 3.61e-07

Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only];


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 53.94  E-value: 3.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPG----GDMMSLLIRMGIFPES--LARFYIAELTC-AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDfglCTG 747
Cdd:COG4248     91 FLMPRIKGarplHKFYSPKTRRQQFPLFdwLFLLRTARNLAaAVAALHAAGYVHGDVNPSNILVSDTALVTLID---TDS 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 FRWTHDSKYYqsgdhprqdsmdfsnewgdpsscRCgdrlkplerraarqhqrclahsLVGTPNYIAPEV----LLRTGYT 823
Cdd:COG4248    168 FQVRDPGKVY-----------------------RC----------------------VVGTPEFTPPELqgksFARVDRT 202
                          170       180
                   ....*....|....*....|...
gi 1178431733  824 QLCDWWSVGVILFEML-VGQPPF 845
Cdd:COG4248    203 EEHDRFGLAVLIFQLLmEGRHPF 225
UBA_LATS cd14322
UBA domain found in serine/threonine-protein kinase LATS and similar proteins; The LATS ...
11-36 4.06e-07

UBA domain found in serine/threonine-protein kinase LATS and similar proteins; The LATS proteins family consists of two isoforms, LATS1 and LATS2, both of which are mammalian homologs of the Drosophila tumor suppressor gene lats/warts. LATS1, also called large tumor suppressor homolog 1, or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. LATS2, also called kinase phosphorylated during mitosis protein, or large tumor suppressor homolog 2, or serine/threonine-protein kinase KPM, or Warts-like kinase, inhibits the G1/S transition and is essential for embryonic development, proliferation control and genomic integrity. LATS proteins contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


Pssm-ID: 270507  Cd Length: 39  Bit Score: 47.08  E-value: 4.06e-07
                           10        20
                   ....*....|....*....|....*.
gi 1178431733   11 QDMVIQALQKTNNRSIEAAIEFISKM 36
Cdd:cd14322     14 EEISMRALKKSGARTIEAAIEFIELM 39
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
706-758 4.21e-07

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: 52.76  E-value: 4.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  706 ELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCTGFRwthDSKYYQ 758
Cdd:cd14125    104 QMISRIEYVHSKNFIHRDIKPDNFLMglgKKGNLVYIIDFGLAKKYR---DPRTHQ 156
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
603-747 4.54e-07

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 52.67  E-value: 4.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVllrNQVAHVKAERDILAE-ADNEWVVRL--YYSFQDKDNLYFV--- 676
Cdd:cd14037      8 EKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDE---HDLNVCKREIEIMKRlSGHKNIVGYidSSANRSGNGVYEVlll 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  677 MDYIPGG---DMMSLLIRMGIF-PESLARFY-IAEltcAVESVH--KMGFIHRDIKPDNILIDRDGHIKLTDFGLCTG 747
Cdd:cd14037     85 MEYCKGGgviDLMNQRLQTGLTeSEILKIFCdVCE---AVAAMHylKPPLIHRDLKVENVLISDSGNYKLCDFGSATT 159
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
603-849 5.74e-07

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 52.39  E-value: 5.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEV----CLARKVDTKAL-YATKTLRKkdvllrnqVAHVKAERDILAEA------DNEWVVRLY-YSFQDK 670
Cdd:cd05036     11 IRALGQGAFGEVyegtVSGMPGDPSPLqVAVKTLPE--------LCSEQDEMDFLMEAlimskfNHPNIVRCIgVCFQRL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DNlYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKmG--------FIHRDIKPDNILIDRDGH---IKL 739
Cdd:cd05036     83 PR-FILLELMAGGDLKSFLRENRPRPEQPSSLTMLDLLQLAQDVAK-GcryleenhFIHRDIAARNCLLTCKGPgrvAKI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  740 TDFGLCtgfRWTHDSKYYQSGdhprqdsmdfsnewgdpsscrcGDRLKPLErraarqhqrclahslvgtpnYIAPEVLLR 819
Cdd:cd05036    161 GDFGMA---RDIYRADYYRKG----------------------GKAMLPVK--------------------WMPPEAFLD 195
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1178431733  820 TGYTQLCDWWSVGVILFE-MLVGQPPFLAQT 849
Cdd:cd05036    196 GIFTSKTDVWSFGVLLWEiFSLGYMPYPGKS 226
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
603-839 6.24e-07

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: 52.33  E-value: 6.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLAR----KVDTKALYATKTLR-KKDVLLRNqvahVKAERDILAEADNEWVVR---LYYSfQDKDNLY 674
Cdd:cd14205      9 LQQLGKGNFGSVEMCRydplQDNTGEVVAVKKLQhSTEEHLRD----FEREIEILKSLQHDNIVKykgVCYS-AGRRNLR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGGDMMSLLIR-MGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwTHD 753
Cdd:cd14205     84 LIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVL--PQD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 SKYY---QSGDHPrqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahslvgtPNYIAPEVLLRTGYTQLCDWWS 830
Cdd:cd14205    162 KEYYkvkEPGESP---------------------------------------------IFWYAPESLTESKFSVASDVWS 196

                   ....*....
gi 1178431733  831 VGVILFEML 839
Cdd:cd14205    197 FGVVLYELF 205
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
603-845 6.33e-07

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: 52.78  E-value: 6.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEW-VVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd14228     20 LEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYnFVRSYECFQHKNHTCLVFEMLE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GgDMMSLLIRMGIFPESLA--RFYIAELTCAVESVHKMGFIHRDIKPDNILIdrdghikltdfglctgfrwthdskyyqs 759
Cdd:cd14228    100 Q-NLYDFLKQNKFSPLPLKyiRPILQQVATALMKLKSLGLIHADLKPENIML---------------------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewGDPssCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14228    151 ---------------VDP--VRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELF 213

                   ....*.
gi 1178431733  840 VGQPPF 845
Cdd:cd14228    214 LGWPLY 219
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
601-890 6.44e-07

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: 51.97  E-value: 6.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  601 VKIKT-LGIGAFGEVCLAR---KVDTKALYATKTLRKKDVLLRNQVAHVKAERDilaeaDNewVVRLYYSFQDKDNLYFV 676
Cdd:cd14063      2 LEIKEvIGKGRFGRVHRGRwhgDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRH-----DN--LVLFMGACMDPPHLAIV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLL-IRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDrDGHIKLTDFGLctgfrwthdsk 755
Cdd:cd14063     75 TSLCKGRTLYSLIhERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDFGL----------- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  756 yyqsgdhprqdsmdFSnewgdpsscrcgdrLKPLERRAARQHQRCLAHslvGTPNYIAPEVL--LRTG--------YTQL 825
Cdd:cd14063    143 --------------FS--------------LSGLLQPGRREDTLVIPN---GWLCYLAPEIIraLSPDldfeeslpFTKA 191
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  826 CDWWSVGVILFEMLVGQPPFLAQTPletqmKVINWQTSL-HIPPQAKLS--PEASDLIIkLC--RGPEDR 890
Cdd:cd14063    192 SDVYAFGTVWYELLAGRWPFKEQPA-----ESIIWQVGCgKKQSLSQLDigREVKDILM-QCwaYDPEKR 255
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
708-891 6.45e-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: 52.13  E-value: 6.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  708 TC-AVESVHKMG--FIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDskyyqsgdhprqdsmdfsNEWGdpsscrcgd 784
Cdd:cd14036    117 TCrAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPD------------------YSWS--------- 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  785 rlkplerraarQHQRCLAH---SLVGTPNYIAPEVL-LRTGY--TQLCDWWSVGVILFEMLVGQPPFLAQTPLetqmKVI 858
Cdd:cd14036    170 -----------AQKRSLVEdeiTRNTTPMYRTPEMIdLYSNYpiGEKQDIWALGCILYLLCFRKHPFEDGAKL----RII 234
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1178431733  859 NWQTSlhIPPQAKLSPEASDLIIKLCR-GPEDRL 891
Cdd:cd14036    235 NAKYT--IPPNDTQYTVFHDLIRSTLKvNPEERL 266
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
645-856 7.37e-07

