NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564339933|ref|XP_006233834|]
View 

serine/threonine-protein kinase N3 isoform X1 [Rattus norvegicus]

Protein Classification

serine/threonine-protein kinase N( domain architecture ID 10184428)

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
553-877 0e+00

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


The actual alignment was detected with superfamily member cd05589:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 326  Bit Score: 611.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTST 712
Cdd:cd05589   81 MEYAAGGDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 713 FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSP 792
Cdd:cd05589  161 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 793 EKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLTPPVPRRSLSARQQAAFRD 872
Cdd:cd05589  241 ERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPKEPRPLTEEEQALFKD 320

                 ....*
gi 564339933 873 FDFVS 877
Cdd:cd05589  321 FDYVA 325
HR1 super family cl00087
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
95-168 2.16e-32

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


The actual alignment was detected with superfamily member cd11632:

Pssm-ID: 469609  Cd Length: 74  Bit Score: 120.03  E-value: 2.16e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933  95 PRAEQSRARLLEALHRQLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKISGLEASG 168
Cdd:cd11632    1 EWATDPRARRLEALKRQLHVELKVKQGAENMIQTYSSGTSKERKLLATAQQMLQDSRTKIELLRMQIVKLEQSG 74
HR1_PKN_1 cd11622
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
14-79 8.36e-29

First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that 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 cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the first HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


:

Pssm-ID: 212012  Cd Length: 66  Bit Score: 109.66  E-value: 8.36e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933  14 QRAPEDEKEMIRRAIQKELKIKEGMENMRRVATDRRHLGHVQQLLRASNRRLEQLHGELRELHAQV 79
Cdd:cd11622    1 QQKLEELKEQIRREIRKELKIKEGAENLRKATTDKKSLAHVESILKKSNRKLEDLHQELQELEAHI 66
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
326-413 1.24e-28

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


The actual alignment was detected with superfamily member cd08687:

Pssm-ID: 472691  Cd Length: 98  Bit Score: 110.17  E-value: 1.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 326 SEVLAVLKVDNRVVGQTGWGLVAEKSWDQAFSISLDRARELEIGVHWRDWRQLCGVAFLKLEEFLdnacHQLSLSLVPQG 405
Cdd:cd08687    9 SEVSAVLKLDNTVVGQTQWKPKSNQAWDQSFTLELERSRELEIAVYWRDWRSLCAVKFLKLEDER----HEVQLDMEPQL 84

                 ....*...
gi 564339933 406 RLFAQVTF 413
Cdd:cd08687   85 CLVAELTF 92
HR1 super family cl00087
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
168-226 9.03e-24

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


The actual alignment was detected with superfamily member cd11637:

Pssm-ID: 469609  Cd Length: 74  Bit Score: 95.31  E-value: 9.03e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 168 GSPEPGPDLLAEELQHRLRIEAAVAAGAKNVVKLLGGQRIQDRKALAEAQAQLQESSQK 226
Cdd:cd11637    1 GRPMSAPELRVEELRHHLRIEAAVAEGAKNVVKLLGGRRFQDRKILAEAQARLQESSQK 59
PHA03378 super family cl33729
EBNA-3B; Provisional
461-549 1.71e-04

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 461 PPCSSPSTVSPPKGCPSAAaceTSSSASPSNFRPVKTLPGEDMKPPPKPPRLYLQEPAPGTPCTKRPHMDPRTGVAPPLA 540
Cdd:PHA03378 716 RPAAATGRARPPAAAPGRA---RPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRG 792

                 ....*....
gi 564339933 541 ALSTRNPPQ 549
Cdd:PHA03378 793 APTPQPPPQ 801
 
Name Accession Description Interval E-value
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
553-877 0e+00

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: 611.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTST 712
Cdd:cd05589   81 MEYAAGGDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 713 FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSP 792
Cdd:cd05589  161 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 793 EKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLTPPVPRRSLSARQQAAFRD 872
Cdd:cd05589  241 ERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPKEPRPLTEEEQALFKD 320

                 ....*
gi 564339933 873 FDFVS 877
Cdd:cd05589  321 FDYVA 325
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
549-873 3.88e-77

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 253.97  E-value: 3.88e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSH 628
Cdd:PTZ00263  16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELS---HPFIVNMMCSFQDENR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFG 707
Cdd:PTZ00263  93 VYFLLEFVVGGELFTHLRKaGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK---VP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKL 787
Cdd:PTZ00263 170 DRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 788 LQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLtppvprRSLSARQQ 867
Cdd:PTZ00263 250 LQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPDSPVDRL------PPLTAAQQ 323

                 ....*.
gi 564339933 868 AAFRDF 873
Cdd:PTZ00263 324 AEFAGF 329
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
553-812 2.23e-76

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 249.37  E-value: 2.23e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFV 632
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLK---HPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   633 TEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRdlkldnllldAQGFLKIADFGLCKEgIGFGDRTS 711
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGrLSEDEARFYLRQILSALEYLHSKGIVHRdlkpenilldEDGHVKLADFGLARQ-LDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   712 TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVPCPHF---LSAQGLELIQKL 787
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPewdISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|....*
gi 564339933   788 LQKSPEKRLGagerdAEEIKVQPFF 812
Cdd:smart00220 235 LVKDPEKRLT-----AEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
558-812 3.03e-44

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 159.33  E-value: 3.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGrDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:pfam00069   6 KLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKK-KKDKNILREIKILK---KLNHPNIVRLYDAFEDKDNLYLVLEYVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  638 GGDLMMQIHED-VFPEPQACFYLACVVLGLqflhekriiyrdlkldnllldaqgflkiadfglckEGigfGDRTSTFCGT 716
Cdd:pfam00069  82 GGSLFDLLSEKgAFSEREAKFIMKQILEGL-----------------------------------ES---GSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHF---LSAQGLELIQKLLQKSPE 793
Cdd:pfam00069 124 PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLKKDPS 203
                         250
                  ....*....|....*....
gi 564339933  794 KRLGagerdAEEIKVQPFF 812
Cdd:pfam00069 204 KRLT-----ATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
546-795 2.18e-33

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 135.14  E-value: 2.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 546 NPPQLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQT 625
Cdd:COG0515    2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLN---HPNIVRVYDVGEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLPGGDL--MMQiHEDVFPEPQACFYLACVVLGLQFLHEKRIIYR---------DlkldnllldAQGFLKI 694
Cdd:COG0515   79 DGRPYLVMEYVEGESLadLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRdikpanillT---------PDGRVKL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLCKE-GIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCP 773
Cdd:COG0515  149 IDFGIARAlGGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPP 228
                        250       260
                 ....*....|....*....|....*.
gi 564339933 774 HFLSAQ---GLE-LIQKLLQKSPEKR 795
Cdd:COG0515  229 SELRPDlppALDaIVLRALAKDPEER 254
HR1_PKN3_2 cd11632
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
95-168 2.16e-32

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3; PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the second HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC.


Pssm-ID: 212022  Cd Length: 74  Bit Score: 120.03  E-value: 2.16e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933  95 PRAEQSRARLLEALHRQLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKISGLEASG 168
Cdd:cd11632    1 EWATDPRARRLEALKRQLHVELKVKQGAENMIQTYSSGTSKERKLLATAQQMLQDSRTKIELLRMQIVKLEQSG 74
HR1_PKN_1 cd11622
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
14-79 8.36e-29

First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that 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 cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the first HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212012  Cd Length: 66  Bit Score: 109.66  E-value: 8.36e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933  14 QRAPEDEKEMIRRAIQKELKIKEGMENMRRVATDRRHLGHVQQLLRASNRRLEQLHGELRELHAQV 79
Cdd:cd11622    1 QQKLEELKEQIRREIRKELKIKEGAENLRKATTDKKSLAHVESILKKSNRKLEDLHQELQELEAHI 66
C2_PKN-like cd08687
C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine ...
326-413 1.24e-28

C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine kinase. It is a member of the protein kinase C (PKC) superfamily, but lacks a C1 domain. There are at least 3 different isoforms of PKN (PRK1/PKNalpha/PAK1; PKNbeta, and PRK2/PAK2/PKNgamma). The C-terminal region contains the Ser/Thr type protein kinase domain, while the N-terminal region of PKN contains three antiparallel coiled-coil (ACC) finger domains which are relatively rich in charged residues and contain a leucine zipper-like sequence. These domains binds to the small GTPase RhoA. Following these domains is a C2-like domain. Its C-terminal part functions as an auto-inhibitory region. PKNs are not activated by classical PKC activators such as diacylglycerol, phorbol ester or Ca2+, but instead are activated by phospholipids and unsaturated fatty acids. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176069  Cd Length: 98  Bit Score: 110.17  E-value: 1.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 326 SEVLAVLKVDNRVVGQTGWGLVAEKSWDQAFSISLDRARELEIGVHWRDWRQLCGVAFLKLEEFLdnacHQLSLSLVPQG 405
Cdd:cd08687    9 SEVSAVLKLDNTVVGQTQWKPKSNQAWDQSFTLELERSRELEIAVYWRDWRSLCAVKFLKLEDER----HEVQLDMEPQL 84

                 ....*...
gi 564339933 406 RLFAQVTF 413
Cdd:cd08687   85 CLVAELTF 92
HR1_PKN3_3 cd11637
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
168-226 9.03e-24

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3; PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the third HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC.


Pssm-ID: 212027  Cd Length: 74  Bit Score: 95.31  E-value: 9.03e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 168 GSPEPGPDLLAEELQHRLRIEAAVAAGAKNVVKLLGGQRIQDRKALAEAQAQLQESSQK 226
Cdd:cd11637    1 GRPMSAPELRVEELRHHLRIEAAVAEGAKNVVKLLGGRRFQDRKILAEAQARLQESSQK 59
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
105-167 2.98e-14

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 67.93  E-value: 2.98e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933  105 LEALHRQLEVELKVKQGAENMIHTCASgtPKERKLLAAAQQMLKDSQLKVALLRMKISGLEAS 167
Cdd:pfam02185   2 LQELRKKIEVEKKIKEGAENMLRLLQA--TKDRKVLAEAESELRESNRKIQLLREQLRELQAR 62
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
19-74 6.83e-14

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 66.83  E-value: 6.83e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933    19 DEKEMIRRAIQKELKIKEGMENMRRVAT-DRRHLGHVQQLLRASNRRLEQLHGELRE 74
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSnDRKVLSEAQSMLRESNQKLDLLKEELEK 57
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
103-161 1.98e-13

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 65.29  E-value: 1.98e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933   103 RLLEALHRQLEVELKVKQGAENMIHTcasgTPKERKLLAAAQQMLKDSQLKVALLRMKI 161
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKL----TSNDRKVLSEAQSMLRESNQKLDLLKEEL 55
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
22-80 2.65e-13

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 65.23  E-value: 2.65e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933   22 EMIRRAIQKELKIKEGMENMRRV---ATDRRHLGHVQQLLRASNRRLEQLHGELRELHAQVL 80
Cdd:pfam02185   3 QELRKKIEVEKKIKEGAENMLRLlqaTKDRKVLAEAESELRESNRKIQLLREQLRELQARHL 64
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
179-226 1.59e-10

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 57.53  E-value: 1.59e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 564339933  179 EELQHRLRIEAAVAAGAKNVVKLLggQRIQDRKALAEAQAQLQESSQK 226
Cdd:pfam02185   3 QELRKKIEVEKKIKEGAENMLRLL--QATKDRKVLAEAESELRESNRK 48
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
179-227 2.28e-08

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 51.04  E-value: 2.28e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564339933   179 EELQHRLRIEAAVAAGAKNVVKLLGgqriQDRKALAEAQAQLQESSQKL 227
Cdd:smart00742   4 EDLRRKIEKELKVKEGAENMRKLTS----NDRKVLSEAQSMLRESNQKL 48
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
632-795 6.84e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 49.79  E-value: 6.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRdlkldnllldaQGFLKIADFGLCkegigfgdR- 709
Cdd:NF033483  85 VMEYVDGRTLKDYIREHgPLSPEEAVEIMIQILSALEHAHRNGIVHRdikpqnilitkDGRVKVTDFGIA--------Ra 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 --------TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDT----------EDEVFECIVNADVP 771
Cdd:NF033483 157 lssttmtqTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSpvsvaykhvqEDPPPPSELNPGIP 236
                        170       180
                 ....*....|....*....|....*
gi 564339933 772 cphflsaQGLE-LIQKLLQKSPEKR 795
Cdd:NF033483 237 -------QSLDaVVLKATAKDPDDR 254
PHA03378 PHA03378
EBNA-3B; Provisional
461-549 1.71e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 461 PPCSSPSTVSPPKGCPSAAaceTSSSASPSNFRPVKTLPGEDMKPPPKPPRLYLQEPAPGTPCTKRPHMDPRTGVAPPLA 540
Cdd:PHA03378 716 RPAAATGRARPPAAAPGRA---RPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRG 792

                 ....*....
gi 564339933 541 ALSTRNPPQ 549
Cdd:PHA03378 793 APTPQPPPQ 801
 
Name Accession Description Interval E-value
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
553-877 0e+00

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: 611.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTST 712
Cdd:cd05589   81 MEYAAGGDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 713 FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSP 792
Cdd:cd05589  161 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 793 EKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLTPPVPRRSLSARQQAAFRD 872
Cdd:cd05589  241 ERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPKEPRPLTEEEQALFKD 320

                 ....*
gi 564339933 873 FDFVS 877
Cdd:cd05589  321 FDYVA 325
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
557-876 1.65e-140

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: 419.70  E-value: 1.65e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 557 AVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRtgHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANR--HPFLTGLHACFQTEDRLYFVMEYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCG 715
Cdd:cd05570   79 NGGDLMFHIQRArRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05570  159 TPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 796 LGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSlPPTLTPPVPRRSLSARQQAAFRDFDF 875
Cdd:cd05570  239 LGCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTS-ESPRLTPVDSDLLTNIDQEEFRGFSY 317

                 .
gi 564339933 876 V 876
Cdd:cd05570  318 I 318
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
558-878 4.77e-108

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: 335.48  E-value: 4.77e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd05571    2 VLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQ---NTRHPFLTSLKYSFQTNDRLCFVMEYVN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd05571   79 GGELFFHLsRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd05571  159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 797 GAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLT--PPVPRRSLSARQQAAFRDFD 874
Cdd:cd05571  239 GGGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTppDRGDLLGLEEEERPHFEQFS 318

                 ....
gi 564339933 875 FVSK 878
Cdd:cd05571  319 YSAS 322
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
557-877 1.98e-104

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: 325.88  E-value: 1.98e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 557 AVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVgrTGHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALA--SQHPFLTHLFCTFQTESHLFFVMEYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCG 715
Cdd:cd05592   79 NGGDLMFHIQQSgRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05592  159 TPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 796 LGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTsLPPTLTPPVPRRSLSARQQAAFRDFDF 875
Cdd:cd05592  239 LGVPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFT-MEKPVLTPVDKKLLASMDQEQFKGFSF 317

                 ..
gi 564339933 876 VS 877
Cdd:cd05592  318 TN 319
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
556-876 1.97e-102

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: 320.88  E-value: 1.97e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTghPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd05587    1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKP--PFLTQLHSCFQTMDRLYFVMEY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFC 714
Cdd:cd05587   79 VNGGDLMYHIqQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEK 794
Cdd:cd05587  159 GTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 795 RLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSlPPTLTPPVPRRSLSARQQAAFRDFD 874
Cdd:cd05587  239 RLGCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTK-EPPVLTPTDKLVIMNIDQSEFEGFS 317

                 ..
gi 564339933 875 FV 876
Cdd:cd05587  318 FV 319
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
559-812 1.08e-97

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: 305.60  E-value: 1.08e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILE---RVNHPFIVKLHYAFQTEEKLYLVLDYVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTP 717
Cdd:cd05123   78 GELFSHLsKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 718 EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKRLG 797
Cdd:cd05123  158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLG 237
                        250
                 ....*....|....*
gi 564339933 798 AGerDAEEIKVQPFF 812
Cdd:cd05123  238 SG--GAEEIKAHPFF 250
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
558-848 1.59e-96

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: 305.40  E-value: 1.59e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetVGRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd05575    2 VIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVL--LKNVKHPFLVGLHYSFQTKDKLYFVLDYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd05575   80 GGELFFHLQrERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd05575  160 PEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339933 797 GAGeRDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTS 848
Cdd:cd05575  240 GSG-NDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTR 290
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
558-876 4.51e-95

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: 301.33  E-value: 4.51e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRtgHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd05591    2 VLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAK--HPFLTALHSCFQTKDRLFFVMEYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd05591   80 GGDLMFQIQRArKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd05591  160 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 797 G--AGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSlPPTLTPPVPRRSLSARQQAAFRDFD 874
Cdd:cd05591  240 GcvASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTK-EEPVLTPVDPAVIKQINQEEFRGFS 318

                 ..
gi 564339933 875 FV 876
Cdd:cd05591  319 FV 320
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
558-875 3.45e-91

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: 291.52  E-value: 3.45e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETvgrTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd05595    2 LLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQN---TRHPFLTALKYAFQTHDRLCFVMEYAN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd05595   79 GGELFFHLsRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd05595  159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 797 GAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLTPPVPRRSLSAR---QQAAFRDF 873
Cdd:cd05595  239 GGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLDLLesdQRTHFPQF 318

                 ..
gi 564339933 874 DF 875
Cdd:cd05595  319 SY 320
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
551-843 3.57e-91

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: 289.86  E-value: 3.57e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILS---EVRHPFIVNLLGSFQDDRNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFGDR 709
Cdd:cd05580   78 MVMEYVPGGELFSLLRrSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKR---VKDR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd05580  155 TYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLV 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 790 KSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05580  235 VDLTKRLGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFD 288
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
558-877 1.46e-90

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: 289.50  E-value: 1.46e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILeTVGRTgHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd05590    2 VLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRIL-SLARN-HPFLTQLYCCFQTPDRLFFVMEFVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd05590   80 GGDLMFHIQKSRrFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd05590  160 PDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 797 GAGERDAEE-IKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSlPPTLTPPVPRRSLSARQQAAFRDFDF 875
Cdd:cd05590  240 GSLTLGGEEaILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIK-EDPVLTPIEESLLPMINQDEFRNFSY 318

                 ..
gi 564339933 876 VS 877
Cdd:cd05590  319 TA 320
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
558-877 2.70e-90

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: 288.77  E-value: 2.70e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRtgHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd05620    2 VLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAWE--NPFLTHLYCTFQTKEHLFFVMEFLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIgFGD-RTSTFCG 715
Cdd:cd05620   80 GGDLMFHIQDKgRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENV-FGDnRASTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIvNADVP-CPHFLSAQGLELIQKLLQKSPEK 794
Cdd:cd05620  159 TPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI-RVDTPhYPRWITKESKDILEKLFERDPTR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 795 RLGAgerdAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSlPPTLTPPVPRRSLSARQQAAFRDFD 874
Cdd:cd05620  238 RLGV----VGNIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLS-EKPRLSYSDKNLIDSMDQSAFAGFS 312

                 ...
gi 564339933 875 FVS 877
Cdd:cd05620  313 FIN 315
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
552-847 3.62e-90

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: 288.82  E-value: 3.62e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTghPFLLSLLACIQTSSHACF 631
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKP--PFLTQLHSCFQTMDRLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRT 710
Cdd:cd05616   79 VMEYVNGGDLMYHIQQvGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd05616  159 KTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTK 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 791 SPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGpADLRYFEGEFT 847
Cdd:cd05616  239 HPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACG-RNAENFDRFFT 294
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
556-847 5.73e-90

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: 288.15  E-value: 5.73e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQY---KGTGKYYAIKALKKQEVLgRDEIDSLY--CEKRILETVGrtgHPFLLSLLACIQTSSHAC 630
Cdd:cd05584    1 LKVLGKGGYGKVFQVRKttgSDKGKIFAMKVLKKASIV-RNQKDTAHtkAERNILEAVK---HPFIVDLHYAFQTGGKLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDR 709
Cdd:cd05584   77 LILEYLSGGELFMHLErEGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd05584  157 THTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLK 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 790 KSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFT 847
Cdd:cd05584  237 RNVSSRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFT 294
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
550-877 3.20e-89

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: 286.43  E-value: 3.20e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRtgHPFLLSLLACIQTSSHA 629
Cdd:cd05619    4 IEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWE--HPFLTHLFCTFQTKENL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIgFGD 708
Cdd:cd05619   82 FFVMEYLNGGDLMFHIQScHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENM-LGD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 -RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIvNADVPC-PHFLSAQGLELIQK 786
Cdd:cd05619  161 aKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI-RMDNPFyPRWLEKEAKDILVK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 787 LLQKSPEKRLGAgerdAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSlPPTLTPPVPRRSLSARQ 866
Cdd:cd05619  240 LFVREPERRLGV----RGDIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEFLN-EKPRLSFADRALINSMD 314
                        330
                 ....*....|.
gi 564339933 867 QAAFRDFDFVS 877
Cdd:cd05619  315 QNMFRNFSFVN 325
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
549-881 2.56e-86

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: 279.19  E-value: 2.56e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTghPFLLSLLACIQTSSH 628
Cdd:cd05615    8 RLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKP--PFLTQLHSCFQTVDR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFG 707
Cdd:cd05615   86 LYFVMEYVNGGDLMYHIQQvGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKL 787
Cdd:cd05615  166 VTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 788 LQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYfeGEFTSLPPTLTPPVPRRSLSARQQ 867
Cdd:cd05615  246 MTKHPAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGKGAENF--DKFFTRGQPVLTPPDQLVIANIDQ 323
                        330
                 ....*....|....
gi 564339933 868 AAFRDFDFVSKRFL 881
Cdd:cd05615  324 ADFEGFSYVNPQFV 337
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
550-848 2.29e-85

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: 276.96  E-value: 2.29e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETvgrTGHPFLLSLLACIQTSSHA 629
Cdd:cd05593   14 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKN---TRHPFLTSLKYSFQTKDRL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd05593   91 CFVMEYVNGGELFFHLsRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLL 788
Cdd:cd05593  171 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLL 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 789 QKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTS 848
Cdd:cd05593  251 IKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTA 310
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
558-848 2.95e-83

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: 270.45  E-value: 2.95e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVgrTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd05588    2 VIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETA--SNHPFLVGLHSCFQTESRLFFVIEFVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLM--MQIHEDVfPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCG 715
Cdd:cd05588   80 GGDLMfhMQRQRRL-PEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF---------PGDTEDEVFECIVNADVPCPHFLSAQGLELIQK 786
Cdd:cd05588  159 TPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnpDQNTEDYLFQVILEKPIRIPRSLSVKAASVLKG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 787 LLQKSPEKRLG----AGERDaeeIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTS 848
Cdd:cd05588  239 FLNKNPAERLGchpqTGFAD---IQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTN 301
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
545-848 8.87e-83

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: 270.36  E-value: 8.87e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 545 RNPPQLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETvgrTGHPFLLSLLACIQ 624
Cdd:cd05594   19 KHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQN---SRHPFLTALKYSFQ 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHACFVTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLH-EKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE 702
Cdd:cd05594   96 THDRLCFVMEYANGGELFFHLSRErVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKE 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 703 GIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLE 782
Cdd:cd05594  176 GIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKS 255
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 783 LIQKLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTS 848
Cdd:cd05594  256 LLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTA 321
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
551-843 1.65e-80

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: 261.57  E-value: 1.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHAC 630
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAIN---FPFLVKLEYSFKDNSNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDlMMQIHEDV--FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGfgd 708
Cdd:cd14209   78 MVMEYVPGGE-MFSHLRRIgrFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKG--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLL 788
Cdd:cd14209  154 RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLL 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 789 QKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFE 843
Cdd:cd14209  234 QVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFD 288
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
556-847 3.51e-78

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: 256.81  E-value: 3.51e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetVGRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVL--LKNVKHPFLVGLHYSFQTTDKLYFVLDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFC 714
Cdd:cd05604   79 VNGGELFFHLQrERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEK 794
Cdd:cd05604  159 GTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564339933 795 RLGAGErDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFT 847
Cdd:cd05604  239 RLGAKE-DFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFT 290
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
549-873 3.88e-77

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 253.97  E-value: 3.88e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSH 628
Cdd:PTZ00263  16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELS---HPFIVNMMCSFQDENR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFG 707
Cdd:PTZ00263  93 VYFLLEFVVGGELFTHLRKaGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK---VP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKL 787
Cdd:PTZ00263 170 DRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 788 LQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLtppvprRSLSARQQ 867
Cdd:PTZ00263 250 LQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPDSPVDRL------PPLTAAQQ 323

                 ....*.
gi 564339933 868 AAFRDF 873
Cdd:PTZ00263 324 AEFAGF 329
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
557-847 3.99e-77

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: 253.74  E-value: 3.99e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 557 AVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetVGRTGHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVL--LKNLKHPFLVGLHYSFQTSEKLYFVLDYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCG 715
Cdd:cd05603   79 NGGELFFHLQrERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05603  159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRR 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339933 796 LGAgERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFT 847
Cdd:cd05603  239 LGA-KADFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFT 289
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
558-876 6.12e-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: 253.09  E-value: 6.12e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQY---KGTGKYYAIKALKKQEVLGRDEIDSlYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd05582    2 VLGQGSFGKVFLVRKitgPDAGTLYAMKVLKKATLKVRDRVRT-KMERDILADVN---HPFIVKLHYAFQTEGKLYLILD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd05582   78 FLRGGDLFTRLSKEVmFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPE 793
Cdd:cd05582  158 CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 794 KRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLTPPVprrSLSARQQAAFRDF 873
Cdd:cd05582  238 NRLGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGV---PPSANAHQLFRGF 314

                 ...
gi 564339933 874 DFV 876
Cdd:cd05582  315 SFV 317
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
551-838 6.64e-77

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: 252.93  E-value: 6.64e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVgrtGHPFLLSLLACIQTSSHAC 630
Cdd:cd05574    1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATL---DHPFLPTLYASFQTSTHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDL--MMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK------ 701
Cdd:cd05574   78 FVMDYCPGGELfrLLQKQpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvtp 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 -------------------------EGIGFgdRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGD 756
Cdd:cd05574  158 ppvrkslrkgsrrssvksieketfvAEPSA--RSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 757 TEDEVFECIVNADVPCP--HFLSAQGLELIQKLLQKSPEKRLGAgERDAEEIKVQPFFRTTNWQalLARTVQPPFVPTLC 834
Cdd:cd05574  236 NRDETFSNILKKELTFPesPPVSSEAKDLIRKLLVKDPSKRLGS-KRGASEIKRHPFFRGVNWA--LIRNMTPPIIPRPD 312

                 ....
gi 564339933 835 GPAD 838
Cdd:cd05574  313 DPID 316
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
553-812 2.23e-76

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 249.37  E-value: 2.23e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFV 632
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLK---HPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   633 TEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRdlkldnllldAQGFLKIADFGLCKEgIGFGDRTS 711
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGrLSEDEARFYLRQILSALEYLHSKGIVHRdlkpenilldEDGHVKLADFGLARQ-LDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   712 TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVPCPHF---LSAQGLELIQKL 787
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPewdISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|....*
gi 564339933   788 LQKSPEKRLGagerdAEEIKVQPFF 812
Cdd:smart00220 235 LVKDPEKRLT-----AEEALQHPFF 254
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
552-847 2.44e-74

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: 246.85  E-value: 2.44e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd05602    8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVL--LKNVKHPFLVGLHFSFQTTDKLYF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRT 710
Cdd:cd05602   86 VLDYINGGELFYHLQrERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd05602  166 STFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQK 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 791 SPEKRLGAGErDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFT 847
Cdd:cd05602  246 DRTKRLGAKD-DFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFT 301
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
550-883 2.76e-73

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: 244.55  E-value: 2.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVgrTGHPFLLSLLACIQTSSHA 629
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQA--SSNPFLVGLHSCFQTTSRL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd05617   92 FLVIEYVNGGDLMFHMQrQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF------PG-DTEDEVFECIVNADVPCPHFLSAQGL 781
Cdd:cd05617  172 TTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnPDmNTEDYLFQVILEKPIRIPRFLSVKAS 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 782 ELIQKLLQKSPEKRLGAGERDA-EEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSlPPTLTPPVPRR 860
Cdd:cd05617  252 HVLKGFLNKDPKERLGCQPQTGfSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTS-EPVQLTPDDED 330
                        330       340
                 ....*....|....*....|...
gi 564339933 861 SLSARQQAAFRDFDFVSKRFLES 883
Cdd:cd05617  331 VIKRIDQSEFEGFEYINPLLLST 353
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
550-848 6.76e-73

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: 243.79  E-value: 6.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVgrTGHPFLLSLLACIQTSSHA 629
Cdd:cd05618   19 LQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQA--SNHPFLVGLHSCFQTESRL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd05618   97 FFVIEYVNGGDLMFHMQrQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF---------PGDTEDEVFECIVNADVPCPHFLSAQ 779
Cdd:cd05618  177 TTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnpDQNTEDYLFQVILEKQIRIPRSLSVK 256
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 780 GLELIQKLLQKSPEKRLGAGERDA-EEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTS 848
Cdd:cd05618  257 AASVLKSFLNKDPKERLGCHPQTGfADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTN 326
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
561-817 1.82e-69

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 231.34  E-value: 1.82e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 561 RGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPGGD 640
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILS---QAQNPFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 641 LM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI--------------- 704
Cdd:cd05579   80 LYsLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLvrrqiklsiqkksng 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHF--LSAQGLE 782
Cdd:cd05579  160 APEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDpeVSDEAKD 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564339933 783 LIQKLLQKSPEKRLGAgeRDAEEIKVQPFFRTTNW 817
Cdd:cd05579  240 LISKLLTPDPEKRLGA--KGIEEIKNHPFFKGIDW 272
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
559-819 8.75e-69

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: 229.03  E-value: 8.75e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECN---SPFIVKLYRTFKDKKYLYMLMEYCLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTSTFCGTP 717
Cdd:cd05572   78 GELWTILRDrGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK-LGSGRKTWTFCGTP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 718 EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED--EVFECIV--NADVPCPHFLSAQGLELIQKLLQKSPE 793
Cdd:cd05572  157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILkgIDKIEFPKYIDKNAKNLIKQLLRRNPE 236
                        250       260
                 ....*....|....*....|....*.
gi 564339933 794 KRLGAGERDAEEIKVQPFFRTTNWQA 819
Cdd:cd05572  237 ERLGYLKGGIRDIKKHKWFEGFDWEG 262
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
559-875 9.07e-68

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: 228.61  E-value: 9.07e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTP 717
Cdd:cd05586   81 GELFWHLqKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGTT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 718 EFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPH-FLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05586  161 EYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNPKHR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 796 LGAgERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLTPPVPRRS-----------LSA 864
Cdd:cd05586  241 LGA-HDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFTNASLLNANIVPWAQrpglpgatstpLSP 319
                        330
                 ....*....|.
gi 564339933 865 RQQAAFRDFDF 875
Cdd:cd05586  320 SVQANFRGFTF 330
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
551-843 1.95e-67

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: 226.55  E-value: 1.95e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHAC 630
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVS---HPFIIRLFWTEHDQRFLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIgfgDR 709
Cdd:cd05612   78 MLMEYVPGGELFSYLRNSgRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR---DR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd05612  155 TWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLV 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 790 KSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05612  235 VDRTRRLGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFD 288
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
552-875 1.71e-66

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: 226.01  E-value: 1.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd05573    2 DFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDIL---ADADSPWIVRLHYAFQDEDHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRT 710
Cdd:cd05573   79 VMEYMPGGDLMnLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGDRE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STF-----------------------------CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEV 761
Cdd:cd05573  159 SYLndsvntlfqdnvlarrrphkqrrvraysaVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVET 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 762 FECIVNADV----PCPHFLSAQGLELIQKLLqKSPEKRLGAgerdAEEIKVQPFFRTTNWQALLARTvqPPFVPTLCGPA 837
Cdd:cd05573  239 YSKIMNWKEslvfPDDPDVSPEAIDLIRRLL-CDPEDRLGS----AEEIKAHPFFKGIDWENLRESP--PPFVPELSSPT 311
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 564339933 838 DLRYFEgEFT-SLPPTLTPPVPRRSLSARQQAAFRDFDF 875
Cdd:cd05573  312 DTSNFD-DFEdDLLLSEYLSNGSPLLGKGKQLAFVGFTF 349
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
552-848 6.85e-66

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: 223.64  E-value: 6.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKG---TGKYYAIKALKKQEVLGRDE-IDSLYCEKRILETVGRTghPFLLSLLACIQTSS 627
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAALVQKAKtVEHTRTERNVLEHVRQS--PFLVTLHYAFQTDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGF 706
Cdd:cd05614   79 KLHLILDYVSGGELFTHLYQrDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 -GDRTSTFCGTPEFLAPEVL-TQEAYTRAVDWWGLGVLLYEMLVGECPFP----GDTEDEVFECIVNADVPCPHFLSAQG 780
Cdd:cd05614  159 eKERTYSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFTlegeKNTQSEVSRRILKCDPPFPSFIGPVA 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 781 LELIQKLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTS 848
Cdd:cd05614  239 RDLLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTN 306
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
558-848 9.69e-66

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: 222.83  E-value: 9.69e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVL---AQVDCPFIVPLKFSFQSPEKLYLVLAFIN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd05585   78 GGELFHHLQrEGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd05585  158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRL 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339933 797 GAGerDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTS 848
Cdd:cd05585  238 GYN--GAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTR 287
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
551-846 2.99e-64

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: 219.02  E-value: 2.99e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHAC 630
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEAD---NPWVVKLYYSFQDEENLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKegiGFgDR 709
Cdd:cd05599   78 LIMEFLPGGDMMtLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCT---GL-KK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 T----STfCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVN--------ADVPcphfLS 777
Cdd:cd05599  154 ShlayST-VGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNwretlvfpPEVP----IS 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 778 AQGLELIQKLLQkSPEKRLGAgeRDAEEIKVQPFFRTTNWQALlaRTVQPPFVPTLCGPADLRYFEgEF 846
Cdd:cd05599  229 PEAKDLIERLLC-DAEHRLGA--NGVEEIKSHPFFKGVDWDHI--RERPAPILPEVKSILDTSNFD-EF 291
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
552-880 1.74e-61

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: 211.79  E-value: 1.74e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd05598    2 MFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDIL---AEADNEWVVKLYYSFQDKENLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIGFGDRT 710
Cdd:cd05598   79 VMDYIPGGDLMsLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWTHDS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFC-----GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVN----ADVPCPHFLSAQGL 781
Cdd:cd05598  158 KYYLahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINwrttLKIPHEANLSPEAK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 782 ELIQKLLqKSPEKRLgaGERDAEEIKVQPFFRTTNWQALlaRTVQPPFVPTLCGPADLRYF---EGEFTSLPPTLTPPVP 858
Cdd:cd05598  238 DLILRLC-CDAEDRL--GRNGADEIKAHPFFAGIDWEKL--RKQKAPYIPTIRHPTDTSNFdpvDPEKLRSSDEEPTTPN 312
                        330       340
                 ....*....|....*....|..
gi 564339933 859 RRSLSARQQAAFRDFDFvsKRF 880
Cdd:cd05598  313 DPDNGKHPEHAFYEFTF--RRF 332
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
558-813 1.43e-60

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: 206.86  E-value: 1.43e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKG---TGKYYAIKALKKQEVLGRDEI-DSLYCEKRILETVGRTghPFLLSLLACIQTSSHACFVT 633
Cdd:cd05583    1 VLGTGAYGKVFLVRKVGghdAGKLYAMKVLKKATIVQKAKTaEHTMTERQVLEAVRQS--PFLVTLHYAFQTDAKLHLIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI-GFGDRTS 711
Cdd:cd05583   79 DYVNGGELFTHLYQrEHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLpGENDRAY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVLT--QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED----EVFECIVNADVPCPHFLSAQGLELIQ 785
Cdd:cd05583  159 SFCGTIEYMAPEVVRggSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERnsqsEISKRILKSHPPIPKTFSAEAKDFIL 238
                        250       260
                 ....*....|....*....|....*...
gi 564339933 786 KLLQKSPEKRLGAGERDAEEIKVQPFFR 813
Cdd:cd05583  239 KLLEKDPKKRLGAGPRGAHEIKEHPFFK 266
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
552-831 5.08e-59

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: 203.19  E-value: 5.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRclaVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd05608    5 DFR---VLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRIL---AKVHSRFIVSLAYAFQTKTDLCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIH---EDV--FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGF 706
Cdd:cd05608   79 VMTIMNGGDLRYHIYnvdEENpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE----DEVFECIVNADVPCPHFLSAQGLE 782
Cdd:cd05608  159 QTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEkvenKELKQRILNDSVTYSEKFSPASKS 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564339933 783 LIQKLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05608  239 ICEALLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
552-831 4.44e-58

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: 200.61  E-value: 4.44e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQY---KGTGKYYAIKALKKQEVLGRDEI-DSLYCEKRILETVGRTghPFLLSLLACIQTSS 627
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRKvsgHDAGKLYAMKVLKKATIVQKAKTaEHTRTERQVLEHIRQS--PFLVTLHYAFQTDT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIG- 705
Cdd:cd05613   79 KLHLILDYINGGELFTHLSQRErFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLd 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCGTPEFLAPEVLT--QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED----EVFECIVNADVPCPHFLSAQ 779
Cdd:cd05613  159 ENERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEMSAL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339933 780 GLELIQKLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05613  239 AKDIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
559-831 9.59e-58

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: 199.29  E-value: 9.59e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRtghPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSS---PFIVSLAYAFETKDKLCLVLTLMNG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIH---EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTSTFCG 715
Cdd:cd05577   78 GDLKYHIYnvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEFLAPEVLTQE-AYTRAVDWWGLGVLLYEMLVGECPFPGDTE----DEVFECIVNADVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd05577  157 THGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKEkvdkEELKRRTLEMAVEYPDSFSPEARSLCEGLLQK 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564339933 791 SPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05577  237 DPERRLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
551-812 6.63e-57