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: 51.76  E-value: 7.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  645 VKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGgDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDI 724
Cdd:cd14112     47 AVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDV 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  725 KPDNILID--RDGHIKLTDFGlctgfrwtHDSKYYQSGDHPRQDSMDFSnewgdpsscrcgdrlkplerraarqhqrcla 802
Cdd:cd14112    126 QPDNIMFQsvRSWQVKLVDFG--------RAQKVSKLGKVPVDGDTDWA------------------------------- 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  803 hslvgTPNYIAPEvllrTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMK 856
Cdd:cd14112    167 -----SPEFHNPE----TPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEETK 211
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
603-845 7.63e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 52.54  E-value: 7.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLA--------RKVDTKALYATKTLRKkdvllrnqvahvkaERDILAEADNEWVVRLYYSFQDKDNLY 674
Cdd:PHA03207    97 LSSLTPGSEGEVFVCtkhgdeqrKKVIVKAVTGGKTPGR--------------EIDILKTISHRAIINLIHAYRWKSTVC 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  675 FVMDYIPGgDMMSLLIRMGIFPESLArFYIAE-LTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthd 753
Cdd:PHA03207   163 MVMPKYKC-DLFTYVDRSGPLPLEQA-ITIQRrLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAC------- 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 skyyQSGDHPrqdsmdfsnewgDPSSCrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGV 833
Cdd:PHA03207   234 ----KLDAHP------------DTPQC----------------------YGWSGTLETNSPELLALDPYCAKTDIWSAGL 275
                          250
                   ....*....|..
gi 1178431733  834 ILFEMLVGQPPF 845
Cdd:PHA03207   276 VLFEMSVKNVTL 287
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
673-891 8.44e-07

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


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 52.06  E-value: 8.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFY------IAELTCAV--ESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd13998     68 LWLVTAFHPNGSL*DYLSLHTIDWVSLCRLAlsvargLAHLHSEIpgCTQGKPAIAHRDLKSKNILVKNDGTCCIADFGL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  745 ctgfrwthdskyyqsgdhprqdSMDFSNEWGDPSscrcgdrlkplerrAARQHQrclahslVGTPNYIAPEVL------- 817
Cdd:cd13998    148 ----------------------AVRLSPSTGEED--------------NANNGQ-------VGTKRYMAPEVLegainlr 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  818 LRTGYTQLcDWWSVGVILFEM------LVG-----QPPFLAQTPLE---TQMKVINWQTSLH--IPPQAKLSPEASDL-- 879
Cdd:cd13998    185 DFESFKRV-DIYAMGLVLWEMasrctdLFGiveeyKPPFYSEVPNHpsfEDMQEVVVRDKQRpnIPNRWLSHPGLQSLae 263
                          250
                   ....*....|....
gi 1178431733  880 IIKLC--RGPEDRL 891
Cdd:cd13998    264 TIEECwdHDAEARL 277
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
604-845 9.03e-07

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 51.96  E-value: 9.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVD-----TKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 678
Cdd:cd05093     11 RELGEGAFGKVFLAECYNlcpeqDKILVAVKTLKDAS---DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMM---------SLLIRMGIFPESLAR---FYIAE-LTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC 745
Cdd:cd05093     88 YMKHGDLNkflrahgpdAVLMAEGNRPAELTQsqmLHIAQqIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  746 tgfRWTHDSKYYQSGDHPrqdsmdfsnewgdpsscrcgdrLKPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQL 825
Cdd:cd05093    168 ---RDVYSTDYYRVGGHT----------------------MLPIR--------------------WMPPESIMYRKFTTE 202
                          250       260
                   ....*....|....*....|.
gi 1178431733  826 CDWWSVGVILFEMLV-GQPPF 845
Cdd:cd05093    203 SDVWSLGVVLWEIFTyGKQPW 223
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
736-841 9.74e-07

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: 51.93  E-value: 9.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  736 HIKLTDFGLCTGFRWTHDSKYYQSGDHPRQD---SMDFSNEWGDPSSCRcGDRLKPLERRAARQHQRCLAH----SLVGT 808
Cdd:cd14214    118 HIRHMAYQLCHALKFLHENQLTHTDLKPENIlfvNSEFDTLYNESKSCE-EKSVKNTSIRVADFGSATFDHehhtTIVAT 196
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1178431733  809 PNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd14214    197 RHYRPPEVILELGWAQPCDVWSLGCILFEYYRG 229
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
603-845 1.05e-06

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: 52.01  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAE-ADNEWVVRLYYSFQDKDNLYFVMDYIP 681
Cdd:cd14227     20 LEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTEsADDYNFVRAYECFQHKNHTCLVFEMLE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GgDMMSLLIRMGIFPESLA--RFYIAELTCAVESVHKMGFIHRDIKPDNILIdrdghikltdfglctgfrwthdskyyqs 759
Cdd:cd14227    100 Q-NLYDFLKQNKFSPLPLKyiRPILQQVATALMKLKSLGLIHADLKPENIML---------------------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdhprqdsmdfsnewGDPSscRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14227    151 ---------------VDPS--RQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELF 213

                   ....*.
gi 1178431733  840 VGQPPF 845
Cdd:cd14227    214 LGWPLY 219
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
597-846 1.13e-06

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: 51.56  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd06634     14 EKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGG--DMMSllirmgIFPESLARFYIAELT----CAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrw 750
Cdd:cd06634     94 MEYCLGSasDLLE------VHKKPLQEVEIAAIThgalQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG------- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  751 thdskyyqsgdhprqdsmdfsnewgdpsscrCGDRLKPlerraarqhqrclAHSLVGTPNYIAPEVLLRTG---YTQLCD 827
Cdd:cd06634    161 -------------------------------SASIMAP-------------ANSFVGTPYWMAPEVILAMDegqYDGKVD 196
                          250
                   ....*....|....*....
gi 1178431733  828 WWSVGVILFEMLVGQPPFL 846
Cdd:cd06634    197 VWSLGITCIELAERKPPLF 215
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
716-841 1.40e-06

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: 51.42  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  716 KMGFIHRDIKPDNILID-RDGHIKLTDFG-LCtgfrWTHDSkyyqsgdhprqdsmdFSNEwgdpsscrcgdrlkplerra 793
Cdd:cd14136    138 KCGIIHTDIKPENVLLCiSKIEVKIADLGnAC----WTDKH---------------FTED-------------------- 178
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1178431733  794 arqhqrclahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd14136    179 ------------IQTRQYRSPEVILGAGYGTPADIWSTACMAFELATG 214
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
603-754 1.62e-06

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 50.75  E-value: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKAlyATKTLrKKDVLLRNQVAhvkaERDILAEADNEWVVRLY-YSFQDKDNLYFVMDYIP 681
Cdd:cd05082     11 LQTIGKGEFGDVMLGDYRGNKV--AVKCI-KNDATAQAFLA----EASVMTQLRHSNLVQLLgVIVEEKGGLYIVTEYMA 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178431733  682 GGDMMSLLIRMG---IFPESLARFYIaELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDS 754
Cdd:cd05082     84 KGSLVDYLRSRGrsvLGGDCLLKFSL-DVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDT 158
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
604-847 1.87e-06

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 50.42  E-value: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVclaRKVD------TKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKdNLYFVM 677
Cdd:cd05040      1 EKLGDGSFGVV---RRGEwttpsgKVIQVAVKCLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMVT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 DYIPGGdmmSLLIRM----GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHD 753
Cdd:cd05040     77 ELAPLG---SLLDRLrkdqGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNED 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 skYYQSGDHPRqdsMDFSneWgdpssCrcgdrlkplerraarqhqrclahslvgtpnyiAPEVLLRTGYTQLCDWWSVGV 833
Cdd:cd05040    154 --HYVMQEHRK---VPFA--W-----C--------------------------------APESLKTRKFSHASDVWMFGV 189
                          250
                   ....*....|....*
gi 1178431733  834 ILFEMLV-GQPPFLA 847
Cdd:cd05040    190 TLWEMFTyGEEPWLG 204
MobB_NDR2 cd21781
Mob-binding domain found in nuclear Dbf2-related kinase 2 (NDR2); NDR2, also called serine ...
535-595 2.58e-06

Mob-binding domain found in nuclear Dbf2-related kinase 2 (NDR2); NDR2, also called serine/threonine-protein kinase 38-like (STK38L), 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. NDR2 belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. NDR kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR2 serine/threonine protein kinase.