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: 197.05  E-value: 6.63e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLS---RLAHPGIVKLYYTFQDESKLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK-------- 701
Cdd:cd05581   78 FVLEYAPNGDLLEYIRKYGsLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKvlgpdssp 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 ---------EGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPC 772
Cdd:cd05581  158 estkgdadsQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEF 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564339933 773 PHFLSAQGLELIQKLLQKSPEKRLGAGE-RDAEEIKVQPFF 812
Cdd:cd05581  238 PENFPPDAKDLIQKLLVLDPSKRLGVNEnGGYDELKAHPFF 278
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
552-843 7.94e-57

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: 198.69  E-value: 7.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIdSLYCEKRilETVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd05601    2 DFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEV-SFFEEER--DIMAKANSPWITKLQYAFQDSENLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDR 709
Cdd:cd05601   79 VMEYHPGGDLLslLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTF-CGTPEFLAPEVLT------QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADvPCPHF-----LS 777
Cdd:cd05601  159 TSKMpVGTPDYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFK-KFLKFpedpkVS 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 778 AQGLELIQKLLQkSPEKRLGagerdAEEIKVQPFFRTTNWQALlaRTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05601  238 ESAVDLIKGLLT-DAKERLG-----YEGLCCHPFFSGIDWNNL--RQTVPPFVPTLTSDDDTSNFD 295
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
552-817 8.48e-57

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: 196.86  E-value: 8.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETvgrTGHPFLLSLLACIQTSSHACF 631
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTF---AENPFVVSMYCSFETKRHLCM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI------ 704
Cdd:cd05609   78 VMEYVEGGDCATLLKNIGpLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLmslttn 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 ---GFGDR-TSTF-----CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPH- 774
Cdd:cd05609  158 lyeGHIEKdTREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEg 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564339933 775 --FLSAQGLELIQKLLQKSPEKRLGAGerDAEEIKVQPFFRTTNW 817
Cdd:cd05609  238 ddALPDDAQDLITRLLQQNPLERLGTG--GAEEVKQHPFFQDLDW 280
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
553-831 8.94e-57

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: 196.81  E-value: 8.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRtghPFLLSLLACIQTSSHACFV 632
Cdd:cd05605    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNS---RFVVSLAYAYETKDALCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIH---EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDR 709
Cdd:cd05605   79 LTIMNGGDLKFHIYnmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVE-IPEGET 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE----DEVFECIVNADVPCPHFLSAQGLELIQ 785
Cdd:cd05605  158 IRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVDRRVKEDQEEYSEKFSEEAKSICS 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 786 KLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05605  238 QLLQKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
561-817 1.98e-56

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: 195.01  E-value: 1.98e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 561 RGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTghPFLLSLLACIQTSSHACFVTEFLPGGD 640
Cdd:cd05611    6 KGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGES--PYVAKLYYSFQSKDYLYLVMEYLNGGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 641 LMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIgFGDRTSTFCGTPEF 719
Cdd:cd05611   84 CASLIKTlGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGL-EKRHNKKFVGTPDY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 720 LAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCP----HFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05611  163 LAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPeevkEFCSPEAVDLINRLLCMDPAKR 242
                        250       260
                 ....*....|....*....|..
gi 564339933 796 LGAgeRDAEEIKVQPFFRTTNW 817
Cdd:cd05611  243 LGA--NGYQEIKSHPFFKSINW 262
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
558-800 5.87e-56

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: 193.46  E-value: 5.87e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEiDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd05117    7 VLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDE-EMLRREIEILKRLD---HPNIVKLYEVFEDDKNLYLVMELCT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYR---------DLKLdnllldAQGFLKIADFGLCKEgIGFG 707
Cdd:cd05117   83 GGELFDRIVKkGSFSEREAAKIMKQILSAVAYLHSQGIVHRdlkpenillASKD------PDSPIKIIDFGLAKI-FEEG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV----PCPHFLSAQGLEL 783
Cdd:cd05117  156 EKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYsfdsPEWKNVSEEAKDL 235
                        250
                 ....*....|....*..
gi 564339933 784 IQKLLQKSPEKRLGAGE 800
Cdd:cd05117  236 IKRLLVVDPKKRLTAAE 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
552-813 4.66e-55

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: 190.76  E-value: 4.66e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLyceKRILETVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQL---RREIEIQSHLRHPNILRLYGYFEDKKRIYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGfgDRT 710
Cdd:cd14007   78 ILEYAPNGELYKELKKQkRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPS--NRR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd14007  156 KTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQK 235
                        250       260
                 ....*....|....*....|...
gi 564339933 791 SPEKRLgagerDAEEIKVQPFFR 813
Cdd:cd14007  236 DPSKRL-----SLEQVLNHPWIK 253
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
544-843 3.98e-53

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: 189.13  E-value: 3.98e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 544 TRNPPQLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETvgrTGHPFLLSLLACI 623
Cdd:cd05596   19 TKLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAH---ANSEWIVQLHYAF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 624 QTSSHACFVTEFLPGGDL--MMQIHEdvFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC- 700
Cdd:cd05596   96 QDDKYLYMVMDYMPGGDLvnLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCm 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 ---KEGIgfgDRTSTFCGTPEFLAPEVLTQEA----YTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVN----AD 769
Cdd:cd05596  174 kmdKDGL---VRSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNhknsLQ 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933 770 VPCPHFLSAQGLELIQKLLQkSPEKRLGAgeRDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05596  251 FPDDVEISKDAKSLICAFLT-DREVRLGR--NGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNFD 321
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
553-812 1.58e-52

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 184.00  E-value: 1.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQ---ELEHPFLVNLWYSFQDEEDMYMV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTS 711
Cdd:cd05578   79 VDLLLGGDLRYHLQQKVkFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATK-LTDGTLAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDT---EDEVFECIVNADVPCPHFLSAQGLELIQKLL 788
Cdd:cd05578  158 STSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSrtsIEEIRAKFETASVLYPAGWSEEAIDLINKLL 237
                        250       260
                 ....*....|....*....|....
gi 564339933 789 QKSPEKRLGagerDAEEIKVQPFF 812
Cdd:cd05578  238 ERDPQKRLG----DLSDLKNHPYF 257
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
553-831 2.68e-52

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: 184.43  E-value: 2.68e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTghpFLLSLLACIQTSSHACFV 632
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSR---FVVSLAYAYETKDALCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHE---DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDR 709
Cdd:cd05631   79 LTIMNGGDLKFHIYNmgnPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQ-IPEGET 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE----DEVFECIVNADVPCPHFLSAQGLELIQ 785
Cdd:cd05631  158 VRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYSEKFSEDAKSICR 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 786 KLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05631  238 MLLTKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
553-831 1.91e-50

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: 179.06  E-value: 1.91e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTghpFLLSLLACIQTSSHACFV 632
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSR---FVVSLAYAYETKDALCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIH---EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC---KEGIGF 706
Cdd:cd05630   79 LTLMNGGDLKFHIYhmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAvhvPEGQTI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTstfcGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE----DEVFECIVNADVPCPHFLSAQGLE 782
Cdd:cd05630  159 KGRV----GTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKkikrEEVERLVKEVPEEYSEKFSPQARS 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564339933 783 LIQKLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05630  235 LCSMLLCKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
545-843 4.55e-50

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 180.18  E-value: 4.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 545 RNPPQLQDFRCLAVLGRGHFGKVLLVQYKgTGKY--YAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLAC 622
Cdd:PTZ00426  24 KNKMKYEDFNFIRTLGTGSFGRVILATYK-NEDFppVAIKRFEKSKIIKQKQVDHVFSERKILNYIN---HPFCVNLYGS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 623 IQTSSHACFVTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK 701
Cdd:PTZ00426 100 FKDESYLYLVLEFVIGGEFFTFLRRNKrFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 EgigFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGL 781
Cdd:PTZ00426 180 V---VDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCK 256
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933 782 ELIQKLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFE 843
Cdd:PTZ00426 257 HLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFE 318
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
551-843 5.50e-50

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: 180.82  E-value: 5.50e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVL---AESDSPWVVSLYYSFQDAQYLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLckeGIGF--- 706
Cdd:cd05629   78 LIMEFLPGGDLMtMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGL---STGFhkq 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 ------------------------------------GDRTSTF-----------CGTPEFLAPEVLTQEAYTRAVDWWGL 739
Cdd:cd05629  155 hdsayyqkllqgksnknridnrnsvavdsinltmssKDQIATWkknrrlmaystVGTPDYIAPEIFLQQGYGQECDWWSL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 740 GVLLYEMLVGECPFPGDTEDEVFECIVN----ADVPCPHFLSAQGLELIQKLLQkSPEKRLGAGerDAEEIKVQPFFRTT 815
Cdd:cd05629  235 GAIMFECLIGWPPFCSENSHETYRKIINwretLYFPDDIHLSVEAEDLIRRLIT-NAENRLGRG--GAHEIKSHPFFRGV 311
                        330       340
                 ....*....|....*....|....*...
gi 564339933 816 NWQALlaRTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05629  312 DWDTI--RQIRAPFIPQLKSITDTSYFP 337
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
552-811 1.78e-49

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: 175.40  E-value: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLG------RDEIDSLycekRILEtvgrtgHPFLLSLLACIQT 625
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEeieekiKREIEIM----KLLN------HPNIIKLYEVIET 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgI 704
Cdd:cd14003   71 ENKIYLVMEYASGGELFDYIVNNGrLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNE-F 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAY-TRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLEL 783
Cdd:cd14003  150 RGGSLLKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDL 229
                        250       260
                 ....*....|....*....|....*...
gi 564339933 784 IQKLLQKSPEKRLGagerdAEEIKVQPF 811
Cdd:cd14003  230 IRRMLVVDPSKRIT-----IEEILNHPW 252
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
548-843 4.47e-48

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 174.68  E-value: 4.47e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 548 PQLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSS 627
Cdd:cd05610    1 PSIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDAL---ALSKSPFIVHLYYSLQSAN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK----- 701
Cdd:cd05610   78 NVYLVMEYLIGGDVKSLLHiYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnr 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 -------------------------------EGIGFGDRT-----------------STFCGTPEFLAPEVLTQEAYTRA 733
Cdd:cd05610  158 elnmmdilttpsmakpkndysrtpgqvlsliSSLGFNTPTpyrtpksvrrgaarvegERILGTPDYLAPELLLGKPHGPA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 734 VDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCP---HFLSAQGLELIQKLLQKSPEKRLGagerdAEEIKVQP 810
Cdd:cd05610  238 VDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAG-----LKELKQHP 312
                        330       340       350
                 ....*....|....*....|....*....|...
gi 564339933 811 FFRTTNWQALLARTvqPPFVPTLCGPADLRYFE 843
Cdd:cd05610  313 LFHGVDWENLQNQT--MPFIPQPDDETDTSYFE 343
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
553-831 5.93e-47

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: 170.15  E-value: 5.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTghpFLLSLLACIQTSSHACFV 632
Cdd:cd05632    4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQ---FVVNLAYAYETKDALCLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHE---DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDR 709
Cdd:cd05632   81 LTIMNGGDLKFHIYNmgnPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK-IPEGES 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE----DEVFECIVNADVPCPHFLSAQGLELIQ 785
Cdd:cd05632  160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYSAKFSEEAKSICK 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 786 KLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05632  240 MLLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP 285
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
545-843 1.40e-46

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: 171.37  E-value: 1.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 545 RNPPQLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETvgrTGHPFLLSLLACIQ 624
Cdd:cd05600    5 RTRLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTT---TNSPWLVKLLYAFQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHACFVTEFLPGGDL-MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEG 703
Cdd:cd05600   82 DPENVYLAMEYVPGGDFrTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 704 IGFG-----------------------DRTSTF--------------CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEM 746
Cdd:cd05600  162 LSPKkiesmkirleevkntafleltakERRNIYramrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFEC 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 747 LVGECPFPGDTEDEVFECIVN----------ADVPCPHFLSAQGLELIQKLLQkSPEKRLgageRDAEEIKVQPFFRTTN 816
Cdd:cd05600  242 LVGFPPFSGSTPNETWANLYHwkktlqrpvyTDPDLEFNLSDEAWDLITKLIT-DPQDRL----QSPEQIKNHPFFKNID 316
                        330       340
                 ....*....|....*....|....*..
gi 564339933 817 WQALLARtVQPPFVPTLCGPADLRYFE 843
Cdd:cd05600  317 WDRLREG-SKPPFIPELESEIDTSYFD 342
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
551-843 4.70e-45

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: 166.71  E-value: 4.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEiDSLYCEKRilETVGRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd05621   52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSD-SAFFWEER--DIMAFANSPWVVQLFCAFQDDKYLY 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD-R 709
Cdd:cd05621  129 MVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMvH 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEA----YTRAVDWWGLGVLLYEMLVGECPFPGD----TEDEVFECIVNADVPCPHFLSAQGL 781
Cdd:cd05621  209 CDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADslvgTYSKIMDHKNSLNFPDDVEISKHAK 288
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933 782 ELIQKLLQKSpEKRLgaGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05621  289 NLICAFLTDR-EVRL--GRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFD 347
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
552-831 1.13e-44

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: 162.77  E-value: 1.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRclaVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRtghPFLLSLLACIQTSSHACF 631
Cdd:cd05607    6 EFR---VLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNS---PFIVSLAYAFETKTHLCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIH---EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGD 708
Cdd:cd05607   80 VMSLMNGGDLKYHIYnvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVE-VKEGK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE----DEVFECIVNADVPCPH-FLSAQGLEL 783
Cdd:cd05607  159 PITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEkvskEELKRRTLEDEVKFEHqNFTEEAKDI 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 564339933 784 IQKLLQKSPEKRLGAGERDAEEIKvQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05607  239 CRLFLAKKPENRLGSRTNDDDPRK-HEFFKSINFPRLEAGLIDPPFVP 285
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
552-843 1.90e-44

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: 163.67  E-value: 1.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRtghPFLLSLLACIQTSSHACF 631
Cdd:cd05597    2 DFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDR---RWITKLHYAFQDENYLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC-KEGIGFGD 708
Cdd:cd05597   79 VMDYYCGGDLltLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSClKLREDGTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLT-----QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADvpcPHF-------- 775
Cdd:cd05597  159 QSSVAVGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHK---EHFsfpddedd 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 776 LSAQGLELIQKLLQkSPEKRLGAGerDAEEIKVQPFFRTTNWQALlaRTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05597  236 VSEEAKDLIRRLIC-SRERRLGQN--GIDDFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNFD 298
Pkinase pfam00069
Protein kinase domain;
558-812 3.03e-44

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 159.33  E-value: 3.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGrDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:pfam00069   6 KLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKK-KKDKNILREIKILK---KLNHPNIVRLYDAFEDKDNLYLVLEYVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  638 GGDLMMQIHED-VFPEPQACFYLACVVLGLqflhekriiyrdlkldnllldaqgflkiadfglckEGigfGDRTSTFCGT 716
Cdd:pfam00069  82 GGSLFDLLSEKgAFSEREAKFIMKQILEGL-----------------------------------ES---GSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHF---LSAQGLELIQKLLQKSPE 793
Cdd:pfam00069 124 PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLKKDPS 203
                         250
                  ....*....|....*....
gi 564339933  794 KRLGagerdAEEIKVQPFF 812
Cdd:pfam00069 204 KRLT-----ATQALQHPWF 217
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
551-843 8.73e-44

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: 164.02  E-value: 8.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEiDSLYCEKRilETVGRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSD-SAFFWEER--DIMAFANSPWVVQLFYAFQDDRYLY 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC----KEGIgf 706
Cdd:cd05622  150 MVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGM-- 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 gDRTSTFCGTPEFLAPEVLTQEA----YTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNAD----VPCPHFLSA 778
Cdd:cd05622  228 -VRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsltFPDDNDISK 306
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 779 QGLELIQKLLQKSpEKRLgaGERDAEEIKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05622  307 EAKNLICAFLTDR-EVRL--GRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 368
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
551-843 3.69e-43

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: 162.10  E-value: 3.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETvgrTGHPFLLSLLACIQTSSHAC 630
Cdd:cd05624   72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVN---GDCQWITTLHYAFQDENYLY 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd05624  149 LVMDYYVGGDLLtlLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGT 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 -RTSTFCGTPEFLAPEVLT-----QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNAD----VPcPHF--L 776
Cdd:cd05624  229 vQSSVAVGTPDYISPEILQamedgMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEerfqFP-SHVtdV 307
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 777 SAQGLELIQKLLQkSPEKRLgaGERDAEEIKVQPFFRTTNWQALlaRTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05624  308 SEEAKDLIQRLIC-SRERRL--GQNGIEDFKKHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNFD 369
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
550-828 6.30e-43

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: 160.22  E-value: 6.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRIL-ETVGrtghPFLLSLLACIQTSSH 628
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILvEADG----AWVVKMFYSFQDKRN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIGFG 707
Cdd:cd05627   77 LYLIMEFLPGGDMMtLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCT-GLKKA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTF------------------------------------CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGEC 751
Cdd:cd05627  156 HRTEFYrnlthnppsdfsfqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 752 PFPGDTEDEVFECIVN--------ADVPcphfLSAQGLELIQKLLQKSpEKRLGAGerDAEEIKVQPFFRTTNWQALLAR 823
Cdd:cd05627  236 PFCSETPQETYRKVMNwketlvfpPEVP----ISEKAKDLILRFCTDA-ENRIGSN--GVEEIKSHPFFEGVDWEHIRER 308

                 ....*
gi 564339933 824 TVQPP 828
Cdd:cd05627  309 PAAIP 313
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
559-800 8.38e-43

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: 155.12  E-value: 8.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLgrDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLK--KLLEELLREIEILKKLN---HPNIVKLYDVFETENFLYLVMEYCEG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRdlkldnlllDAQGFLKIADFGLCK--EGIGFGDRTSTFC 714
Cdd:cd00180   76 GSLkdLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRdlkpenillDSDGTVKLADFGLAKdlDSDDSLLKTTGGT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMlvgecpfpgdtedevfECIVnadvpcphflsaqglELIQKLLQKSPEK 794
Cdd:cd00180  156 TPPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------EELK---------------DLIRRMLQYDPKK 204

                 ....*.
gi 564339933 795 RLGAGE 800
Cdd:cd00180  205 RPSAKE 210
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
552-812 9.46e-43

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: 156.47  E-value: 9.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIK--ALKKqevLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHA 629
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKeiDLSN---MSEKEREEALNEVKLLSKLK---HPNIVKYYESFEENGKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIHE-----DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI 704
Cdd:cd08215   75 CIVMEYADGGDLAQKIKKqkkkgQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV-PCPHFLSAQGLEL 783
Cdd:cd08215  155 STTDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYpPIPSQYSSELRDL 234
                        250       260
                 ....*....|....*....|....*....
gi 564339933 784 IQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd08215  235 VNSMLQKDPEKRP-----SANEILSSPFI 258
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
553-843 4.79e-42

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: 158.25  E-value: 4.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd05626    3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDIL---AEADNEWVVKLYYSFQDKDNLYFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKegiGF----- 706
Cdd:cd05626   80 MDYIPGGDMMsLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCT---GFrwthn 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 -----------------------------GDRTST----------------FCGTPEFLAPEVLTQEAYTRAVDWWGLGV 741
Cdd:cd05626  157 skyyqkgshirqdsmepsdlwddvsncrcGDRLKTleqratkqhqrclahsLVGTPNYIAPEVLLRKGYTQLCDWWSVGV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 742 LLYEMLVGECPF----PGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQkSPEKRLgaGERDAEEIKVQPFFRTTNW 817
Cdd:cd05626  237 ILFEMLVGQPPFlaptPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCC-SAEERL--GRNGADDIKAHPFFSEVDF 313
                        330       340
                 ....*....|....*....|....*.
gi 564339933 818 QALLaRTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05626  314 SSDI-RTQPAPYVPKISHPMDTSNFD 338
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
552-800 5.56e-42

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: 154.22  E-value: 5.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACF 631
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDS-EEELEALEREIRILSSLK---HPNIVRYLGTERTENTLNI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDL--MMQiHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK--EGIGFG 707
Cdd:cd06606   77 FLEYVPGGSLasLLK-KFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFP--GDTEDEVFECIVNADVPC-PHFLSAQGLELI 784
Cdd:cd06606  156 EGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSelGNPVAALFKIGSSGEPPPiPEHLSEEAKDFL 235
                        250
                 ....*....|....*.
gi 564339933 785 QKLLQKSPEKRLGAGE 800
Cdd:cd06606  236 RKCLQRDPKKRPTADE 251
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
559-812 1.60e-41

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: 153.09  E-value: 1.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKR-ILETVGRT-------GHPFLLSLLACI--QTSSH 628
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREGKNDRGKIKnALDDVRREiaimkklDHPNIVRLYEVIddPESDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMM---QIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIG 705
Cdd:cd14008   81 LYLVLEYCEGGPVMEldsGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCGTPEFLAPEVLTQEAYT---RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHF--LSAQG 780
Cdd:cd14008  161 GNDTLQKTAGTPAFLAPELCDGDSKTysgKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPpeLSPEL 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564339933 781 LELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14008  241 KDLLRRMLEKDPEKRI-----TLKEIKEHPWV 267
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
558-831 4.95e-41

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: 152.21  E-value: 4.95e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEV-LGRDEIDSLYcEKRILETVGRTGH-PFLLSLLACIQTSSHACFVTEF 635
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkMKQGETLALN-ERIMLSLVSTGGDcPFIVCMTYAFQTPDKLCFILDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFGDRTSTFC 714
Cdd:cd05606   80 MNGGDLHYHLSQhGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACD---FSKKKPHAS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 -GTPEFLAPEVLTQ-EAYTRAVDWWGLGVLLYEMLVGECPF-PGDTED--EVFECIVNADVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd05606  157 vGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFrQHKTKDkhEIDRMTLTMNVELPDSFSPELKSLLEGLLQ 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 564339933 790 KSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05606  237 RDVSKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
553-843 6.93e-41

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: 154.82  E-value: 6.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd05625    3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDIL---AEADNEWVVRLYYSFQDKDNLYFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC----------- 700
Cdd:cd05625   80 MDYIPGGDMMsLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsky 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 --------KEGIGF----GDRTSTFCG------------------------TPEFLAPEVLTQEAYTRAVDWWGLGVLLY 744
Cdd:cd05625  160 yqsgdhlrQDSMDFsnewGDPENCRCGdrlkplerraarqhqrclahslvgTPNYIAPEVLLRTGYTQLCDWWSVGVILF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 745 EMLVGECPF----PGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLqKSPEKRLgaGERDAEEIKVQPFFRTTNWQAL 820
Cdd:cd05625  240 EMLVGQPPFlaqtPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRL--GKNGADEIKAHPFFKTIDFSSD 316
                        330       340
                 ....*....|....*....|...
gi 564339933 821 LaRTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05625  317 L-RQQSAPYIPKITHPTDTSNFD 338
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
551-828 2.20e-39

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 150.57  E-value: 2.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTghpFLLSLLACIQTSSHAC 630
Cdd:cd05628    1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSL---WVVKMFYSFQDKLNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIGFGDR 709
Cdd:cd05628   78 LIMEFLPGGDMMtLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCT-GLKKAHR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTF------------------------------------CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd05628  157 TEFYrnlnhslpsdftfqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPF 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 754 PGDTEDEVFECIVN--------ADVPcphfLSAQGLELIQKLLQKSpEKRLGAgeRDAEEIKVQPFFRTTNWQALLARTV 825
Cdd:cd05628  237 CSETPQETYKKVMNwketlifpPEVP----ISEKAKDLILRFCCEW-EHRIGA--PGVEEIKTNPFFEGVDWEHIRERPA 309

                 ...
gi 564339933 826 QPP 828
Cdd:cd05628  310 AIP 312
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
514-843 6.28e-39

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: 149.78  E-value: 6.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 514 LQEPAPGTPCTKRPHMDPRTGVAPPLAALSTRNPPQLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRD 593
Cdd:cd05623   35 LYDECSNSPLRREKNILEYLEWAKPFTSKVKQMRLHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 594 EIDSLYCEKRILETvgrTGHPFLLSLLACIQTSSHACFVTEFLPGGDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHE 671
Cdd:cd05623  115 ETACFREERDVLVN---GDSQWITTLHYAFQDDNNLYLVMDYYVGGDLLtlLSKFEDRLPEDMARFYLAEMVLAIDSVHQ 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 672 KRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD-RTSTFCGTPEFLAPEVLT-----QEAYTRAVDWWGLGVLLYE 745
Cdd:cd05623  192 LHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTvQSSVAVGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYE 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 746 MLVGECPFPGDTEDEVFECIVN-----------ADVpcphflSAQGLELIQKLLQkSPEKRLgaGERDAEEIKVQPFFRT 814
Cdd:cd05623  272 MLYGETPFYAESLVETYGKIMNhkerfqfptqvTDV------SENAKDLIRRLIC-SREHRL--GQNGIEDFKNHPFFVG 342
                        330       340
                 ....*....|....*....|....*....
gi 564339933 815 TNWQALlaRTVQPPFVPTLCGPADLRYFE 843
Cdd:cd05623  343 IDWDNI--RNCEAPYIPEVSSPTDTSNFD 369
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
552-831 6.45e-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: 144.42  E-value: 6.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRdEIDSLYCEKRILETVGRTGH-PFLLSLLACIQTSSHAC 630
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK-QGETLALNERIMLSLVSTGDcPFIVCMSYAFHTPDKLS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDR 709
Cdd:cd14223   80 FILDLMNGGDLHYHLSQHgVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTfcGTPEFLAPEVLTQE-AYTRAVDWWGLGVLLYEMLVGECPF-PGDTED--EVFECIVNADVPCPHFLSAQGLELIQ 785
Cdd:cd14223  160 ASV--GTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFrQHKTKDkhEIDRMTLTMAVELPDSFSPELRSLLE 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 786 KLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd14223  238 GLLQRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIP 283
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
552-812 6.49e-38

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 142.34  E-value: 6.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACF 631
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLES---KEKKESILNEIAILKKCK---HPNIVKYYGSYLKKDELWI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDR 709
Cdd:cd05122   75 VMEFCSGGSLkdLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 tSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP---CPHFLSAQGLELIQK 786
Cdd:cd05122  155 -NTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPglrNPKKWSKEFKDFLKK 233
                        250       260
                 ....*....|....*....|....*.
gi 564339933 787 LLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd05122  234 CLQKDPEKRP-----TAEQLLKHPFI 254
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
550-831 1.18e-36

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: 141.74  E-value: 1.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRdEIDSLYCEKRILETVGRTGH-PFLLSLLACIQTSSH 628
Cdd:cd05633    4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK-QGETLALNERIMLSLVSTGDcPFIVCMTYAFHTPDK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFG 707
Cdd:cd05633   83 LCFILDLMNGGDLHYHLSQHgVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTfcGTPEFLAPEVLTQ-EAYTRAVDWWGLGVLLYEMLVGECPF-PGDTED--EVFECIVNADVPCPHFLSAQGLEL 783
Cdd:cd05633  163 PHASV--GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrQHKTKDkhEIDRMTLTVNVELPDSFSPELKSL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 564339933 784 IQKLLQKSPEKRLGAGERDAEEIKVQPFFRTTNWQALLARTVQPPFVP 831
Cdd:cd05633  241 LEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIP 288
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
558-800 2.44e-36

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: 137.84  E-value: 2.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDE-IDSlycEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd14095    7 VIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHmIEN---EVAILR---RVKHPNIVQLIEEYDTDTELYLVMELV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF----LKIADFGL---CKEGIgfgd 708
Cdd:cd14095   81 KGGDLFDAITSSTkFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDgsksLKLADFGLateVKEPL---- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 rtSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF--PGDTEDEVFECIVNADV--PCPHF--LSAQGLE 782
Cdd:cd14095  157 --FTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFrsPDRDQEELFDLILAGEFefLSPYWdnISDSAKD 234
                        250
                 ....*....|....*...
gi 564339933 783 LIQKLLQKSPEKRLGAGE 800
Cdd:cd14095  235 LISRMLVVDPEKRYSAGQ 252
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
559-795 1.50e-35

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: 135.36  E-value: 1.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGT--GKYYAIKALKKQevlgrDEIDSLYCE-KRILETVGRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd13999    1 IGSGSFGEV----YKGKwrGTDVAIKKLKVE-----DDNDELLKEfRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHED--VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd13999   72 MPGGSLYDLLHKKkiPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP------CPHFLSaqglELIQKL 787
Cdd:cd13999  152 VGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRppippdCPPELS----KLIKRC 227

                 ....*...
gi 564339933 788 LQKSPEKR 795
Cdd:cd13999  228 WNEDPEKR 235
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
552-800 2.10e-35

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: 135.41  E-value: 2.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAikaLKKQEVLGRDEIDSLYCekRILETVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd06623    2 DLERVKVLGQGSSGVVYKVRHKPTGKIYA---LKKIHVDGDEEFRKQLL--RELKTLRSCESPYVVKCYGAFYKEGEISI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDL--MMQIHEdVFPEPqacfYLAC----VVLGLQFLH-EKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI 704
Cdd:cd06623   77 VLEYMDGGSLadLLKKVG-KIPEP----VLAYiarqILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFE--CIVNaDVPCP----HFLSA 778
Cdd:cd06623  152 NTLDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFElmQAIC-DGPPPslpaEEFSP 230
                        250       260
                 ....*....|....*....|..
gi 564339933 779 QGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd06623  231 EFRDFISACLQKDPKKRPSAAE 252
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
552-812 2.37e-35

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 134.99  E-value: 2.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACF 631
Cdd:cd14099    2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLK---HPNIVKFHDCFEDEENVYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGF-GDR 709
Cdd:cd14099   79 LLELCSNGSLMeLLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAAR-LEYdGER 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLT-QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNAD--VPCPHFLSAQGLELIQK 786
Cdd:cd14099  158 KKTLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEysFPSHLSISDEAKDLIRS 237
                        250       260
                 ....*....|....*....|....*.
gi 564339933 787 LLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14099  238 MLQPDPTKRP-----SLDEILSHPFF 258
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
559-800 5.25e-35

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: 133.93  E-value: 5.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQevlgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKR----DKKKEAVLREISILNQLQ---HPRIIQLHEAYESPTELVLILELCSG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRI----------IYRDLKLDNllldaqgfLKIADFGLCKEgIGFG 707
Cdd:cd14006   74 GELLDRLaERGSLSEEEVRTYMRQLLEGLQYLHNHHIlhldlkpeniLLADRPSPQ--------IKIIDFGLARK-LNPG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDE----VFECIVNADVPCPHFLSAQGLEL 783
Cdd:cd14006  145 EELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQEtlanISACRVDFSEEYFSSVSQEAKDF 224
                        250
                 ....*....|....*..
gi 564339933 784 IQKLLQKSPEKRLGAGE 800
Cdd:cd14006  225 IRKLLVKEPRKRPTAQE 241
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
559-797 6.25e-35

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: 133.50  E-value: 6.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKK-LNKKLQENLESEIAILKSIK---HPNIVRLYDVQKTEDFIYLVLEYCAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLD---NLLLDAQGFLKIADFGLCKEgIGFGDRTSTFC 714
Cdd:cd14009   77 GDLSQYIRkRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQnllLSTSGDDPVLKIADFGFARS-LQPASMAETLC 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV----PCPHFLSAQGLELIQKLLQK 790
Cdd:cd14009  156 GSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAvipfPIAAQLSPDCKDLLRRLLRR 235

                 ....*..
gi 564339933 791 SPEKRLG 797
Cdd:cd14009  236 DPAERIS 242
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
552-811 1.62e-34

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: 132.53  E-value: 1.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLyceKRILETVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQI---KREIAIMKLLRHPNIVELHEVMATKTKIFF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC--KEGIGFGD 708
Cdd:cd14663   78 VMELVTGGELFSKIAKNGrLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQDG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRA-VDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKL 787
Cdd:cd14663  158 LLHTTCGTPNYVAPEVLARRGYDGAkADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRI 237
                        250       260
                 ....*....|....*....|....
gi 564339933 788 LQKSPEKRLgagerDAEEIKVQPF 811
Cdd:cd14663  238 LDPNPSTRI-----TVEQIMASPW 256
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
552-800 2.06e-34

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: 132.60  E-value: 2.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYceKRILETVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLF--QREINILKSLEHPGIVRLIDWYEDDQHIYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHED-VFPEpQACFYLACVVL-GLQFLHEKRIIYRDLKLDNLLLDAQG--FLKIADFGLCKEgIGFG 707
Cdd:cd14098   79 VMEYVEGGDLMDFIMAWgAIPE-QHARELTKQILeAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKV-IHTG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQE------AYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFL----S 777
Cdd:cd14098  157 TFLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVdfniS 236
                        250       260
                 ....*....|....*....|...
gi 564339933 778 AQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14098  237 EEAIDFILRLLDVDPEKRMTAAQ 259
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
553-795 3.47e-34

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: 132.81  E-value: 3.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvLGRDEidSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSP-LSRDS--SLENEIAVLK---RIKHENIVTLEDIYESTTHYYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDA---QGFLKIADFGLCK---EGIg 705
Cdd:cd14166   79 MQLVSGGELFDRILErGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTpdeNSKIMITDFGLSKmeqNGI- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 fgdrTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA--DVPCPHF--LSAQGL 781
Cdd:cd14166  158 ----MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGyyEFESPFWddISESAK 233
                        250
                 ....*....|....
gi 564339933 782 ELIQKLLQKSPEKR 795
Cdd:cd14166  234 DFIRHLLEKNPSKR 247
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
558-800 7.44e-34

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: 131.36  E-value: 7.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQE--VLGRDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd14084   13 TLGSGACGEVKLAYDKSTCKKVAIKIINKRKftIGSRREINKPRNIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLEL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG---FLKIADFGLCKegigFGDRTS 711
Cdd:cd14084   93 MEGGELFDRVVSNKrLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEeecLIKITDFGLSK----ILGETS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 ---TFCGTPEFLAPEVLT---QEAYTRAVDWWGLGVLLYEMLVGECPFPGD-TEDEVFECIVNA----DVPCPHFLSAQG 780
Cdd:cd14084  169 lmkTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEQILSGkytfIPKAWKNVSEEA 248
                        250       260
                 ....*....|....*....|
gi 564339933 781 LELIQKLLQKSPEKRLGAGE 800
Cdd:cd14084  249 KDLVKKMLVVDPSRRPSIEE 268
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
558-795 9.70e-34

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: 130.57  E-value: 9.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDeiDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14083   10 VLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKE--DSLENEIAVLR---KIKHPNIVQLLDIYESKSHLYLVMELVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDlkldnllldaqgfLK----------------IADFGLC 700
Cdd:cd14083   85 GGELFDRIVEKgSYTEKDASHLIRQVLEAVDYLHSLGIVHRD-------------LKpenllyyspdedskimISDFGLS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 K-EGIGFgdrTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA----DVPCPHF 775
Cdd:cd14083  152 KmEDSGV---MSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAeyefDSPYWDD 228
                        250       260
                 ....*....|....*....|
gi 564339933 776 LSAQGLELIQKLLQKSPEKR 795
Cdd:cd14083  229 ISDSAKDFIRHLMEKDPNKR 248
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
559-796 1.38e-33

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: 129.77  E-value: 1.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKAL-------KKQEVLGRdEIDSLYCekriletvgrTGHPFLLSLLACIQTSSHACF 631
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKILdktkldqKTQRLLSR-EISSMEK----------LHHPNIIRLYEVVETLSKLHL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG---LCKEGigfg 707
Cdd:cd14075   79 VMEYASGGELYTKISTEgKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGfstHAKRG---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQK 786
Cdd:cd14075  155 ETLNTFCGSPPYAAPELFKDEHYIgIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRG 234
                        250
                 ....*....|
gi 564339933 787 LLQKSPEKRL 796
Cdd:cd14075  235 ILQPVPSDRY 244
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
552-795 1.48e-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: 130.15  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRclAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDeiDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACF 631
Cdd:cd14167    6 DFR--EVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKE--TSIENEIAVLHKIK---HPNIVALDDIYESGGHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHEDVFPEPQACFYLACVVL-GLQFLHEKRIIYRDLKLDNLLLDA---QGFLKIADFGLCKEGiGFG 707
Cdd:cd14167   79 IMQLVSGGELFDRIVEKGFYTERDASKLIFQILdAVKYLHDMGIVHRDLKPENLLYYSldeDSKIMISDFGLSKIE-GSG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA----DVPCPHFLSAQGLEL 783
Cdd:cd14167  158 SVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAeyefDSPYWDDISDSAKDF 237
                        250
                 ....*....|..
gi 564339933 784 IQKLLQKSPEKR 795
Cdd:cd14167  238 IQHLMEKDPEKR 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
546-795 2.18e-33

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 135.14  E-value: 2.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 546 NPPQLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQT 625
Cdd:COG0515    2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLN---HPNIVRVYDVGEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLPGGDL--MMQiHEDVFPEPQACFYLACVVLGLQFLHEKRIIYR---------DlkldnllldAQGFLKI 694
Cdd:COG0515   79 DGRPYLVMEYVEGESLadLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRdikpanillT---------PDGRVKL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLCKE-GIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCP 773
Cdd:COG0515  149 IDFGIARAlGGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPP 228
                        250       260
                 ....*....|....*....|....*.
gi 564339933 774 HFLSAQ---GLE-LIQKLLQKSPEKR 795
Cdd:COG0515  229 SELRPDlppALDaIVLRALAKDPEER 254
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
559-800 2.58e-33

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: 129.39  E-value: 2.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvLGRDeidslyCEKRILETVG----RTGHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd14106   16 LGRGKFAVVRKCIHKETGKEYAAKFLRKRR-RGQD------CRNEILHEIAvlelCKDCPRVVNLHEVYETRSELILILE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIY---RDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRT 710
Cdd:cd14106   89 LAAGGELQTLLdEEECLTEADVRRLMRQILEGVQYLHERNIVHldlKPQNILLTSEFPLGDIKLCDFGISRV-IGEGEEI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI--VNADVPCPHF--LSAQGLELIQK 786
Cdd:cd14106  168 REILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNIsqCNLDFPEELFkdVSPLAIDFIKR 247
                        250
                 ....*....|....
gi 564339933 787 LLQKSPEKRLGAGE 800
Cdd:cd14106  248 LLVKDPEKRLTAKE 261
HR1_PKN3_2 cd11632
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
95-168 2.16e-32

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3; PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the second HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC.