Pssm-ID: 439275  Cd Length: 68  Bit Score: 45.87  E-value: 2.58e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  535 KFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKM 595
Cdd:cd21781      6 KLTLENFYSNLILQHEERETRQKKLEVAMEEEGLADEEKKLRRSQHARKETEFLRLKRTRL 66
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
595-845 3.10e-06

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 50.11  E-value: 3.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  595 MDKSMFVKIKTLGIGAFGEVCLARKVDT------KALYATKTLrKKDvllrnqvAHVKAERDILAEAD-------NEWVV 661
Cdd:cd05053      9 LPRDRLTLGKPLGEGAFGQVVKAEAVGLdnkpneVVTVAVKML-KDD-------ATEKDLSDLVSEMEmmkmigkHKNII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  662 RLYYSFQDKDNLYFVMDYIPGGDMMSLLiRMGIFPESLARFYIAELT-----------CAVESVHKMGF------IHRDI 724
Cdd:cd05053     81 NLLGACTQDGPLYVVVEYASKGNLREFL-RARRPPGEEASPDDPRVPeeqltqkdlvsFAYQVARGMEYlaskkcIHRDL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  725 KPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYQsgdhprqdsmdfsnewgdpsscRCGDRLKPLErraarqhqrclahs 804
Cdd:cd05053    160 AARNVLVTEDNVMKIADFGLA---RDIHHIDYYR----------------------KTTNGRLPVK-------------- 200
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1178431733  805 lvgtpnYIAPEVLLRTGYTQLCDWWSVGVILFE-MLVGQPPF 845
Cdd:cd05053    201 ------WMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPY 236
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
606-925 3.32e-06

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: 50.03  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLAR---KVDTKALYATKTLRKKDVLLRNQVAHVKAERDIlaeadnewVVRLYYSFQDKDNLYFVMDYIPG 682
Cdd:cd14149     20 IGSGSFGTVYKGKwhgDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHV--------NILLFMGYMTKDNLAIVTQWCEG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESLARFYIAELTC-AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWTHDSKYYQsg 760
Cdd:cd14149     92 SSLYKHLHVQETKFQMFQLIDIARQTAqGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRWSGSQQVEQ-- 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  761 dhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLL---RTGYTQLCDWWSVGVILFE 837
Cdd:cd14149    170 --------------------------------------------PTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYE 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  838 MLVGQPPFlaqtpletqMKVINWQTSLHIPPQAKLSPEASDLiIKLCRGPEDRLGKNGADEIK-AHPFFKTIDFSSDLRQ 916
Cdd:cd14149    206 LMTGELPY---------SHINNRDQIIFMVGRGYASPDLSKL-YKNCPKAMKRLVADCIKKVKeERPLFPQILSSIELLQ 275

                   ....*....
gi 1178431733  917 QSasyIPKI 925
Cdd:cd14149    276 HS---LPKI 281
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
620-845 3.49e-06

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 50.01  E-value: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  620 VDTKALYATKTLrkKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRM------- 692
Cdd:cd05090     31 MDHAQLVAIKTL--KDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRsphsdvg 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  693 ------GIFPESLAR---FYIA-ELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYqsgdh 762
Cdd:cd05090    109 cssdedGTVKSSLDHgdfLHIAiQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLS---REIYSSDYY----- 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  763 prqdsmdfsnewgdpsscrcgdRLKPLERRAARqhqrclahslvgtpnYIAPEVLLRTGYTQLCDWWSVGVILFEML-VG 841
Cdd:cd05090    181 ----------------------RVQNKSLLPIR---------------WMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFG 223

                   ....
gi 1178431733  842 QPPF 845
Cdd:cd05090    224 LQPY 227
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
604-890 3.88e-06

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: 49.64  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLArKVDTKALYATKTLRKKDVllrnQVAHVKAERDILAEADNEWVVRLYySFQDKDNLYFVMDYIPGG 683
Cdd:cd05073     17 KKLGAGQFGEVWMA-TYNKHTKVAVKTMKPGSM----SVEAFLAEANVMKTLQHDKLVKLH-AVVTKEPIYIITEFMAKG 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLIRMGIFPESLARF--YIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYQsgd 761
Cdd:cd05073     91 SLLDFLKSDEGSKQPLPKLidFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLA---RVIEDNEYTA--- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  762 hprQDSMDFSNEWgdpsscrcgdrlkplerraarqhqrclahslvgtpnyIAPEVLLRTGYTQLCDWWSVGVILFEMLV- 840
Cdd:cd05073    165 ---REGAKFPIKW-------------------------------------TAPEAINFGSFTIKSDVWSFGILLMEIVTy 204
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  841 GQPPFLAQTPLETqmkVINWQTSLHIPPQAKLSPEASDLIIKLCRG-PEDR 890
Cdd:cd05073    205 GRIPYPGMSNPEV---IRALERGYRMPRPENCPEELYNIMMRCWKNrPEER 252
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
606-845 3.95e-06

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 49.72  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTKALYATKTLRKKDvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQD----KDNLYFVMDYIP 681
Cdd:cd14031     18 LGRGAFKTVYKGLDTETWVEVAWCELQDRK-LTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMT 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  682 GGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMG--FIHRDIKPDNILID-RDGHIKLTDFGLCTGFRWThdskyyq 758
Cdd:cd14031     97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTS------- 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEvLLRTGYTQLCDWWSVGVILFEM 838
Cdd:cd14031    170 ------------------------------------------FAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEM 206

                   ....*..
gi 1178431733  839 LVGQPPF 845
Cdd:cd14031    207 ATSEYPY 213
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
601-845 4.30e-06

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 49.29  E-value: 4.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  601 VKI-KTLGIGAFGEVCLARKVDTKALY---ATKTLRKKdvllrnqvAHVKAERDILAEA------DNEWVVRLYYSFQDK 670
Cdd:cd05033      6 VTIeKVIGGGEFGEVCSGSLKLPGKKEidvAIKTLKSG--------YSDKQRLDFLTEAsimgqfDHPNVIRLEGVVTKS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 DNLYFVMDYIPGGDMMSLLirmgifPESLARFYIAELT---CAVES----VHKMGFIHRDIKPDNILIDRDGHIKLTDFG 743
Cdd:cd05033     78 RPVMIVTEYMENGSLDKFL------RENDGKFTVTQLVgmlRGIASgmkyLSEMNYVHRDLAARNILVNSDLVCKVSDFG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LCTGFRWTHDSKYYQSGDHPrqdsmdfsnewgdpsscrcgdrlkplerraARqhqrclahslvgtpnYIAPEVLLRTGYT 823
Cdd:cd05033    152 LSRRLEDSEATYTTKGGKIP------------------------------IR---------------WTAPEAIAYRKFT 186
                          250       260
                   ....*....|....*....|...
gi 1178431733  824 QLCDWWSVGVILFE-MLVGQPPF 845
Cdd:cd05033    187 SASDVWSFGIVMWEvMSYGERPY 209
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
604-744 4.61e-06

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 49.48  E-value: 4.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLAR-KVDTK--ALYATKTLRkkdvllrnqVAHV-KAERDILAEA------DNEWVVRLYYSFQDKDNL 673
Cdd:cd05066     10 KVIGAGEFGEVCSGRlKLPGKreIPVAIKTLK---------AGYTeKQRRDFLSEAsimgqfDHPNIIHLEGVVTRSKPV 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178431733  674 YFVMDYIPGGDMMSLLIRMGifpeslARFYIAELTCAVESV-------HKMGFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd05066     81 MIVTEYMENGSLDAFLRKHD------GQFTVIQLVGMLRGIasgmkylSDMGYVHRDLAARNILVNSNLVCKVSDFGL 152
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
604-868 4.82e-06