Pssm-ID: 212022  Cd Length: 74  Bit Score: 120.03  E-value: 2.16e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933  95 PRAEQSRARLLEALHRQLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKISGLEASG 168
Cdd:cd11632    1 EWATDPRARRLEALKRQLHVELKVKQGAENMIQTYSSGTSKERKLLATAQQMLQDSRTKIELLRMQIVKLEQSG 74
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
553-795 2.70e-32

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: 126.16  E-value: 2.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARAL---ARLSHPNIVRVYDVGEDDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYR---------DlkldnllldAQGFLKIADFGLCK- 701
Cdd:cd14014   79 MEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRdikpanillT---------EDGRVKLTDFGIARa 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 EGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP--------CP 773
Cdd:cd14014  150 LGDSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPppsplnpdVP 229
                        250       260
                 ....*....|....*....|..
gi 564339933 774 HFLSAqgleLIQKLLQKSPEKR 795
Cdd:cd14014  230 PALDA----IILRALAKDPEER 247
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
559-812 2.86e-32

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: 126.21  E-value: 2.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14081    9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIE---HPNVLKLYDVYENKKYLYLVLEYVSG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG---LCKEgigfGDRTSTFC 714
Cdd:cd14081   86 GELFDYLVKKgRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGmasLQPE----GSLLETSC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPE 793
Cdd:cd14081  162 GSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPE 241
                        250
                 ....*....|....*....
gi 564339933 794 KRLgagerDAEEIKVQPFF 812
Cdd:cd14081  242 KRI-----TIEEIKKHPWF 255
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
550-796 3.68e-32

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: 125.84  E-value: 3.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlgrDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHA 629
Cdd:cd14116    4 LEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQL---EKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGfgD 708
Cdd:cd14116   81 YLILEYAPLGTVYRELQKlSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPS--S 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLL 788
Cdd:cd14116  159 RRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLL 238

                 ....*...
gi 564339933 789 QKSPEKRL 796
Cdd:cd14116  239 KHNPSQRP 246
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
552-797 4.69e-32

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: 125.58  E-value: 4.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYcEKRILETVGrtgHPFLLSLLACIQTSSHACF 631
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVN-EIRLLASVN---HPNIIRYKEAFLDGNRLCI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHED-----VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKegIGF 706
Cdd:cd08530   77 VMEYAPFGDLSKLISKRkkkrrLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK--VLK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDT-EDEVFECIVNADVPCPHFLSAQGLELIQ 785
Cdd:cd08530  155 KNLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTmQELRYKVCRGKFPPIPPVYSQDLQQIIR 234
                        250
                 ....*....|..
gi 564339933 786 KLLQKSPEKRLG 797
Cdd:cd08530  235 SLLQVNPKKRPS 246
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
551-796 6.71e-32

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: 124.97  E-value: 6.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEkriLETVGRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNE---VEIHCQLKHPSILELYNYFEDSNYVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHEDV--FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd14186   78 LVLEMCHNGEMSRYLKNRKkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLL 788
Cdd:cd14186  158 KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLL 237

                 ....*...
gi 564339933 789 QKSPEKRL 796
Cdd:cd14186  238 RKNPADRL 245
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
559-797 9.22e-32

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: 125.10  E-value: 9.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgRDEIDSlycEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14010    8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSK---RPEVLN---EVRLTHELK---HPNVLKFYEWYETSNHLWLVVEYCTG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK---------------- 701
Cdd:cd14010   79 GDLETLLRQDGnLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkelfgqfsde 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 EGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCP-----HFL 776
Cdd:cd14010  159 GNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPppkvsSKP 238
                        250       260
                 ....*....|....*....|.
gi 564339933 777 SAQGLELIQKLLQKSPEKRLG 797
Cdd:cd14010  239 SPDFKSLLKGLLEKDPAKRLS 259
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
552-797 3.11e-31

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: 123.13  E-value: 3.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQevlGR--DEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHA 629
Cdd:cd14002    2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKR---GKseKELRNLRQEIEILRKLN---HPNIIEMLDSFETKKEF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFlPGGDLMmQIHED--VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFG 707
Cdd:cd14002   76 VVVTEY-AQGELF-QILEDdgTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARA-MSCN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTST-FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQK 786
Cdd:cd14002  153 TLVLTsIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQG 232
                        250
                 ....*....|.
gi 564339933 787 LLQKSPEKRLG 797
Cdd:cd14002  233 LLNKDPSKRLS 243
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
558-798 3.28e-31

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: 123.13  E-value: 3.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIdsLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14185    7 TIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDM--IESEILIIKSLS---HPNIVKLFEVYETEKEIYLILEYVR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLD----NLLLDAQGFLKIADFGLCKEGIGfgdRTST 712
Cdd:cd14185   82 GGDLFDAIIESVkFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPEnllvQHNPDKSTTLKLADFGLAKYVTG---PIFT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 713 FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF--PGDTEDEVFECIVNADV----PCPHFLSAQGLELIQK 786
Cdd:cd14185  159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFrsPERDQEELFQIIQLGHYeflpPYWDNISEAAKDLISR 238
                        250
                 ....*....|..
gi 564339933 787 LLQKSPEKRLGA 798
Cdd:cd14185  239 LLVVDPEKRYTA 250
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
556-800 4.35e-31

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: 123.03  E-value: 4.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvLGRDEIDSlycEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd14087    6 KALIGRGSFSRVVRVEHRVTRQPYAIKMIETKC-RGREVCES---ELNVLR---RVRHTNIIQLIEVFETKERVYMVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF---LKIADFGLCKEGIGFGDRT- 710
Cdd:cd14087   79 ATGGELFDRIiAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKKGPNCLm 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNAD-VPCPHF---LSAQGLELIQK 786
Cdd:cd14087  159 KTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKySYSGEPwpsVSNLAKDFIDR 238
                        250
                 ....*....|....
gi 564339933 787 LLQKSPEKRLGAGE 800
Cdd:cd14087  239 LLTVNPGERLSATQ 252
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
559-800 4.69e-31

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: 122.33  E-value: 4.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALK------KQEVlgRDEIDSLycekRILEtvgrtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKcrkakdREDV--RNEIEIM----NQLR------HPRLLQLYDAFETPREMVLV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDVF--PEPQACFYLACVVLGLQFLHEKRIIY------------RDLKLdnllldaqgfLKIADFG 698
Cdd:cd14103   69 MEYVAGGELFERVVDDDFelTERDCILFMRQICEGVQYMHKQGILHldlkpenilcvsRTGNQ----------IKIIDFG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 LCKEgigFGDRTST--FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA--DVPCPH 774
Cdd:cd14103  139 LARK---YDPDKKLkvLFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAkwDFDDEA 215
                        250       260
                 ....*....|....*....|....*...
gi 564339933 775 F--LSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14103  216 FddISDEAKDFISKLLVKDPRKRMSAAQ 243
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
559-810 9.60e-31

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: 122.47  E-value: 9.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGR--------------------DEIDSLYCEKRILETVGrtgHPFLLS 618
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQagffrrppprrkpgalgkplDPLDRVYREIAILKKLD---HPNVVK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 619 LLACIQ--TSSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIAD 696
Cdd:cd14118   79 LVEVLDdpNEDNLYMVFELVDKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIAD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 697 FGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYT---RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCP 773
Cdd:cd14118  159 FGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKfsgKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFP 238
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564339933 774 --HFLSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQP 810
Cdd:cd14118  239 ddPVVSEQLKDLILRMLDKNPSERI-----TLPEIKEHP 272
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
553-795 1.77e-30

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: 121.09  E-value: 1.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQ-LNPSSLQKLFREVRIMKILN---HPNIVKLFEVIETEKTLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTS 711
Cdd:cd14072   78 MEYASGGEVFdYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNE-FTPGNKLD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd14072  157 TFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVL 236

                 ....*
gi 564339933 791 SPEKR 795
Cdd:cd14072  237 NPSKR 241
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
559-800 3.76e-30

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: 120.22  E-value: 3.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEV--LGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd08222    8 LGSGNFGTVYLVSDLKATADEELKVLKEISVgeLQPDETVDANREAKLLSKLD---HPAIVKFHDSFVEKESFCIVTEYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHE-----DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDaQGFLKIADFGLCKEGIGFGDRTS 711
Cdd:cd08222   85 EGGDLDDKISEykksgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK-NNVIKVGDFGISRILMGTSDLAT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP-CPHFLSAQGLELIQKLLQK 790
Cdd:cd08222  164 TFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPsLPDKYSKELNAIYSRMLNK 243
                        250
                 ....*....|
gi 564339933 791 SPEKRLGAGE 800
Cdd:cd08222  244 DPALRPSAAE 253
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
553-795 4.82e-30

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: 120.92  E-value: 4.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEidSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKES--SIENEIAVLRKIK---HENIVALEDIYESPNHLYLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDVF-PEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ---GFLKIADFGLCKEGiGFGD 708
Cdd:cd14168   87 MQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQdeeSKIMISDFGLSKME-GKGD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA----DVPCPHFLSAQGLELI 784
Cdd:cd14168  166 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAdyefDSPYWDDISDSAKDFI 245
                        250
                 ....*....|.
gi 564339933 785 QKLLQKSPEKR 795
Cdd:cd14168  246 RNLMEKDPNKR 256
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
552-800 7.58e-30

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: 120.05  E-value: 7.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDslycekrILETVGRtgHPFLLSLLACIQTSSHACF 631
Cdd:cd14091    1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIE-------ILLRYGQ--HPNIITLRDVYDDGNSVYL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKR----------IIYRDLKLDNLLldaqgfLKIADFGLC 700
Cdd:cd14091   72 VTELLRGGELLDRIlRQKFFSEREASAVMKTLTKTVEYLHSQGvvhrdlkpsnILYADESGDPES------LRICDFGFA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 KE-----GIgfgdrTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF---PGDTEDEVFECIVNADVPC 772
Cdd:cd14091  146 KQlraenGL-----LMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFasgPNDTPEVILARIGSGKIDL 220
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564339933 773 PH----FLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14091  221 SGgnwdHVSDSAKDLVRKMLHVDPSQRPTAAQ 252
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
559-795 1.93e-29

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: 118.49  E-value: 1.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvLGRDEIDSLYCEKRILETVgrTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14198   16 LGRGKFAVVRQCISKSTGQEYAAKFLKKRR-RGQDCRAEILHEIAVLELA--KSNPRVVNLHEVYETTSEIILILEYAAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GD---LMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIY---RDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTST 712
Cdd:cd14198   93 GEifnLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHldlKPQNILLSSIYPLGDIKIVDFGMSRK-IGHACELRE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 713 FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI--VNADVPCPHFLSAQGL--ELIQKLL 788
Cdd:cd14198  172 IMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNIsqVNVDYSEETFSSVSQLatDFIQKLL 251

                 ....*..
gi 564339933 789 QKSPEKR 795
Cdd:cd14198  252 VKNPEKR 258
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
559-796 1.99e-29

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: 118.45  E-value: 1.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIdslyCEKRIlETVGRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14169   11 LGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAM----VENEI-AVLRRINHENIVSLEDIYESPTHLYLAMELVTG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDA---QGFLKIADFGLCKegIGFGDRTSTFC 714
Cdd:cd14169   86 GELFDRIIErGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSK--IEAQGMLSTAC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA----DVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd14169  164 GTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAeyefDSPYWDDISESAKDFIRHLLER 243

                 ....*.
gi 564339933 791 SPEKRL 796
Cdd:cd14169  244 DPEKRF 249
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
559-796 3.89e-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: 117.10  E-value: 3.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKqEVLGRD------EIDSLycekRILEtvgrtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd14078   11 IGSGGFAKVKLATHILTGEKVAIKIMDK-KALGDDlprvktEIEAL----KNLS------HQHICRLYHVIETDNKIFMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC-KEGIGFGDRT 710
Cdd:cd14078   80 LEYCPGGELFDYIVAkDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCaKPKGGMDHHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRA-VDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd14078  160 ETCCGSPAYAAPELIQGKPYIGSeADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQ 239

                 ....*..
gi 564339933 790 KSPEKRL 796
Cdd:cd14078  240 VDPKKRI 246
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
559-800 4.17e-29

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: 117.59  E-value: 4.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEV------LGRDEIDSlycEKRILETVGrtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd14105   13 LGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgVSREDIER---EVSILRQVL---HPNIITLHDVFENKTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF----LKIADFGLCKEgIGFG 707
Cdd:cd14105   87 LELVAGGELFDFLAEkESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHK-IEDG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI--VNADVPCPHF--LSAQGLEL 783
Cdd:cd14105  166 NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItaVNYDFDDEYFsnTSELAKDF 245
                        250
                 ....*....|....*..
gi 564339933 784 IQKLLQKSPEKRLGAGE 800
Cdd:cd14105  246 IRQLLVKDPRKRMTIQE 262
HR1_PKN_1 cd11622
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
14-79 8.36e-29

First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that 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 cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the first HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212012  Cd Length: 66  Bit Score: 109.66  E-value: 8.36e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933  14 QRAPEDEKEMIRRAIQKELKIKEGMENMRRVATDRRHLGHVQQLLRASNRRLEQLHGELRELHAQV 79
Cdd:cd11622    1 QQKLEELKEQIRREIRKELKIKEGAENLRKATTDKKSLAHVESILKKSNRKLEDLHQELQELEAHI 66
C2_PKN-like cd08687
C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine ...
326-413 1.24e-28

C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine kinase. It is a member of the protein kinase C (PKC) superfamily, but lacks a C1 domain. There are at least 3 different isoforms of PKN (PRK1/PKNalpha/PAK1; PKNbeta, and PRK2/PAK2/PKNgamma). The C-terminal region contains the Ser/Thr type protein kinase domain, while the N-terminal region of PKN contains three antiparallel coiled-coil (ACC) finger domains which are relatively rich in charged residues and contain a leucine zipper-like sequence. These domains binds to the small GTPase RhoA. Following these domains is a C2-like domain. Its C-terminal part functions as an auto-inhibitory region. PKNs are not activated by classical PKC activators such as diacylglycerol, phorbol ester or Ca2+, but instead are activated by phospholipids and unsaturated fatty acids. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176069  Cd Length: 98  Bit Score: 110.17  E-value: 1.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 326 SEVLAVLKVDNRVVGQTGWGLVAEKSWDQAFSISLDRARELEIGVHWRDWRQLCGVAFLKLEEFLdnacHQLSLSLVPQG 405
Cdd:cd08687    9 SEVSAVLKLDNTVVGQTQWKPKSNQAWDQSFTLELERSRELEIAVYWRDWRSLCAVKFLKLEDER----HEVQLDMEPQL 84

                 ....*...
gi 564339933 406 RLFAQVTF 413
Cdd:cd08687   85 CLVAELTF 92
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
559-795 1.98e-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: 115.20  E-value: 1.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlgrDEI--DSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd14074   11 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DDVskAHLFQEVRCMKLVQ---HPNVVRLYEVIDTQTKLYLILELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQI--HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLL-LDAQGFLKIADFGLCKEGIGfGDRTSTF 713
Cdd:cd14074   85 DGGDMYDYImkHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQP-GEKLETS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAY-TRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSP 792
Cdd:cd14074  164 CGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIRDP 243

                 ...
gi 564339933 793 EKR 795
Cdd:cd14074  244 KKR 246
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
550-796 4.62e-28

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: 114.58  E-value: 4.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLyceKRILETVGRTGHPFLLSLLACIQTSSHA 629
Cdd:cd14117    5 IDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQL---RREIEIQSHLRHPNILRLYNYFHDRKRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFgd 708
Cdd:cd14117   82 YLILEYAPRGELYKELQKhGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSL-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLL 788
Cdd:cd14117  160 RRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLL 239

                 ....*...
gi 564339933 789 QKSPEKRL 796
Cdd:cd14117  240 RYHPSERL 247
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
552-812 6.50e-28

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: 113.58  E-value: 6.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKA--LKKQEVLGRDEIDSLYCEKRILEtvgrtgHPFLLSLLACIQTSSHA 629
Cdd:cd14069    2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFvdMKRAPGDCPENIKKEVCIQKMLS------HKNVVRFYGHRREGEFQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFG- 707
Cdd:cd14069   76 YLFLEYASGGELFDKIEPDVgMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGk 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTST-FCGTPEFLAPEVLTQEAYtRA--VDWWGLGVLLYEMLVGECPF--PGDTEDEvFECIVNADVP--CP-HFLSAQ 779
Cdd:cd14069  156 ERLLNkMCGTLPYVAPELLAKKKY-RAepVDVWSCGIVLFAMLAGELPWdqPSDSCQE-YSDWKENKKTylTPwKKIDTA 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564339933 780 GLELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14069  234 ALSLLRKILTENPNKRI-----TIEDIKKHPWY 261
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
552-795 6.54e-28

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: 113.64  E-value: 6.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLG----RD-EIDSLYCEKRILETVGRTGHPFLLSLLACIQTS 626
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVdtwvRDrKLGTVPLEIHILDTLNKRSHPNIVKLLDFFEDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 627 SHACFVTE-FLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG---LCK 701
Cdd:cd14004   81 EFYYLVMEkHGSGMDLFDFIErKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGsaaYIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 EGigfgdRTSTFCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPgdtedEVFEcIVNADVPCPHFLSAQG 780
Cdd:cd14004  161 SG-----PFDTFVGTIDYAAPEVLRGNPYGgKEQDIWALGVLLYTLVFKENPFY-----NIEE-ILEADLRIPYAVSEDL 229
                        250
                 ....*....|....*
gi 564339933 781 LELIQKLLQKSPEKR 795
Cdd:cd14004  230 IDLISRMLNRDVGDR 244
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
553-795 6.75e-28

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: 114.46  E-value: 6.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVL-LVQYKGTGKYYAIKALKKQEV----LGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSS 627
Cdd:cd14096    3 YRLINKIGEGAFSNVYkAVPLRNTGKPVAIKVVRKADLssdnLKGSSRANILKEVQIMKRLS---HPNIVKLLDFQESDE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYR-------------DLKLDNLLLDAQ---- 689
Cdd:cd14096   80 YYYIVLELADGGEIFHQIVRlTYFSEDLSRHVITQVASAVKYLHEIGVVHRdikpenllfepipFIPSIVKLRKADddet 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 690 ----------------GFLKIADFGLCKegIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14096  160 kvdegefipgvggggiGIVKLADFGLSK--QVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPF 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564339933 754 PGDTEDEVFECIVNADVPcphFL-------SAQGLELIQKLLQKSPEKR 795
Cdd:cd14096  238 YDESIETLTEKISRGDYT---FLspwwdeiSKSAKDLISHLLTVDPAKR 283
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
559-796 7.12e-28

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: 113.73  E-value: 7.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLL-----VQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVT 633
Cdd:cd14076    9 LGEGEFGKVKLgwplpKANHRSGVQVAIKLIRRDTQQENCQTSKIMREINILKGLT---HPNIVRLLDVLKTKKYIGIVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE-GIGFGDRTS 711
Cdd:cd14076   86 EFVSGGELFDYIlARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfDHFNGDLMS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPE-VLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTED-------EVFECIVNADVPCPHFLSAQGLE 782
Cdd:cd14076  166 TSCGSPCYAAPElVVSDSMYAgRKADIWSCGVILYAMLAGYLPFDDDPHNpngdnvpRLYRYICNTPLIFPEYVTPKARD 245
                        250
                 ....*....|....
gi 564339933 783 LIQKLLQKSPEKRL 796
Cdd:cd14076  246 LLRRILVPNPRKRI 259
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
558-795 7.44e-28

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: 113.57  E-value: 7.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLG---RDEIDSLYCEKRILEtvgrtgHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd14188    8 VLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKphqREKIDKEIELHRILH------HKHVVQFYHYFEDKENIYILLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd14188   82 YCSRRSMAHILKaRKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPE 793
Cdd:cd14188  162 CGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPE 241

                 ..
gi 564339933 794 KR 795
Cdd:cd14188  242 DR 243
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
558-812 1.39e-27

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: 112.33  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVL---GRDEIdslycekRILETVGRT-GHPFLLSLLACI--QTSSHACF 631
Cdd:cd05118    6 KIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHpkaALREI-------KLLKHLNDVeGHPNIVKLLDVFehRGGNHLCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLpGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF-LKIADFGLCKEgigFGD 708
Cdd:cd05118   79 VFELM-GMNLyeLIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGqLKLADFGLARS---FTS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTST-FCGTPEFLAPEV-LTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVnaDVpcphFLSAQGLELIQK 786
Cdd:cd05118  155 PPYTpYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIV--RL----LGTPEALDLLSK 228
                        250       260
                 ....*....|....*....|....*.
gi 564339933 787 LLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd05118  229 MLKYDPAKRI-----TASQALAHPYF 249
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
559-800 2.90e-27

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: 111.55  E-value: 2.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKG----TGKYYAIKALKKqEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd06627    8 IGRGAFGSV----YKGlnlnTGEFVAIKQISL-EKIPKSDLKSVMGEIDLLKKLN---HPNIVKYIGSVKTKDSLYIILE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd06627   80 YVENGSLASIIKKfGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFpgdtedevFE--------CIVNAD-VPCPHFLSAQGLELI 784
Cdd:cd06627  160 VGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPY--------YDlqpmaalfRIVQDDhPPLPENISPELRDFL 231
                        250
                 ....*....|....*.
gi 564339933 785 QKLLQKSPEKRLGAGE 800
Cdd:cd06627  232 LQCFQKDPTLRPSAKE 247
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
552-810 3.05e-27

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: 111.73  E-value: 3.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYcEKRILetvGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAID-EARVL---SKLNSPYVIKYYDSFVDKGKLNI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHEDV---FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd08529   77 VMEYAENGDLHSLIKSQRgrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV-PCPHFLSAQGLELIQKL 787
Cdd:cd08529  157 FAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYpPISASYSQDLSQLIDSC 236
                        250       260
                 ....*....|....*....|...
gi 564339933 788 LQKSPEKRlgageRDAEEIKVQP 810
Cdd:cd08529  237 LTKDYRQR-----PDTTELLRNP 254
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
559-800 4.82e-27

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: 110.96  E-value: 4.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKalkkqEV-LGRDEIDSLYCEKRILETV---GRTGHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd06632    8 LGSGSFGSVYEGFNGDTGDFFAVK-----EVsLVDDDKKSRESVKQLEQEIallSKLRHPNIVQYYGTEREEDNLYIFLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTSTF 713
Cdd:cd06632   83 YVPGGSIHKLLQRyGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKH-VEAFSFAKSF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQE--AYTRAVDWWGLGVLLYEMLVGECPFpGDTE--DEVFECIVNADVP-CPHFLSAQGLELIQKLL 788
Cdd:cd06632  162 KGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPW-SQYEgvAAIFKIGNSGELPpIPDHLSPDAKDFIRLCL 240
                        250
                 ....*....|..
gi 564339933 789 QKSPEKRLGAGE 800
Cdd:cd06632  241 QRDPEDRPTASQ 252
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
551-800 5.62e-27

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: 111.18  E-value: 5.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlGRDEIDSLycEKRIletvgrtghpFLLSLLACIQ-TSSHA 629
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE--AEDEIEDI--QQEI----------QFLSQCDSPYiTKYYG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CF--------VTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK 701
Cdd:cd06609   67 SFlkgsklwiIMEYCGGGSVLDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 EGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPC--PHFLSAQ 779
Cdd:cd06609  147 QLTSTMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSleGNKFSKP 226
                        250       260
                 ....*....|....*....|.
gi 564339933 780 GLELIQKLLQKSPEKRLGAGE 800
Cdd:cd06609  227 FKDFVELCLNKDPKERPSAKE 247
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
559-812 6.82e-27

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: 110.44  E-value: 6.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtVGRtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14079   10 LGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILK-LFR--HPHIIRLYEVIETPTDIFMVMEYVSG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC---KEGIGFgdRTStfC 714
Cdd:cd14079   87 GELFDYIVQkGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSnimRDGEFL--KTS--C 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRA-VDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPE 793
Cdd:cd14079  163 GSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPL 242
                        250
                 ....*....|....*....
gi 564339933 794 KRLgagerDAEEIKVQPFF 812
Cdd:cd14079  243 KRI-----TIPEIRQHPWF 256
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
559-796 8.09e-27

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: 110.88  E-value: 8.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEV------LGRDEIDSlycEKRILETVGrtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd14194   13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkssrrgVSREDIER---EVSILKEIQ---HPNVITLHEVYENKTDVILI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF----LKIADFGLCKEgIGFG 707
Cdd:cd14194   87 LELVAGGELFDFLAEkESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHK-IDFG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI--VNADVPCPHFLSAQGL--EL 783
Cdd:cd14194  166 NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVsaVNYEFEDEYFSNTSALakDF 245
                        250
                 ....*....|...
gi 564339933 784 IQKLLQKSPEKRL 796
Cdd:cd14194  246 IRRLLVKDPKKRM 258
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
551-795 1.12e-26

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: 110.05  E-value: 1.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrdEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd06612    3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEE-----DLQEIIKEISILK---QCDSPYIVKYYGSYFKNTDLW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd06612   75 IVMEYCGAGSVsdIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPC---PHFLSAQGLELIQ 785
Cdd:cd06612  155 KRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTlsdPEKWSPEFNDFVK 234
                        250
                 ....*....|
gi 564339933 786 KLLQKSPEKR 795
Cdd:cd06612  235 KCLVKDPEER 244
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
556-795 1.28e-26

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: 109.66  E-value: 1.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQyKGTGKYYAIKALKKQEVlgRDEIDSLYCEKRIlETVGRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd14161    8 LETLGKGTYGRVKKAR-DSSGRLVAIKSIRKDRI--KDEQDLLHIRREI-EIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLckEGIGFGDR-TSTF 713
Cdd:cd14161   84 ASRGDLYDYISErQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGL--SNLYNQDKfLQTY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSaQGLELIQKLLQKSP 792
Cdd:cd14161  162 CGSPLYASPEIVNGRPYIgPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLIRWLLMVNP 240

                 ...
gi 564339933 793 EKR 795
Cdd:cd14161  241 ERR 243
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
559-811 2.31e-26

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: 110.04  E-value: 2.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGR-----------------------DEIDSLYCEKRILEtvgRTGHPF 615
Cdd:cd14200    8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgeqakplAPLERVYQEIAILK---KLDHVN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 616 LLSLLACIQ--TSSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLK 693
Cdd:cd14200   85 IVKLIEVLDdpAEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 694 IADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLT---QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV 770
Cdd:cd14200  165 IADFGVSNQFEGNDALLSSTAGTPAFMAPETLSdsgQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPV 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564339933 771 PCPH--FLSAQGLELIQKLLQKSPEKRLGagerdAEEIKVQPF 811
Cdd:cd14200  245 EFPEepEISEELKDLILKMLDKNPETRIT-----VPEIKVHPW 282
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
559-795 2.54e-26

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: 109.13  E-value: 2.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALK--KQEVLGRDEidslycEKRILETVGRTGHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd08218    8 IGEGSFGKALLVKSKEDGKQYVIKEINisKMSPKEREE------SRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHED---VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd08218   82 DGGDLYKRINAQrgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF-PGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSP 792
Cdd:cd08218  162 IGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFeAGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRNP 241

                 ...
gi 564339933 793 EKR 795
Cdd:cd08218  242 RDR 244
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
557-800 3.01e-26

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: 109.18  E-value: 3.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 557 AVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd14097    7 RKLGQGSFGVVIEATHKETQTKWAIKKINREKA-GSSAVKLLEREVDILKHVN---HAHIIHLEEVFETPKRMYLVMELC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDL-MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYR-------DLKLDNLLLDAQGFLKIADFGLCKEGIGFG- 707
Cdd:cd14097   83 EDGELkELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRdlkleniLVKSSIIDNNDKLNIKVTDFGLSVQKYGLGe 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHF----LSAQGLEL 783
Cdd:cd14097  163 DMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSvwqsVSDAAKNV 242
                        250
                 ....*....|....*..
gi 564339933 784 IQKLLQKSPEKRLGAGE 800
Cdd:cd14097  243 LQQLLKVDPAHRMTASE 259
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
551-795 3.75e-26

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: 108.24  E-value: 3.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlgRDEIDSLYCEKRIlETVGRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd14073    1 HRYELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKI--EDEQDMVRIRREI-EIMSSLNHPHIIRIYEVFENKDKIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFGDR 709
Cdd:cd14073   78 IVMEYASGGELYDYISErRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNL---YSKD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 T--STFCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLS-AQGleLIQ 785
Cdd:cd14073  155 KllQTFCGSPLYASPEIVNGTPYQgPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPSdASG--LIR 232
                        250
                 ....*....|
gi 564339933 786 KLLQKSPEKR 795
Cdd:cd14073  233 WMLTVNPKRR 242
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
559-811 5.60e-26

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: 108.90  E-value: 5.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVL-----------------------GRDEIDSLYCEKRILEtvgRTGHPF 615
Cdd:cd14199   10 IGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMrqagfprrppprgaraapegctqPRGPIERVYQEIAILK---KLDHPN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 616 LLSLLACIQTSS--HACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLK 693
Cdd:cd14199   87 VVKLVEVLDDPSedHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 694 IADFGLCKEGIGFGDRTSTFCGTPEFLAPEVL--TQEAYT-RAVDWWGLGVLLYEMLVGECPFpgdtEDEVFECIVNA-- 768
Cdd:cd14199  167 IADFGVSNEFEGSDALLTNTVGTPAFMAPETLseTRKIFSgKALDVWAMGVTLYCFVFGQCPF----MDERILSLHSKik 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 564339933 769 ----DVPCPHFLSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPF 811
Cdd:cd14199  243 tqplEFPDQPDISDDLKDLLFRMLDKNPESRI-----SVPEIKLHPW 284
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
559-800 6.19e-26

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 108.66  E-value: 6.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDeIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14086    9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARD-HQKLEREARICRLLK---HPNIVRLHDSISEEGFHYLVFDLVTG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ---GFLKIADFGLCKEGIGFGDRTSTFC 714
Cdd:cd14086   85 GELFEDIvAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKskgAAVKLADFGLAIEVQGDQQAWFGFA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA--DVPCPHF--LSAQGLELIQKLLQK 790
Cdd:cd14086  165 GTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGayDYPSPEWdtVTPEAKDLINQMLTV 244
                        250
                 ....*....|
gi 564339933 791 SPEKRLGAGE 800
Cdd:cd14086  245 NPAKRITAAE 254
HR1_PKN_2 cd11623
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
98-162 8.55e-26

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that 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 cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212013  Cd Length: 71  Bit Score: 101.16  E-value: 8.55e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339933  98 EQSRARLLEALHRQLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKIS 162
Cdd:cd11623    1 ENAQNSRLAGLEKQLNIELKVKQGAENMIQMYSNGKSKDRKLLAEAQQMLEDSKAKIEFLRMQIL 65
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
556-812 1.21e-25

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: 106.91  E-value: 1.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKkqevLGRDEIDSLYCEKRILETvgrTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd06614    5 LEKIGEGASGEVYKATDRATGKEVAIKKMR----LRKQNKELIINEILIMKE---CKHPNIVDYYDSYLVGDELWVVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd06614   78 MDGGSLtdIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNSV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP---CPHFLSAQGLELIQKLLQK 790
Cdd:cd06614  158 VGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPplkNPEKWSPEFKDFLNKCLVK 237
                        250       260
                 ....*....|....*....|..
gi 564339933 791 SPEKRLgagerDAEEIKVQPFF 812
Cdd:cd06614  238 DPEKRP-----SAEELLQHPFL 254
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
559-795 2.47e-25

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: 106.17  E-value: 2.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLA---HQHVVGFHGFFEDNDFVYVVLELCRR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMmQIHE--DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd14187   92 RSLL-ELHKrrKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLCGT 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd14187  171 PNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 249
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
559-796 2.55e-25

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: 106.63  E-value: 2.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEV------LGRDEIDSlycEKRILETVGrtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd14195   13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLsssrrgVSREEIER---EVNILREIQ---HPNIITLHDIFENKTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF----LKIADFGLCKEgIGFG 707
Cdd:cd14195   87 LELVSGGELFDFLAEkESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIAHK-IEAG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI--VNADVPCPHFLSAQGL--EL 783
Cdd:cd14195  166 NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNIsaVNYDFDEEYFSNTSELakDF 245
                        250
                 ....*....|...
gi 564339933 784 IQKLLQKSPEKRL 796
Cdd:cd14195  246 IRRLLVKDPKKRM 258
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
552-798 3.30e-25

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: 105.83  E-value: 3.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKkqevLGRDEIDSLYCEKRILeTVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIR----LPKSSSAVEDSRKEAV-LLAKMKHPNIVAFKESFEADGHLYI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHED---VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd08219   76 VMEYCDGGDLMQKIKLQrgkLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV-PCPHFLSAQGLELIQKL 787
Cdd:cd08219  156 YACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYkPLPSHYSYELRSLIKQM 235
                        250
                 ....*....|.
gi 564339933 788 LQKSPEKRLGA 798
Cdd:cd08219  236 FKRNPRSRPSA 246
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
558-800 3.85e-25

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: 106.86  E-value: 3.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKAL-----KKQEVLGRDEIDSlycEKRILETVGrtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd14094   10 VIGKGPFSVVRRCIHRETGQQFAVKIVdvakfTSSPGLSTEDLKR---EASICHMLK---HPHIVELLETYSSDGMLYMV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHED-----VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ---GFLKIADFGLCKEGI 704
Cdd:cd14094   84 FEFMDGADLCFEIVKRadagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDeVFECIVNADVP-----CPHfLSAQ 779
Cdd:cd14094  164 ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKmnprqWSH-ISES 241
                        250       260
                 ....*....|....*....|.
gi 564339933 780 GLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14094  242 AKDLVRRMLMLDPAERITVYE 262
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
559-800 4.64e-25

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: 106.27  E-value: 4.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGkyyAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd06644   20 LGDGAFGKVYKAKNKETG---ALAAAKVIETKSEEELEDYMVEIEILATCN---HPYIVKLLGAFYWDGKLWIMIEFCPG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 G--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd06644   94 GavDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEA-----YTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP---CPHFLSAQGLELIQKLL 788
Cdd:cd06644  174 PYWMAPEVVMCETmkdtpYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPtlsQPSKWSMEFRDFLKTAL 253
                        250
                 ....*....|..
gi 564339933 789 QKSPEKRLGAGE 800
Cdd:cd06644  254 DKHPETRPSAAQ 265
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
558-812 5.22e-25

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 105.51  E-value: 5.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIK-----ALKKQEVLGRDEIDSLYCEKRILETVgrTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd14093   10 ILGRGVSSTVRRCIEKETGQEFAVKiiditGEKSSENEAEELREATRREIEILRQV--SGHPNIIELHDVFESPTFIFLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTS 711
Cdd:cd14093   88 FELCRKGELFDYLTEVVtLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR-LDEGEKLR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVL------TQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNAD--VPCPHF--LSAQGL 781
Cdd:cd14093  167 ELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKyeFGSPEWddISDTAK 246
                        250       260       270
                 ....*....|....*....|....*....|.
gi 564339933 782 ELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14093  247 DLISKLLVVDPKKRL-----TAEEALEHPFF 272
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
559-798 6.31e-25

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: 106.06  E-value: 6.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQevlgrdeidslyCEKRILET-VG---RTGHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd14085   11 LGRGATSVVYRCRQKGTQKPYAVKKLKKT------------VDKKIVRTeIGvllRLSHPNIIKLKEIFETPTEISLVLE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF---LKIADFGLCKEgIGFGDRT 710
Cdd:cd14085   79 LVTGGELFDRIVEKgYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKI-VDQQVTM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDE-VFECIVNADV----PCPHFLSAQGLELIQ 785
Cdd:cd14085  158 KTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQyMFKRILNCDYdfvsPWWDDVSLNAKDLVK 237
                        250
                 ....*....|...
gi 564339933 786 KLLQKSPEKRLGA 798
Cdd:cd14085  238 KLIVLDPKKRLTT 250
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
559-795 8.54e-25

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: 104.51  E-value: 8.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEI-DSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14070   10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVtKNLRREGRIQQMIR---HPNITQLLDILETENSYYLVMELCP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL--CKEGIGFGDRTSTFC 714
Cdd:cd14070   87 GGNLMHRIYDKKrLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLsnCAGILGYSDPFSTQC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGD--TEDEVFECIVNADV-PCPHFLSAQGLELIQKLLQKS 791
Cdd:cd14070  167 GSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMnPLPTDLSPGAISFLRSLLEPD 246

                 ....
gi 564339933 792 PEKR 795
Cdd:cd14070  247 PLKR 250
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
559-798 1.18e-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: 105.11  E-value: 1.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDslycekrILETVGRtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14175    9 IGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIE-------ILLRYGQ--HPNIITLKDVYDDGKHVYLVTELMRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG----FLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd14175   80 GELLDKIlRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGFAKQLRAENGLLMTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF---PGDTEDEVFECIVNADVPCP----HFLSAQGLELIQK 786
Cdd:cd14175  160 CYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSggnwNTVSDAAKDLVSK 239
                        250
                 ....*....|..
gi 564339933 787 LLQKSPEKRLGA 798
Cdd:cd14175  240 MLHVDPHQRLTA 251
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
558-797 1.64e-24

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: 103.63  E-value: 1.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14071    7 TIGKGNFAVVKLARHRITKTEVAIKIIDKSQ-LDEENLKKIYREVQIMKMLN---HPHIIKLYQVMETKDMLYLVTEYAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLckeGIGF--GDRTSTFC 714
Cdd:cd14071   83 NGEIFDYLaQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGF---SNFFkpGELLKTWC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPE 793
Cdd:cd14071  160 GSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPS 239

                 ....
gi 564339933 794 KRLG 797
Cdd:cd14071  240 KRLT 243
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
558-795 1.99e-24

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: 103.40  E-value: 1.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   558 VLGRGHFGKVLLVQYKGTGKYY----AIKALKKQEvlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVT 633
Cdd:smart00221   6 KLGEGAFGEVYKGTLKGKGDGKevevAVKTLKEDA--SEQQIEEFLREARIMRKLD---HPNIVKLLGVCTEEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   634 EFLPGGDL---MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRdlkldnllldaqgFL-------------KIADF 697
Cdd:smart00221  81 EYMPGGDLldyLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHR-------------DLaarnclvgenlvvKISDF 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   698 GLCKEGigfGDRTSTFCGTPEF----LAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNADV-P 771
Cdd:smart00221 148 GLSRDL---YDDDYYKVKGGKLpirwMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLKKGYRlP 224
                          250       260
                   ....*....|....*....|....
gi 564339933   772 CPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:smart00221 225 KPPNCPPELYKLMLQCWAEDPEDR 248
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
559-800 2.42e-24

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: 103.48  E-value: 2.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlGRDEIDSLYCEKRILETVgrTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14197   17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRK-GQDCRMEIIHEIAVLELA--QANPWVINLHEVYETASEMILVLEYAAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQI---HEDVFPEPQACFYLACVVLGLQFLHEKRIIY---RDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTST 712
Cdd:cd14197   94 GEIFNQCvadREEAFKEKDVKRLMKQILEGVSFLHNNNVVHldlKPQNILLTSESPLGDIKIVDFGLSRI-LKNSEELRE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 713 FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCP----HFLSAQGLELIQKLL 788
Cdd:cd14197  173 IMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSeeefEHLSESAIDFIKTLL 252
                        250
                 ....*....|..
gi 564339933 789 QKSPEKRLGAGE 800
Cdd:cd14197  253 IKKPENRATAED 264
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
558-795 3.00e-24

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 102.99  E-value: 3.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   558 VLGRGHFGKVLLVQYKGTGKYY----AIKALKKQEvlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVT 633
Cdd:smart00219   6 KLGEGAFGEVYKGKLKGKGGKKkvevAVKTLKEDA--SEQQIEEFLREARIMRKLD---HPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   634 EFLPGGDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRdlkldnllldaqgFL-------------KIADFG 698
Cdd:smart00219  81 EYMEGGDLLsyLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHR-------------DLaarnclvgenlvvKISDFG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933   699 LCKEgiGFGDRTSTFCGTPE---FLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNADV-PCP 773
Cdd:smart00219 148 LSRD--LYDDDYYRKRGGKLpirWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLKNGYRlPQP 225
                          250       260
                   ....*....|....*....|..
gi 564339933   774 HFLSAQGLELIQKLLQKSPEKR 795
Cdd:smart00219 226 PNCPPELYDLMLQCWAEDPEDR 247
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
552-797 3.32e-24

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: 102.91  E-value: 3.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIK-------ALKKQEVLGRDEIDsLYCEKR-----ILETVGRtgHPFLLSL 619
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKiiprasnAGLKKEREKRLEKE-ISRDIRtireaALSSLLN--HPHICRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 620 LACIQTSSHACFVTEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG 698
Cdd:cd14077   79 RDFLRTPNHYYMLFEYVDGGQLLdYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 LcKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLS 777
Cdd:cd14077  159 L-SNLYDPRRLLRTFCGSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLS 237
                        250       260
                 ....*....|....*....|
gi 564339933 778 AQGLELIQKLLQKSPEKRLG 797
Cdd:cd14077  238 SECKSLISRMLVVDPKKRAT 257
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
553-795 6.50e-24

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: 101.96  E-value: 6.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSlyceKRILETVGRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEAS----KKEVILLAKMKHPNIVTFFASFQENGRLFIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQI---HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFL-KIADFGLCKEGIGFGD 708
Cdd:cd08225   78 MEYCDGGDLMKRInrqRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSME 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP--CPHFlSAQGLELIQK 786
Cdd:cd08225  158 LAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFApiSPNF-SRDLRSLISQ 236

                 ....*....
gi 564339933 787 LLQKSPEKR 795
Cdd:cd08225  237 LFKVSPRDR 245
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
559-800 7.77e-24

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: 102.51  E-value: 7.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd06611   13 LGDGAFGKVYKAQHKETGLFAAAKIIQIES---EEELEDFMVEIDILSECK---HPNIVGLYEAYFYENKLWILIEFCDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 G--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd06611   87 GalDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQE-----AYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPC---PHFLSAQGLELIQKLL 788
Cdd:cd06611  167 PYWMAPEVVACEtfkdnPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTldqPSKWSSSFNDFLKSCL 246
                        250
                 ....*....|..
gi 564339933 789 QKSPEKRLGAGE 800
Cdd:cd06611  247 VKDPDDRPTAAE 258
HR1_PKN3_3 cd11637
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
168-226 9.03e-24

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3; PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the third HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC.