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 49.58  E-value: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLAR-------KVDTKALYATKTLrkKDVLLRNQVAHVKAERDILAEAD-NEWVVRLYYSFQDKDNLYF 675
Cdd:cd05099     18 KPLGEGCFGQVVRAEaygidksRPDQTVTVAVKML--KDNATDKDLADLISEMELMKLIGkHKNIINLLGVCTQEGPLYV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLL-----------IRMGIFPESLARFYiAELTCAVESVHKMGF------IHRDIKPDNILIDRDGHIK 738
Cdd:cd05099     96 IVEYAAKGNLREFLrarrppgpdytFDITKVPEEQLSFK-DLVSCAYQVARGMEYlesrrcIHRDLAARNVLVTEDNVMK 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  739 LTDFGLCTGfrwTHDSKYYQSGDHPRQdsmdfsnewgdpsscrcgdrlkPLErraarqhqrclahslvgtpnYIAPEVLL 818
Cdd:cd05099    175 IADFGLARG---VHDIDYYKKTSNGRL----------------------PVK--------------------WMAPEALF 209
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  819 RTGYTQLCDWWSVGVILFEML-VGQPPFlAQTPLETQMKVINWQTSLHIPP 868
Cdd:cd05099    210 DRVYTHQSDVWSFGILMWEIFtLGGSPY-PGIPVEELFKLLREGHRMDKPS 259
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
594-845 4.97e-06

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 49.17  E-value: 4.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  594 KMDKSMFVKIKtLGIGAFGEVclarkvdTKALYatkTLRKKDV-----LLRNQvaHVKAERD-------ILAEADNEWVV 661
Cdd:cd05115      1 KRDNLLIDEVE-LGSGNFGCV-------KKGVY---KMRKKQIdvaikVLKQG--NEKAVRDemmreaqIMHQLDNPYIV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  662 RLYySFQDKDNLYFVMDYIPGGDMMSLLI--RMGIFPESLARFyIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKL 739
Cdd:cd05115     68 RMI-GVCEAEALMLVMEMASGGPLNKFLSgkKDEITVSNVVEL-MHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKI 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  740 TDFGLCTGFrwTHDSKYYQSGDhprqdsmdfSNEWgdpsscrcgdrlkPLErraarqhqrclahslvgtpnYIAPEVLLR 819
Cdd:cd05115    146 SDFGLSKAL--GADDSYYKARS---------AGKW-------------PLK--------------------WYAPECINF 181
                          250       260
                   ....*....|....*....|....*..
gi 1178431733  820 TGYTQLCDWWSVGVILFEML-VGQPPF 845
Cdd:cd05115    182 RKFSSRSDVWSYGVTMWEAFsYGQKPY 208
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
715-845 5.06e-06

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: 49.31  E-value: 5.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  715 HKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWthdskyyqSGDHPRQDSMdfsnewgdpsscrcgdrlkplerra 793
Cdd:cd14062    106 HAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATvKTRW--------SGSQQFEQPT------------------------- 152
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  794 arqhqrclahslvGTPNYIAPEVLL---RTGYTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd14062    153 -------------GSILWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLTGQLPY 194
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
673-890 5.72e-06

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: 49.15  E-value: 5.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  673 LYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTC----AVESVHKMGFIHRDIKPDNILI-----DRDGHIKLTDFG 743
Cdd:cd14000     83 LMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALqvadGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIKIADYG 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LctgfrwthdSKYyqsgdhprqdsmdfsnewgdpsSCRCGdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTG-Y 822
Cdd:cd14000    163 I---------SRQ----------------------CCRMG------------------AKGSEGTPGFRAPEIARGNViY 193
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  823 TQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDR 890
Cdd:cd14000    194 NEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLRPPLKQYECAPWPEVEVLMKKcWKENPQQR 262
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
714-891 6.18e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 49.49  E-value: 6.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  714 VHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqSGDHPRQDSMDFSnewgdpsscrcgdrlkplerra 793
Cdd:PHA03209   173 LHAQRIIHRDVKTENIFINDVDQVCIGDLG---------------AAQFPVVAPAFLG---------------------- 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  794 arqhqrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSL-HIPPQAKL 872
Cdd:PHA03209   216 -----------LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPSTIFEDPPSTPEEYVKSCHSHLlKIISTLKV 284
                          170
                   ....*....|....*....
gi 1178431733  873 SPEasdliiKLCRGPEDRL 891
Cdd:PHA03209   285 HPE------EFPRDPGSRL 297
MobB_NDR1 cd21782
Mob-binding domain found in nuclear Dbf2-related kinase 1 (NDR1) and similar proteins; NDR1, ...
535-595 7.21e-06

Mob-binding domain found in nuclear Dbf2-related kinase 1 (NDR1) and similar proteins; NDR1, also called serine/threonine-protein kinase 38 (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 hypersensitive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR1 belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. NDR kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR1 serine/threonine protein kinase.


Pssm-ID: 439276  Cd Length: 75  Bit Score: 44.71  E-value: 7.21e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  535 KFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKM 595
Cdd:cd21782     14 KVTLENFYSNLIAQHEEREMRQKKLEKVMEEEGLKDEEKRMRRSAHARKETEFLRLKRTRL 74
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
600-731 7.68e-06

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: 48.77  E-value: 7.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAhvkAERDILAEA---DNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd14139      2 FLELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQL---ALHEVYAHAvlgHHPHVVRYYSAWAEDDHMIIQ 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  677 MDYIPGGDMMSLLI---RMG-IFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILI 731
Cdd:cd14139     79 NEYCNGGSLQDAISentKSGnHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFI 137
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
604-890 8.73e-06

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: 48.37  E-value: 8.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALyATKTLRKKDVllrNQVAHVKaERDILAEADNEWVVRLYySFQDKDNLYFVMDYIPGG 683
Cdd:cd14203      1 VKLGQGCFGEVWMGTWNGTTKV-AIKTLKPGTM---SPEAFLE-EAQIMKKLRHDKLVQLY-AVVSEEPIYIVTEFMSKG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  684 DMMSLLI----RMGIFPESLArfYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYyqs 759
Cdd:cd14203     75 SLLDFLKdgegKYLKLPQLVD--MAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLA---RLIEDNEY--- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  760 gdHPRQDSmDFSNEWgdpsscrcgdrlkplerraarqhqrclahslvgtpnyIAPEVLLRTGYTQLCDWWSVGVILFEML 839
Cdd:cd14203    147 --TARQGA-KFPIKW-------------------------------------TAPEAALYGRFTIKSDVWSFGILLTELV 186
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  840 V-GQPPFLAQTPLETQMKVinwQTSLHIPPQAKLSPEASDLIIKLCRG-PEDR 890
Cdd:cd14203    187 TkGRVPYPGMNNREVLEQV---ERGYRMPCPPGCPESLHELMCQCWRKdPEER 236
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
710-747 9.22e-06

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 48.97  E-value: 9.22e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1178431733  710 AVESVHKMGFIHRDIKPDNILI-DRDGHIKLTDFG----LCTG 747
Cdd:cd14013    132 ALRKLHSTGIVHRDVKPQNIIVsEGDGQFKIIDLGaaadLRIG 174
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
595-852 9.98e-06

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 48.32  E-value: 9.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  595 MDKSMFVKIKTLGIGAFGEVCLArKVDTKALYATKTLRKKDVllrnqvahvkAERDILAEAD------NEWVVRLYYSFQ 668
Cdd:cd05114      1 INPSELTFMKELGSGLFGVVRLG-KWRAQYKVAIKAIREGAM----------SEEDFIEEAKvmmkltHPKLVQLYGVCT 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  669 DKDNLYFVMDYIPGGDMMSLL-IRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtg 747
Cdd:cd05114     70 QQKPIYIVTEFMENGCLLNYLrQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMT-- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 fRWTHDSKYYQSgdhprqdsmdfsnewgdpsscrCGDRLkPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCD 827
Cdd:cd05114    148 -RYVLDDQYTSS----------------------SGAKF-PVK--------------------WSPPEVFNYSKFSSKSD 183
                          250       260
                   ....*....|....*....|....*.
gi 1178431733  828 WWSVGVILFEMLV-GQPPFLAQTPLE 852
Cdd:cd05114    184 VWSFGVLMWEVFTeGKMPFESKSNYE 209
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
604-845 1.41e-05