Pssm-ID: 212027  Cd Length: 74  Bit Score: 95.31  E-value: 9.03e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 168 GSPEPGPDLLAEELQHRLRIEAAVAAGAKNVVKLLGGQRIQDRKALAEAQAQLQESSQK 226
Cdd:cd11637    1 GRPMSAPELRVEELRHHLRIEAAVAEGAKNVVKLLGGRRFQDRKILAEAQARLQESSQK 59
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
558-795 9.75e-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: 101.42  E-value: 9.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  558 VLGRGHFGKVLLVQYKGTGKYY----AIKALKKQevLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHACFVT 633
Cdd:pfam07714   6 KLGEGAFGEVYKGTLKGEGENTkikvAVKTLKEG--ADEEEREDFLEEASIM---KKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  634 EFLPGGDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLkldnllldA--------QGFLKIADFGLCKEG 703
Cdd:pfam07714  81 EYMPGGDLLdfLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDL--------AarnclvseNLVVKISDFGLSRDI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  704 IGFGD-RTSTFCGTPEF-LAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNADV-PCPHFLSAQ 779
Cdd:pfam07714 153 YDDDYyRKRGGGKLPIKwMAPESLKDGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLEDGYRlPQPENCPDE 232
                         250
                  ....*....|....*.
gi 564339933  780 GLELIQKLLQKSPEKR 795
Cdd:pfam07714 233 LYDLMKQCWAYDPEDR 248
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
559-796 1.62e-23

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: 100.83  E-value: 1.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYK-----GTGKYYAIKALKKQEvLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVT 633
Cdd:cd14121    3 LGSGTYATV----YKayrksGAREVVAVKCVSKSS-LNKASTENLLTEIELLKKLK---HPHIVELKDFQWDEEHIYLIM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYR--DLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRT 710
Cdd:cd14121   75 EYCSGGDLSRFIRSRrTLPESTVRRFLQQLASALQFLREHNISHMdlKPQNLLLSSRYNPVLKLADFGFAQH-LKPNDEA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNAD---VPCPHFLSAQGLELIQKL 787
Cdd:cd14121  154 HSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpieIPTRPELSADCRDLLLRL 233

                 ....*....
gi 564339933 788 LQKSPEKRL 796
Cdd:cd14121  234 LQRDPDRRI 242
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
558-795 2.10e-23

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: 100.69  E-value: 2.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYY---AIKALKKQEVlgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd00192    2 KLGEGAFGEVYKGKLKGGDGKTvdvAVKTLKEDAS--ESERKDFLKEARVMKKLG---HPNVVRLLGVCTEEEPLYLVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDL--MMQIHEDVFPEPQA-----------CFYLACvvlGLQFLHEKRIIYRDLkldnllldA--------QGFLK 693
Cdd:cd00192   77 YMEGGDLldFLRKSRPVFPSPEPstlslkdllsfAIQIAK---GMEYLASKKFVHRDL--------AarnclvgeDLVVK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 694 IADFGLCKEG-IGFGDRTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNADV 770
Cdd:cd00192  146 ISDFGLSRDIyDDDYYRKKTGGKLPiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKGYR 225
                        250       260
                 ....*....|....*....|....*.
gi 564339933 771 -PCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd00192  226 lPKPENCPDELYELMLSCWQLDPEDR 251
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
545-800 5.69e-23

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: 101.25  E-value: 5.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 545 RNPPQLQD-FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgRDEIDslycEKRILETVGRtgHPFLLSLLACI 623
Cdd:cd14176   12 RNSIQFTDgYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTE----EIEILLRYGQ--HPNIITLKDVY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 624 QTSSHACFVTEFLPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG----FLKIADFG 698
Cdd:cd14176   83 DDGKYVYVVTELMKGGELLDKIlRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 LCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF---PGDTEDEVFECIVNADVPCP-- 773
Cdd:cd14176  163 FAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSgg 242
                        250       260
                 ....*....|....*....|....*....
gi 564339933 774 --HFLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14176  243 ywNSVSDTAKDLVSKMLHVDPHQRLTAAL 271
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
652-796 7.69e-23

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: 98.85  E-value: 7.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 652 EPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYT 731
Cdd:cd14189  100 EPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICGTPNYLAPEVLLRQGHG 179
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 732 RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd14189  180 PESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRL 244
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
558-800 1.17e-22

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 98.45  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQevlGRDEIDSLYCEkriLETVGRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14190   11 VLGGGKFGKVHTCTEKRTGLKLAAKVINKQ---NSKDKEMVLLE---IQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHEDVFP--EPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG--FLKIADFGLCKEgIGFGDRTSTF 713
Cdd:cd14190   85 GGELFERIVDEDYHltEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTghQVKIIDFGLARR-YNPREKLKVN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA----DVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd14190  164 FGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGnwyfDEETFEHVSDEAKDFVSNLII 243
                        250
                 ....*....|.
gi 564339933 790 KSPEKRLGAGE 800
Cdd:cd14190  244 KERSARMSATQ 254
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
631-795 1.22e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 102.40  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHEDV-----FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE--- 702
Cdd:PTZ00267 142 LIMEYGSGGDLNKQIKQRLkehlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQysd 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 703 GIGFgDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIV--NADvPCPHFLSAQG 780
Cdd:PTZ00267 222 SVSL-DVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLygKYD-PFPCPVSSGM 299
                        170
                 ....*....|....*
gi 564339933 781 LELIQKLLQKSPEKR 795
Cdd:PTZ00267 300 KALLDPLLSKNPALR 314
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
558-812 1.89e-22

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: 98.12  E-value: 1.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALK-KQEVLGRDEID----SLYCEKRILETVgrTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd14181   17 VIGRGVSSVVRRCVHRHTGQEFAVKIIEvTAERLSPEQLEevrsSTLKEIHILRQV--SGHPSIITLIDSYESSTFIFLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL-CKegIGFGDRT 710
Cdd:cd14181   95 FDLMRRGELFDYLTEKVtLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFsCH--LEPGEKL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVL------TQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA--DVPCPHF--LSAQG 780
Cdd:cd14181  173 RELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGryQFSSPEWddRSSTV 252
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564339933 781 LELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14181  253 KDLISRLLVVDPEIRL-----TAEQALQHPFF 279
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
559-800 2.39e-22

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: 97.27  E-value: 2.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKkqevLGRDEIDSLYCEKRILetvGRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14107   10 IGRGTFGFVKRVTHKGNGECCAAKFIP----LRSSTRARAFQERDIL---ARLSHRRLTCLLDQFETRKTLILILELCSS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYR--DLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFcG 715
Cdd:cd14107   83 EELLDRLFlKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLdiKPDNILMVSPTREDIKICDFGFAQEITPSEHQFSKY-G 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED----EVFECIVNADVPCPHFLSAQGLELIQKLLQKS 791
Cdd:cd14107  162 SPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRatllNVAEGVVSWDTPEITHLSEDAKDFIKRVLQPD 241

                 ....*....
gi 564339933 792 PEKRLGAGE 800
Cdd:cd14107  242 PEKRPSASE 250
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
559-800 2.46e-22

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: 97.27  E-value: 2.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIdslyceKRILETVGRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14114   10 LGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETV------RKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHED--VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ--GFLKIADFGLCKEgIGFGDRTSTFC 714
Cdd:cd14114   84 GELFERIAAEhyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKrsNEVKLIDFGLATH-LDPKESVKVTT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDE----VFECIVNADVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd14114  163 GTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDEtlrnVKSCDWNFDDSAFSGISEEAKDFIRKLLLA 242
                        250
                 ....*....|
gi 564339933 791 SPEKRLGAGE 800
Cdd:cd14114  243 DPNKRMTIHQ 252
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
551-812 2.72e-22

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: 97.42  E-value: 2.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALkkqevlgRDEIDSLYcEKRI---LETVGRTGHPFLLSLLACIQTSS 627
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVI-------RLEIDEAL-QKQIlreLDVLHKCNSPYIVGFYGAFYSEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGGDLMmQIHEDV--FPEPQACFYLACVVLGLQFLHEKR-IIYRDLKLDNLLLDAQGFLKIADFGLCKEGI 704
Cdd:cd06605   73 DISICMEYMDGGSLD-KILKEVgrIPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQLV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GfgDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED------EVFECIVNADVP-CP-HFL 776
Cdd:cd06605  152 D--SLAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifELLSYIVDEPPPlLPsGKF 229
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564339933 777 SAQGLELIQKLLQKSPEKRlgageRDAEEIKVQPFF 812
Cdd:cd06605  230 SPDFQDFVSQCLQKDPTER-----PSYKELMEHPFI 260
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
558-800 3.33e-22

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: 97.02  E-value: 3.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIdsLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14184    8 VIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHL--IENEVSILR---RVKHPNIIMLIEEMDTPAELYLVMELVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLL----LDAQGFLKIADFGLCK--EGIGFgdrt 710
Cdd:cd14184   83 GGDLFDAITSSTkYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLvceyPDGTKSLKLGDFGLATvvEGPLY---- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 sTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDT--EDEVFECIV--NADVPCPHF--LSAQGLELI 784
Cdd:cd14184  159 -TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILlgKLEFPSPYWdnITDSAKELI 237
                        250
                 ....*....|....*.
gi 564339933 785 QKLLQKSPEKRLGAGE 800
Cdd:cd14184  238 SHMLQVNVEARYTAEQ 253
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
558-800 5.79e-22

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 97.10  E-value: 5.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGR----DEIDSLY-CEkriletvgrtGHPFLLSLLACIQTSSHACFV 632
Cdd:cd14090    9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRsrvfREVETLHqCQ----------GHPNILQLIEYFEDDERFYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF---LKIADFGLcKEGIGFGD 708
Cdd:cd14090   79 FEKMRGGPLLSHIEKRVhFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDL-GSGIKLSS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTS---------TFCGTPEFLAPEVL---TQEA--YTRAVDWWGLGVLLYEMLVGECPFPG---------------DTED 759
Cdd:cd14090  158 TSMtpvttpellTPVGSAEYMAPEVVdafVGEAlsYDKRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdrgeacqDCQE 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564339933 760 EVFECIVNADVPCP----HFLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14090  238 LLFHSIQEGEYEFPekewSHISAEAKDLISHLLVRDASQRYTAEQ 282
HR1_PKN1_2 cd11630
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
95-161 6.46e-22

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


Pssm-ID: 212020  Cd Length: 78  Bit Score: 90.47  E-value: 6.46e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933  95 PRAEQSRarlLEALHRQLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKI 161
Cdd:cd11630    3 SAANQSR---IAGLEKQLNIELKVKQGAENMIQTYANGSTKDRKLLQTAQQMLQDSKTKIDIIRMQI 66
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
559-796 7.33e-22

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: 96.23  E-value: 7.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALK----KQEVLGRDEIDSLYCekriletvgrTGHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd14191   10 LGSGKFGQVFRLVEKKTKKVWAGKFFKaysaKEKENIRQEISIMNC----------LHHPKLVQCVDAFEEKANIVMVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIHEDVF--PEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ--GFLKIADFGLCKEGIGFGDRT 710
Cdd:cd14191   80 MVSGGELFERIIDEDFelTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTKIKLIDFGLARRLENAGSLK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFcGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA--DVPCPHF--LSAQGLELIQK 786
Cdd:cd14191  160 VLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSAtwDFDDEAFdeISDDAKDFISN 238
                        250
                 ....*....|
gi 564339933 787 LLQKSPEKRL 796
Cdd:cd14191  239 LLKKDMKARL 248
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
557-800 1.79e-21

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: 95.29  E-value: 1.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 557 AVLGRGHFGKVLLVQYKGTGKYYAIKALK------KQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHAC 630
Cdd:cd06628    6 ALIGSGSFGSVYLGMNASSGELMAVKQVElpsvsaENKDRKKSMLDALQREIALLRELQ---HENIVQYLGSSSDANHLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE------G 703
Cdd:cd06628   83 IFLEYVPGGSVATLLNNyGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKleanslS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 704 IGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVPCPHFLSAQGLE 782
Cdd:cd06628  163 TKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQmQAIFKIGENASPTIPSNISSEARD 242
                        250
                 ....*....|....*...
gi 564339933 783 LIQKLLQKSPEKRLGAGE 800
Cdd:cd06628  243 FLEKTFEIDHNKRPTADE 260
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
558-812 2.03e-21

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: 94.67  E-value: 2.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKK--------QEVLGRdEIDSLycekRILEtvgrtgHPFLLSLLACIQTSSHA 629
Cdd:cd14162    7 TLGHGSYAVVKKAYSTKHKCKVAIKIVSKkkapedylQKFLPR-EIEVI----KGLK------HPNLICFYEAIETTSRV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIHEDVF-PEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI---- 704
Cdd:cd14162   76 YIIMELAENGDLLDYIRKNGAlPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMktkd 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFpGDTEDEVFECIVNADV--PCPHFLSAQGL 781
Cdd:cd14162  156 GKPKLSETYCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLPF-DDSNLKVLLKQVQRRVvfPKNPTVSEECK 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 564339933 782 ELIQKLLQKSPeKRLgagerDAEEIKVQPFF 812
Cdd:cd14162  235 DLILRMLSPVK-KRI-----TIEEIKRDPWF 259
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
557-747 2.27e-21

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: 94.73  E-value: 2.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 557 AVLGRGHFGKVLLVQYKGTGKYYAIKA--LKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd06625    6 KLLGQGAFGQVYLCYDADTGRELAVKQveIDPINTEASKEVKALECEIQLLKNLQ---HERIVQYYGCLQDEKSLSIFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK--EGIGFGDRTS 711
Cdd:cd06625   83 YMPGGSVKDEIKAyGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTICSSTGMK 162
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564339933 712 TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd06625  163 SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEML 198
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
558-798 2.77e-21

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: 94.26  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIdslyceKRILETVGRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14192   11 VLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEV------KNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHEDVF--PEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ--GFLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd14192   85 GGELFDRITDESYqlTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNStgNQIKIIDFGLARRYKPREKLKVNF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 cGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA----DVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd14192  165 -GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCkwdfDAEAFENLSEEAKDFISRLLV 243

                 ....*....
gi 564339933 790 KSPEKRLGA 798
Cdd:cd14192  244 KEKSCRMSA 252
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
549-796 2.86e-21

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: 94.64  E-value: 2.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLA-VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEV------LGRDEIDSlycEKRILETVGrtgHPFLLSLLA 621
Cdd:cd14196    2 KVEDFYDIGeELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVL---HPNIITLHD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 CIQTSSHACFVTEFLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF----LKIAD 696
Cdd:cd14196   76 VYENRTDVVLILELVSGGELFdFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLID 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 697 FGLCKEgIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI--VNADVPCPH 774
Cdd:cd14196  156 FGLAHE-IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItaVSYDFDEEF 234
                        250       260
                 ....*....|....*....|....
gi 564339933 775 FLSAQGL--ELIQKLLQKSPEKRL 796
Cdd:cd14196  235 FSHTSELakDFIRKLLVKETRKRL 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
559-812 3.36e-21

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: 93.86  E-value: 3.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVL----GRDEIDSlycEKRILEtvgRTGHPFLLSLLACIQT--SSHACFV 632
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRripnGEANVKR---EIQILR---RLNHRNVIKLVDVLYNeeKQKLYMV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGF--GD 708
Cdd:cd14119   75 MEYCVGGlqEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFaeDD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLT-QEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQK 786
Cdd:cd14119  155 TCTTSQGSPAFQPPEIANgQDSFSgFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRG 234
                        250       260
                 ....*....|....*....|....*.
gi 564339933 787 LLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14119  235 MLEKDPEKRF-----TIEQIRQHPWF 255
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
559-800 3.55e-21

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: 94.30  E-value: 3.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQ--YKGTGKYYAIKALKKQ--EVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHA-CFVT 633
Cdd:cd13994    1 IGKGATSVVRIVTkkNPRSGVLYAVKEYRRRddESKRKDYVKRLTSEYIISSKLH---HPNIVKVLDLCQDLHGKwCLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHEDVFPEPQA--CFYLAcVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTS 711
Cdd:cd13994   78 EYCPGGDLFTLIEKADSLSLEEkdCFFKQ-ILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEKES 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TF----CGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPF--PGDTEDEVFECIVNADVPCPHFLSAQGL--- 781
Cdd:cd13994  157 PMsaglCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWrsAKKSDSAYKAYEKSGDFTNGPYEPIENLlps 236
                        250       260
                 ....*....|....*....|..
gi 564339933 782 ---ELIQKLLQKSPEKRLGAGE 800
Cdd:cd13994  237 ecrRLIYRMLHPDPEKRITIDE 258
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
559-796 3.80e-21

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: 95.06  E-value: 3.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQevlgrdeIDSLyCEKRILETVgrTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14092   14 LGDGSFSVCRKCVHKKTGQEFAVKIVSRR-------LDTS-REVQLLRLC--QGHPNIVKLHEVFQDELHTYLVMELLRG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF---LKIADFGLCKEGIGfGDRTSTFC 714
Cdd:cd14092   84 GELLERIRKkKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDdaeIKIVDFGFARLKPE-NQPLKTPC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVL----TQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED----EVFECIVNADV----PCPHFLSAQGLE 782
Cdd:cd14092  163 FTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSGDFsfdgEEWKNVSSEAKS 242
                        250
                 ....*....|....
gi 564339933 783 LIQKLLQKSPEKRL 796
Cdd:cd14092  243 LIQGLLTVDPSKRL 256
HR1_PKN2_2 cd11631
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
96-167 5.81e-21

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2; PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the second HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation.


Pssm-ID: 212021  Cd Length: 74  Bit Score: 87.44  E-value: 5.81e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933  96 RAEQSRARLLEALHRQLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKIsgLEAS 167
Cdd:cd11631    2 TRMSTNNNRLMALKKQLDIELKVKQGAENMIQMYSNGSSKDRKLLATAQQMLQDSKTKIEVIRMQI--LQAV 71
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
553-800 8.54e-21

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: 93.02  E-value: 8.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYK--GTGKYYAIKALKKQEVlGRDEIdslycEK---RILETVGRTGHPFLLSLLACIQTSS 627
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTksGLKEKVACKIIDKKKA-PKDFL-----EKflpRELEILRKLRHPNIIQVYSIFERGS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGF 706
Cdd:cd14080   76 KVFIFMEYAEHGDLLEYIqKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARL-CPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDR---TSTFCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV---PCPHFLSAQ 779
Cdd:cd14080  155 DDGdvlSKTFCGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVrfpSSVKKLSPE 234
                        250       260
                 ....*....|....*....|.
gi 564339933 780 GLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14080  235 CKDLIDQLLEPDPTKRATIEE 255
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
558-796 1.26e-20

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: 93.57  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKAL-KKQEVLGRDEIDSL-YCEkriletvgrtGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd14179   14 PLGEGSFSICRKCLHKKTNQEYAVKIVsKRMEANTQREIAALkLCE----------GHPNIVKLHEVYHDQLHTFLVMEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG---FLKIADFGLCKEGIGFGDRTS 711
Cdd:cd14179   84 LKGGELLERIKkKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGFARLKPPDNQPLK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGD-------TEDEVFECIVNADVPCP----HFLSAQG 780
Cdd:cd14179  164 TPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHdksltctSAEEIMKKIKQGDFSFEgeawKNVSQEA 243
                        250
                 ....*....|....*.
gi 564339933 781 LELIQKLLQKSPEKRL 796
Cdd:cd14179  244 KDLIQGLLTVDPNKRI 259
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
558-800 1.89e-20

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 91.90  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQevlGRDEIDSLYCEkriLETVGRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14193   11 ILGGGRFGQVHKCEEKSSGLKLAAKIIKAR---SQKEKEEVKNE---IEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHEDVF--PEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF--LKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd14193   85 GGELFDRIIDENYnlTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAnqVKIIDFGLARRYKPREKLRVNF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 cGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIV--NADVPCPHF--LSAQGLELIQKLLQ 789
Cdd:cd14193  165 -GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILacQWDFEDEEFadISEEAKDFISKLLI 243
                        250
                 ....*....|.
gi 564339933 790 KSPEKRLGAGE 800
Cdd:cd14193  244 KEKSWRMSASE 254
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
559-800 1.94e-20

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: 92.40  E-value: 1.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd06643   13 LGDGAFGKVYKAQNKETGILAAAKVIDTKS---EEELEDYMVEIDILASCD---HPNIVKLLDAFYYENNLWILIEFCAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 G--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd06643   87 GavDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDSFIGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEA-----YTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPC---PHFLSAQGLELIQKLL 788
Cdd:cd06643  167 PYWMAPEVVMCETskdrpYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTlaqPSRWSPEFKDFLRKCL 246
                        250
                 ....*....|..
gi 564339933 789 QKSPEKRLGAGE 800
Cdd:cd06643  247 EKNVDARWTTSQ 258
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
558-798 2.01e-20

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 91.98  E-value: 2.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIdsLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14183   13 TIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHM--IQNEVSILR---RVKHPNIVLLIEEMDMPTELYLVMELVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDN----LLLDAQGFLKIADFGLCKEGIGfgdRTST 712
Cdd:cd14183   88 GGDLFDAItSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENllvyEHQDGSKSLKLGDFGLATVVDG---PLYT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 713 FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDE--VFECIV--NADVPCPHF--LSAQGLELIQK 786
Cdd:cd14183  165 VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQevLFDQILmgQVDFPSPYWdnVSDSAKELITM 244
                        250
                 ....*....|..
gi 564339933 787 LLQKSPEKRLGA 798
Cdd:cd14183  245 MLQVDVDQRYSA 256
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
553-800 2.24e-20

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 92.15  E-value: 2.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVllvqYKG----TGKYYAIKALKKQEvlGRDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSH 628
Cdd:cd06917    3 YRRLELVGRGSYGAV----YRGyhvkTGRVVALKVLNLDT--DDDDVSDIQKEVALLSQLKLGQPKNIIKYYGSYLKGPS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd06917   77 LWIIMDYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQ-EAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP---CPHFlSAQGLELI 784
Cdd:cd06917  157 KRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPrleGNGY-SPLLKEFV 235
                        250
                 ....*....|....*.
gi 564339933 785 QKLLQKSPEKRLGAGE 800
Cdd:cd06917  236 AACLDEEPKDRLSADE 251
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
552-800 2.49e-20

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: 92.39  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIK--ALKKQEvlgrDEI-DSLYCEKRILETVGrtGHPFLLSLLACIQTSSH 628
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGETVALKkvALRKLE----GGIpNQALREIKALQACQ--GHPYVVKLRDVFPHGTG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGgDLMMQIH--EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGF 706
Cdd:cd07832   75 FVLVFEYMLS-SLSEVLRdeERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRT-STFCGTPEFLAPEVL--TQEaYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVN---------------- 767
Cdd:cd07832  154 DPRLySHQVATRWYRAPELLygSRK-YDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRtlgtpnektwpeltsl 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 564339933 768 ---------ADVPCP---HF--LSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd07832  233 pdynkitfpESKGIRleeIFpdCSPEAIDLLKGLLVYNPKKRLSAEE 279
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
559-800 2.64e-20

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: 91.59  E-value: 2.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrdeidslycekRILETVGRT-------GHPFLLSLLACIQTSSHACF 631
Cdd:cd14665    8 IGSGNFGVARLMRDKQTKELVAVKYIERGE--------------KIDENVQREiinhrslRHPNIVRFKEVILTPTHLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF--LKIADFGLCKEGIGFGD 708
Cdd:cd14665   74 VMEYAAGGELFERIcNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSSVLHSQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTfCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPF--PGDTED--EVFECIVNADVPCPHF--LSAQGL 781
Cdd:cd14665  154 PKST-VGTPAYIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFedPEEPRNfrKTIQRILSVQYSIPDYvhISPECR 232
                        250
                 ....*....|....*....
gi 564339933 782 ELIQKLLQKSPEKRLGAGE 800
Cdd:cd14665  233 HLISRIFVADPATRITIPE 251
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
552-795 2.98e-20

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: 91.34  E-value: 2.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRdEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTssHACF 631
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKR-ERKAAEQEAKLLS---KLKHPNIVSYKESFEG--EDGF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 ---VTEFLPGGDLMMQIHED---VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIG 705
Cdd:cd08223   75 lyiVMGFCEGGDLYTRLKEQkgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLES 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP-CPHFLSAQGLELI 784
Cdd:cd08223  155 SSDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPpMPKQYSPELGELI 234
                        250
                 ....*....|.
gi 564339933 785 QKLLQKSPEKR 795
Cdd:cd08223  235 KAMLHQDPEKR 245
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
552-800 3.49e-20

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: 91.18  E-value: 3.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLgrDEIDSLYCEKRIlETVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMM--DAKARQDCLKEI-DLLQQLNHPNIIKYLASFIENNELNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQI-----HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLckeGIGF 706
Cdd:cd08224   78 VLELADAGDLSRLIkhfkkQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL---GRFF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTS---TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED--EVFECIVNAD---VPCPHFlSA 778
Cdd:cd08224  155 SSKTTaahSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEyppLPADLY-SQ 233
                        250       260
                 ....*....|....*....|..
gi 564339933 779 QGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd08224  234 ELRDLVAACIQPDPEKRPDISY 255
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
558-796 3.61e-20

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: 91.20  E-value: 3.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKqEVLGRDEIDsLYCEKriletvgrTGHPFLLSLLACIQTS--SHACF--VT 633
Cdd:cd14089    8 VLGLGINGKVLECFHKKTGEKFALKVLRD-NPKARREVE-LHWRA--------SGCPHIVRIIDVYENTyqGRKCLlvVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHEDV---FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDN---LLLDAQGFLKIADFGLCKEGIGFg 707
Cdd:cd14089   78 ECMEGGELFSRIQERAdsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENllySSKGPNAILKLTDFGFAKETTTK- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF---------PGDTEDevfecIVNA--DVPCPHF- 775
Cdd:cd14089  157 KSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnhglaisPGMKKR-----IRNGqyEFPNPEWs 231
                        250       260
                 ....*....|....*....|..
gi 564339933 776 -LSAQGLELIQKLLQKSPEKRL 796
Cdd:cd14089  232 nVSEEAKDLIRGLLKTDPSERL 253
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
553-812 3.90e-20

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: 91.39  E-value: 3.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVllvqYKG----TGKYYAIKALKK-QEVLG------RdEIDSLyceKRIletvgrtGHPFLLSLLA 621
Cdd:cd07829    1 YEKLEKLGEGTYGVV----YKAkdkkTGEIVALKKIRLdNEEEGipstalR-EISLL---KEL-------KHPNIVKLLD 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 CIQTSSHACFVTEFLPGgDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL 699
Cdd:cd07829   66 VIHTENKLYLVFEYCDQ-DLkkYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 CKEgIGFGDRTStfcgTPE-----FLAPEVLTQE-AYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFEcI------- 765
Cdd:cd07829  145 ARA-FGIPLRTY----THEvvtlwYRAPEILLGSkHYSTAVDIWSVGCIFAELITGKPLFPGDSEiDQLFK-Ifqilgtp 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 766 -----------VNADVPCPHF-----------LSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd07829  219 teeswpgvtklPDYKPTFPKWpkndlekvlprLDPEGIDLLSKMLQYNPAKRI-----SAKEALKHPYF 282
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
557-813 3.97e-20

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: 91.34  E-value: 3.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 557 AVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd06630    6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG-FLKIADFG----LCKEGIGFGDRT 710
Cdd:cd06630   86 AGGSVASLLSKyGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGaaarLASKGTGAGEFQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI-----VNADVPCPHFLSAQGLELIQ 785
Cdd:cd06630  166 GQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIfkiasATTPPPIPEHLSPGLRDVTL 245
                        250       260
                 ....*....|....*....|....*...
gi 564339933 786 KLLQKSPEKRLGagerdAEEIKVQPFFR 813
Cdd:cd06630  246 RCLELQPEDRPP-----ARELLKHPVFT 268
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
546-800 4.09e-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: 91.29  E-value: 4.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 546 NPPQLqdFRCLAVLGRGHFGKVLL-VQYKgTGKYYAIKALKKQEvlGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQ 624
Cdd:cd06641    1 DPEEL--FTKLEKIGKGSFGEVFKgIDNR-TQKVVAIKIIDLEE--AEDEIEDIQQEITVLS---QCDSPYVTKYYGSYL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI 704
Cdd:cd06641   73 KDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGL-EL 783
Cdd:cd06641  153 DTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLkEF 232
                        250
                 ....*....|....*..
gi 564339933 784 IQKLLQKSPEKRLGAGE 800
Cdd:cd06641  233 VEACLNKEPSFRPTAKE 249
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
554-801 4.90e-20

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: 90.91  E-value: 4.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 554 RCLAVLGRGHFGKVLLVQYKGtgKYYAIKALKKQEVlGRDEIDSLYCEKRILetvgRTGHPFLLSLLACIQTSSHACFVT 633
Cdd:cd13979    6 RLQEPLGSGGFGSVYKATYKG--ETVAVKIVRRRRK-NRASRQSFWAELNAA----RLRHENIVRVLAAETGTDFASLGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 ---EFLPGGDLMMQIHEDVFPEP--QACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG---LCKEGIG 705
Cdd:cd13979   79 iimEYCGNGTLQQLIYEGSEPLPlaHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGcsvKLGEGNE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTedevfECIVNA---------DVPCPHFL 776
Cdd:cd13979  159 VGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLR-----QHVLYAvvakdlrpdLSGLEDSE 233
                        250       260
                 ....*....|....*....|....*.
gi 564339933 777 SAQGLE-LIQKLLQKSPEKRLGAGER 801
Cdd:cd13979  234 FGQRLRsLISRCWSAQPAERPNADES 259
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
552-795 5.12e-20

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: 90.68  E-value: 5.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKAL---------KKQEVlgrDEIDSLycekRILEtvgrtgHPFLLSLLAC 622
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIdygkmsekeKQQLV---SEVNIL----RELK------HPNIVRYYDR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 623 IQ-TSSHACF-VTEFLPGGDLMMQI-----HEDVFPEPQACFYLACVVLGLQFLH-----EKRIIYRDLKLDNLLLDAQG 690
Cdd:cd08217   68 IVdRANTTLYiVMEYCEGGDLAQLIkkckkENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 691 FLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV 770
Cdd:cd08217  148 NVKLGDFGLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKF 227
                        250       260
                 ....*....|....*....|....*.
gi 564339933 771 PC-PHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd08217  228 PRiPSRYSSELNEVIKSMLNVDPDKR 253
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
632-812 6.88e-20

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 90.49  E-value: 6.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGG---DLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFG 707
Cdd:cd06610   77 VMPLLSGGsllDIMKSSYpRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTS----TFCGTPEFLAPEVLTQE-AYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHF------L 776
Cdd:cd06610  157 DRTRkvrkTFVGTPCWMAPEVMEQVrGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETgadykkY 236
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564339933 777 SAQGLELIQKLLQKSPEKRlgageRDAEEIKVQPFF 812
Cdd:cd06610  237 SKSFRKMISLCLQKDPSKR-----PTAEELLKHKFF 267
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
559-813 7.05e-20

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: 90.37  E-value: 7.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSlycekRILeTVGRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd06647   15 IGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIIN-----EIL-VMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPE 718
Cdd:cd06647   89 GSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 719 FLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVN---ADVPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd06647  169 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATngtPELQNPEKLSAIFRDFLNRCLEMDVEKR 248
                        250
                 ....*....|....*...
gi 564339933 796 LgagerDAEEIKVQPFFR 813
Cdd:cd06647  249 G-----SAKELLQHPFLK 261
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
558-796 7.09e-20

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: 90.43  E-value: 7.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlGRDEIDslyCEKRIletvgrTGHPFLLSLLACIQTSSHA--CF--VT 633
Cdd:cd14172   11 VLGLGVNGKVLECFHRRTGQKCALKLLYDSPK-ARREVE---HHWRA------SGGPHIVHILDVYENMHHGkrCLliIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHE---DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ---GFLKIADFGLCKEgIGFG 707
Cdd:cd14172   81 ECMEGGELFSRIQErgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKekdAVLKLTDFGFAKE-TTVQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIV------NADVPCPHF--LSAQ 779
Cdd:cd14172  160 NALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKrrirmgQYGFPNPEWaeVSEE 239
                        250
                 ....*....|....*..
gi 564339933 780 GLELIQKLLQKSPEKRL 796
Cdd:cd14172  240 AKQLIRHLLKTDPTERM 256
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
559-800 7.54e-20