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 48.25  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLAR-----------KVDTKALYATKTLRKKDVLLrnqvahvkAERDILAE-ADNEWVVRLYYSFQDKD 671
Cdd:cd05055     41 KTLGAGAFGKVVEATayglsksdavmKVAVKMLKPTAHSSEREALM--------SELKIMSHlGNHENIVNLLGACTIGG 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGDMMSLLIRMGifpESLARFYiaELTCAVESVHK-MGF------IHRDIKPDNILIDrDGHI-KLTDFG 743
Cdd:cd05055    113 PILVITEYCCYGDLLNFLRRKR---ESFLTLE--DLLSFSYQVAKgMAFlaskncIHRDLAARNVLLT-HGKIvKICDFG 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 LCTGFRwtHDSKYYQSGDhprqdsmdfsnewgdpsscrcgDRLkPLErraarqhqrclahslvgtpnYIAPEVLLRTGYT 823
Cdd:cd05055    187 LARDIM--NDSNYVVKGN----------------------ARL-PVK--------------------WMAPESIFNCVYT 221
                          250       260
                   ....*....|....*....|...
gi 1178431733  824 QLCDWWSVGVILFEML-VGQPPF 845
Cdd:cd05055    222 FESDVWSYGILLWEIFsLGSNPY 244
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
695-845 1.57e-05

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: 48.31  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  695 FPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRdghiklTDFGLCTGFRWTHDSKYYQSGDhprQDSMDFSNew 774
Cdd:cd14213    113 FPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQ------SDYVVKYNPKMKRDERTLKNPD---IKVVDFGS-- 181
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178431733  775 gdpsscrcgdrlkplerrAARQHQRclaHS-LVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPF 845
Cdd:cd14213    182 ------------------ATYDDEH---HStLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 232
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
706-750 1.59e-05

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 48.91  E-value: 1.59e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1178431733  706 ELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG----LCTGFRW 750
Cdd:PLN03224   317 QVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDFGaavdMCTGINF 365
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
603-843 1.66e-05

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 48.21  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRnqvaHVKAERDILA-----EADNEWVVRLYYSFQDKDNLYFVM 677
Cdd:cd14211      4 LEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYAR----QGQIEVSILSrlsqeNADEFNFVRAYECFQHKNHTCLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  678 --------DYIPGGDMMSLLIRMgIFPESLarfyiaELTCAVESVHKMGFIHRDIKPDNI-LID---RDGHIKLTDFGLC 745
Cdd:cd14211     80 emleqnlyDFLKQNKFSPLPLKY-IRPILQ------QVLTALLKLKSLGLIHADLKPENImLVDpvrQPYRVKVIDFGSA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  746 TGFRWTHDSKYYQSgdhprqdsmdfsnewgdpsscrcgdRLkplerraarqhqrclahslvgtpnYIAPEVLLRTGYTQL 825
Cdd:cd14211    153 SHVSKAVCSTYLQS-------------------------RY------------------------YRAPEIILGLPFCEA 183
                          250
                   ....*....|....*...
gi 1178431733  826 CDWWSVGVILFEMLVGQP 843
Cdd:cd14211    184 IDMWSLGCVIAELFLGWP 201
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
600-733 2.78e-05

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: 47.01  E-value: 2.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKIKTLGIGAFGEV--CLARkVDtKALYATKTLRKKdvlLRNQVAHVKAERDILAEA---DNEWVVRLYYSFQDKDNLY 674
Cdd:cd14051      2 FHEVEKIGSGEFGSVykCINR-LD-GCVYAIKKSKKP---VAGSVDEQNALNEVYAHAvlgKHPHVVRYYSAWAEDDHMI 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  675 FVMDYIPGGDMMSLLIR----MGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR 733
Cdd:cd14051     77 IQNEYCNGGSLADAISEnekaGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISR 139
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
592-858 2.89e-05

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 47.31  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  592 RAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQvAHVKAERDILAEAD-------NEWVVRLY 664
Cdd:cd05098      7 RWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSD-ATEKDLSDLISEMEmmkmigkHKNIINLL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  665 YSFQDKDNLYFVMDYIPGGDMMSLL-IRMgifPESLARFYIAE------------LTCAVESVHKMGF------IHRDIK 725
Cdd:cd05098     86 GACTQDGPLYVIVEYASKGNLREYLqARR---PPGMEYCYNPShnpeeqlsskdlVSCAYQVARGMEYlaskkcIHRDLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  726 PDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYQSGDHPRQdsmdfsnewgdpsscrcgdrlkPLErraarqhqrclahsl 805
Cdd:cd05098    163 ARNVLVTEDNVMKIADFGLA---RDIHHIDYYKKTTNGRL----------------------PVK--------------- 202
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  806 vgtpnYIAPEVLLRTGYTQLCDWWSVGVILFEML-VGQPPFlAQTPLETQMKVI 858
Cdd:cd05098    203 -----WMAPEALFDRIYTHQSDVWSFGVLLWEIFtLGGSPY-PGVPVEELFKLL 250
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
710-841 3.16e-05

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: 46.85  E-value: 3.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  710 AVESVHKMGFIHRDIKPDNILIDRDGH-IKLTDFGLctGFRWTH-DSKYYQSGDHprqdsmdfsnewgdpsscrcgdrlk 787
Cdd:cd14020    122 ALAFLHHEGYVHADLKPRNILWSAEDEcFKLIDFGL--SFKEGNqDVKYIQTDGY------------------------- 174
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  788 pleRRAARQHQRCLAHSLVGTpnyiapevllRTGYTQLCDWWSVGVILFEMLVG 841
Cdd:cd14020    175 ---RAPEAELQNCLAQAGLQS----------ETECTSAVDLWSLGIVLLEMFSG 215
UBA_LATS2 cd14398
UBA domain found in vertebrate serine/threonine-protein kinase LATS2; LATS2, also called ...
11-38 3.22e-05

UBA domain found in vertebrate serine/threonine-protein kinase LATS2; LATS2, also called kinase phosphorylated during mitosis protein, or large tumor suppressor homolog 2, or serine/threonine-protein kinase KPM, or Warts-like kinase, is a novel mammalian homolog of the Drosophila tumor suppressor gene lats/warts. It inhibits the G1/S transition and is essential for embryonic development, proliferation control, and genomic integrity. LATS2 is a serine/threonine kinase that negatively regulates CyclinE/CDK2 and plays a role in tumor suppression. It also acts as the negative regulator of androgen receptor (AR) through inhibiting androgen-regulated gene expression and thus plays an important role in AR -regulated transcription and in the development of prostate cancer. Moreover, LATS2 induces apoptosis via down-regulation of anti-apoptotic proteins, BCL-2 and BCL-x(L), in human lung cancer cells. It is a centrosomal protein and forms a complex with Ajuba, a LIM protein, to regulate organization of the spindle apparatus through recruitment of gamma-tubulin to the centrosome during mitosis. Furthermore, LATS2 interacts with Mdm2 to inhibit p53 ubiquitination and promote p53 activation. It stabilizes the cellular protein level of Snail1, a central regulator of epithelial cell adhesion and movement in epithelial-to-mesenchymal transitions (EMTs) during embryo development, and enhances its EMT activity. LATS2 contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


Pssm-ID: 270581  Cd Length: 41  Bit Score: 42.02  E-value: 3.22e-05
                           10        20
                   ....*....|....*....|....*...
gi 1178431733   11 QDMVIQALQKTNNRSIEAAIEFISKMSY 38
Cdd:cd14398     14 QEMAVRALKQTGSRSIEAALEYISKMSY 41
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
606-840 3.51e-05

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 46.89  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEV--CLARKV------------DTKALYATKTLRKkDVLLRNQVAHVKaERDILAEADNEWVVRLYYSFQDKD 671
Cdd:cd05097     13 LGEGQFGEVhlCEAEGLaeflgegapefdGQPVLVAVKMLRA-DVTKTARNDFLK-EIKIMSRLKNPNIIRLLGVCVSDD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  672 NLYFVMDYIPGGDMMSLLIRMGIFPE--------SLAR----FYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKL 739
Cdd:cd05097     91 PLCMITEYMENGDLNQFLSQREIESTfthannipSVSIanllYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKI 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  740 TDFGLctgfrwthdSKYYQSGDHPRqdsmdfsnewgdpsscrcgdrlkpLERRAarqhqrclahslVGTPNYIAPEVLLR 819
Cdd:cd05097    171 ADFGM---------SRNLYSGDYYR------------------------IQGRA------------VLPIRWMAWESILL 205
                          250       260
                   ....*....|....*....|.
gi 1178431733  820 TGYTQLCDWWSVGVILFEMLV 840
Cdd:cd05097    206 GKFTTASDVWAFGVTLWEMFT 226
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
650-746 3.85e-05

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 44.99  E-value: 3.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  650 DILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAEltcAVESVHKM---GFIHRDIKP 726
Cdd:cd05120     44 QLLAGKLSLPVPKVYGFGESDGWEYLLMERIEGETLSEVWPRLSEEEKEKIADQLAE---ILAALHRIdssVLTHGDLHP 120
                           90       100
                   ....*....|....*....|.
gi 1178431733  727 DNILIDRDGHI-KLTDFGLCT 746
Cdd:cd05120    121 GNILVKPDGKLsGIIDWEFAG 141
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
606-844 3.95e-05

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 46.74  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEVCLARKVDTkaLYATKTLRKKDVLlrnqvahvkaERDILAEADNEWVVRLY------------YSFQdKDNL 673
Cdd:cd14159      1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSEL----------DWSVVKNSFLTEVEKLSrfrhpnivdlagYSAQ-QGNY 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  674 YFVMDYIPGGDMMSLLIRMGIFP--ESLARFYIAELT-CAVESVHKM--GFIHRDIKPDNILIDRDGHIKLTDFGLctgf 748
Cdd:cd14159     68 CLIYVYLPNGSLEDRLHCQVSCPclSWSQRLHVLLGTaRAIQYLHSDspSLIHGDVKSSNILLDAALNPKLGDFGL---- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  749 rwthdSKYYQSGDHPRQDSMdfsnewgdpsscrcgdrlkpLERRAARQhqrclahslvGTPNYIaPEVLLRTG-YTQLCD 827
Cdd:cd14159    144 -----ARFSRRPKQPGMSST--------------------LARTQTVR----------GTLAYL-PEEYVKTGtLSVEID 187
                          250
                   ....*....|....*..
gi 1178431733  828 WWSVGVILFEMLVGQPP 844
Cdd:cd14159    188 VYSFGVVLLELLTGRRA 204
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
679-857 4.17e-05

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: 46.50  E-value: 4.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  679 YIPGGDMMSllirmgifpeslarFYIA-ELTCAVESVHKMGFIHRDIKPDNILI---DRDGHI--KLTDFGLctgfrwth 752
Cdd:cd14067    108 FMPLGHMLT--------------FKIAyQIAAGLAYLHKKNIIFCDLKSDNILVwslDVQEHIniKLSDYGI-------- 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 dskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd14067    166 -----------------------------------------SRQSFHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYG 204
                          170       180
                   ....*....|....*....|....*
gi 1178431733  833 VILFEMLVGQPPFLAQTPLETQMKV 857
Cdd:cd14067    205 MVLYELLSGQRPSLGHHQLQIAKKL 229
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
603-845 4.34e-05

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 46.55  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  603 IKTLGIGAFGEVCLAR---KVDTKALYATKTLRKKDVLLRNQVAHVKAERDIlaeadnewVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd14150      5 LKRIGTGSFGTVFRGKwhgDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHV--------NILLFMGFMTRPNFAIITQW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTC-AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWthdskyy 757
Cdd:cd14150     77 CEGSSLYRHLHVTETRFDTMQLIDVARQTAqGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATvKTRW------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  758 qSGDHPRQdsmdfsnewgDPSscrcgdrlkplerraarqhqrclahslvGTPNYIAPEVLL---RTGYTQLCDWWSVGVI 834
Cdd:cd14150    150 -SGSQQVE----------QPS----------------------------GSILWMAPEVIRmqdTNPYSFQSDVYAYGVV 190
                          250
                   ....*....|.
gi 1178431733  835 LFEMLVGQPPF 845
Cdd:cd14150    191 LYELMSGTLPY 201
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
604-845 5.61e-05

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: 46.21  E-value: 5.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLAR---KVDTKALYATKTLRKKDVLLRNQVAHVKAERDIlaeadnewVVRLYYSFQDKDNLYFVMDYI 680
Cdd:cd14151     14 QRIGSGSFGTVYKGKwhgDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHV--------NILLFMGYSTKPQLAIVTQWC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  681 PGGDMMSLLIRMGIFPESLARFYIAELTC-AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWTHDSKYYQ 758
Cdd:cd14151     86 EGSSLYHHLHIIETKFEMIKLIDIARQTAqGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvKSRWSGSHQFEQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  759 sgdhprqdsmdfsnewgdpsscrcgdrlkplerraarqhqrclahsLVGTPNYIAPEVLL---RTGYTQLCDWWSVGVIL 835
Cdd:cd14151    166 ----------------------------------------------LSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVL 199
                          250
                   ....*....|
gi 1178431733  836 FEMLVGQPPF 845
Cdd:cd14151    200 YELMTGQLPY 209
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
690-745 5.92e-05

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 45.94  E-value: 5.92e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  690 IRMGIfpESLARFYIA-ELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC 745
Cdd:cd13975     95 IKAGL--SLEERLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFC 149
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
600-845 6.05e-05

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 46.02  E-value: 6.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  600 FVKI-KTLGIGAFGEVCLAR-KVDTKALY--ATKTLrkKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYF 675
Cdd:cd05065      5 CVKIeEVIGAGEFGEVCRGRlKLPGKREIfvAIKTL--KSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  676 VMDYIPGGDMMSLLiRM--GIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthd 753
Cdd:cd05065     83 ITEFMENGALDSFL-RQndGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGL--------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  754 SKYYQSGDhprqdsmdfsnewGDPSSCRCGDRLKPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCDWWSVGV 833
Cdd:cd05065    153 SRFLEDDT-------------SDPTYTSSLGGKIPIR--------------------WTAPEAIAYRKFTSASDVWSYGI 199
                          250
                   ....*....|...
gi 1178431733  834 ILFE-MLVGQPPF 845
Cdd:cd05065    200 VMWEvMSYGERPY 212
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
670-914 8.06e-05

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 45.56  E-value: 8.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  670 KDNLYFVMDYIPGGDMMSLLIRmgifpESLA---RFYIA-ELTCAVESVHKMG--FIHRDIKPDNILIDRDGHIKLTDFG 743
Cdd:cd14025     65 SEPVGLVMEYMETGSLEKLLAS-----EPLPwelRFRIIhETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFG 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  744 L--CTGFRWTHDskyyqsgdhprqdsmdfsnewgdpsscrcgdrlkpLERRAARqhqrclahslvGTPNYIAPEVLLR-- 819
Cdd:cd14025    140 LakWNGLSHSHD-----------------------------------LSRDGLR-----------GTIAYLPPERFKEkn 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  820 ----TGYtqlcDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLcrgpedrLGKNG 895
Cdd:cd14025    174 rcpdTKH----DVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKGHRPSLSPIPRQRPSECQQMICL-------MKRCW 242
                          250
                   ....*....|....*....
gi 1178431733  896 ADEIKAHPFFKTIDFSSDL 914
Cdd:cd14025    243 DQDPRKRPTFQDITSETEN 261
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
606-764 8.14e-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: 45.75  E-value: 8.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  606 LGIGAFGEV--CLARKV--------------DTKALYATKTLRKKDVllRNQVAHVKAERDILAEADNEWVVRLYYSFQD 669
Cdd:cd05095     13 LGEGQFGEVhlCEAEGMekfmdkdfalevseNQPVLVAVKMLRADAN--KNARNDFLKEIKIMSRLKDPNIIRLLAVCIT 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  670 KDNLYFVMDYIPGGDMMSLLIR------MGIFPESLA------RFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHI 737
Cdd:cd05095     91 DDPLCMITEYMENGDLNQFLSRqqpegqLALPSNALTvsysdlRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 170
                          170       180
                   ....*....|....*....|....*..
gi 1178431733  738 KLTDFGLctgfrwthdSKYYQSGDHPR 764
Cdd:cd05095    171 KIADFGM---------SRNLYSGDYYR 188
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
711-749 8.31e-05