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: 90.94  E-value: 7.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRiletvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd06654   28 IGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMR------ENKNPNIVNYLDSYLVGDELWVVMEYLAG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPE 718
Cdd:cd06654  102 GSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 719 FLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP---CPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd06654  182 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPelqNPEKLSAIFRDFLNRCLEMDVEKR 261

                 ....*
gi 564339933 796 LGAGE 800
Cdd:cd06654  262 GSAKE 266
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
559-811 1.00e-19

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 89.74  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKG-----TGKYYAIKA------LKKQEVLGRdeidslycEKRILETVGrtgHPFLLSLLACIQTSS 627
Cdd:cd14120    1 IGHGAFAVV----FKGrhrkkPDLPVAIKCitkknlSKSQNLLGK--------EIKILKELS---HENVVALLDCQETSS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYR---------DLKLDNLLLDAQGFLKIADF 697
Cdd:cd14120   66 SVYLVMEYCNGGDLADYLQAKgTLSEDTIRVFLQQIAAAMKALHSKGIVHRdlkpqnillSHNSGRKPSPNDIRLKIADF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 698 GLCKEGIGfGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEV---FECIVNADVPCPH 774
Cdd:cd14120  146 GFARFLQD-GMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKNANLRPNIPS 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564339933 775 FLSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPF 811
Cdd:cd14120  225 GTSPALKDLLLGLLKRNPKDRI-----DFEDFFSHPF 256
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
559-798 2.15e-19

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: 89.69  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDslycekrILETVGRtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14178   11 IGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIE-------ILLRYGQ--HPNIITLKDVYDDGKFVYLVMELMRG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG----FLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd14178   82 GELLDRIlRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQLRAENGLLMTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF---PGDTEDEVFECIVNADVPCP----HFLSAQGLELIQK 786
Cdd:cd14178  162 CYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFangPDDTPEEILARIGSGKYALSggnwDSISDAAKDIVSK 241
                        250
                 ....*....|..
gi 564339933 787 LLQKSPEKRLGA 798
Cdd:cd14178  242 MLHVDPHQRLTA 253
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
556-798 2.66e-19

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 88.49  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQeVLGRDEIDSlycEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd14113   12 VAELGRGRFSVVKKCDQRGTKRAVATKFVNKK-LMKRDQVTH---ELGVLQ---SLQHPQLVGLLDTFETPTSYILVLEM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIY---RDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTS 711
Cdd:cd14113   85 ADQGRLLDYVVRwGNLTEEKIRFYLREILEALQYLHNCRIAHldlKPENILVDQSLSKPTIKLADFGDAVQ-LNTTYYIH 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCP--HF--LSAQGLELIQKL 787
Cdd:cd14113  164 QLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddYFkgVSQKAKDFVCFL 243
                        250
                 ....*....|.
gi 564339933 788 LQKSPEKRLGA 798
Cdd:cd14113  244 LQMDPAKRPSA 254
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
559-813 2.72e-19

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: 89.40  E-value: 2.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtvgrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd06655   27 IGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELK------NPNIVNFLDSFLVGDELFVVMEYLAG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPE 718
Cdd:cd06655  101 GSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 719 FLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP---CPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd06655  181 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPelqNPEKLSPIFRDFLNRCLEMDVEKR 260
                        250
                 ....*....|....*...
gi 564339933 796 lgageRDAEEIKVQPFFR 813
Cdd:cd06655  261 -----GSAKELLQHPFLK 273
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
559-813 2.97e-19

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: 88.27  E-value: 2.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKA--LKKQEvlgRDEIdsLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKmdLRKQQ---RREL--LFNEVVIMRDYQ---HPNIVEMYSSYLVGDELWVVMEFL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHEDVFPEPQ-ACFYLACVVlGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCG 715
Cdd:cd06648   87 EGGALTDIVTHTRMNEEQiATVCRAVLK-ALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSLVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPC---PHFLSAQGLELIQKLLQKSP 792
Cdd:cd06648  166 TPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKlknLHKVSPRLRSFLDRMLVRDP 245
                        250       260
                 ....*....|....*....|.
gi 564339933 793 EKRLgagerDAEEIKVQPFFR 813
Cdd:cd06648  246 AQRA-----TAAELLNHPFLA 261
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
562-812 3.63e-19

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 88.37  E-value: 3.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 562 GHFGKVLLVQYKGTGKYYAIKALKKQEVLGrDEIDSLYCEKriletvgrtGHPFLLSLLACIQTSSHACFVTEFLPGGDL 641
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFNA-IEPMVHQLMK---------DNPNFIKLYYSVTTLKGHVLIMDYIKDGDL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 642 --MMQiHEDVFPEPQACFYLACVVLGLQFLHEKRII----------YRDLKLDnllldaqgfLKIADFGLCKEgIGfgdR 709
Cdd:PHA03390  97 fdLLK-KEGKLSEAEVKKIIRQLVEALNDLHKHNIIhndiklenvlYDRAKDR---------IYLCDYGLCKI-IG---T 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDtEDEVFE------CIVNaDVPCPHFLSAQGLEL 783
Cdd:PHA03390 163 PSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKED-EDEELDlesllkRQQK-KLPFIKNVSKNANDF 240
                        250       260
                 ....*....|....*....|....*....
gi 564339933 784 IQKLLQKSPEKRLgageRDAEEIKVQPFF 812
Cdd:PHA03390 241 VQSMLKYNINYRL----TNYNEIIKHPFL 265
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
559-813 3.64e-19

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: 89.01  E-value: 3.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRiletvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd06656   27 IGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMR------ENKNPNIVNYLDSYLVGDELWVVMEYLAG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPE 718
Cdd:cd06656  101 GSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 719 FLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP---CPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd06656  181 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPelqNPERLSAVFRDFLNRCLEMDVDRR 260
                        250
                 ....*....|....*...
gi 564339933 796 lgageRDAEEIKVQPFFR 813
Cdd:cd06656  261 -----GSAKELLQHPFLK 273
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
559-795 4.02e-19

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


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 88.28  E-value: 4.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLgRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNC-IEERKALLKEAEKME---RARHSYVLPLLGVCVERRSLGLVMEYMEN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVFPEPQACFY--LACVVLGLQFLH--EKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEG---IGFGDRTS 711
Cdd:cd13978   77 GSLKSLLEREIQDVPWSLRFriIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGmksISANRRRG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 T--FCGTPEFLAPEVL--TQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEV-FECIVNADVP--------CPHFLSA 778
Cdd:cd13978  157 TenLGGTPIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLLiMQIVSKGDRPslddigrlKQIENVQ 236
                        250
                 ....*....|....*..
gi 564339933 779 QGLELIQKLLQKSPEKR 795
Cdd:cd13978  237 ELISLMIRCWDGNPDAR 253
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
559-800 4.46e-19

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: 88.38  E-value: 4.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKkqeVLGRDEIdslYCEKRIlETVGRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14104    8 LGRGQFGIVHRCVETSSKKTYMAKFVK---VKGADQV---LVKKEI-SILNIARHRNILRLHESFESHEELVMIFEFISG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVF--PEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ--GFLKIADFGLCKEgIGFGDRTSTFC 714
Cdd:cd14104   81 VDIFERITTARFelNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSRQ-LKPGDKFRLQY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA----DVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd14104  160 TSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAeyafDDEAFKNISIEALDFVDRLLVK 239
                        250
                 ....*....|
gi 564339933 791 SPEKRLGAGE 800
Cdd:cd14104  240 ERKSRMTAQE 249
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
558-799 7.94e-19

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: 87.08  E-value: 7.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKAL------KKQEVLGRDEIDslycekrILETVGrtgHPFLLSLLACIQTSSHACF 631
Cdd:cd14082   10 VLGSGQFGIVYGGKHRKTGRDVAIKVIdklrfpTKQESQLRNEVA-------ILQQLS---HPGVVNLECMFETPERVFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHEDV--FPEPQACFYLACVVLGLQFLHEKRIIY-RDLKLDNLLLDAQGF--LKIADFGLCKEgIGF 706
Cdd:cd14082   80 VMEKLHGDMLEMILSSEKgrLPERITKFLVTQILVALRYLHSKNIVHcDLKPENVLLASAEPFpqVKLCDFGFARI-IGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFpgDTEDEVFECIVNADVPCP----HFLSAQGLE 782
Cdd:cd14082  159 KSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDINDQIQNAAFMYPpnpwKEISPDAID 236
                        250
                 ....*....|....*..
gi 564339933 783 LIQKLLQKSPEKRLGAG 799
Cdd:cd14082  237 LINNLLQVKMRKRYSVD 253
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
553-800 8.22e-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: 87.32  E-value: 8.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDslycEKRILETVGRTG---HPFLLSLLACIQTSSHA 629
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLD----EIRLLELLNKKDkadKYHIVRLKDVFYFKNHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRII-------------YRDLKldnllldaqgfLKI 694
Cdd:cd14133   77 CIVFELLSQNlyEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIhcdlkpenillasYSRCQ-----------IKI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLCKEgigFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPH 774
Cdd:cd14133  146 IDFGSSCF---LTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPA 222
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564339933 775 FLSAQG-------LELIQKLLQKSPEKRLGAGE 800
Cdd:cd14133  223 HMLDQGkaddelfVDFLKKLLEIDPKERPTASQ 255
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
553-798 8.37e-19

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: 87.72  E-value: 8.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQevLGRDEID-SLYCEKRILETVGRTGHPFLLSLLaciqTSSHACF 631
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVP--LSEEGIPlSTIREIALLKQLESFEHPNVVRLL----DVCHGPR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLpggDLMM---QIHED-----------VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADF 697
Cdd:cd07838   75 TDREL---KLTLvfeHVDQDlatyldkcpkpGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 698 GLCKegigFGDRTSTFCG---TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE----DEVFECI----- 765
Cdd:cd07838  152 GLAR----IYSFEMALTSvvvTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEadqlGKIFDVIglpse 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564339933 766 ----VNADVPCPHF--------------LSAQGLELIQKLLQKSPEKRLGA 798
Cdd:cd07838  228 eewpRNSALPRSSFpsytprpfksfvpeIDEEGLDLLKKMLTFNPHKRISA 278
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
553-800 9.38e-19

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: 87.33  E-value: 9.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQ-----EVLGRDEIDSLyceKRIletvgrTGHPFLLSLLACIQTSS 627
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHfksleQVNNLREIQAL---RRL------SPHPNILRLIEVLFDRK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HAC--FVTEflpggdLM-MQIHEDV------FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDaQGFLKIADFG 698
Cdd:cd07831   72 TGRlaLVFE------LMdMNLYELIkgrkrpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIK-DDILKLADFG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 LCKegigfgdrtSTFCGTP--EFL------APE-VLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI---- 765
Cdd:cd07831  145 SCR---------GIYSKPPytEYIstrwyrAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIhdvl 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564339933 766 ----------------VNADVP----------CPHfLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd07831  216 gtpdaevlkkfrksrhMNYNFPskkgtglrklLPN-ASAEGLDLLKKLLAYDPDERITAKQ 275
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
559-811 1.42e-18

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: 86.36  E-value: 1.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQevlgrdeidslyceKRILETVGRT-------GHPFLLSLLACIQTSSHACF 631
Cdd:cd14662    8 IGSGNFGVARLMRNKETKELVAVKYIERG--------------LKIDENVQREiinhrslRHPNIIRFKEVVLTPTHLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ--GFLKIADFGLCKEGIGFGD 708
Cdd:cd14662   74 VMEYAAGGELFERIcNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKSSVLHSQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTfCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPgDTED-----EVFECIVNADVPCPHF--LSAQG 780
Cdd:cd14662  154 PKST-VGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFE-DPDDpknfrKTIQRIMSVQYKIPDYvrVSQDC 231
                        250       260       270
                 ....*....|....*....|....*....|.
gi 564339933 781 LELIQKLLQKSPEKRLgagerDAEEIKVQPF 811
Cdd:cd14662  232 RHLLSRIFVANPAKRI-----TIPEIKNHPW 257
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
572-798 1.47e-18

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: 87.38  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 572 YKGTGKYYAIKALKKQEVLGRDEIDslycekrILETVGRtgHPFLLSLLACIQTSSHACFVTEFLPGGDLMMQI-HEDVF 650
Cdd:cd14177   25 HRATNMEFAVKIIDKSKRDPSEEIE-------ILMRYGQ--HPNIITLKDVYDDGRYVYLVTELMKGGELLDRIlRQKFF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 651 PEPQACFYLACVVLGLQFLHEKRIIYRDLKLD----NLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLT 726
Cdd:cd14177   96 SEREASAVLYTITKTVDYLHCQGVVHRDLKPSnilyMDDSANADSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLM 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 727 QEAYTRAVDWWGLGVLLYEMLVGECPF---PGDTEDEVFECIVNADVPCP----HFLSAQGLELIQKLLQKSPEKRLGA 798
Cdd:cd14177  176 RQGYDAACDIWSLGVLLYTMLAGYTPFangPNDTPEEILLRIGSGKFSLSggnwDTVSDAAKDLLSHMLHVDPHQRYTA 254
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
546-752 2.66e-18

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: 85.87  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 546 NPPQLqdFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQT 625
Cdd:cd06640    1 DPEEL--FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEE--AEDEIEDIQQEITVLS---QCDSPYVTKYYGSYLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIG 705
Cdd:cd06640   74 GTKLWIIMEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTD 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564339933 706 FGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECP 752
Cdd:cd06640  154 TQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
558-800 4.29e-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: 4.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRD----EIDSLY-CEkriletvgrtGHPFLLSLLACIQTSSHACFV 632
Cdd:cd14174    9 LLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSrvfrEVETLYqCQ----------GNKNILELIEFFEDDTRFYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ---GFLKIADFGLcKEGIGFGD 708
Cdd:cd14174   79 FEKLRGGSILAHIQKrKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPdkvSPVKICDFDL-GSGVKLNS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 --------RTSTFCGTPEFLAPEVL---TQEA--YTRAVDWWGLGVLLYEMLVGECPFPGD---------------TEDE 760
Cdd:cd14174  158 actpittpELTTPCGSAEYMAPEVVevfTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevcrvCQNK 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564339933 761 VFECIVNADVPCPH----FLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14174  238 LFESIQEGKYEFPDkdwsHISSEAKDLISKLLVRDAKERLSAAQ 281
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
553-800 5.10e-18

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: 84.91  E-value: 5.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKgtgKYYAIKALKkqeVLGRDEIDSLYCEK---RILETVGRTGHPFLLSLLACIQ-TSSH 628
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQ---KYCCKVAIK---IVDRRRASPDFVQKflpRELSILRRVNHPNIVQMFECIEvANGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEfLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF-LKIADFGLCKEGIGF 706
Cdd:cd14164   76 LYIVME-AAATDLLQKIQEVhHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRkIKIADFGFARFVEDY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTSTFCGTPEFLAPEVLTQEAY-TRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQ 785
Cdd:cd14164  155 PELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSGVALEEPCRALIR 234
                        250
                 ....*....|....*
gi 564339933 786 KLLQKSPEKRLGAGE 800
Cdd:cd14164  235 TLLQFNPSTRPSIQQ 249
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
546-753 6.23e-18

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: 85.11  E-value: 6.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 546 NPPQLqdFRCLAVLGRGHFGKVllvqYKG----TGKYYAIKALKKQEvlGRDEIDSLYCEKRILEtvgRTGHPFLLSLLA 621
Cdd:cd06642    1 DPEEL--FTKLERIGKGSFGEV----YKGidnrTKEVVAIKIIDLEE--AEDEIEDIQQEITVLS---QCDSPYITRYYG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 CIQTSSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK 701
Cdd:cd06642   70 SYLKGTKLWIIMEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339933 702 EGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd06642  150 QLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
553-798 6.40e-18

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: 85.31  E-value: 6.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlGRDE--IDSLYcEKRILEtvgRTGHPFLLSLLaCIQTSSHAC 630
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN--EKEGfpITAIR-EIKLLQ---KLDHPNVVRLK-EIVTSKGSA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 F-------VTEFLPGgDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCk 701
Cdd:cd07840   74 KykgsiymVFEYMDH-DLtgLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLA- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 egigfgdRTSTFCGTPEFL---------APEVLTQE-AYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIvnADV- 770
Cdd:cd07840  152 -------RPYTKENNADYTnrvitlwyrPPELLLGAtRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKI--FELc 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 771 --PCP------------------------------HFLSAQGLELIQKLLQKSPEKRLGA 798
Cdd:cd07840  223 gsPTEenwpgvsdlpwfenlkpkkpykrrlrevfkNVIDPSALDLLDKLLTLDPKKRISA 282
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
552-795 7.13e-18

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: 84.36  E-value: 7.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYcEKRILETVGrtGHPFLLSLLACIQTSSHACF 631
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALR-EVEAHAALG--QHPNIVRYYSSWEEGGHLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHEDV----FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFG 707
Cdd:cd13997   78 QMELCENGSLQDALEELSpiskLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTStfcGTPEFLAPEVLTQE-AYTRAVDWWGLGVLLYEMLVGEcPFPgdTEDEVFECIVNADVPCP--HFLSAQGLELI 784
Cdd:cd13997  158 DVEE---GDSRYLAPELLNENyTHLPKADIFSLGVTVYEAATGE-PLP--RNGQQWQQLRQGKLPLPpgLVLSQELTRLL 231
                        250
                 ....*....|.
gi 564339933 785 QKLLQKSPEKR 795
Cdd:cd13997  232 KVMLDPDPTRR 242
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
559-753 7.20e-18

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: 83.70  E-value: 7.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGtgKYYAIKALKKQEvlgrdEIDSLYCEKriletvgrTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14059    1 LGSGAQGAVFLGKFRG--EEVAVKKVRDEK-----ETDIKHLRK--------LNHPNIIKFKGVCTQAPCYCILMEYCPY 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVFPEPQ-ACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFGDRTS--TFCG 715
Cdd:cd14059   66 GQLYEVLRAGREITPSlLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKE---LSEKSTkmSFAG 142
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564339933 716 TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14059  143 TVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPY 180
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
558-813 8.23e-18

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: 84.58  E-value: 8.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKAL--KKQEVLGRDEIDSL----YCEKRILETVgrTGHPFLLSLLACIQTSSHACF 631
Cdd:cd14182   10 ILGRGVSSVVRRCIHKPTRQEYAVKIIdiTGGGSFSPEEVQELreatLKEIDILRKV--SGHPNIIQLKDTYETNTFFFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRT 710
Cdd:cd14182   88 VFDLMKKGELFDYLTEKVtLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ-LDPGEKL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVL------TQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVpcpHFLSAQG---- 780
Cdd:cd14182  167 REVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNY---QFGSPEWddrs 243
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564339933 781 ---LELIQKLLQKSPEKRLgagerDAEEIKVQPFFR 813
Cdd:cd14182  244 dtvKDLISRFLVVQPQKRY-----TAEEALAHPFFQ 274
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
558-795 8.44e-18

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: 83.90  E-value: 8.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVllvqYKGTGKYYAIKALKK-QEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd05085    3 LLGKGNFGEV----YKGTLKDKTPVAVKTcKEDLPQELKIKFLSEARILK---QYDHPNIVKLIGVCTQRQPIYIVMELV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFC 714
Cdd:cd05085   76 PGGDFLsfLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLELIQKLLQKS 791
Cdd:cd05085  156 QIPiKWTAPEALNYGRYSSESDVWSFGILLWETFsLGVCPYPGMTNQQAREQVEKGyRMSAPQRCPEDIYKIMQRCWDYN 235

                 ....
gi 564339933 792 PEKR 795
Cdd:cd05085  236 PENR 239
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
559-796 1.28e-17

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: 84.54  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKAL-KKQEVLGRDEIDSLycekRILEtvgrtGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIIsRRMEANTQREVAAL----RLCQ-----SHPNIVALHEVLHDQYHTYLVMELLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG---FLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd14180   85 GGELLDRIKkKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESdgaVLKVIDFGFARLRPQGSRPLQTP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPG-----------DTEDEVFECIVNADVPCPHFLSAQGLE 782
Cdd:cd14180  165 CFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSkrgkmfhnhaaDIMHKIKEGDFSLEGEAWKGVSEEAKD 244
                        250
                 ....*....|....
gi 564339933 783 LIQKLLQKSPEKRL 796
Cdd:cd14180  245 LVRGLLTVDPAKRL 258
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
632-795 1.56e-17

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 86.85  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHEDV-----FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK--EGI 704
Cdd:PTZ00283 117 VLDYANAGDLRQEIKSRAktnrtFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKmyAAT 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV-PCPHFLSAQGLEL 783
Cdd:PTZ00283 197 VSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYdPLPPSISPEMQEI 276
                        170
                 ....*....|..
gi 564339933 784 IQKLLQKSPEKR 795
Cdd:PTZ00283 277 VTALLSSDPKRR 288
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
557-795 1.58e-17

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: 83.55  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 557 AVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSL----YCEKRILETVGRtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd13993    6 SPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQklpqLREIDLHRRVSR--HPNIITLHDVFETEVAIYIV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDVF----PEPQACFYLAcVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF-LKIADFGL-CKEgigf 706
Cdd:cd13993   84 LEYCPNGDLFEAITENRIyvgkTELIKNVFLQ-LIDAVKHCHSLGIYHRDIKPENILLSQDEGtVKLCDFGLaTTE---- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 gDRTSTF-CGTPEFLAPEVLTQEA------YTRAVDWWGLGVLLYEMLVGECPF-PGDTEDEVFECIVNADvpcPHFL-- 776
Cdd:cd13993  159 -KISMDFgVGSEFYMAPECFDEVGrslkgyPCAAGDIWSLGIILLNLTFGRNPWkIASESDPIFYDYYLNS---PNLFdv 234
                        250       260
                 ....*....|....*....|...
gi 564339933 777 ----SAQGLELIQKLLQKSPEKR 795
Cdd:cd13993  235 ilpmSDDFYNLLRQIFTVNPNNR 257
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
549-800 1.84e-17

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: 83.92  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDfrclAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRD----EIDSLY-CEkriletvgrtGHPFLLSLLACI 623
Cdd:cd14173    4 QLQE----EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSrvfrEVEMLYqCQ----------GHRNVLELIEFF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 624 QTSSHACFVTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ---GFLKIADFGL 699
Cdd:cd14173   70 EEEDKFYLVFEKMRGGSILSHIHRRRhFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPnqvSPVKICDFDL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 cKEGIGFGDRTS--------TFCGTPEFLAPEVL---TQEA--YTRAVDWWGLGVLLYEMLVGECPFPGD---------- 756
Cdd:cd14173  150 -GSGIKLNSDCSpistpellTPCGSAEYMAPEVVeafNEEAsiYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrg 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564339933 757 -----TEDEVFECIVNADVPCPH----FLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14173  229 eacpaCQNMLFESIQEGKYEFPEkdwaHISCAAKDLISKLLVRDAKQRLSAAQ 281
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
549-812 1.96e-17

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: 83.36  E-value: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGrghfgKVLLVQYKGTGKYYAIKALKKQEVLGRDEidslycekrilETVGRTGHPFLLSLLACIQTSSH 628
Cdd:cd05576    2 ELKAFRVLGVID-----KVLLVMDTRTQETFILKGLRKSSEYSRER-----------KTIIPRCVPNMVCLRKYIISEES 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDL------------MMQIHEDV-----------FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLL 685
Cdd:cd05576   66 VFLVLQHAEGGKLwsylskflndkeIHQLFADLderlaaasrfyIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNIL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 686 LDAQGFLKIADFGLCKEGIGFGDRTST---FCgtpeflAPEVLTQEAYTRAVDWWGLGVLLYEMLVG----ECPFPGdte 758
Cdd:cd05576  146 LNDRGHIQLTYFSRWSEVEDSCDSDAIenmYC------APEVGGISEETEACDWWSLGALLFELLTGkalvECHPAG--- 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 759 devfeciVNA--DVPCPHFLSAQGLELIQKLLQKSPEKRLGAGERDAEEIKVQPFF 812
Cdd:cd05576  217 -------INThtTLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
551-795 2.23e-17

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


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 82.87  E-value: 2.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYyAIKALKKQEVLGRDEIDSlycEKRILEtvgRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd05148    6 EEFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQDFQK---EVQALK---RLRHKHLISLFAVCSVGEPVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHEdvfPEPQA-----CFYLAC-VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC---K 701
Cdd:cd05148   79 IITELMEKGSLLAFLRS---PEGQVlpvasLIDMACqVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArliK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 EGIGFGDRTStfcgTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIV-NADVPCPHFLSA 778
Cdd:cd05148  156 EDVYLSSDKK----IPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITaGYRMPCPAKCPQ 231
                        250
                 ....*....|....*..
gi 564339933 779 QGLELIQKLLQKSPEKR 795
Cdd:cd05148  232 EIYKIMLECWAAEPEDR 248
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
556-814 2.53e-17

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: 83.39  E-value: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEV-LGRDEID-SLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVT 633
Cdd:cd07841    5 GKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERkEAKDGINfTALREIKLLQELK---HPNIIGLLDVFGHKSNINLVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGgDLMMQIH--EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFGD--- 708
Cdd:cd07841   82 EFMET-DLEKVIKdkSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARS---FGSpnr 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVL-TQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA------------------- 768
Cdd:cd07841  158 KMTHQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEAlgtpteenwpgvtslpdyv 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 769 ---DVPCPHF------LSAQGLELIQKLLQKSPEKRLGAgeRDAEEikvQPFFRT 814
Cdd:cd07841  238 efkPFPPTPLkqifpaASDDALDLLQRLLTLNPNKRITA--RQALE---HPYFSN 287
HR1_PKN_3 cd11625
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
168-227 2.65e-17

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that 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 cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212015  Cd Length: 74  Bit Score: 76.95  E-value: 2.65e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 168 GSPEPGPDLLAEELQHRLRIEAAVAAGAKNVVKLLGGQRIQDRKALAEAQAQLQESSQKL 227
Cdd:cd11625    1 GPLLLPLELRIEELRHHLRVETAVVEGAKNVIKLLQNAKKDDKKALQEAQKSLSESSQKL 60
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
552-753 3.15e-17

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: 82.77  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKAL----KKQEVlgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSS 627
Cdd:cd06653    3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfdpDSQET--SKEVNALECEIQLLKNLR---HDRIVQYYGCLRDPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 H---ACFVtEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG----- 698
Cdd:cd06653   78 EkklSIFV-EYMPGGSVKDQLKAyGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskri 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 699 --LCKEGIGFGDRTstfcGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd06653  157 qtICMSGTGIKSVT----GTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
558-755 4.53e-17

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: 82.06  E-value: 4.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVllvqYKGT--GKYYAIKALKkQEVlgrDE-----IDSLYCEKRILetvGRTGHPFLLSLLA-CIQTSsHA 629
Cdd:cd14061    1 VIGVGGFGKV----YRGIwrGEEVAVKAAR-QDP---DEdisvtLENVRQEARLF---WMLRHPNIIALRGvCLQPP-NL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIHEDVFPePQACFYLAC-VVLGLQFLHEKR---IIYRD--------LKLDNLLLDAQGFLKIADF 697
Cdd:cd14061   69 CLVMEYARGGALNRVLAGRKIP-PHVLVDWAIqIARGMNYLHNEApvpIIHRDlkssniliLEAIENEDLENKTLKITDF 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 698 GLCKEgIGFGDRTSTfCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPG 755
Cdd:cd14061  148 GLARE-WHKTTRMSA-AGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKG 203
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
559-793 5.28e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 82.50  E-value: 5.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKkQEVLGRDEIDSLYC-EKRILEtvgRTGHPFLLSllAC-------IQTSSHAC 630
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCR-QELSPSDKNRERWClEVQIMK---KLNHPNVVS--ARdvppeleKLSPNDLP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVT-EFLPGGDLmmqihEDVFPEPQACF---------YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG---FLKIADF 697
Cdd:cd13989   75 LLAmEYCSGGDL-----RKVLNQPENCCglkesevrtLLSDISSAISYLHENRIIHRDLKPENIVLQQGGgrvIYKLIDL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 698 GLCKEgIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFpgdtedevfecivnadvpCPHFLS 777
Cdd:cd13989  150 GYAKE-LDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF------------------LPNWQP 210
                        250
                 ....*....|....*.
gi 564339933 778 AQGLELIQkllQKSPE 793
Cdd:cd13989  211 VQWHGKVK---QKKPE 223
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
559-795 5.49e-17

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 82.32  E-value: 5.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKkQEVLGRDEiDSLYCEKRILEtvgRTGHPFLLSL------LACIQTSSHACFV 632
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCR-QELSPKNR-ERWCLEIQIMK---RLNHPNVVAArdvpegLQKLAPNDLPLLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDL--MMQIHEDV--FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDaQG----FLKIADFGLCKEgI 704
Cdd:cd14038   77 MEYCQGGDLrkYLNQFENCcgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQ-QGeqrlIHKIIDLGYAKE-L 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGD----------TEDEVFECIVNAD----- 769
Cdd:cd14038  155 DQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNwqpvqwhgkvRQKSNEDIVVYEDltgav 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564339933 770 -----VPCPHFLS---AQGLE-LIQKLLQKSPEKR 795
Cdd:cd14038  235 kfssvLPTPNNLNgilAGKLErWLQCMLMWHPRQR 269
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
564-805 7.90e-17

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: 81.61  E-value: 7.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 564 FGKVLLVQYKGTGKYYAIKALKKQEvlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPGGDLMM 643
Cdd:cd14088   14 FCEIFRAKDKTTGKLYTCKKFLKRD--GRKVRKAAKNEINILKMVK---HPNILQLVDVFETRKEYFIFLELATGREVFD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 644 QI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLL---LDAQGFLKIADFGLCKEGIGFgdrTSTFCGTPEF 719
Cdd:cd14088   89 WIlDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyynRLKNSKIVISDFHLAKLENGL---IKEPCGTPEY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 720 LAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDE--------VFECIVNAD--VPCPHF--LSAQGLELIQKL 787
Cdd:cd14088  166 LAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDdyenhdknLFRKILAGDyeFDSPYWddISQAAKDLVTRL 245
                        250
                 ....*....|....*...
gi 564339933 788 LQKSPEKRLGAGERDAEE 805
Cdd:cd14088  246 MEVEQDQRITAEEAISHE 263
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
559-800 9.40e-17

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: 81.96  E-value: 9.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKA--LKKQEvlgRDEIdsLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKMmdLRKQQ---RREL--LFNEVVIMRDYQ---HPNVVEMYKSYLVGEELWVLMEYL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd06659  101 QGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIvnADVPCP-----HFLSAQGLELIQKLLQKS 791
Cdd:cd06659  181 PYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRL--RDSPPPklknsHKASPVLRDFLERMLVRD 258

                 ....*....
gi 564339933 792 PEKRLGAGE 800
Cdd:cd06659  259 PQERATAQE 267
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
559-795 1.24e-16

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 80.83  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSlYCEKRILETvgrtgHPFLLSLLA-CIQTSSHACFVTEFLP 637
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLRE-YNISLELSV-----HPHIIKTYDvAFETEDYYVFAQEYAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF--LKIADFGLCKEgigFGDRTSTFC 714
Cdd:cd13987   75 YGDLFSIIPPQVgLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTRR---VGSTVKRVS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVL-TQEAYTRAV----DWWGLGVLLYEMLVGECPFP-GDTEDEVFECIV------NADVPcPHF--LSAQG 780
Cdd:cd13987  152 GTIPYTAPEVCeAKKNEGFVVdpsiDVWAFGVLLFCCLTGNFPWEkADSDDQFYEEFVrwqkrkNTAVP-SQWrrFTPKA 230
                        250
                 ....*....|....*
gi 564339933 781 LELIQKLLQKSPEKR 795
Cdd:cd13987  231 LRMFKKLLAPEPERR 245
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
550-795 1.30e-16

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: 80.84  E-value: 1.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVllvqYKGT----GKYYAIKALKKQEVLgrDEIDSLYCEKRIlETVGRTGHPFLLSLLACIQT 625
Cdd:cd08228    1 LANFQIEKKIGRGQFSEV----YRATclldRKPVALKKVQIFEMM--DAKARQDCVKEI-DLLKQLNHPNVIKYLDSFIE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLPGGDLMMQI-----HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLc 700
Cdd:cd08228   74 DNELNIVLELADAGDLSQMIkyfkkQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 keGIGFGDRTS---TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFEC--IVNAD---VPC 772
Cdd:cd08228  153 --GRFFSSKTTaahSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCqkIEQCDyppLPT 230
                        250       260
                 ....*....|....*....|...
gi 564339933 773 PHFlSAQGLELIQKLLQKSPEKR 795
Cdd:cd08228  231 EHY-SEKLRELVSMCIYPDPDQR 252
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
551-816 1.37e-16

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: 81.08  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKkqevlgrdeID-SLYCEKRI---LETVGRTGHPFLLSLLACIQTS 626
Cdd:cd06619    1 QDIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIP---------LDiTVELQKQImseLEILYKCDSPYIIGFYGAFFVE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 627 SHACFVTEFLPGGDLmmqiheDVF---PEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEG 703
Cdd:cd06619   72 NRISICTEFMDGGSL------DVYrkiPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 704 IGfgDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED-------EVFECIVNADVPC--PH 774
Cdd:cd06619  146 VN--SIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNqgslmplQLLQCIVDEDPPVlpVG 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 564339933 775 FLSAQGLELIQKLLQKSPEKRLGagerdAEEIKVQPFFRTTN 816
Cdd:cd06619  224 QFSEKFVHFITQCMRKQPKERPA-----PENLMDHPFIVQYN 260
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
559-811 1.39e-16

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 80.89  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIK-------ALKKQEVLGRDEIDSLYCEkriLETVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEMLAVKqvelpktSSDRADSRQKTVVDALKSE---IDTLKDLDHPNIVQYLGFEETEDYFSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK--EGIGFGD 708
Cdd:cd06629   86 FLEYVPGGSIGSCLRKyGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKksDDIYGNN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVL--TQEAYTRAVDWWGLGVLLYEMLVGECPFPgdtEDEVFECIVN-------ADVPCPHFLSAQ 779
Cdd:cd06629  166 GATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWS---DDEAIAAMFKlgnkrsaPPVPEDVNLSPE 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564339933 780 GLELIQKLLQKSPEKRlgageRDAEEIKVQPF 811
Cdd:cd06629  243 ALDFLNACFAIDPRDR-----PTAAELLSHPF 269
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
558-800 1.42e-16

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: 80.92  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKalkkqEVLGRD--EIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd06624   15 VLGKGTFGVVYAARDLSTQVRIAIK-----EIPERDsrEVQPLHEEIALHS---RLSHKNIVQYLGSVSEDGFFKIFMEQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHEDVFP----EPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDA-QGFLKIADFGLCKEGIGFGDRT 710
Cdd:cd06624   87 VPGGSLSALLRSKWGPlkdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGINPCT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLT--QEAYTRAVDWWGLGVLLYEMLVGECPF--PGDTEDEVFECIVNADVP-CPHFLSAQGLELIQ 785
Cdd:cd06624  167 ETFTGTLQYMAPEVIDkgQRGYGPPADIWSLGCTIIEMATGKPPFieLGEPQAAMFKVGMFKIHPeIPESLSEEAKSFIL 246
                        250
                 ....*....|....*
gi 564339933 786 KLLQKSPEKRLGAGE 800
Cdd:cd06624  247 RCFEPDPDKRATASD 261
HR1_PKN2_3 cd11635
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
175-226 1.56e-16

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2; PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the third HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation.