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: 45.57  E-value: 8.31e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1178431733  711 VESVHKMGFIHRDIKPDNILIDRDGH---IKLTDFGLCTGFR 749
Cdd:cd14128    109 IEYVHNKNFIHRDIKPDNFLMGIGRHcnkLFLIDFGLAKKYR 150
Pkinase_C pfam00433
Protein kinase C terminal domain;
925-975 8.88e-05

Protein kinase C terminal domain;


Pssm-ID: 459809 [Multi-domain]  Cd Length: 42  Bit Score: 40.65  E-value: 8.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1178431733  925 ITHPTDTSNFDPVDpdklwsddnEEENVNDTLNGWYKNGKHPEHAFYEFTF 975
Cdd:pfam00433    1 VKSETDTSNFDPEF---------TEEPPVLTPPDSSILSSNDQEEFRGFSY 42
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
906-977 9.98e-05

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 41.19  E-value: 9.98e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733   906 KTIDFSsDLRQQ--SASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTlngwykngkHPEHAFYEFTFRR 977
Cdd:smart00133    1 RGIDWD-KLENKeiEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDSPLSGG---------IQQEPFRGFSYVF 64
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
597-890 1.03e-04

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 45.12  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKTLGIGAFGEVCLARKVDTKALyATKTLRKKDVLLRNQVAhvkAERDILAEADNEWVVRLYYSFQDKDNLYFV 676
Cdd:cd05148      5 REEFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQDFQ---KEVQALKRLRHKHLISLFAVCSVGEPVYII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLL-------IRMgifpESLARF--YIAELTCAVESVHkmgFIHRDIKPDNILIDRDGHIKLTDFGLCtg 747
Cdd:cd05148     81 TELMEKGSLLAFLrspegqvLPV----ASLIDMacQVAEGMAYLEEQN---SIHRDLAARNILVGEDLVCKVADFGLA-- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  748 fRWTHDSKYYQSgdhprqdsmdfsnewgdpsscrcgDRLKPLErraarqhqrclahslvgtpnYIAPEVLLRTGYTQLCD 827
Cdd:cd05148    152 -RLIKEDVYLSS------------------------DKKIPYK--------------------WTAPEAASHGTFSTKSD 186
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178431733  828 WWSVGVILFEMLV-GQPPFLAQTPLETQMKVinwQTSLHIPPQAKLSPEASDLIIKL-CRGPEDR 890
Cdd:cd05148    187 VWSFGILLYEMFTyGQVPYPGMNNHEVYDQI---TAGYRMPCPAKCPQEIYKIMLECwAAEPEDR 248
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
604-838 1.16e-04

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 45.16  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLAR----KVDTKALYAT-------KTLRKKDVLLR--NQVAHVKAerDIlaEADNEWVvrlyysfqdk 670
Cdd:cd14144      1 RSVGKGRYGEVWKGKwrgeKVAVKIFFTTeeaswfrETEIYQTVLMRheNILGFIAA--DI--KGTGSWT---------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  671 dNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAeLTCAVESVH--------KMGFIHRDIKPDNILIDRDGHIKLTDF 742
Cdd:cd14144     67 -QLYLITDYHENGSLYDFLRGNTLDTQSMLKLAYS-AACGLAHLHteifgtqgKPAIAHRDIKSKNILVKKNGTCCIADL 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  743 GLCTGFrwthdskyyqsgdhprqdsMDFSNEWGDPSSCRcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLRT-- 820
Cdd:cd14144    145 GLAVKF-------------------ISETNEVDLPPNTR------------------------VGTKRYMAPEVLDESln 181
                          250       260
                   ....*....|....*....|...
gi 1178431733  821 -----GYTQlCDWWSVGVILFEM 838
Cdd:cd14144    182 rnhfdAYKM-ADMYSFGLVLWEI 203
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
669-838 1.50e-04

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 44.74  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  669 DKDN-----LYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAeLTCAVESVH--------KMGFIHRDIKPDNILIDRDG 735
Cdd:cd14143     59 NKDNgtwtqLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALS-IASGLAHLHmeivgtqgKPAIAHRDLKSKNILVKKNG 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  736 HIKLTDFGLCTgfrwTHDSKyyqsgdhprQDSMDFsnewgdPSSCRcgdrlkplerraarqhqrclahslVGTPNYIAPE 815
Cdd:cd14143    138 TCCIADLGLAV----RHDSA---------TDTIDI------APNHR------------------------VGTKRYMAPE 174
                          170       180
                   ....*....|....*....|....*....
gi 1178431733  816 VLLRTGYTQL------CDWWSVGVILFEM 838
Cdd:cd14143    175 VLDDTINMKHfesfkrADIYALGLVFWEI 203
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
676-745 1.52e-04

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 44.41  E-value: 1.52e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  676 VMDYIPGgdmMSL-----LIRMGIFPESLARfyiaeltCAVESVHKM----GFIHRDIKPDNILIDRDGHIKLTDFGLC 745
Cdd:cd05121    149 VMEYIDG---VKLtdleaLRAAGIDRKELAR-------RLVDAYLKQifedGFFHADPHPGNILVLPDGRIALLDFGMV 217
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
711-758 1.55e-04

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: 44.79  E-value: 1.55e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1178431733  711 VESVHKMGFIHRDIKPDNILIDRDGH-----IKLTDFGLCTGFRwthDSKYYQ 758
Cdd:cd14127    109 VQTIHEKNLIYRDIKPDNFLIGRPGTknanvIHVVDFGMAKQYR---DPKTKQ 158
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
695-867 1.82e-04

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


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 44.86  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  695 FPESLARFYIAELTC----AVESVHKMGFIHRDIKPDNILIDRDGHIKLTDF-GLCTGFRWTHDSKYYQsgDHPrqdsmD 769
Cdd:cd08226     94 FPEGMNEALIGNILYgaikALNYLHQNGCIHRSVKASHILISGDGLVSLSGLsHLYSMVTNGQRSKVVY--DFP-----Q 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  770 FSNEwgdpsscrcgdrLKPlerraarqhqrclahslvgtpnYIAPEVLLR--TGYTQLCDWWSVGVILFEMLVGQPPFla 847
Cdd:cd08226    167 FSTS------------VLP----------------------WLSPELLRQdlHGYNVKSDIYSVGITACELARGQVPF-- 210
                          170       180
                   ....*....|....*....|
gi 1178431733  848 QTPLETQMKVINWQTSLHIP 867
Cdd:cd08226    211 QDMRRTQMLLQKLKGPPYSP 230
PRK14879 PRK14879
Kae1-associated kinase Bud32;
667-744 2.09e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 43.74  E-value: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  667 FQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLAR---FYIAELtcavesvHKMGFIHRDIKPDNILIdRDGHIKLTDFG 743
Cdd:PRK14879    68 FVDPENFIIVMEYIEGEPLKDLINSNGMEELELSReigRLVGKL-------HSAGIIHGDLTTSNMIL-SGGKIYLIDFG 139

                   .
gi 1178431733  744 L 744
Cdd:PRK14879   140 L 140
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
604-853 2.45e-04

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: 43.81  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVCLARKVDTKALyATKTLR----KKDVLLRnqvahvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 679
Cdd:cd05034      1 KKLGAGQFGEVWMGVWNGTTKV-AVKTLKpgtmSPEAFLQ--------EAQIMKKLRHDKLVQLYAVCSDEEPIYIVTEL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  680 IPGGDMMSLL-------IRMGIFPESLARfyIAELTCAVESvhkMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTH 752
Cdd:cd05034     72 MSKGSLLDYLrtgegraLRLPQLIDMAAQ--IASGMAYLES---RNYIHRDLAARNILVGENNVCKVADFGLA---RLIE 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  753 DSKYyqsgdHPRQDSmDFSNEWgdpsscrcgdrlkplerraarqhqrclahslvgtpnyIAPEVLLRTGYTQLCDWWSVG 832
Cdd:cd05034    144 DDEY-----TAREGA-KFPIKW-------------------------------------TAPEAALYGRFTIKSDVWSFG 180
                          250       260
                   ....*....|....*....|..
gi 1178431733  833 VILFEMLV-GQPPFLAQTPLET 853
Cdd:cd05034    181 ILLYEIVTyGRVPYPGMTNREV 202
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
662-748 3.17e-04

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 43.79  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  662 RLYYSFQDKDNLYFvmdyipggDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTD 741
Cdd:PHA02882    98 RMYYRFILLEKLVE--------NTKEIFKRIKCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGYIID 169

                   ....*..
gi 1178431733  742 FGLCTGF 748
Cdd:PHA02882   170 YGIASHF 176
PRK10263 PRK10263
DNA translocase FtsK; Provisional
343-491 3.18e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.08  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  343 GHEIPTWQPNI---PVRSNSFNNPLGNRASHSANSQPSATTVTAITPAPIQQPV--KSMRVLKPELQTALAPTHPSWIPQ 417
Cdd:PRK10263   348 SVDVPPAQPTVawqPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVqpQQPYYAPAAEQPAQQPYYAPAPEQ 427
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178431733  418 PIQTVQPSPFPEGTASNVTVMPPVAEAPnYQgPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKS 491
Cdd:PRK10263   428 PAQQPYYAPAPEQPVAGNAWQAEEQQST-FA-PQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEET 499
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
683-745 3.63e-04

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


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 44.02  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  683 GDMMSLLIRMGIFPESL-------------ARFYIAELTCAVESVHKMGFIHRDIKPDNILI--DRDG--HIKLTDFGLC 745
Cdd:cd14018    110 GHNRTLFLVMKNYPCTLrqylwvntpsyrlARVMILQLLEGVDHLVRHGIAHRDLKSDNILLelDFDGcpWLVIADFGCC 189
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
604-744 3.72e-04

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


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 43.32  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  604 KTLGIGAFGEVC----LARKVDTKALyatktlrKKDVLLRNQVAhvkaERDILAEADNEWVVRLYYSFQdKDNLYFVMDY 679
Cdd:cd05083     12 EIIGEGEFGAVLqgeyMGQKVAVKNI-------KCDVTAQAFLE----ETAVMTKLQHKNLVRLLGVIL-HNGLYIVMEL 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178431733  680 IPGGDMMSLLIRMGIFPESLARFYIAELTCA--VESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 744
Cdd:cd05083     80 MSKGNLVNFLRSRGRALVPVIQLLQFSLDVAegMEYLESKKLVHRDLAARNILVSEDGVAKISDFGL 146
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
809-884 3.89e-04

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 43.25  E-value: 3.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178431733  809 PNYIAPEVLLRTGYT---QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPqaKLSPEASDLiIKLC 884
Cdd:cd14057    155 PAWMAPEALQKKPEDinrRSADMWSFAILLWELVTREVPFADLSNMEIGMKIALEGLRVTIPP--GISPHMCKL-MKIC 230
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
589-749 4.10e-04

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 44.40  E-value: 4.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  589 RLKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKK-------DVLL--RNQVAHVKAERDILA------ 653
Cdd:PLN03225   123 GLFRPSFKKDDFVLGKKLGEGAFGVVYKASLVNKQSKKEGKYVLKKateygavEIWMneRVRRACPNSCADFVYgflepv 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  654 ---EADNEWVV-------RLYYSFQDKDNLYFVMDYIPG--GDMMSLLIRMGIFPESLARfyiaELTCAVESVHKMGFIH 721
Cdd:PLN03225   203 sskKEDEYWLVwryegesTLADLMQSKEFPYNVEPYLLGkvQDLPKGLERENKIIQTIMR----QILFALDGLHSTGIVH 278
                          170       180
                   ....*....|....*....|....*....
gi 1178431733  722 RDIKPDNILID-RDGHIKLTDFGLCTGFR 749
Cdd:PLN03225   279 RDVKPQNIIFSeGSGSFKIIDLGAAADLR 307
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
368-453 4.33e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 44.03  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  368 ASHSANSQPSATTVTAITPAPIQQPVKSMRVLKPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPNY 447
Cdd:PRK14950   365 APQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKPKY 444

                   ....*.
gi 1178431733  448 QGPPPP 453
Cdd:PRK14950   445 TPPAPP 450
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
597-756 5.03e-04

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: 43.14  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  597 KSMFVKIKtLGIGAFGEVCLARKVDTKALyATKTLRKKDVllrNQVAHVKaERDILAEADNEWVVRLYySFQDKDNLYFV 676
Cdd:cd05071      9 ESLRLEVK-LGQGCFGEVWMGTWNGTTRV-AIKTLKPGTM---SPEAFLQ-EAQVMKKLRHEKLVQLY-AVVSEEPIYIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  677 MDYIPGGDMMSLLI----RMGIFPESLArfYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTH 752
Cdd:cd05071     82 TEYMSKGSLLDFLKgemgKYLRLPQLVD--MAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLA---RLIE 156

                   ....
gi 1178431733  753 DSKY 756
Cdd:cd05071    157 DNEY 160
PRK10263 PRK10263
DNA translocase FtsK; Provisional
362-550 1.21e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  362 NPLGNRASHSA--NSQPSATTVTAITPAPIQQPVKSMRVLKPElqTALAPTHPSWIPQP-IQTVQPS--PFPEGtasnvt 436
Cdd:PRK10263   308 DPLLNGAPITEpvAVAAAATTATQSWAAPVEPVTQTPPVASVD--VPPAQPTVAWQPVPgPQTGEPViaPAPEG------ 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  437 vMPPvaeAPNYQGPPPPYPKHLlhQNPsVPPYESISKPSKEDQPSLPKEDESEKSYENVDSgdkekkqitTSPITVRKNK 516
Cdd:PRK10263   380 -YPQ---QSQYAQPAVQYNEPL--QQP-VQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPY---------YAPAPEQPVA 443
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1178431733  517 KDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQ 550
Cdd:PRK10263   444 GNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPL 477
PRK10263 PRK10263
DNA translocase FtsK; Provisional
264-483 2.90e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.61  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  264 NRQPPPPY----PLTaaNGQS---PSALQTGGSAAPSSYTNGSIP----QSMMVPNRNSHNMELYNISVPGLQTNWPQSS 332
Cdd:PRK10263   297 NRATQPEYdeydPLL--NGAPitePVAVAAAATTATQSWAAPVEPvtqtPPVASVDVPPAQPTVAWQPVPGPQTGEPVIA 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  333 SAPAQSSPSSGHEIPTWQPNIPVRSNSFNNPLGNRASHSANSQPSATTVTAITPAPIQQPVKSMRVLKPELQTALAPTHP 412
Cdd:PRK10263   375 PAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQS 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178431733  413 SWIPQPIQTVQpSPFPEgtasnvtvmpPVAEAPNYQGPPPPYPKHLLHQNPSV-------PP------------------ 467
Cdd:PRK10263   455 TFAPQSTYQTE-QTYQQ----------PAAQEPLYQQPQPVEQQPVVEPEPVVeetkparPPlyyfeeveekrarereql 523
                          250
                   ....*....|....*....
gi 1178431733  468 ---YESISKPSKEDQPSLP 483
Cdd:PRK10263   524 aawYQPIPEPVKEPEPIKS 542
 
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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