Pssm-ID: 212025  Cd Length: 74  Bit Score: 75.08  E-value: 1.56e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339933 175 DLLAEELQHRLRIEAAVAAGAKNVVKLLGGQRIQDRKALAEAQAQLQESSQK 226
Cdd:cd11635    8 ELRMEELRHHFRIESAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQK 59
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
550-800 1.98e-16

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: 80.49  E-value: 1.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKkqevlgRDEIDSLYceKRIL---ETVGRTGHPFLLSLLAC-IQT 625
Cdd:cd14046    5 LTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK------LRSESKNN--SRILrevMLLSRLNHQHVVRYYQAwIER 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 ssHACFVT-EFLPGGDLMMQIHEDVF-PEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEG 703
Cdd:cd14046   77 --ANLYIQmEYCEKSTLRDLIDSGLFqDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 704 ------------------IGFGDRTSTFCGTPEFLAPEVL--TQEAYTRAVDWWGLGVLLYEMLvgecpFPGDTEDEVFE 763
Cdd:cd14046  155 klnvelatqdinkstsaaLGSSGDLTGNVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIFFEMC-----YPFSTGMERVQ 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564339933 764 CIVNADVPCPHFLSA--------QGlELIQKLLQKSPEKRLGAGE 800
Cdd:cd14046  230 ILTALRSVSIEFPPDfddnkhskQA-KLIRWLLNHDPAKRPSAQE 273
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
551-800 2.29e-16

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: 80.23  E-value: 2.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKalkkqevlgRDEIDSLYCEKRIlETVGRTGHPFLLSLLAC-------I 623
Cdd:cd14047    6 QDFKEIELIGSGGFGQVFKAKHRIDGKTYAIK---------RVKLNNEKAEREV-KALAKLDHPNIVRYNGCwdgfdydP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 624 QTSSHA--------CFV-TEFLPGGDLMMQI----HEDVFP-EPQACFYLacVVLGLQFLHEKRIIYRDLKLDNLLLDAQ 689
Cdd:cd14047   76 ETSSSNssrsktkcLFIqMEFCEKGTLESWIekrnGEKLDKvLALEIFEQ--ITKGVEYIHSKKLIHRDLKPSNIFLVDT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 690 GFLKIADFGLCKEGIGFGDRTSTFcGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLvgECPFPGDTEDEVFECIVNAD 769
Cdd:cd14047  154 GKVKIGDFGLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELL--HVCDSAFEKSKFWTDLRNGI 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564339933 770 VPcPHFLSAQGLE--LIQKLLQKSPEKRLGAGE 800
Cdd:cd14047  231 LP-DIFDKRYKIEktIIKKMLSKKPEDRPNASE 262
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
559-796 2.37e-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: 79.86  E-value: 2.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDeidslycekriLETVGRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14109   12 EKRAAQGAPFHVTERSTGRNFLAQLRYGDPFLMRE-----------VDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQI----HEDVFPEPQACFYLACVVLGLQFLHEKRIIYrDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTSTFC 714
Cdd:cd14109   81 TIELVRDnllpGKDYYTERQVAVFVRQLLLALKHMHDLGIAH-LDLRPEDILLQDDKLKLADFGQSRR-LLRGKLTTLIY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA----DVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd14109  159 GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGkwsfDSSPLGNISDDARDFIKKLLVY 238

                 ....*.
gi 564339933 791 SPEKRL 796
Cdd:cd14109  239 IPESRL 244
HR1_PKN1_3 cd11636
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
174-226 3.35e-16

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


Pssm-ID: 212026  Cd Length: 74  Bit Score: 73.86  E-value: 3.35e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 174 PDLLA-----EELQHRLRIEAAVAAGAKNVVKLLGGQRIQDRKALAEAQAQLQESSQK 226
Cdd:cd11636    2 PDLCAvelriEELRHHFRVEHAVAEGAKNVLRLLGAGKAQDRKAISEAQSKLSESSQK 59
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
650-842 3.84e-16

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: 80.10  E-value: 3.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 650 FPEPQacfyLACVVL----GLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE-GIGFGDRTSTFCgTPEFLAPEV 724
Cdd:cd07845  105 FSESQ----VKCLMLqllrGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTyGLPAKPMTPKVV-TLWYRAPEL 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 725 LT-QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVN-------------ADVPCPH---------------- 774
Cdd:cd07845  180 LLgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQllgtpnesiwpgfSDLPLVGkftlpkqpynnlkhkf 259
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 775 -FLSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFFRTTnwqallartvqppfvPTLCGPADLRYF 842
Cdd:cd07845  260 pWLSEAGLRLLNFLLMYDPKKRA-----TAEEALESSYFKEK---------------PLPCEPEMMPTF 308
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
559-812 3.90e-16

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: 79.89  E-value: 3.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKK-----QEVLGRDEIDSLyceKRIletvgrTGHPFLLSLLACIQTSSHACFVT 633
Cdd:cd07830    7 LGDGTFGSVYLARNKETGELVAIKKMKKkfyswEECMNLREVKSL---RKL------NEHPNIVKLKEVFRENDELYFVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEkriiyrdlkldnllldaQGF-----------------LKI 694
Cdd:cd07830   78 EYMEGNlyQLMKDRKGKPFSESVIRSIIYQILQGLAHIHK-----------------HGFfhrdlkpenllvsgpevVKI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLCKEgIGFGDRTSTFCGTPEFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFE-CIV----- 766
Cdd:cd07830  141 ADFGLARE-IRSRPPYTDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSEiDQLYKiCSVlgtpt 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 767 --------------------NADVPCPHFL---SAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd07830  220 kqdwpegyklasklgfrfpqFAPTSLHQLIpnaSPEAIDLIKDMLRWDPKKRP-----TASQALQHPYF 283
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
556-795 4.17e-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: 79.77  E-value: 4.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIK--------ALKKQEVlgrdeidslycekRILETVGRTGHPFLL----SLLACI 623
Cdd:cd06621    6 LSSLGEGAGGSVTKCRLRNTKTIFALKtittdpnpDVQKQIL-------------RELEINKSCASPYIVkyygAFLDEQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 624 QTSSHACFvtEFLPGGDL----------MMQIHEDVFPEpqacfYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLK 693
Cdd:cd06621   73 DSSIGIAM--EYCEGGSLdsiykkvkkkGGRIGEKVLGK-----IAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 694 IADFGLCKEGIGFGDrtSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED-----EVFECIVNA 768
Cdd:cd06621  146 LCDFGVSGELVNSLA--GTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIVNM 223
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564339933 769 DVP----CPH---FLSAQGLELIQKLLQKSPEKR 795
Cdd:cd06621  224 PNPelkdEPEngiKWSESFKDFIEKCLEKDGTRR 257
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
559-795 4.39e-16

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: 79.51  E-value: 4.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQevLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd06622    9 LGKGNYGSVYKVLHRPTGVTMAMKEIRLE--LDESKFNQIIMELDILH---KAVSPYIVDFYGAFFIEGAVYMCMEYMDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDL----MMQIHEDVFPEPQACFYLACVVLGLQFLHEK-RIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTF 713
Cdd:cd06622   84 GSLdklyAGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVASLAKTNIG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTpeFLAPEVLTQE------AYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVF---ECIVNADVP-CPHFLSAQGLEL 783
Cdd:cd06622  164 CQS--YMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFaqlSAIVDGDPPtLPSGYSDDAQDF 241
                        250
                 ....*....|..
gi 564339933 784 IQKLLQKSPEKR 795
Cdd:cd06622  242 VAKCLNKIPNRR 253
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
559-753 4.41e-16

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: 79.11  E-value: 4.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGT--GKYYAIKALKKQEVLGRDEIDSLYCEKRILetvGRTGHPFLLSLL-ACIQTSSHACFVTEF 635
Cdd:cd14064    1 IGSGSFGKV----YKGRcrNKIVAIKRYRANTYCSKSDVDMFCREVSIL---CRLNHPCVIQFVgACLDDPSQFAIVTQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHEDV-FPEPQACFYLAC-VVLGLQFLHE--KRIIYRDLKLDNLLLDAQGFLKIADFG----LCKEGigfG 707
Cdd:cd14064   74 VSGGSLFSLLHEQKrVIDLQSKLIIAVdVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGesrfLQSLD---E 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14064  151 DNMTKQPGNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF 197
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
552-753 4.79e-16

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: 78.93  E-value: 4.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALK--KQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHA 629
Cdd:cd06652    3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQfdPESPETSKEVNALECEIQLLKNLL---HERIVQYYGCLRDPQER 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CF--VTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG-------L 699
Cdd:cd06652   80 TLsiFMEYMPGGSIKDQLKSyGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGaskrlqtI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 700 CKEGIGFGDRTstfcGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd06652  160 CLSGTGMKSVT----GTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
550-795 7.97e-16

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: 78.92  E-value: 7.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLgrDEIDSLYCEKRIlETVGRTGHPFLLSLLACIQTSSHA 629
Cdd:cd08229   23 LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLM--DAKARADCIKEI-DLLKQLNHPNVIKYYASFIEDNEL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQI-----HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLckeGI 704
Cdd:cd08229  100 NIVLELADAGDLSRMIkhfkkQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL---GR 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTS---TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFEC--IVNAD---VPCPHFl 776
Cdd:cd08229  177 FFSSKTTaahSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCkkIEQCDyppLPSDHY- 255
                        250
                 ....*....|....*....
gi 564339933 777 SAQGLELIQKLLQKSPEKR 795
Cdd:cd08229  256 SEELRQLVNMCINPDPEKR 274
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
552-800 9.15e-16

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 78.12  E-value: 9.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEP---GDDFEIIQQEISMLK---ECRHPNIVAYFGSYLRRDKLWI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRT 710
Cdd:cd06613   75 VMEYCGGGSLQDIYQVtGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQE---AYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHF-----LSAQGLE 782
Cdd:cd06613  155 KSFIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNFDPPKLkdkekWSPDFHD 234
                        250
                 ....*....|....*...
gi 564339933 783 LIQKLLQKSPEKRLGAGE 800
Cdd:cd06613  235 FIKKCLTKNPKKRPTATK 252
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
553-770 9.24e-16

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: 78.04  E-value: 9.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVllvqYKG----TGKYYAIKALKKQEvLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSH 628
Cdd:cd13983    3 LKFNEVLGRGSFKTV----YRAfdteEGIEVAWNEIKLRK-LPKAERQRFKQEIEILKSLK---HPNIIKFYDSWESKSK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 AC--FVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVL-GLQFLH--EKRIIYRDLKLDNL-LLDAQGFLKIADFGLCKE 702
Cdd:cd13983   75 KEviFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILeGLNYLHtrDPPIIHRDLKCDNIfINGNTGEVKIGDLGLATL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 703 GIGfgDRTSTFCGTPEFLAPEVLtQEAYTRAVDWWGLGVLLYEMLVGECPFPgdtedevfECIVNADV 770
Cdd:cd13983  155 LRQ--SFAKSVIGTPEFMAPEMY-EEHYDEKVDIYAFGMCLLEMATGEYPYS--------ECTNAAQI 211
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
552-795 9.80e-16

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: 78.49  E-value: 9.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrdeiDSLYCEKRILETVgrtghpfllsLLACIQTSS---- 627
Cdd:cd13996    7 DFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTE-------KSSASEKVLREVK----------ALAKLNHPNivry 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFV--------TEFLPGGDLMMQIHE-DVFP---EPQACFYLACVVLGLQFLHEKRIIYRDLKLDNL-LLDAQGFLKI 694
Cdd:cd13996   70 YTAWVeepplyiqMELCEGGTLRDWIDRrNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIfLDNDDLQVKI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLCKEgIGFGDRT---------------STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLvgeCPFpgDTED 759
Cdd:cd13996  150 GDFGLATS-IGNQKRElnnlnnnnngntsnnSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPF--KTAM 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 564339933 760 EVFECIVNA-DVPCPHFLSAQG---LELIQKLLQKSPEKR 795
Cdd:cd13996  224 ERSTILTDLrNGILPESFKAKHpkeADLIQSLLSKNPEER 263
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
558-800 1.09e-15

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: 78.92  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKqevlgrdeidslyCEK--RILETVGRTGH-PFLLSLLACIQT--SSHACF- 631
Cdd:cd14170    9 VLGLGINGKVLQIFNKRTQEKFALKMLQD-------------CPKarREVELHWRASQcPHIVRIVDVYENlyAGRKCLl 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 -VTEFLPGGDLMMQIHE---DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ---GFLKIADFGLCKEGI 704
Cdd:cd14170   76 iVMECLDGGELFSRIQDrgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFgDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF---------PGDTEDEVfecIVNADVPCPHF 775
Cdd:cd14170  156 SH-NSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnhglaisPGMKTRIR---MGQYEFPNPEW 231
                        250       260
                 ....*....|....*....|....*..
gi 564339933 776 --LSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14170  232 seVSEEVKMLIRNLLKTEPTQRMTITE 258
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
559-776 1.13e-15

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: 78.85  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYY-------AIKALKKQevlGRD-EIDSLYCEKRILETVGRtgHPFLLSLLA-CIQTSSHA 629
Cdd:cd05099   20 LGEGCFGQVVRAEAYGIDKSRpdqtvtvAVKMLKDN---ATDkDLADLISEMELMKLIGK--HKNIINLLGvCTQEGPLY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVT--------EFL-----PGGDLMMQIHEdvFPEPQACF--YLAC---VVLGLQFLHEKRIIYRDLKLDNLLLDAQGF 691
Cdd:cd05099   95 VIVEyaakgnlrEFLrarrpPGPDYTFDITK--VPEEQLSFkdLVSCayqVARGMEYLESRRCIHRDLAARNVLVTEDNV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 692 LKIADFGLCK--EGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNA 768
Cdd:cd05099  173 MKIADFGLARgvHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFtLGGSPYPGIPVEELFKLLREG 252
                        250
                 ....*....|...
gi 564339933 769 ---DVP--CPHFL 776
Cdd:cd05099  253 hrmDKPsnCTHEL 265
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
549-795 2.30e-15

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: 77.48  E-value: 2.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKAL---KKQEVlgRDEIdslyceKRILETVGRTGHPFLLSLL-ACIQ 624
Cdd:cd06620    3 KNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIhidAKSSV--RKQI------LRELQILHECHSPYIVSFYgAFLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHACFVTEFLPGGDL------MMQIHEDVfpepqaCFYLACVVL-GLQFLHEK-RIIYRDLKLDNLLLDAQGFLKIAD 696
Cdd:cd06620   75 ENNNIIICMEYMDCGSLdkilkkKGPFPEEV------LGKIAVAVLeGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 697 FGLCKEGIGfgDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTED-----------EVFECI 765
Cdd:cd06620  149 FGVSGELIN--SIADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDddgyngpmgilDLLQRI 226
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564339933 766 VNAD---VPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd06620  227 VNEPpprLPKDRIFPKDLRDFVDRCLLKDPRER 259
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
559-753 4.09e-15

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: 76.54  E-value: 4.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGT---GKYYAIKALKKQEVLGRDEidSLYCEkriLETVGRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd14066    1 IGSGGFGTV----YKGVlenGTVVAVKRLNEMNCAASKK--EFLTE---LEMLGRLRHPNLVRLLGYCLESDEKLLVYEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHE----DVFPEPQ---ACFYLACvvlGLQFLHE---KRIIYRDLKLdnllldAQGFL------KIADFGL 699
Cdd:cd14066   72 MPNGSLEDRLHChkgsPPLPWPQrlkIAKGIAR---GLEYLHEecpPPIIHGDIKS------SNILLdedfepKLTDFGL 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 700 CKEGIGFGD--RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14066  143 ARLIPPSESvsKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAV 198
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
559-805 5.98e-15

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: 76.49  E-value: 5.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQ-EVLGRDEidslYCEKriLETVGRTGHPFLLSLLACIQTSSHAC-----FV 632
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLElSVKNKDR----WCHE--IQIMKKLNHPNVVKACDVPEEMNFLVndvplLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDL--MMQIHEDV--FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG---FLKIADFGLCKEgIG 705
Cdd:cd14039   75 MEYCSGGDLrkLLNKPENCcgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkiVHKIIDLGYAKD-LD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF-----------------PGD---TEDEVFECI 765
Cdd:cd14039  154 QGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFlhnlqpftwhekikkkdPKHifaVEEMNGEVR 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564339933 766 VNADVPCPHFLSAQGLE----LIQKLLQKSPEKRLGAGERDAEE 805
Cdd:cd14039  234 FSTHLPQPNNLCSLIVEpmegWLQLMLNWDPVQRGGGLDTDSKQ 277
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
558-812 6.46e-15

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 75.82  E-value: 6.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKY-YAIKAL------KKQEVLGRdeidslycEKRILETVGrtgHPFLLSLLACIQTSSHAC 630
Cdd:cd14202    9 LIGHGAFAVVFKGRHKEKHDLeVAVKCInkknlaKSQTLLGK--------EIKILKELK---HENIVALYDFQEIANSVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG---------FLKIADFGLC 700
Cdd:cd14202   78 LVMEYCNGGDLADYLHTmRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 KEGIGfGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEV---FECIVNADVPCPHFLS 777
Cdd:cd14202  158 RYLQN-NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLrlfYEKNKSLSPNIPRETS 236
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564339933 778 AQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14202  237 SHLRQLLLGLLQRNQKDRM-----DFDEFFHHPFL 266
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
553-798 6.70e-15

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: 76.00  E-value: 6.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALK---KQEVLGRDEIdslycekRILETVGRTGHPFLLSLLACIQTSSHA 629
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRldtETEGVPSTAI-------REISLLKELNHPNIVKLLDVIHTENKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLpGGDL---MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIGF 706
Cdd:cd07860   75 YLVFEFL-HQDLkkfMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLAR-AFGV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTSTF-CGTPEFLAPEVLT-QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVP----------CP 773
Cdd:cd07860  153 PVRTYTHeVVTLWYRAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEiDQLFRIFRTLGTPdevvwpgvtsMP 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564339933 774 HF------------------LSAQGLELIQKLLQKSPEKRLGA 798
Cdd:cd07860  233 DYkpsfpkwarqdfskvvppLDEDGRDLLSQMLHYDPNKRISA 275
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
559-753 8.39e-15

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: 75.85  E-value: 8.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKA--LKKQEvlgRDEIdsLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKmdLRKQQ---RREL--LFNEVVIMRDYH---HENVVDMYNSYLVGDELWVVMEFL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd06658  102 EGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGT 181
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd06658  182 PYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPY 218
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
545-811 8.73e-15

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: 75.50  E-value: 8.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 545 RNPPQLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALK--KQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLAC 622
Cdd:cd06651    1 KSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQfdPESPETSKEVSALECEIQLLKNLQ---HERIVQYYGC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 623 IQTSSHACFV--TEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG- 698
Cdd:cd06651   78 LRDRAEKTLTifMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGa 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 ------LCKEGIGFGDRTstfcGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFpgdTEDEVFECIVN----- 767
Cdd:cd06651  158 skrlqtICMSGTGIRSVT----GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKiatqp 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564339933 768 ADVPCPHFLSAQGLELIQKLLQKSPEKrlgageRDAEEIKVQPF 811
Cdd:cd06651  231 TNPQLPSHISEHARDFLGCIFVEARHR------PSAEELLRHPF 268
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
559-812 9.06e-15

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: 75.79  E-value: 9.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKyyaIKALKKQEVLGRD---------EIdSLYCEKRiletvgrtgHPFLLSLLACIQTSSHA 629
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGE---IVALKKIRLETEDegvpstairEI-SLLKELN---------HPNIVRLLDVVHSENKL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLpggDL-----MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKegi 704
Cdd:cd07835   74 YLVFEFL---DLdlkkyMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLAR--- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFcgTPE-----FLAPEVLT-QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFEC---------IVNA 768
Cdd:cd07835  148 AFGVPVRTY--THEvvtlwYRAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEiDQLFRIfrtlgtpdeDVWP 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 769 DVPC-PHF------------------LSAQGLELIQKLLQKSPEKRLGAgeRDAEEikvQPFF 812
Cdd:cd07835  226 GVTSlPDYkptfpkwarqdlskvvpsLDEDGLDLLSQMLVYDPAKRISA--KAALQ---HPYF 283
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
550-795 9.71e-15

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: 75.45  E-value: 9.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVllvqYKGT--GKYYAIKALKKQEvlgrDEIDSLYCE--KRILETVGRTGHPFLLSLLACIQT 625
Cdd:cd14147    2 FQELRLEEVIGIGGFGKV----YRGSwrGELVAVKAARQDP----DEDISVTAEsvRQEARLFAMLAHPNIIALKAVCLE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRI---IYRDLKLDNLLLDAQGF--------LKI 694
Cdd:cd14147   74 EPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIEnddmehktLKI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLCKEGigfgDRTSTF--CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECIVNA-DV 770
Cdd:cd14147  154 TDFGLAREW----HKTTQMsaAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGiDCLAVAYGVAVNKlTL 229
                        250       260
                 ....*....|....*....|....*
gi 564339933 771 PCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd14147  230 PIPSTCPEPFAQLMADCWAQDPHRR 254
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
558-812 1.15e-14

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 75.05  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQY-KGTGKYYAIKALKKQEvLGRDEIdSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd14201   13 LVGHGAFAVVFKGRHrKKTDWEVAIKSINKKN-LSKSQI-LLGKEIKILKELQ---HENIVALYDVQEMPNSVFLVMEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF---------LKIADFGLCKEgIGF 706
Cdd:cd14201   88 NGGDLADYLQaKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRkkssvsgirIKIADFGFARY-LQS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEV---FECIVNADVPCPHFLSAQGLEL 783
Cdd:cd14201  167 NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLrmfYEKNKNLQPSIPRETSPYLADL 246
                        250       260
                 ....*....|....*....|....*....
gi 564339933 784 IQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14201  247 LLGLLQRNQKDRM-----DFEAFFSHPFL 270
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
558-795 1.35e-14

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: 75.07  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVllvqYKGT--GKYYAIKALKKQ-EVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd14146    1 IIGVGGFGKV----YRATwkGQEVAVKAARQDpDEDIKATAESVRQEAKLFSMLR---HPNIIKLEGVCLEEPNLCLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIH-EDVFPEPQACFYLACVVL---------GLQFLHEKR---IIYRDLKLDNLLLDAQ--------GFLK 693
Cdd:cd14146   74 FARGGTLNRALAaANAAPGPRRARRIPPHILvnwavqiarGMLYLHEEAvvpILHRDLKSSNILLLEKiehddicnKTLK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 694 IADFGLCKEGigfgDRTSTF--CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECIVNA-D 769
Cdd:cd14146  154 ITDFGLAREW----HRTTKMsaAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGiDGLAVAYGVAVNKlT 229
                        250       260
                 ....*....|....*....|....*.
gi 564339933 770 VPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd14146  230 LPIPSTCPEPFAKLMKECWEQDPHIR 255
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
545-753 1.40e-14

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: 75.03  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 545 RNPPQlqDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrDEIDSLYCEKRILETVGRtgHPFLLSLLACIQ 624
Cdd:cd06608    2 PDPAG--IFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIE----DEEEEIKLEINILRKFSN--HPNIATFYGAFI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHAC------FVTEFLPGG---DLMMQIHED--VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLK 693
Cdd:cd06608   74 KKDPPGgddqlwLVMEYCGGGsvtDLVKGLRKKgkRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVK 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 694 IADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQE-----AYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd06608  154 LVDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGITAIELADGKPPL 218
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
552-795 1.63e-14

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: 74.85  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYK-GTGKYYAIKALK-KQEVLGRDEIDSLYCEKRILETVG----RTGHPFLLSLLACIQT 625
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKVRKKsNGQTLLALKEINmTNPAFGRTEQERDKSVGDIISEVNiikeQLRHPNIVRYYKTFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLPG---GDLMMQIHE--DVFPEPQACFYLACVVLGLQFLH-EKRIIYRDLKLDNLLLDAQGFLKIADFGL 699
Cdd:cd08528   81 NDRLYIVMELIEGaplGEHFSSLKEknEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 CKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV-PCPHFLSA 778
Cdd:cd08528  161 AKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYePLPEGMYS 240
                        250
                 ....*....|....*...
gi 564339933 779 QGLE-LIQKLLQKSPEKR 795
Cdd:cd08528  241 DDITfVIRSCLTPDPEAR 258
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
553-795 1.63e-14

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: 75.02  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKAL----KKQEVLGRDEIDslYCEkriletvgRTGHPFLLSLLA-CI---- 623
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKIlchsKEDVKEAMREIE--NYR--------LFNHPNILRLLDsQIvkea 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 624 QTSSHACFVTEFLPGGDLM-----MQIHEDVFPEPQACFYLACVVLGLQFLHE---KRIIYRDLKLDNLLLDAQGFLKIA 695
Cdd:cd13986   72 GGKKEVYLLLPYYKRGSLQdeierRLVKGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILM 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 696 DFGLC----------KEGIGFGDRTSTFCgTPEFLAPEVLTQEAY---TRAVDWWGLGVLLYEMLVGECPFP--GDTEDE 760
Cdd:cd13986  152 DLGSMnparieiegrREALALQDWAAEHC-TMPYRAPELFDVKSHctiDEKTDIWSLGCTLYALMYGESPFEriFQKGDS 230
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564339933 761 VFECIVNADV--PCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd13986  231 LALAVLSGNYsfPDNSRYSEELHQLVKSMLVVNPAER 267
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
552-813 2.44e-14

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: 74.78  E-value: 2.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALK---KQEVlgRDEIdslyceKRILETVGRTGHPFLLSLLACIQTSSH 628
Cdd:cd06615    2 DFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHleiKPAI--RNQI------IRELKVLHECNSPYIVGFYGAFYSDGE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGG--DLMMQ----IHEDVFPEPQACfylacVVLGLQFLHEKR-IIYRDLKLDNLLLDAQGFLKIADFGLCK 701
Cdd:cd06615   74 ISICMEHMDGGslDQVLKkagrIPENILGKISIA-----VLRGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 EGIGfgDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDE--------------------- 760
Cdd:cd06615  149 QLID--SMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKEleamfgrpvsegeakeshrpv 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 761 ------------VFEC---IVNADVP-CPH-FLSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFFR 813
Cdd:cd06615  227 sghppdsprpmaIFELldyIVNEPPPkLPSgAFSDEFQDFVDKCLKKNPKERA-----DLKELTKHPFIK 291
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
105-167 2.98e-14

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 67.93  E-value: 2.98e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933  105 LEALHRQLEVELKVKQGAENMIHTCASgtPKERKLLAAAQQMLKDSQLKVALLRMKISGLEAS 167
Cdd:pfam02185   2 LQELRKKIEVEKKIKEGAENMLRLLQA--TKDRKVLAEAESELRESNRKIQLLREQLRELQAR 62
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
552-745 3.64e-14

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: 73.61  E-value: 3.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYK-GTGKYYAIKALKKQEVLGRDEIDSLYcEKRILETVGRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRRLE-EVSILRELTLDGHDNIVQLIDSWEYHGHLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHE----DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC-----K 701
Cdd:cd14052   80 IQTELCENGSLDVFLSElgllGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAtvwplI 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564339933 702 EGI-GFGDRtstfcgtpEFLAPEVLTQEAYTRAVDWWGLGVLLYE 745
Cdd:cd14052  160 RGIeREGDR--------EYIAPEILSEHMYDKPADIFSLGLILLE 196
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
559-747 3.92e-14

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: 73.95  E-value: 3.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYK----GTGKYYAIKALK--KQEVLGRD---EID---SLYCE-----KRILETVGRTGHpfllslla 621
Cdd:cd05038   12 LGEGHFGSVELCRYDplgdNTGEQVAVKSLQpsGEEQHMSDfkrEIEilrTLDHEyivkyKGVCESPGRRSL-------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 ciqtsshaCFVTEFLPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL 699
Cdd:cd05038   84 --------RLIMEYLPSGSLrdYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGL 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 700 CK---EGIGF----GDRTStfcgtPEF-LAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd05038  156 AKvlpEDKEYyyvkEPGES-----PIFwYAPECLRESRFSSASDVWSFGVTLYELF 206
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
556-813 4.03e-14

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: 73.61  E-value: 4.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrdeiDSLYCEK---RILETVGRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd07846    6 LGLVGEGSYGMVMKCRHKETGQIVAIKKFLESE-------DDKMVKKiamREIKMLKQLRHENLVNLIEVFRRKKRWYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDL-MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTS 711
Cdd:cd07846   79 FEFVDHTVLdDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVPCPHFlsaqgleliQKLLQ 789
Cdd:cd07846  159 DYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDiDQLYHIIKCLGNLIPRH---------QELFQ 229
                        250       260
                 ....*....|....*....|....
gi 564339933 790 KSPekrLGAGERDAEEIKVQPFFR 813
Cdd:cd07846  230 KNP---LFAGVRLPEVKEVEPLER 250
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
552-755 4.20e-14

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: 73.54  E-value: 4.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLA---VLGRGHFGKVllvqYKG--TGKYYAIKALKKQEvlgrDE-----IDSLYCEKRILETVGrtgHPFLLSLLA 621
Cdd:cd14145    4 DFSELVleeIIGIGGFGKV----YRAiwIGDEVAVKAARHDP----DEdisqtIENVRQEAKLFAMLK---HPNIIALRG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 CIQTSSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRI---IYRDLKLD--------NLLLDAQG 690
Cdd:cd14145   73 VCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSnililekvENGDLSNK 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 691 FLKIADFGLCKEGigfgDRTSTF--CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPG 755
Cdd:cd14145  153 ILKITDFGLAREW----HRTTKMsaAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRG 215
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
559-765 4.35e-14

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 74.28  E-value: 4.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGK-------YYAIKALKKQEVlgRDEIDSLYCEKRILETVGRtgHPFLLSLL-ACIQTSSHAC 630
Cdd:cd05101   32 LGEGCFGQVVMAEAVGIDKdkpkeavTVAVKMLKDDAT--EKDLSDLVSEMEMMKMIGK--HKNIINLLgACTQDGPLYV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVtEFLPGGDLM----------MQIHEDV--FPEPQACF--YLAC---VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLK 693
Cdd:cd05101  108 IV-EYASKGNLReylrarrppgMEYSYDInrVPEEQMTFkdLVSCtyqLARGMEYLASQKCIHRDLAARNVLVTENNVMK 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 694 IADFGLCKE--GIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECI 765
Cdd:cd05101  187 IADFGLARDinNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFtLGGSPYPGIPVEELFKLL 261
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
558-800 4.69e-14

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: 73.24  E-value: 4.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVllvqYKG---TGKYYAIKalkkQEVLgrDEIDSLYCEK---RILETVGrtghpfLLSLL----------A 621
Cdd:cd06631    8 VLGKGAYGTV----YCGltsTGQLIAVK----QVEL--DTSDKEKAEKeyeKLQEEVD------LLKTLkhvnivgylgT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 CIQTSSHACFVtEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG-- 698
Cdd:cd06631   72 CLEDNVVSIFM-EFVPGGSIASILARfGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGca 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 --LCKEG--IGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCP- 773
Cdd:cd06631  151 krLCINLssGSQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPr 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 564339933 774 ---HFlSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd06631  231 lpdKF-SPEARDFVHACLTRDQDERPSAEQ 259
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
558-753 6.37e-14

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: 72.71  E-value: 6.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVllvqYKGT--GKYYAIKALKKQEvlgrDEIDSLYCEKRILET--VGRTGHPFLLSLLACIQTSSHACFVT 633
Cdd:cd14148    1 IIGVGGFGKV----YKGLwrGEEVAVKAARQDP----DEDIAVTAENVRQEArlFWMLQHPNIIALRGVCLNPPHLCLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKR---IIYRDLK--------LDNLLLDAQGFLKIADFGLCKE 702
Cdd:cd14148   73 EYARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKssnililePIENDDLSGKTLKITDFGLARE 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564339933 703 GigfgDRTSTF--CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14148  153 W----HKTTKMsaAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
560-800 6.40e-14

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: 72.72  E-value: 6.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 560 GRGHFGKVLLVQYKGTGKYYAIKALKKQEvLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPGG 639
Cdd:cd06626    9 GEGTFGKVYTAVNLDTGELMAMKEIRFQD-NDPKTIKEIADEMKVLE---GLDHPNLVRYYGVEVHREEVYIFMEYCQEG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 640 DLmmqihEDVF----PEPQACF--YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGlCKEGIGFGDRT--- 710
Cdd:cd06626   85 TL-----EELLrhgrILDEAVIrvYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG-SAVKLKNNTTTmap 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 ---STFCGTPEFLAPEVLT---QEAYTRAVDWWGLGVLLYEMLVGECPFPgdTEDEVFECIVNA------DVPCPHFLSA 778
Cdd:cd06626  159 gevNSLVGTPAYMAPEVITgnkGEGHGRAADIWSLGCVVLEMATGKRPWS--ELDNEWAIMYHVgmghkpPIPDSLQLSP 236
                        250       260
                 ....*....|....*....|..
gi 564339933 779 QGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd06626  237 EGKDFLSRCLESDPKKRPTASE 258
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
19-74 6.83e-14

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 66.83  E-value: 6.83e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933    19 DEKEMIRRAIQKELKIKEGMENMRRVAT-DRRHLGHVQQLLRASNRRLEQLHGELRE 74
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSnDRKVLSEAQSMLRESNQKLDLLKEELEK 57
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
559-795 8.15e-14

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: 72.77  E-value: 8.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYyAIKALKKqevlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05072   15 LGAGQFGEVWMGYYNNSTKV-AVKTLKP----GTMSVQAFLEEANLMKTLQ---HDKLVRLYAVVTKEEPIYIITEYMAK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVFPE---PQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL----------CKEGIG 705
Cdd:cd05072   87 GSLLDFLKSDEGGKvllPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLarviedneytAREGAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FgdrtstfcgtP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLE 782
Cdd:cd05072  167 F----------PiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGyRMPRMENCPDELYD 236
                        250
                 ....*....|...
gi 564339933 783 LIQKLLQKSPEKR 795
Cdd:cd05072  237 IMKTCWKEKAEER 249
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
559-798 8.29e-14

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: 72.30  E-value: 8.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIK----ALKKQEVLGRdeidslycEKRILETVGrtgHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKfvskKMKKKEQAAH--------EAALLQHLQ---HPQYITLHDTYESPTSYILVLE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIY---RDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRT 710
Cdd:cd14115   70 LMDDGRLLdYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHldiKPENLLIDLRIPVPRVKLIDLEDAVQ-ISGHRHV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDE--VFECIVNADVPCPHF--LSAQGLELIQK 786
Cdd:cd14115  149 HHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEEtcINVCRVDFSFPDEYFgdVSQAARDFINV 228
                        250
                 ....*....|..
gi 564339933 787 LLQKSPEKRLGA 798
Cdd:cd14115  229 ILQEDPRRRPTA 240
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
551-800 8.52e-14

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: 73.49  E-value: 8.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrdeiDSLYC-----EKRILEtvgRTGHPFLLSLLAcIQT 625
Cdd:cd07849    5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFE-------HQTYClrtlrEIKILL---RFKHENIIGILD-IQR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHAC------FVTEFLPGgDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL 699
Cdd:cd07849   74 PPTFEsfkdvyIVQELMET-DLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 CKEGIGFGDRTST---FCGTPEFLAPEV-LTQEAYTRAVDWWGLGVLLYEMLVGECPFPGD----------------TED 759
Cdd:cd07849  153 ARIADPEHDHTGFlteYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKdylhqlnlilgilgtpSQE 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 760 EvFECIVNA-------DVPC----------PHfLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd07849  233 D-LNCIISLkarnyikSLPFkpkvpwnklfPN-ADPKALDLLDKMLTFNPHKRITVEE 288
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
559-747 1.18e-13

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: 71.75  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQevlgrDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRF-----DEQRSFLKEVKLMR---RLSHPNILRFIGVCVKDNKLNFITEYVNG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDL--MMQIHEDVFPEPQAcFYLAC-VVLGLQFLHEKRIIYRDLKLD--NLLLDAQGFLKI-ADFGLCKE----GIGFGD 708
Cdd:cd14065   73 GTLeeLLKSMDEQLPWSQR-VSLAKdIASGMAYLHSKNIIHRDLNSKncLVREANRGRNAVvADFGLAREmpdeKTKKPD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564339933 709 RTS--TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd14065  152 RKKrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII 192
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
559-796 1.24e-13

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: 72.49  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALkkqevlgrdeIDSLYCEKRILETVGRTGHPFLLSLLACIQTS----------SH 628
Cdd:cd14171   14 LGTGISGPVRVCVKKSTGERFALKIL----------LDRPKARTEVRLHMMCSGHPNIVQIYDVYANSvqfpgessprAR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQI-HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLD---NLLLDAQGFLKIADFGLCKEGI 704
Cdd:cd14171   84 LLIVMELMEGGELFDRIsQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPEnllLKDNSEDAPIKLCDFGFAKVDQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GfGDRTSTFcgTPEFLAPEVL-----------------TQEAYTRAVDWWGLGVLLYEMLVGECPFPGDT-----EDEVF 762
Cdd:cd14171  164 G-DLMTPQF--TPYYVAPQVLeaqrrhrkersgiptspTPYTYDKSCDMWSLGVIIYIMLCGYPPFYSEHpsrtiTKDMK 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564339933 763 ECIVNADVPCPH----FLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd14171  241 RKIMTGSYEFPEeewsQISEMAKDIVRKLLCVDPEERM 278
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
559-765 1.31e-13

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: 72.74  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGK-------YYAIKALKKQEVlgRDEIDSLYCEKRILETVGRtgHPFLLSLL-ACIQTSSHAC 630
Cdd:cd05098   21 LGEGCFGQVVLAEAIGLDKdkpnrvtKVAVKMLKSDAT--EKDLSDLISEMEMMKMIGK--HKNIINLLgACTQDGPLYV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVtEFLPGGDLMMQIHEDVFPEPQACFYLAC-----------------VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLK 693
Cdd:cd05098   97 IV-EYASKGNLREYLQARRPPGMEYCYNPSHnpeeqlsskdlvscayqVARGMEYLASKKCIHRDLAARNVLVTEDNVMK 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 694 IADFGLCKE--GIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECI 765
Cdd:cd05098  176 IADFGLARDihHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFtLGGSPYPGVPVEELFKLL 250
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
558-747 1.41e-13

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: 72.24  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYK----GTGKYYAIKALKKQevLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACI--QTSSHACF 631
Cdd:cd05080   11 DLGEGHFGKVSLYCYDptndGTGEMVAVKALKAD--CGPQHRSGWKQEIDILKTLY---HENIVKYKGCCseQGGKSLQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIGFGD--- 708
Cdd:cd05080   86 IMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAK-AVPEGHeyy 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEF-LAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd05080  165 RVREDGDSPVFwYAPECLKEYKFYYASDVWSFGVTLYELL 204
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
559-795 1.52e-13

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: 71.97  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGrDEIDSLYcekRILETVgrTGHPFLLSLLAC-----IQTSSHACFVT 633
Cdd:cd06638   26 IGKGTYGKVFKVLNKKNGSKAAVKILDPIHDID-EEIEAEY---NILKAL--SDHPNVVKFYGMyykkdVKNGDQLWLVL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGG---DLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd06638  100 ELCNGGsvtDLVkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQE-----AYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPC---PHFLSAQG 780
Cdd:cd06638  180 RRNTSVGTPFWMAPEVIACEqqldsTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPTlhqPELWSNEF 259
                        250
                 ....*....|....*
gi 564339933 781 LELIQKLLQKSPEKR 795
Cdd:cd06638  260 NDFIRKCLTKDYEKR 274
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
551-795 1.59e-13

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: 71.19  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSlYCEKRILETVGRtgHPFLLSLLACIQTSSHAC 630
Cdd:cd14050    1 QCFTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRK-LEEVERHEKLGE--HPNCVRFIKAWEEKGILY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEfLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDR 709
Cdd:cd14050   78 IQTE-LCDTSLQQYCEEtHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVE-LDKEDI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLtQEAYTRAVDWWGLGVLLYEMLVG-ECPFPGDTedevFECIVNADVPCPHF--LSAQGLELIQK 786
Cdd:cd14050  156 HDAQEGDPRYMAPELL-QGSFTKAADIFSLGITILELACNlELPSGGDG----WHQLRQGYLPEEFTagLSPELRSIIKL 230

                 ....*....
gi 564339933 787 LLQKSPEKR 795
Cdd:cd14050  231 MMDPDPERR 239
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
559-800 1.61e-13

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 71.98  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKA--LKKQEvlgRDEIdsLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKmdLRKQQ---RREL--LFNEVVIMRDYQ---HENVVEMYNSYLVGDELWVVMEFL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGT 716
Cdd:cd06657  100 EGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGT 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 PEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNaDVPcPHFLSAQGLE-----LIQKLLQKS 791
Cdd:cd06657  180 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD-NLP-PKLKNLHKVSpslkgFLDRLLVRD 257

                 ....*....
gi 564339933 792 PEKRLGAGE 800
Cdd:cd06657  258 PAQRATAAE 266
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
549-798 1.65e-13

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: 72.35  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAikaLKKqeVLGRDEIDSLYC----EKRILEtvgRTGHPFLLSLLACI- 623
Cdd:cd07866    6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVA---LKK--ILMHNEKDGFPItalrEIKILK---KLKHPNVVPLIDMAv 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 624 -----QTSSHACF--VTEFLpGGDLMMQIH-EDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKI 694
Cdd:cd07866   78 erpdkSKRKRGSVymVTPYM-DHDLSGLLEnPSVkLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLC----------KEGIGFGDRTSTFC-GTPEFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVF 762
Cdd:cd07866  157 ADFGLArpydgpppnpKGGGGGGTRKYTNLvVTRWYRPPELLLGERrYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQL 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 763 ECI-----------------------VNADVPCP-----HF--LSAQGLELIQKLLQKSPEKRLGA 798
Cdd:cd07866  237 HLIfklcgtpteetwpgwrslpgcegVHSFTNYPrtleeRFgkLGPEGLDLLSKLLSLDPYKRLTA 302
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
559-795 1.98e-13

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: 71.46  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYyAIKALKKqevlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIqTSSHACFVTEFLPG 638
Cdd:cd05067   15 LGAGQFGEVWMGYYNGHTKV-AIKSLKQ----GSMSPDAFLAEANLMKQLQ---HQRLVRLYAVV-TQEPIYIITEYMEN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDV---FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK----------EGIG 705
Cdd:cd05067   86 GSLVDFLKTPSgikLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARliedneytarEGAK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FgdrtstfcgtP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECI-VNADVPCPHFLSAQGLE 782
Cdd:cd05067  166 F----------PiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVIQNLeRGYRMPRPDNCPEELYQ 235
                        250
                 ....*....|...
gi 564339933 783 LIQKLLQKSPEKR 795
Cdd:cd05067  236 LMRLCWKERPEDR 248
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
103-161 1.98e-13

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 65.29  E-value: 1.98e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933   103 RLLEALHRQLEVELKVKQGAENMIHTcasgTPKERKLLAAAQQMLKDSQLKVALLRMKI 161
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKL----TSNDRKVLSEAQSMLRESNQKLDLLKEEL 55
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
553-796 2.29e-13

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 71.11  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVllvqYKGT----GKYYAIKALKKQEVLGRDEIDS---LYCEKRILETVGRTGHPFLLSLLACIQT 625
Cdd:cd14005    2 YEVGDLLGKGGFGTV----YSGVrirdGLPVAVKFVPKSRVTEWAMINGpvpVPLEIALLLKASKPGVPGVIRLLDWYER 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEF-LPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYR-DLKLDNLLLDAQGFLKIADFG---L 699
Cdd:cd14005   78 PDGFLLIMERpEPCQDLFDFITErGALSENLARIIFRQVVEAVRHCHQRGVLHRdIKDENLLINLRTGEVKLIDFGcgaL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 CKEGIgfgdrTSTFCGTPEFLAPEVLTQEAY-TRAVDWWGLGVLLYEMLVGECPFPGDTEdevfecIVNADVPCPHFLSA 778
Cdd:cd14005  158 LKDSV-----YTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFENDEQ------ILRGNVLFRPRLSK 226
                        250
                 ....*....|....*...
gi 564339933 779 QGLELIQKLLQKSPEKRL 796
Cdd:cd14005  227 ECCDLISRCLQFDPSKRP 244
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
22-80 2.65e-13

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 65.23  E-value: 2.65e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933   22 EMIRRAIQKELKIKEGMENMRRV---ATDRRHLGHVQQLLRASNRRLEQLHGELRELHAQVL 80
Cdd:pfam02185   3 QELRKKIEVEKKIKEGAENMLRLlqaTKDRKVLAEAESELRESNRKIQLLREQLRELQARHL 64
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
559-753 3.15e-13

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: 71.18  E-value: 3.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGrDEIDSLYcekRILETVgrTGHPFLLSLLACIQTSSHAC-----FVT 633
Cdd:cd06639   30 IGKGTYGKVYKVTNKKDGSLAAVKILDPISDVD-EEIEAEY---NILRSL--PNHPNVVKFYGMFYKADQYVggqlwLVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLM-----MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd06639  104 ELCNGGSVTelvkgLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSARL 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFLAPEVLTQE-----AYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd06639  184 RRNTSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPL 233
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
558-795 3.16e-13

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: 70.83  E-value: 3.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlgrDEIDSLYCEKRILETVGrtGHPFLLSLLACIQTSSH----ACFVT 633
Cdd:cd13985    7 QLGEGGFSYVYLAHDVNTGRRYALKRMYFNDE---EQLRVAIKEIEIMKRLC--GHPNIVQYYDSAILSSEgrkeVLLLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEK--RIIYRDLKLDNLLLDAQGFLKIADFG---------LC 700
Cdd:cd13985   82 EYCPGSlvDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQspPIIHRDIKIENILFSNTGRFKLCDFGsattehyplER 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 KEGIGFGDRTSTFCGTPEFLAPEVLTQEAY---TRAVDWWGLGVLLYEMLVGECPFpgDTEDEVFECIVNADVPCPHFLS 777
Cdd:cd13985  162 AEEVNIIEEEIQKNTTPMYRAPEMIDLYSKkpiGEKADIWALGCLLYKLCFFKLPF--DESSKLAIVAGKYSIPEQPRYS 239
                        250
                 ....*....|....*...
gi 564339933 778 AQGLELIQKLLQKSPEKR 795
Cdd:cd13985  240 PELHDLIRHMLTPDPAER 257
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
556-800 3.33e-13

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: 71.94  E-value: 3.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKK--QevlgrDEIDS--LYCEKRILETVGrtgHPFLLSLLACIQTSSHA-- 629
Cdd:cd07851   20 LSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpfQ-----SAIHAkrTYRELRLLKHMK---HENVIGLLDVFTPASSLed 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 ----CFVTEFLpGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGig 705
Cdd:cd07851   92 fqdvYLVTHLM-GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHT-- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 fGDRTSTFCGTPEFLAPEV-LTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVN-ADVPCPHFL------- 776
Cdd:cd07851  169 -DDEMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNlVGTPDEELLkkisses 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 564339933 777 -----------------------SAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd07851  248 arnyiqslpqmpkkdfkevfsgaNPLAIDLLEKMLVLDPDKRITAAE 294
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
560-795 3.41e-13

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: 70.62  E-value: 3.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 560 GRGHFGKVLLVQYKGTGKYYAIK-----ALKKQEVLGRDEI-DSLYCEKriletvgrtghpfLLSLLACIQTSSHACFVT 633
Cdd:cd14111   12 ARGRFGVIRRCRENATGKNFPAKivpyqAEEKQGVLQEYEIlKSLHHER-------------IMALHEAYITPRYLVLIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRT-S 711
Cdd:cd14111   79 EFCSGKELLHSLIDRFrYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQlG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF----PGDTEDEVFECIVNADVPCPHfLSAQGLELIQKL 787
Cdd:cd14111  159 RRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFedqdPQETEAKILVAKFDAFKLYPN-VSQSASLFLKKV 237

                 ....*...
gi 564339933 788 LQKSPEKR 795
Cdd:cd14111  238 LSSYPWSR 245
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
559-763 3.56e-13

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: 70.91  E-value: 3.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYY------AIKALKkQEVLGRDEIDsLYCEKRILETVGRtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd05053   20 LGEGAFGQVVKAEAVGLDNKPnevvtvAVKMLK-DDATEKDLSD-LVSEMEMMKMIGK--HKNIINLLGACTQDGPLYVV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMmQIHEDVFPEPQACFYLACVVL------------------GLQFLHEKRIIYRDLKLDNLLLDAQGFLKI 694
Cdd:cd05053   96 VEYASKGNLR-EFLRARRPPGEEASPDDPRVPeeqltqkdlvsfayqvarGMEYLASKKCIHRDLAARNVLVTEDNVMKI 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 695 ADFGLCKeGIGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYE-MLVGECPFPGDTEDEVFE 763
Cdd:cd05053  175 ADFGLAR-DIHHIDyyRKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIPVEELFK 246
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
559-796 3.94e-13

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: 70.83  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGTGKYY---------AIKALkkQEVLGRDEIDSLYCEKRILETVGRtghPFLLSLLACIQTSSHA 629
Cdd:cd05032   14 LGQGSFGMV----YEGLAKGVvkgepetrvAIKTV--NENASMRERIEFLNEASVMKEFNC---HHVVRLLGVVSTGQPT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQI--------HEDVFPEPQAC-FYLACVVL--GLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG 698
Cdd:cd05032   85 LVVMELMAKGDLKSYLrsrrpeaeNNPGLGPPTLQkFIQMAAEIadGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 LCKEgIGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNADV---P 771
Cdd:cd05032  165 MTRD-IYETDyyRKGGKGLLPvRWMAPESLKDGVFTTKSDVWSFGVVLWEMAtLAEQPYQGLSNEEVLKFVIDGGHldlP 243
                        250       260
                 ....*....|....*....|....*..
gi 564339933 772 --CPHFLsaqgLELIQKLLQKSPEKRL 796
Cdd:cd05032  244 enCPDKL----LELMRMCWQYNPKMRP 266
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
552-746 4.56e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 70.15  E-value: 4.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKkQEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIP-VEQMTKEERQAALNEVKVLS---MLHHPNIIEYYESFLEDKALMI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIH---EDVFPEPQACFYLACVVLGLQFLHEKRIIYR-DLKLDNLLLDAQGFLKIADFGLCKEgIGFG 707
Cdd:cd08220   77 VMEYAPGGTLFEYIQqrkGSLLSEEEILHFFVQILLALHHVHSKQILHRdLKTQNILLNKKRTVVKIGDFGISKI-LSSK 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEM 746
Cdd:cd08220  156 SKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYEL 194
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
559-753 4.85e-13

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: 70.98  E-value: 4.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLgrdeiDSLYCEKRILETVGRTGHPFLLSLLAC--IQTSSHACFVTEFL 636
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFM-----RPLDVQMREFEVLKKLNHKNIVKLFAIeeELTTRHKVLVMELC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDL--MMQIHEDVF--PEPQACFYLACVVLGLQFLHEKRIIYRDLK----LDNLLLDAQGFLKIADFGLCKEgIGFGD 708
Cdd:cd13988   76 PCGSLytVLEEPSNAYglPESEFLIVLRDVVAGMNHLRENGIVHRDIKpgniMRVIGEDGQSVYKLTDFGAARE-LEDDE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564339933 709 RTSTFCGTPEFLAPE-----VL---TQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd13988  155 QFVSLYGTEEYLHPDmyeraVLrkdHQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
558-800 4.94e-13

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: 71.02  E-value: 4.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKalKKQEVLgRDEIDSlyceKRILETV---GRTGHPFLLSLLACIQTSSHACF--- 631
Cdd:cd07834    7 PIGSGAYGVVCSAYDKRTGRKVAIK--KISNVF-DDLIDA----KRILREIkilRHLKHENIIGLLDILRPPSPEEFndv 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 --VTEFLPGgDLMMQIHEDVFPEPQACFYLACVVL-GLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCkegigfgd 708
Cdd:cd07834   80 yiVTELMET-DLHKVIKSPQPLTDDHIQYFLYQILrGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLA-------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPEFL----------APEV-LTQEAYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDE---VFECIvnaDVPCP 773
Cdd:cd07834  151 RGVDPDEDKGFLteyvvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGrDYIDQlnlIVEVL---GTPSE 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 774 HFL------------------------------SAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd07834  228 EDLkfissekarnylkslpkkpkkplsevfpgaSPEAIDLLEKMLVFNPKKRITADE 284
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
553-800 7.37e-13

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: 69.82  E-value: 7.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRD-----EIdSLYCEKRiletvgrtgHPFLLSLLACIQTSS 627
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPstairEI-SLMKELK---------HENIVRLHDVIHTEN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGgDL--MMQIHEDVFPEP--QACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeg 703
Cdd:cd07836   72 KLMLVFEYMDK-DLkkYMDTHGVRGALDpnTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLAR-- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 704 iGFGDRTSTFCG---TPEFLAPEVLT-QEAYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECI------------- 765
Cdd:cd07836  149 -AFGIPVNTFSNevvTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLFPGtNNEDQLLKIFrimgtptestwpg 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339933 766 ------VNADVP-CPH--------FLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd07836  228 isqlpeYKPTFPrYPPqdlqqlfpHADPLGIDLLHRLLQLNPELRISAHD 277
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
634-812 8.59e-13

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 69.38  E-value: 8.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDL---MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRT 710
Cdd:cd08221   79 EYCNGGNLhdkIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMA 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGL-ELIQKLLQ 789
Cdd:cd08221  159 ESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQYSEEIiQLVHDCLH 238
                        170       180
                 ....*....|....*....|...
gi 564339933 790 KSPEKRlgageRDAEEIKVQPFF 812
Cdd:cd08221  239 QDPEDR-----PTAEELLERPLL 256
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
556-795 9.13e-13

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: 69.66  E-value: 9.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVllvqYKG----TGKYYAIK--ALKKQ--EVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSS 627
Cdd:cd13990    5 LNLLGKGGFSEV----YKAfdlvEQRYVACKihQLNKDwsEEKKQNYIKHALREYEIHKSLD---HPRIVKLYDVFEIDT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HA-CFVTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKR--IIY---RDLKLDNLLLDAQGFLKIADFGLC 700
Cdd:cd13990   78 DSfCTVLEYCDGNDLDFYLKQHkSIPEREARSIIMQVVSALKYLNEIKppIIHydlKPGNILLHSGNVSGEIKITDFGLS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 K---------EGIgfgDRTSTFCGTPEFLAPEVL----TQEAYTRAVDWWGLGVLLYEMLVGECPFPGD--TEDEVFE-C 764
Cdd:cd13990  158 KimddesynsDGM---ELTSQGAGTYWYLPPECFvvgkTPPKISSKVDVWSVGVIFYQMLYGRKPFGHNqsQEAILEEnT 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564339933 765 IVNA---DVPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd13990  235 ILKAtevEFPSKPVVSSEAKDFIRRCLTYRKEDR 268
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
558-795 9.90e-13

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: 69.11  E-value: 9.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEI-DSLYC--EKRILETVGR-TGHPFLLSLLACIQTSSHACFVT 633
Cdd:cd14101    7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLpGVNPVpnEVALLQSVGGgPGHRGVIRLLDWFEIPEGFLLVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EF-LPGGDLMMQIHED-VFPE-PQACFYLAcVVLGLQFLHEKRIIYRDLKLDNLLLDAQ-GFLKIADFGlckEGIGFGDR 709
Cdd:cd14101   87 ERpQHCQDLFDYITERgALDEsLARRFFKQ-VVEAVQHCHSKGVVHRDIKDENILVDLRtGDIKLIDFG---SGATLKDS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TST-FCGTPEFLAPE-VLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEdevfecIVNADVPCPHFLSAQGLELIQKL 787
Cdd:cd14101  163 MYTdFDGTRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPFERDTD------ILKAKPSFNKRVSNDCRSLIRSC 236

                 ....*...
gi 564339933 788 LQKSPEKR 795
Cdd:cd14101  237 LAYNPSDR 244
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
559-765 9.99e-13

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 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 FGFR3 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: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 70.43  E-value: 9.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDE-----IDSLYCEKRILETVGRtgHPFLLSLL-ACIQTSSHACFV 632
Cdd:cd05100   20 LGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDatdkdLSDLVSEMEMMKMIGK--HKNIINLLgACTQDGPLYVLV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 T--------EFL-----PGGDLMMQIHEdvFPEPQACF--YLAC---VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKI 694
Cdd:cd05100   98 EyaskgnlrEYLrarrpPGMDYSFDTCK--LPEEQLTFkdLVSCayqVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933 695 ADFGLCKE--GIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECI 765
Cdd:cd05100  176 ADFGLARDvhNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELFKLL 249
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
560-755 1.21e-12

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: 68.45  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 560 GRGHFGKVLLVQYKGTGKYYAIKALKKQEvlGRDEIDSLYCEKRILETVGrtghpfllsllACIQTSSHaCFVTEFLPGG 639
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIE--KEAEILSVLSHRNIIQFYG-----------AILEAPNY-GIVTEYASYG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 640 DLMMQIHEDVFPE---PQACFYLACVVLGLQFLHEK---RIIYRDLKLDNLLLDAQGFLKIADFGLCKegigFGDRTS-- 711
Cdd:cd14060   68 SLFDYLNSNESEEmdmDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASR----FHSHTThm 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564339933 712 TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPG 755
Cdd:cd14060  144 SLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG 187
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
559-796 1.30e-12

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: 69.04  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlGRDeidslYCEK---RILETVGRTGHPFLLSLLACIQTSSHACF-VTE 634
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKA-PDD-----FVEKflpRELEILARLNHKSIIKTYEIFETSDGKVYiVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLM------MQIHEDVfpePQACFYLACvvLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK----EGI 704
Cdd:cd14165   83 LGVQGDLLefiklrGALPEDV---ARKMFHQLS--SAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKrclrDEN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVpcpHFLSAQGL-- 781
Cdd:cd14165  158 GRIVLSKTFCGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRV---RFPRSKNLts 234
                        250
                 ....*....|....*...
gi 564339933 782 ---ELIQKLLQKSPEKRL 796
Cdd:cd14165  235 eckDLIYRLLQPDVSQRL 252
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
559-795 1.37e-12

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: 68.62  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKkqEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLA-CIQTSShACFVTEFLP 637
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCR--ETLPPDLKRKFLQEARILK---QYDHPNIVKLIGvCVQKQP-IMIVMELVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTfcG 715
Cdd:cd05041   77 GGSLLtfLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSD--G 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPE----FLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECI-VNADVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd05041  155 LKQipikWTAPEALNYGRYTSESDVWSFGILLWEIFsLGATPYPGMSNQQTREQIeSGYRMPAPELCPEAVYRLMLQCWA 234

                 ....*.
gi 564339933 790 KSPEKR 795
Cdd:cd05041  235 YDPENR 240
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
559-795 1.44e-12

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: 68.46  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYyAIKALKKqevlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05034    3 LGAGQFGEVWMGVWNGTTKV-AVKTLKP----GTMSPEAFLQEAQIMKKLR---HDKLVQLYAVCSDEEPIYIVTELMSK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHED---VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC---KEGIGFGDRTST 712
Cdd:cd05034   75 GSLLDYLRTGegrALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLArliEDDEYTAREGAK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 713 FcgtP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECI-VNADVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd05034  155 F---PiKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVLEQVeRGYRMPKPPGCPDELYDIMLQCWK 231

                 ....*.
gi 564339933 790 KSPEKR 795
Cdd:cd05034  232 KEPEER 237
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
559-747 1.63e-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: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKELIRCD---EETQKTFLTEVKVMRSLD---HPNVLKFIGVLYKDKRLNLLTEFIEG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC----------------- 700
Cdd:cd14222   75 GTLKDFLRAdDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveekkkpppdkptt 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 -KEGIGFGDRTS--TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd14222  155 kKRTLRKNDRKKryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
552-812 1.67e-12

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: 68.40  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVllvqYKGT-----------GKYYAIKALKKQEVLGRdeidsLYCEKRILETVGrtGHPFLLSLL 620
Cdd:cd14019    2 KYRIIEKIGEGTFSSV----YKAEdklhdlydrnkGRLVALKHIYPTSSPSR-----ILNELECLERLG--GSNNVSGLI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 621 ACIQTSSHACFVTEFLPGGDLMMQIHEDVFPEPQAcfYLACVVLGLQFLHEKRIIYRDLKLD---NLLLDAQGFLkiADF 697
Cdd:cd14019   71 TAFRNEDQVVAVLPYIEHDDFRDFYRKMSLTDIRI--YLRNLFKALKHVHSFGIIHRDVKPGnflYNRETGKGVL--VDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 698 GLCKegiGFGDRTS---TFCGTPEFLAPEVLTQ-EAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDevFECIVNAdvpCP 773
Cdd:cd14019  147 GLAQ---REEDRPEqraPRAGTRGFRAPEVLFKcPHQTTAIDIWSAGVILLSILSGRFPFFFSSDD--IDALAEI---AT 218
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564339933 774 HFLSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14019  219 IFGSDEAYDLLDKLLELDPSKRI-----TAEEALKHPFF 252
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
558-795 4.03e-12

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 67.28  E-value: 4.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGtgKYYAIKALKKQEvlgrdeidSLYCEKRILETVGRTGHPFLLSLLAciqTSSHA-CFVTEFL 636
Cdd:cd14068    1 LLGDGGFGSVYRAVYRG--EDVAVKIFNKHT--------SFRLLRQELVVLSHLHHPSLVALLA---AGTAPrMLVMELA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGG--DLMMQiHEDVFPEPQACFYLAC-VVLGLQFLHEKRIIYRDLKLD-----NLLLDAQGFLKIADFGLCKEGIGFGD 708
Cdd:cd14068   68 PKGslDALLQ-QDNASLTRTLQHRIALhVADGLRYLHSAMIIYRDLKPHnvllfTLYPNCAIIAKIADYGIAQYCCRMGI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTStfCGTPEFLAPEVLTQE-AYTRAVDWWGLGVLLYEMLVG------ECPFPgdteDEVFECIVNADVPCP--HFLSA- 778
Cdd:cd14068  147 KTS--EGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILTCgeriveGLKFP----NEFDELAIQGKLPDPvkEYGCAp 220
                        250
                 ....*....|....*....
gi 564339933 779 -QGLE-LIQKLLQKSPEKR 795
Cdd:cd14068  221 wPGVEaLIKDCLKENPQCR 239
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
532-800 4.09e-12

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: 68.14  E-value: 4.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 532 RTGVA--PPLAALSTRNPPQlQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVG 609
Cdd:cd06633    1 RKGVLkdPEIADLFYKDDPE-EIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 610 rtgHPFLLSLLACIQTSSHACFVTEF-LPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDA 688
Cdd:cd06633   80 ---HPNTIEYKGCYLKDHTAWLVMEYcLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 689 QGFLKIADFGlckeGIGFGDRTSTFCGTPEFLAPEV---LTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI 765
Cdd:cd06633  157 PGQVKLADFG----SASIASPANSFVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHI 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 564339933 766 VNADVPcphflSAQGLE-------LIQKLLQKSPEKRLGAGE 800
Cdd:cd06633  233 AQNDSP-----TLQSNEwtdsfrgFVDYCLQKIPQERPSSAE 269
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
559-747 5.21e-12

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: 67.15  E-value: 5.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrDEIDSLYCEK----RILEtvgrtgHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIRFD----EEAQRNFLKEvkvmRSLD------HPNVLKFIGVLYKDKKLNLITE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIHE--DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK----------- 701
Cdd:cd14154   71 YIPGGTLKDVLKDmaRPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARliveerlpsgn 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 702 EGIGFGDRTS---------TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd14154  151 MSPSETLRHLkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
559-789 5.52e-12

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: 66.94  E-value: 5.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlGRDEIDSLYCeKRILETVGRTGHPFLLSLLACIQTSS-HACFVTEFLP 637
Cdd:cd14163    8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSG--GPEEFIQRFL-PRELQIVERLDHKNIIHVYEMLESADgKIYLVMELAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLM-MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLdaQGF-LKIADFGLCKE-GIGFGDRTSTFC 714
Cdd:cd14163   85 DGDVFdCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL--QGFtLKLTDFGFAKQlPKGGRELSQTFC 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 715 GTPEFLAPEVLTQEAY-TRAVDWWGLGVLLYEMLVGECPFpGDTEDEVFECIVNADVPCPHFL--SAQGLELIQKLLQ 789
Cdd:cd14163  163 GSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPF-DDTDIPKMLCQQQKGVSLPGHLgvSRTCQDLLKRLLE 239
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
559-818 8.02e-12

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 66.66  E-value: 8.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYyAIKALKkqevLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05068   16 LGSGQFGEVWEGLWNNTTPV-AVKTLK----PGTMDPEDFLREAQIMK---KLRHPKLIQLYAVCTLEEPIYIITELMKH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHED--VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTSTFCGT 716
Cdd:cd05068   88 GSLLEYLQGKgrSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARV-IKVEDEYEAREGA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 P---EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLELIQKLLQKS 791
Cdd:cd05068  167 KfpiKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQVERGyRMPCPPNCPPQLYDIMLECWKAD 246
                        250       260
                 ....*....|....*....|....*..
gi 564339933 792 PEKRlgagerdaeeikvqPFFRTTNWQ 818
Cdd:cd05068  247 PMER--------------PTFETLQWK 259
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
645-800 8.05e-12

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: 67.05  E-value: 8.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 645 IHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDlkldnllldaqgfLK--------------IADFGLCKEGIGFGDRT 710
Cdd:cd13974  124 IREKRLSEREALVIFYDVVRVVEALHKKNIVHRD-------------LKlgnmvlnkrtrkitITNFCLGKHLVSEDDLL 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTPEFLAPEVLTQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNAD--VPCPHFLSAQGLELIQKL 787
Cdd:cd13974  191 KDQRGSPAYISPDVLSGKPYLgKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEytIPEDGRVSENTVCLIRKL 270
                        170
                 ....*....|...
gi 564339933 788 LQKSPEKRLGAGE 800
Cdd:cd13974  271 LVLNPQKRLTASE 283
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
556-747 8.88e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 66.58  E-value: 8.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYK----GTGKYYAIKALKKQ------------EVLGRDEIDSLYCEKRILETVGRTGhpflLSL 619
Cdd:cd14205    9 LQQLGKGNFGSVEMCRYDplqdNTGEVVAVKKLQHSteehlrdfereiEILKSLQHDNIVKYKGVCYSAGRRN----LRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 620 laciqtsshacfVTEFLPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADF 697
Cdd:cd14205   85 ------------IMEYLPYGSLrdYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDF 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 698 GLCKegIGFGDRTSTFCGTPE-----FLAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd14205  153 GLTK--VLPQDKEYYKVKEPGespifWYAPESLTESKFSVASDVWSFGVVLYELF 205
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
556-747 1.19e-11

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: 66.46  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYK----GTGKYYAIKALKKQEVlgrDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACF 631
Cdd:cd05081    9 ISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGP---DQQRDFQREIQILKALH---SDFIVKYRGVSYGPGRRSL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 --VTEFLPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKegIGFG 707
Cdd:cd05081   83 rlVMEYLPSGCLrdFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAK--LLPL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564339933 708 DRTSTFCGTPE-----FLAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd05081  161 DKDYYVVREPGqspifWYAPESLSDNIFSRQSDVWSFGVVLYELF 205
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
559-765 1.19e-11

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: 65.83  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYK---GTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSShACFVTEF 635
Cdd:cd05040    3 LGDGSFGVVRRGEWTtpsGKVIQVAVKCLKSDVLSQPNAMDDFLKEVNAMHSLD---HPNLIRLYGVVLSSP-LMMVTEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHED--VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIGFGDR--TS 711
Cdd:cd05040   79 APLGSLLDRLRKDqgHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMR-ALPQNEDhyVM 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 712 TF--------CgtpeflAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECI 765
Cdd:cd05040  158 QEhrkvpfawC------APESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKI 214
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
559-795 1.25e-11

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: 65.72  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKkqEVLGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPVAVKSCR--ETLPPDLKAKFLQEARILK---QYSHPNIVRLIGVCTQKQPIYIVMELVQG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK-EGIGFGDRTSTFCG 715
Cdd:cd05084   79 GDFLtfLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSReEEDGVYAATGGMKQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLELIQKLLQKSP 792
Cdd:cd05084  159 IPvKWTAPEALNYGRYSSESDVWSFGILLWETFsLGAVPYANLSNQQTREAVEQGvRLPCPENCPDEVYRLMEQCWEYDP 238

                 ...
gi 564339933 793 EKR 795
Cdd:cd05084  239 RKR 241
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
553-762 1.48e-11

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: 66.17  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlGRDEI-DSLYCEKRILETVGRTGhpfLLSLLACIQTSSHACF 631
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSE--ENEEVkETTLRELKMLRTLKQEN---IVELKEAFRRRGKLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDL-MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE-GIGFGDR 709
Cdd:cd07848   78 VFEYVEKNMLeLLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNlSEGSNAN 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVF 762
Cdd:cd07848  158 YTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEiDQLF 211
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
556-795 1.57e-11

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: 65.95  E-value: 1.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGT---GKY--YAIKALKKqevlgRDEIDSLYCEKRILETVGRTGHPFLLSLLA-CIQTSSHa 629
Cdd:cd05046   10 ITTLGRGEFGEVFLAKAKGIeeeGGEtlVLVKALQK-----TKDENLQSEFRRELDMFRKLSHKNVVRLLGlCREAEPH- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDL--MMQIH----EDVFPEP---QACFYLA-CVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL 699
Cdd:cd05046   84 YMILEYTDLGDLkqFLRATkskdEKLKPPPlstKQKVALCtQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 CKEgiGFGDRTSTFCGT--P-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNAD----VP 771
Cdd:cd05046  164 SKD--VYNSEYYKLRNAliPlRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKlelpVP 241
                        250       260       270
                 ....*....|....*....|....*....|
gi 564339933 772 --CPhflsaqglELIQKLLQK----SPEKR 795
Cdd:cd05046  242 egCP--------SRLYKLMTRcwavNPKDR 263
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
555-810 1.59e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 66.71  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 555 CLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLG-----RDEIDSL---YCEKRILETVGRTGHPFLLSLLACIQTS 626
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNdvtkdRQLVGMCgihFTTLRELKIMNEIKHENIMGLVDVYVEG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 627 SHACFVTEFLpGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC-KEGI 704
Cdd:PTZ00024  93 DFINLVMDIM-ASDLKKVVDRKIrLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLArRYGY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTP---EFLAPEVLT-----------QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE----DEVFECI- 765
Cdd:PTZ00024 172 PPYSDTLSKDETMqrrEEMTSKVVTlwyrapellmgAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEidqlGRIFELLg 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 766 --VNADVP--------CPH-------------FLSAQGLELIQKLLQKSPEKRLGAGER-DAEEIKVQP 810
Cdd:PTZ00024 252 tpNEDNWPqakklplyTEFtprkpkdlktifpNASDDAIDLLQSLLKLNPLERISAKEAlKHEYFKSDP 320
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
553-755 1.87e-11

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 65.51  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVllvqYKG-------TGKY-YAIKALKKQEvlGRDEIDSLYCEKRILETVGrtgHPFLLSLLaCIQ 624
Cdd:cd05057    9 LEKGKVLGSGAFGTV----YKGvwipegeKVKIpVAIKVLREET--GPKANEEILDEAYVMASVD---HPHLVRLL-GIC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHACFVTEFLPGGDLMMQI--HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE 702
Cdd:cd05057   79 LSSQVQLITQLMPLGCLLDYVrnHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 703 gIGFGDRTSTFCG--TP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPG 755
Cdd:cd05057  159 -LDVDEKEYHAEGgkVPiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEG 214
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
559-795 2.08e-11

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: 65.72  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYK----GTGKYYAIKALKKQEvlGRDEIDSLYCEKRILETVGrtgHPFLLSLLA-CIQTSSHAC-FV 632
Cdd:cd05079   12 LGEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLY---HENIVKYKGiCTEDGGNGIkLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDV--FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIGFGDRT 710
Cdd:cd05079   87 MEFLPSGSLKEYLPRNKnkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKEY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STF---CGTPEF-LAPEVLTQEAYTRAVDWWGLGVLLYEMLV---GEC-PFP------GDTEDEV-FECIVNA-----DV 770
Cdd:cd05079  166 YTVkddLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLTycdSESsPMTlflkmiGPTHGQMtVTRLVRVleegkRL 245
                        250       260
                 ....*....|....*....|....*
gi 564339933 771 PCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05079  246 PRPPNCPEEVYQLMRKCWEFQPSKR 270
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
715-812 2.69e-11

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: 64.68  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVL-TQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSP 792
Cdd:cd14023  148 GCPAYVSPEILnTTGTYSgKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREP 227
                         90       100
                 ....*....|....*....|
gi 564339933 793 EKRLgagerDAEEIKVQPFF 812
Cdd:cd14023  228 SERL-----TAPEILLHPWF 242
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
558-795 3.12e-11

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: 65.20  E-value: 3.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGK-----YYAIKALKkqEVLGRDEIDSLYCEKRILETVGRtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd05055   42 TLGAGAFGKVVEATAYGLSKsdavmKVAVKMLK--PTAHSSEREALMSELKIMSHLGN--HENIVNLLGACTIGGPILVI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHE--DVFPEPQACFYLAC-VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI---GF 706
Cdd:cd05055  118 TEYCCYGDLLNFLRRkrESFLTLEDLLSFSYqVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMndsNY 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTSTFCGTpEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNA--DVPCPHFLSAQGLEL 783
Cdd:cd05055  198 VVKGNARLPV-KWMAPESIFNCVYTFESDVWSYGILLWEIFsLGSNPYPGMPVDSKFYKLIKEgyRMAQPEHAPAEIYDI 276
                        250
                 ....*....|..
gi 564339933 784 IQKLLQKSPEKR 795
Cdd:cd05055  277 MKTCWDADPLKR 288
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
552-769 3.30e-11

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: 65.46  E-value: 3.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQ-EVLGRDEIdslyceKRILETVGRTGHPFLLSLLACIQTSSHAC 630
Cdd:cd06650    6 DFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEiKPAIRNQI------IRELQVLHECNSPYIVGFYGAFYSDGEIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEK-RIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGfgD 708
Cdd:cd06650   80 ICMEHMDGGSLDQVLKKaGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID--S 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933 709 RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDE---VFECIVNAD 769
Cdd:cd06650  158 MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKElelMFGCQVEGD 221
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
705-812 3.62e-11

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: 64.29  E-value: 3.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVL-TQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLE 782
Cdd:cd14022  138 GHDDSLSDKHGCPAYVSPEILnTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKC 217
                         90       100       110
                 ....*....|....*....|....*....|
gi 564339933 783 LIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14022  218 LIRSILRREPSERL-----TSQEILDHPWF 242
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
559-795 3.62e-11

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: 64.17  E-value: 3.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYyAIKALKKqevlGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIqTSSHACFVTEFLPG 638
Cdd:cd14203    3 LGQGCFGEVWMGTWNGTTKV-AIKTLKP----GTMSPEAFLEEAQIMK---KLRHDKLVQLYAVV-SEEPIYIVTEFMSK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHED---VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFGDRTSTFCG 715
Cdd:cd14203   74 GSLLDFLKDGegkYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARL---IEDNEYTARQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEF----LAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd14203  151 GAKFpikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPPGCPESLHELMCQCWR 230

                 ....*.
gi 564339933 790 KSPEKR 795
Cdd:cd14203  231 KDPEER 236
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
558-763 3.68e-11

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 64.68  E-value: 3.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVL--LVQYKGTGKYYAIKALKkqEVLGRDEIDSLYCEKRILETVGRtgHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd05047    2 VIGEGNFGQVLkaRIKKDGLRMDAAIKRMK--EYASKDDHRDFAGELEVLCKLGH--HPNIINLLGACEHRGYLYLAIEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHEDVFPEPQACF-----------------YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG 698
Cdd:cd05047   78 APHGNLLDFLRKSRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 699 LCKEGIGFGDRTSTFCGTpEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFE 763
Cdd:cd05047  158 LSRGQEVYVKKTMGRLPV-RWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYE 222
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
559-747 4.12e-11

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: 64.59  E-value: 4.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrDEIDSLYCEK----RILEtvgrtgHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELIRFD----EETQRTFLKEvkvmRCLE------HPNVLKFIGVLYKDKRLNFITE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK----------- 701
Cdd:cd14221   71 YIKGGTLrgIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARlmvdektqpeg 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564339933 702 -EGIGFGDRTS--TFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd14221  151 lRSLKKPDRKKryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
559-795 4.64e-11

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: 64.01  E-value: 4.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYyAIKALKKQEVLGRDEIDslycEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05059   12 LGSGQFGVVHLGKWRGKIDV-AIKMIKEGSMSEDDFIE----EAKVMM---KLSHPKLVQLYGVCTKQRPIFIVTEYMAN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL----------CKEGIGF 706
Cdd:cd05059   84 GCLLnyLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLaryvlddeytSSVGTKF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 GDRTStfcgtpeflAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLELI 784
Cdd:cd05059  164 PVKWS---------PPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQGyRLYRPHLAPTEVYTIM 234
                        250
                 ....*....|.
gi 564339933 785 QKLLQKSPEKR 795
Cdd:cd05059  235 YSCWHEKPEER 245
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
551-758 5.22e-11

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: 64.67  E-value: 5.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQ-YKGTGKYYAIKALKKQEVLGRDEIDSLYcEKRILETVGRTGHPFLLSL--LACIQTSS 627
Cdd:cd07862    1 QQYECVAEIGEGAYGKVFKARdLKNGGRFVALKRVRVQTGEEGMPLSTIR-EVAVLRHLETFEHPNVVRLfdVCTVSRTD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGGDLMMQIHEDVFPEPQACF-----YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE 702
Cdd:cd07862   80 RETKLTLVFEHVDQDLTTYLDKVPEPGVPTetikdMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 703 gIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE 758
Cdd:cd07862  160 -YSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSD 214
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
553-794 5.31e-11

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: 65.08  E-value: 5.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQevlgrdeIDSLYCEKRILETVG---RTGHPFLLSLLACIQTSSHA 629
Cdd:cd07855    7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNA-------FDVVTTAKRTLRELKilrHFKHDNIIAIRDILRPKVPY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 -----CFVTEFLPGGDLMMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEG 703
Cdd:cd07855   80 adfkdVYVVLDLMESDLHHIIHSDQpLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 704 IGFGDRTSTF----CGTPEFLAPEV-LTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA-DVPCPHFLS 777
Cdd:cd07855  160 CTSPEEHKYFmteyVATRWYRAPELmLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVlGTPSQAVIN 239
                        250
                 ....*....|....*..
gi 564339933 778 AQGLELIQKLLQKSPEK 794
Cdd:cd07855  240 AIGADRVRRYIQNLPNK 256
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
549-795 5.35e-11

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: 63.91  E-value: 5.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKVLLVQYKGtgKYYAIKALKKQEvlgrDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSH 628
Cdd:cd05039    4 NKKDLKLGELIGKGEFGDVMLGDYRG--QKVAVKCLKDDS----TAAQAFLAEASVMTTLR---HPNLVQLLGVVLEGNG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQIHED----VFPEPQACFYLAcVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGi 704
Cdd:cd05039   75 LYIVTEYMAKGSLVDYLRSRgravITRKDQLGFALD-VCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEA- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFcgtP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNA---DVP--CPHFLs 777
Cdd:cd05039  153 SSNQDGGKL---PiKWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYPRIPLKDVVPHVEKGyrmEAPegCPPEV- 228
                        250
                 ....*....|....*...
gi 564339933 778 aqgLELIQKLLQKSPEKR 795
Cdd:cd05039  229 ---YKVMKNCWELDPAKR 243
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
104-167 6.00e-11

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


Pssm-ID: 212008 [Multi-domain]  Cd Length: 68  Bit Score: 58.88  E-value: 6.00e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933 104 LLEALHRQLEVELKVKQGAENMIHTcaSGTPKERKLLAAAQQMLKDSQLKVALLRMKISGLEAS 167
Cdd:cd00089    6 RLEELRRKLEKELKIREGAENLLKL--YSNPKVKKDLAEVQLNLKESKEKIDLLKRQLERYNAL 67
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
558-755 6.18e-11

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: 64.17  E-value: 6.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGtgKYYAIKALKKQEVLGRDEIDSL--------------YCEKRILETVGRT-GHPFLLSLLA- 621
Cdd:cd14000    1 LLGDGGFGSVYRASYKG--EPVAVKIFNKHTSSNFANVPADtmlrhlratdamknFRLLRQELTVLSHlHHPSIVYLLGi 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 CIQTsshACFVTEFLPGGDLMMQIHED------VFPEPQACFYLAcVVLGLQFLHEKRIIYRDLKLD-----NLLLDAQG 690
Cdd:cd14000   79 GIHP---LMLVLELAPLGSLDHLLQQDsrsfasLGRTLQQRIALQ-VADGLRYLHSAMIIYRDLKSHnvlvwTLYPNSAI 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 691 FLKIADFGL----CKEGIgfgdrtSTFCGTPEFLAPEVLT-QEAYTRAVDWWGLGVLLYEMLVGECPFPG 755
Cdd:cd14000  155 IIKIADYGIsrqcCRMGA------KGSEGTPGFRAPEIARgNVIYNEKVDVFSFGMLLYEILSGGAPMVG 218
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
662-812 6.30e-11

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: 63.83  E-value: 6.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 662 VVLGLQFLHEKRIIYRDLK-----LDNLLLDAQGFLKIADFGLCKEgIGFGD----RTSTFCGTPEFLAPEVLTQEAY-- 730
Cdd:cd13982  108 IASGLAHLHSLNIVHRDLKpqnilISTPNAHGNVRAMISDFGLCKK-LDVGRssfsRRSGVAGTSGWIAPEMLSGSTKrr 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 731 -TRAVDWWGLGVLLYEMLVGEC-PFpGDTedevFECIVN-----ADVPCPHFLSAQGLE---LIQKLLQKSPEKRlgage 800
Cdd:cd13982  187 qTRAVDIFSLGCVFYYVLSGGShPF-GDK----LEREANilkgkYSLDKLLSLGEHGPEaqdLIERMIDFDPEKR----- 256
                        170
                 ....*....|..
gi 564339933 801 RDAEEIKVQPFF 812
Cdd:cd13982  257 PSAEEVLNHPFF 268
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
558-773 6.72e-11

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 63.84  E-value: 6.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKY---YAIKALK-------KQEVLGRDEIDSLYCEKRILETVGrtghpfllsllaCIQTSS 627
Cdd:cd05063   12 VIGAGEFGEVFRGILKMPGRKevaVAIKTLKpgytekqRQDFLSEASIMGQFSHHNIIRLEG------------VVTKFK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIG 705
Cdd:cd05063   80 PAMIITEYMENGalDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLED 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 706 FGDRTSTFCGTP---EFLAPEVLTQEAYTRAVDWWGLGVLLYE-MLVGECPFPGDTEDEVFECIVNA-DVPCP 773
Cdd:cd05063  160 DPEGTYTTSGGKipiRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSFGERPYWDMSNHEVMKAINDGfRLPAP 232
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
813-876 9.47e-11

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 58.14  E-value: 9.47e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933   813 RTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSlPPTLTPPVPRRSLSARQQAAFRDFDFV 876
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTE-ETPVLTPVDSPLSGGIQQEPFRGFSYV 63
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
542-752 9.52e-11

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: 63.53  E-value: 9.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 542 LSTRNPPQlqDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlGRDeIDSLYCEKRILETVGrtgHPFLLSLLA 621
Cdd:cd06645    4 LSRRNPQE--DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEP--GED-FAVVQQEIIMMKDCK---HSNIVAYFG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 CIQTSSHACFVTEFLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC 700
Cdd:cd06645   76 SYLRRDKLWICMEFCGGGSLQDIYHvTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 701 KEGIGFGDRTSTFCGTPEFLAPEVLTQE---AYTRAVDWWGLGVLLYEMLVGECP 752
Cdd:cd06645  156 AQITATIAKRKSFIGTPYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAELQPP 210
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
551-808 1.02e-10

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: 64.30  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKK--QEVLgrdEIDSLYCEKRILETVGrtgHPFLLSLL------AC 622
Cdd:cd07878   15 ERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfQSLI---HARRTYRELRLLKHMK---HENVIGLLdvftpaTS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 623 IQTSSHACFVTEFLpGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE 702
Cdd:cd07878   89 IENFNEVYLVTNLM-GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 703 GigfGDRTSTFCGTPEFLAPEV-LTQEAYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECIVNADVPCPHFLSAQG 780
Cdd:cd07878  168 A---DDEMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGnDYIDQLKRIMEVVGTPSPEVLKKIS 244
                        250       260       270
                 ....*....|....*....|....*....|.
gi 564339933 781 LELIQKLLQK---SPEKRLGAGERDAEEIKV 808
Cdd:cd07878  245 SEHARKYIQSlphMPQQDLKKIFRGANPLAI 275
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
552-800 1.03e-10

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: 63.78  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLycekRILETVGRTGHPFLLSLLACI--QTSSHA 629
Cdd:cd07843    6 EYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKEGFPITSL----REINILLKLQHPNIVTVKEVVvgSNLDKI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGG--DLMMQIHEDVFPEPQACFYLAcVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFG 707
Cdd:cd07843   82 YMVMEYVEHDlkSLMETMKQPFLQSEVKCLMLQ-LLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLARE---YG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFcgTPE-----FLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA-----DVPCPHF- 775
Cdd:cd07843  158 SPLKPY--TQLvvtlwYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLlgtptEKIWPGFs 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564339933 776 --------------------------LSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd07843  236 elpgakkktftkypynqlrkkfpalsLSDNGFDLLNRLLTYDPAKRISAED 286
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
549-769 1.52e-10

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: 63.01  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKV---LLVQYKGTGKYYAIKALKKqEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLAcIQT 625
Cdd:cd05074    7 QEQQFTLGRMLGKGEFGSVreaQLKSEDGSFQKVAVKMLKA-DIFSSSDIEEFLREAACMKEFD---HPNVIKLIG-VSL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHA-------CFVTEFLPGGDL-----MMQIHEDVFPEPQACF--YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF 691
Cdd:cd05074   82 RSRAkgrlpipMVILPFMKHGDLhtfllMSRIGEEPFTLPLQTLvrFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 692 LKIADFGLCKEgIGFGDRTSTFCGTP---EFLAPEVLTQEAYTRAVDWWGLGVLLYE-MLVGECPFPGDTEDEVFECIVN 767
Cdd:cd05074  162 VCVADFGLSKK-IYSGDYYRQGCASKlpvKWLALESLADNVYTTHSDVWAFGVTMWEiMTRGQTPYAGVENSEIYNYLIK 240

                 ..
gi 564339933 768 AD 769
Cdd:cd05074  241 GN 242
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
559-753 1.53e-10

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: 62.90  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKG--TGKYYAIKALKKQEVLGRDEIDSLYCEKriLETVGRTGHPFLLSLLACIQTSSHACFVTEFL 636
Cdd:cd14158   23 LGEGGFGVV----FKGyiNDKNVAVKKLAAMVDISTEDLTKQFEQE--IQVMAKCQHENLVELLGYSCDGPQLCLVYTYM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIH--EDVFPEP--QACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDaQGFL-KIADFGLCKEGIGFGD--R 709
Cdd:cd14158   97 PNGSLLDRLAclNDTPPLSwhMRCKIAQGTANGINYLHENNHIHRDIKSANILLD-ETFVpKISDFGLARASEKFSQtiM 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAyTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14158  176 TERIVGTTAYMAPEALRGEI-TPKSDIFSFGVVLLEIITGLPPV 218
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
179-226 1.59e-10

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 57.53  E-value: 1.59e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 564339933  179 EELQHRLRIEAAVAAGAKNVVKLLggQRIQDRKALAEAQAQLQESSQK 226
Cdd:pfam02185   3 QELRKKIEVEKKIKEGAENMLRLL--QATKDRKVLAEAESELRESNRK 48
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
551-763 1.64e-10

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 63.09  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVL--LVQYKGTGKYYAIKALKkqEVLGRDEIDSLYCEKRILETVGRtgHPFLLSLLACIQTSSH 628
Cdd:cd05089    2 EDIKFEDVIGEGNFGQVIkaMIKKDGLKMNAAIKMLK--EFASENDHRDFAGELEVLCKLGH--HPNIINLLGACENRGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQIHEDVFPEPQACF-----------------YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF 691
Cdd:cd05089   78 LYIAIEYAPYGNLLDFLRKSRVLETDPAFakehgtastltsqqllqFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLV 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 692 LKIADFGLCKEGIGFGDRTSTFCGTpEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFE 763
Cdd:cd05089  158 SKIADFGLSRGEEVYVKKTMGRLPV-RWMAIESLNYSVYTTKSDVWSFGVLLWEIVsLGGTPYCGMTCAELYE 229
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
549-765 1.71e-10

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: 63.10  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDeidslyCEK-RILETVGRTGHPFLLSLLACIQTSS 627
Cdd:cd07871    3 KLETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAP------CTAiREVSLLKNLKHANIVTLHDIIHTER 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPG---------GDLMMQIHEDVFpepqaCFYLacvVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG 698
Cdd:cd07871   77 CLTLVFEYLDSdlkqyldncGNLMSMHNVKIF-----MFQL---LRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFG 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 699 LCKEGIGFGDRTSTFCGTPEFLAPEVLT-QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECI 765
Cdd:cd07871  149 LARAKSVPTKTYSNEVVTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLI 216
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
558-762 1.75e-10

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 62.89  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKY-----YAIKALKkqEVLGRDEIDSLYCEKRILETVGRtgHPFLLSLL-ACIQTSSHACF 631
Cdd:cd05054   14 PLGRGAFGKVIQASAFGIDKSatcrtVAVKMLK--EGATASEHKALMTELKILIHIGH--HLNVVNLLgACTKPGGPLMV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTE-----------------FLPGGDLMMQIHE------DVFPEPQACFYLAC----VVLGLQFLHEKRIIYRDLKLDNL 684
Cdd:cd05054   90 IVEfckfgnlsnylrskreeFVPYRDKGARDVEeeedddELYKEPLTLEDLICysfqVARGMEFLASRKCIHRDLAARNI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 685 LLDAQGFLKIADFGLCKEGIGFGDR-TSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEV 761
Cdd:cd05054  170 LLSENNVVKICDFGLARDIYKDPDYvRKGDARLPlKWMAPESIFDKVYTTQSDVWSFGVLLWEIFsLGASPYPGVQMDEE 249

                 .
gi 564339933 762 F 762
Cdd:cd05054  250 F 250
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
715-812 2.00e-10

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: 62.06  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 715 GTPEFLAPEVL-TQEAYT-RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSP 792
Cdd:cd13976  148 GCPAYVSPEILnSGATYSgKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREP 227
                         90       100
                 ....*....|....*....|
gi 564339933 793 EKRLgagerDAEEIKVQPFF 812
Cdd:cd13976  228 SERL-----TAEDILLHPWL 242
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
556-798 2.26e-10

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: 62.67  E-value: 2.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlGRDEID-SLYCEKRILETVGRTGHPFLLSLLACIQTS--SHACFV 632
Cdd:cd07863    5 VAEIGVGAYGTVYKARDPHSGHFVALKSVRVQT--NEDGLPlSTVREVALLKRLEAFDHPNIVRLMDVCATSrtDRETKV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDVFPEPQACF-----YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL-----CKE 702
Cdd:cd07863   83 TLVFEHVDQDLRTYLDKVPPPGLPAetikdLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLariysCQM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 703 GIgfgdrtSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDE----VFECI-------VNADVP 771
Cdd:cd07863  163 AL------TPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADqlgkIFDLIglppeddWPRDVT 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564339933 772 CPHF----------------LSAQGLELIQKLLQKSPEKRLGA 798
Cdd:cd07863  237 LPRGafsprgprpvqsvvpeIEESGAQLLLEMLTFNPHKRISA 279
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
537-746 2.43e-10

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 62.76  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 537 PPLAALSTRNPPQlQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtvgRTGHPFL 616
Cdd:cd06635   12 PDIAELFFKEDPE-KLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQ---RIKHPNS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 617 LSLLACIQTSSHACFVTEF-LPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIA 695
Cdd:cd06635   88 IEYKGCYLREHTAWLVMEYcLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLA 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 696 DFGlckeGIGFGDRTSTFCGTPEFLAPEV---LTQEAYTRAVDWWGLGVLLYEM 746
Cdd:cd06635  168 DFG----SASIASPANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIEL 217
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
559-795 2.87e-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: 61.60  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQY---KGTGKYYAIKALKK-QEVLGRDEIdslyceKRILETVGRTGHPFLLSLLACIQTSShACFVTE 634
Cdd:cd05060    3 LGHGNFGSVRKGVYlmkSGKEVEVAVKTLKQeHEKAGKKEF------LREASVMAQLDHPCIVRLIGVCKGEP-LMLVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIGFGD---RT 710
Cdd:cd05060   76 LAPLGPLLKYLKKRrEIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSR-ALGAGSdyyRA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNAD-VPCPHFLSAQGLELIQKL 787
Cdd:cd05060  155 TTAGRWPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFsYGAKPYGEMKGPEVIAMLESGErLPRPEECPQEIYSIMLSC 234

                 ....*...
gi 564339933 788 LQKSPEKR 795
Cdd:cd05060  235 WKYRPEDR 242
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
551-795 3.24e-10

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 62.01  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYyAIKALKKqevlGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIqTSSHAC 630
Cdd:cd05069   12 ESLRLDVKLGQGCFGEVWMGTWNGTTKV-AIKTLKP----GTMMPEAFLQEAQIMK---KLRHDKLVPLYAVV-SEEPIY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHE---DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK--EGIG 705
Cdd:cd05069   83 IVTEFMGKGSLLDFLKEgdgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARliEDNE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCGTpEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLEL 783
Cdd:cd05069  163 YTARQGAKFPI-KWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGyRMPCPQGCPESLHEL 241
                        250
                 ....*....|..
gi 564339933 784 IQKLLQKSPEKR 795
Cdd:cd05069  242 MKLCWKKDPDER 253
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
503-798 4.04e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 62.53  E-value: 4.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 503 MKP-PPKPPRLYLQEPAPGTPCTKR---------PHMDPRTGVAPPL---------------AALSTRNPPQLQDFRCLA 557
Cdd:PLN00034   1 MKPiQPPPGVPLPSTARHTTKSRPRrrpdltlplPQRDPSLAVPLPLpppsssssssssssaSGSAPSAAKSLSELERVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgRDEIDSLYC-EKRILETVGrtgHPfllSLLACIQTSSHAC---FVT 633
Cdd:PLN00034  81 RIGSGAGGTVYKVIHRPTGRLYALKVIYGNH---EDTVRRQICrEIEILRDVN---HP---NVVKCHDMFDHNGeiqVLL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMmqiHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTF 713
Cdd:PLN00034 152 EFMDGGSLE---GTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSS 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEV----LTQEAYT-RAVDWWGLGVLLYEMLVGECPFP----GDTEdEVFECIVNADVP-CPHFLSAQGLEL 783
Cdd:PLN00034 229 VGTIAYMSPERintdLNHGAYDgYAGDIWSLGVSILEFYLGRFPFGvgrqGDWA-SLMCAICMSQPPeAPATASREFRHF 307
                        330
                 ....*....|....*
gi 564339933 784 IQKLLQKSPEKRLGA 798
Cdd:PLN00034 308 ISCCLQREPAKRWSA 322
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
556-798 4.07e-10

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: 62.02  E-value: 4.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrdEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd07869   10 LEKLGEGSYATVYKGKSKVNGKLVALKVIRLQE-----EEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 L-----------PGGdlmmqIHEDvfpepQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI 704
Cdd:cd07869   85 VhtdlcqymdkhPGG-----LHPE-----NVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLT-QEAYTRAVDWWGLGVLLYEMLVGECPFPG--DTEDEVFECIVNADVP---------- 771
Cdd:cd07869  155 VPSHTYSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmkDIQDQLERIFLVLGTPnedtwpgvhs 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 564339933 772 CPHF-------LSAQGL--------------ELIQKLLQKSPEKRLGA 798
Cdd:cd07869  235 LPHFkperftlYSPKNLrqawnklsyvnhaeDLASKLLQCFPKNRLSA 282
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
559-800 4.46e-10

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: 62.20  E-value: 4.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKK---QEVLGRdeidSLYCEKRILETVGrtgHPFLLSLLAC-IQTSSHACFVTE 634
Cdd:cd07856   18 VGMGAFGLVCSARDQLTGQNVAVKKIMKpfsTPVLAK----RTYRELKLLKHLR---HENIISLSDIfISPLEDIYFVTE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLpGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKegigFGDRTST-F 713
Cdd:cd07856   91 LL-GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR----IQDPQMTgY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 714 CGTPEFLAPEV-LTQEAYTRAVDWWGLGVLLYEMLVGECPFPGD---------TE------DEVFECIVNAD-------- 769
Cdd:cd07856  166 VSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKdhvnqfsiiTEllgtppDDVINTICSENtlrfvqsl 245
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564339933 770 -----VPCPHFL---SAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd07856  246 pkrerVPFSEKFknaDPDAIDLLEKMLVFDPKKRISAAE 284
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
558-786 5.06e-10

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: 61.42  E-value: 5.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGK---YYAIKALK-------KQEVLGRDEIdslycekriletVGRTGHPFLLSLLACIQTSS 627
Cdd:cd05065   11 VIGAGEFGEVCRGRLKLPGKreiFVAIKTLKsgytekqRRDFLSEASI------------MGQFDHPNIIHLEGVVTKSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK---E 702
Cdd:cd05065   79 PVMIITEFMENGalDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfleD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 703 GIGFGDRTSTFCGT-P-EFLAPEVLTQEAYTRAVDWWGLGVLLYE-MLVGECPFPGDTEDEVFECI-----VNADVPCPH 774
Cdd:cd05065  159 DTSDPTYTSSLGGKiPiRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYWDMSNQDVINAIeqdyrLPPPMDCPT 238
                        250
                 ....*....|..
gi 564339933 775 FLSAQGLELIQK 786
Cdd:cd05065  239 ALHQLMLDCWQK 250
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
550-765 5.33e-10

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: 61.04  E-value: 5.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYkgTGKYYAIKALKkQEVLGRDEIDslycekrilETVGRTG--HPFLLSLLACIQTSS 627
Cdd:cd05083    5 LQKLTLGEIIGEGEFGAVLQGEY--MGQKVAVKNIK-CDVTAQAFLE---------ETAVMTKlqHKNLVRLLGVILHNG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 hACFVTEFLPGGDLMMQIH---EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI 704
Cdd:cd05083   73 -LYIVMELMSKGNLVNFLRsrgRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGS 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933 705 gFGDRTSTFcgTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECI 765
Cdd:cd05083  152 -MGVDNSRL--PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFsYGRAPYPKMSVKEVKEAV 210
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
665-800 5.56e-10

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: 61.24  E-value: 5.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 665 GLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK-EGIgfgdRTSTFCG---TPEFLAPEVLT-QEAYTRAVDWWGL 739
Cdd:cd07844  110 GLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARaKSV----PSKTYSNevvTLWYRPPDVLLgSTEYSTSLDMWGV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 740 GVLLYEMLVGECPFPG--DTEDEV--------------------FECIVNADVPCP-------HF----LSAQGLELIQK 786
Cdd:cd07844  186 GCIFYEMATGRPLFPGstDVEDQLhkifrvlgtpteetwpgvssNPEFKPYSFPFYpprplinHAprldRIPHGEELALK 265
                        170
                 ....*....|....
gi 564339933 787 LLQKSPEKRLGAGE 800
Cdd:cd07844  266 FLQYEPKKRISAAE 279
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
558-795 5.58e-10

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: 61.23  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYY---AIKALKKQEVlGRDEIDSLYcEKRILetvGRTGHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd05033   11 VIGGGEFGEVCSGSLKLPGKKEidvAIKTLKSGYS-DKQRLDFLT-EASIM---GQFDHPNVIRLEGVVTKSRPVMIVTE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTST 712
Cdd:cd05033   86 YMENGSLdkFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRR-LEDSEATYT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 713 FCG--TP-EFLAPEVLTQEAYTRAVDWWGLGVLLYE-MLVGECPFPGDTEDEVFECI-----VNADVPCPHFLSaqglEL 783
Cdd:cd05033  165 TKGgkIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSYGERPYWDMSNQDVIKAVedgyrLPPPMDCPSALY----QL 240
                        250
                 ....*....|..
gi 564339933 784 IQKLLQKSPEKR 795
Cdd:cd05033  241 MLDCWQKDRNER 252
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
546-795 5.62e-10

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: 61.03  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 546 NPPQLQDFRclaVLGRGHFGKVLLVQYKGTGKYyAIKALKKQEVLGRDEIDslycEKRILEtvgRTGHPFLLSLLACIQT 625
Cdd:cd05114    2 NPSELTFMK---ELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEEDFIE----EAKVMM---KLTHPKLVQLYGVCTQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLAC--VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEG 703
Cdd:cd05114   71 QKPIYIVTEFMENGCLLNYLRQRRGKLSRDMLLSMCqdVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 704 IgfGDRTSTFCGTP---EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNAD-VPCPHFLSA 778
Cdd:cd05114  151 L--DDQYTSSSGAKfpvKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVSRGHrLYRPKLASK 228
                        250
                 ....*....|....*..
gi 564339933 779 QGLELIQKLLQKSPEKR 795
Cdd:cd05114  229 SVYEVMYSCWHEKPEGR 245
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
559-765 6.39e-10

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: 60.81  E-value: 6.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYyAIKALKKqevlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIqTSSHACFVTEFLPG 638
Cdd:cd05073   19 LGAGQFGEVWMATYNKHTKV-AVKTMKP----GSMSVEAFLAEANVMKTLQ---HDKLVKLHAVV-TKEPIYIITEFMAK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHED---VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL----------CKEGIG 705
Cdd:cd05073   90 GSLLDFLKSDegsKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLarviedneytAREGAK 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564339933 706 FgdrtstfcgTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECI 765
Cdd:cd05073  170 F---------PIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRAL 221
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
552-812 8.85e-10

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: 60.90  E-value: 8.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKkqevLGRDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACF 631
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIR----LESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLpggDLMMQIHEDVFPEPQAC------FYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIG 705
Cdd:cd07861   77 VFEFL---SMDLKKYLDSLPKGKYMdaelvkSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLAR-AFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTF-CGTPEFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVF----------ECIVNADVPC 772
Cdd:cd07861  153 IPVRVYTHeVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEiDQLFrifrilgtptEDIWPGVTSL 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 773 PHF------------------LSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd07861  233 PDYkntfpkwkkgslrtavknLDEDGLDLLEKMLIYDPAKRI-----SAKKALVHPYF 285
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
553-766 9.15e-10

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: 61.69  E-value: 9.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDslycEKRILETVGR---TGHPFLLSLLACIQTSSHA 629
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAE----EIRILEHLKKqdkDNTMNVIHMLESFTFRNHI 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPggdlmMQIHEDV-------FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF--LKIADFGL- 699
Cdd:cd14224  143 CMTFELLS-----MNLYELIkknkfqgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSs 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 700 CKEGigfgDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIV 766
Cdd:cd14224  218 CYEH----QRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMI 280
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
558-793 1.06e-09

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: 60.27  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGK---YYAIKALK-----KQEvlgRDeidsLYCEKRILetvGRTGHPFLLSLLACIQTSSHA 629
Cdd:cd05066   11 VIGAGEFGEVCSGRLKLPGKreiPVAIKTLKagyteKQR---RD----FLSEASIM---GQFDHPNIIHLEGVVTRSKPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK--EGIG 705
Cdd:cd05066   81 MIVTEYMENGslDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvlEDDP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYE-MLVGECPFPGDTEDEVFECI-----VNADVPCPHFLSA 778
Cdd:cd05066  161 EAAYTTRGGKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYWEMSNQDVIKAIeegyrLPAPMDCPAALHQ 240
                        250
                 ....*....|....*
gi 564339933 779 QGLELIQKLLQKSPE 793
Cdd:cd05066  241 LMLDCWQKDRNERPK 255
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
547-793 1.13e-09

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 61.21  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 547 PPQLQDfrcLAVLGRGHFGKVLLVQYKGTGKYYAIKALKK--QEVLgrdEIDSLYCEKRILEtvgRTGHPFLLSLLACIQ 624
Cdd:cd07877   16 PERYQN---LSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRpfQSII---HAKRTYRELRLLK---HMKHENVIGLLDVFT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSS-----HACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL 699
Cdd:cd07877   87 PARsleefNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 CKEGigfGDRTSTFCGTPEFLAPEV-LTQEAYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECIVNADVPCPHFLS 777
Cdd:cd07877  167 ARHT---DDEMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGtDHIDQLKLILRLVGTPGAELLK 243
                        250
                 ....*....|....*.
gi 564339933 778 AQGLELIQKLLQKSPE 793
Cdd:cd07877  244 KISSESARNYIQSLTQ 259
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
650-812 1.25e-09

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: 60.69  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 650 FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigfGDRTST-FCGTPEFLAPEV-LTQ 727
Cdd:cd07879  114 LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARH----ADAEMTgYVVTRWYRAPEViLNW 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 728 EAYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECIVNADVPCPHFL------------------------------ 776
Cdd:cd07879  190 MHYNQTVDIWSVGCIMAEMLTGKTLFKGkDYLDQLTQILKVTGVPGPEFVqkledkaaksyikslpkyprkdfstlfpka 269
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 777 SAQGLELIQKLLQKSPEKRLGAGE----------RDAEEIKVQPFF 812
Cdd:cd07879  270 SPQAVDLLEKMLELDVDKRLTATEalehpyfdsfRDADEETEQQPY 315
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
613-795 1.28e-09

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 59.85  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 613 HPFLLSLLACIQTSSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDA--QG 690
Cdd:cd14112   59 HENVQRLIAAFKPSNFAYLVMEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSvrSW 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 691 FLKIADFGLCKEGIGFGDRTStfCGTPEFLAPEVLTQEAY-TRAVDWWGLGVLLYEMLVGECPFPG--DTEDEVFECIVN 767
Cdd:cd14112  139 QVKLVDFGRAQKVSKLGKVPV--DGDTDWASPEFHNPETPiTVQSDIWGLGVLTFCLLSGFHPFTSeyDDEEETKENVIF 216
                        170       180       190
                 ....*....|....*....|....*....|...
gi 564339933 768 adVPC-PHFL----SAQGLELIQKLLQKSPEKR 795
Cdd:cd14112  217 --VKCrPNLIfveaTQEALRFATWALKKSPTRR 247
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
582-813 1.32e-09

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: 60.03  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 582 KALKKQEVLGRDEI-DSLyceKRILETVGRTGHPFLLSLLACIQTSS-HACFVTE--FLPGGDLMMQIHEDVFPEPQACF 657
Cdd:cd14011   32 KQLEEYSKRDREQIlELL---KRGVKQLTRLRHPRILTVQHPLEESReSLAFATEpvFASLANVLGERDNMPSPPPELQD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 658 Y----------LACVVLGLQFLH-EKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCG----------- 715
Cdd:cd14011  109 YklydveikygLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREydpnlpplaqp 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEFLAPEVLTQEAYTRAVDWWGLGVLLYEmLVGECPFPGDTEDEVFECIVNADVPCPHFLSAQGL------ELIQKLLQ 789
Cdd:cd14011  189 NLNYLAPEYILSKTCDPASDMFSLGVLIYA-IYNKGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEKvpeelrDHVKTLLN 267
                        250       260
                 ....*....|....*....|....
gi 564339933 790 KSPEKRLgagerDAEEIKVQPFFR 813
Cdd:cd14011  268 VTPEVRP-----DAEQLSKIPFFD 286
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
539-753 1.33e-09

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: 60.02  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 539 LAALstRNPPQLqdFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrDEIDSLYCEKRILETVGRtgHPFLLS 618
Cdd:cd06636    8 LSAL--RDPAGI--FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTE----DEEEEIKLEINMLKKYSH--HRNIAT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 619 LLACIQTSSHA------CFVTEFLPGG---DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ 689
Cdd:cd06636   78 YYGAFIKKSPPghddqlWLVMEFCGAGsvtDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 690 GFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQE-----AYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd06636  158 AEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPL 226
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
17-79 1.34e-09

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


Pssm-ID: 212008 [Multi-domain]  Cd Length: 68  Bit Score: 55.03  E-value: 1.34e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933  17 PEDEKEMIRRAIQKELKIKEGMENMRRVATD---RRHLGHVQQLLRASNRRLEQLHGELRELHAQV 79
Cdd:cd00089    3 LQQRLEELRRKLEKELKIREGAENLLKLYSNpkvKKDLAEVQLNLKESKEKIDLLKRQLERYNALV 68
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
571-800 1.41e-09

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: 59.68  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 571 QYKGTGKYYAIKALKKQEVLGRDEIDSLyceKRIletvgrtGHPFLLSLLA-----CIQTSSH-ACFVTEFLPGGDL--M 642
Cdd:cd14012   25 KFLTSQEYFKTSNGKKQIQLLEKELESL---KKL-------RHPNLVSYLAfsierRGRSDGWkVYLLTEYAPGGSLseL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 643 MQIHEDVfPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDN---LLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEF 719
Cdd:cd14012   95 LDSVGSV-PLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNvllDRDAGTGIVKLTDYSLGKTLLDMCSRGSLDEFKQTY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 720 -LAPEVLTQ-EAYTRAVDWWGLGVLLYEMLVG-ECPFPGDTEDEVfecIVNADvpcphfLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd14012  174 wLPPELAQGsKSPTRKTDVWDLGLLFLQMLFGlDVLEKYTSPNPV---LVSLD------LSASLQDFLSKCLSLDPKKRP 244

                 ....
gi 564339933 797 GAGE 800
Cdd:cd14012  245 TALE 248
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
627-800 1.82e-09

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: 59.12  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 627 SHACFVTEFLPGGDLMM--------QIHEDV-----FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLK 693
Cdd:cd14024   45 EGVCSVLEVVIGQDRAYaffsrhygDMHSHVrrrrrLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 694 IADFGL--CKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYT--RAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNAD 769
Cdd:cd14024  125 LVLVNLedSCPLNGDDDSLTDKHGCPAYVGPEILSSRRSYsgKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGA 204
                        170       180       190
                 ....*....|....*....|....*....|.
gi 564339933 770 VPCPHFLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14024  205 FSLPAWLSPGARCLVSCMLRRSPAERLKASE 235
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
551-812 2.07e-09

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: 59.64  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgRDEI--DSLYCEKRILETVGrtgHPFLLSLLACIQTSSH 628
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESE---DDEDvkKTALREVKVLRQLR---HENIVNLKEAFRRKGR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPggdlmMQIHE--DVFP---EPQAC-FYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE 702
Cdd:cd07833   75 LYLVFEYVE-----RTLLEllEASPgglPPDAVrSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 703 GIGFGDRTST-FCGTPEFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPGDTE---------------------- 758
Cdd:cd07833  150 LTARPASPLTdYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFPGDSDidqlyliqkclgplppshqelf 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933 759 --DEVFECIVNADVPCPHFL--------SAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd07833  230 ssNPRFAGVAFPEPSQPESLerrypgkvSSPALDFLKACLRMDPKERL-----TCDELLQHPYF 288
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
558-763 2.56e-09

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer 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 Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 59.18  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVL---LVQYKGTGKYYAIKALKKQEVLGRdEIDSLYCEKRILETVGrtgHPFLLSLLA-CIQTSSH----A 629
Cdd:cd14204   14 VLGEGEFGSVMegeLQQPDGTNHKVAVKTMKLDNFSQR-EIEEFLSEAACMKDFN---HPNVIRLLGvCLEVGSQripkP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDL-------MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE 702
Cdd:cd14204   90 MVILPFMKYGDLhsfllrsRLGSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKK 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 703 gIGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFE 763
Cdd:cd14204  170 -IYSGDyyRQGRIAKMPvKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYD 233
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
549-763 2.73e-09

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 59.63  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRtgHPFLLSLLACIQTSSH 628
Cdd:cd05088    5 EWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGH--HPNIINLLGACEHRGY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQIHEDVFPEPQACF-----------------YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF 691
Cdd:cd05088   83 LYLAIEYAPHGNLLDFLRKSRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 692 LKIADFGLCKEGIGFGDRTSTFCGTpEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFE 763
Cdd:cd05088  163 AKIADFGLSRGQEVYVKKTMGRLPV-RWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYE 234
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
657-812 2.86e-09

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: 59.25  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 657 FYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEA-YTRAVD 735
Cdd:cd07873  104 LFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTdYSTQID 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 736 WWGLGVLLYEMLVGECPFPGDTEDEVFECIVN----------------------------ADVPCPHF--LSAQGLELIQ 785
Cdd:cd07873  184 MWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRilgtpteetwpgilsneefksynypkyrADALHNHAprLDSDGADLLS 263
                        170       180
                 ....*....|....*....|....*..
gi 564339933 786 KLLQKSPEKRLGagerdAEEIKVQPFF 812
Cdd:cd07873  264 KLLQFEGRKRIS-----AEEAMKHPYF 285
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
561-799 2.95e-09

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 59.26  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 561 RGHFGKVLLVQYkgTGKYYAIKALKKQEVlgrdeiDSLYCEKRILETVGRTgHPfllSLLACIQTSSHAC-------FVT 633
Cdd:cd14053    5 RGRFGAVWKAQY--LNRLVAVKIFPLQEK------QSWLTEREIYSLPGMK-HE---NILQFIGAEKHGEsleaeywLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKR----------IIYRDLKLDNLlldaqgFLK------IADF 697
Cdd:cd14053   73 EFHERGSLCDYLKGNVISWNELCKIAESMARGLAYLHEDIpatngghkpsIAHRDFKSKNV------LLKsdltacIADF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 698 GLC---KEGIGFGDrTSTFCGTPEFLAPEVL------TQEAYTRaVDWWGLGVLLYEML---------VGE--CPF---- 753
Cdd:cd14053  147 GLAlkfEPGKSCGD-THGQVGTRRYMAPEVLegainfTRDAFLR-IDMYAMGLVLWELLsrcsvhdgpVDEyqLPFeeev 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 754 -PGDTEDEVFECIVNAD---VPCPHFLSAQGLELIQKLLQKS----PEKRLGAG 799
Cdd:cd14053  225 gQHPTLEDMQECVVHKKlrpQIRDEWRKHPGLAQLCETIEECwdhdAEARLSAG 278
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
559-795 3.25e-09

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 58.81  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYyAIKALKKQEVLGRDEIDslycEKRILEtvgRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05112   12 IGSGQFGLVHLGYWLNKDKV-AIKTIREGAMSEEDFIE----EAEVMM---KLSHPKLVQLYGVCLEQAPICLVFEFMEH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVFPEPQACFYLAC--VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKegIGFGDRTSTFCGT 716
Cdd:cd05112   84 GCLSDYLRTQRGLFSAETLLGMCldVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTR--FVLDDQYTSSTGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 717 P---EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIvNADVPC--PHFLSAQGLELIQKLLQK 790
Cdd:cd05112  162 KfpvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDI-NAGFRLykPRLASTHVYEIMNHCWKE 240

                 ....*
gi 564339933 791 SPEKR 795
Cdd:cd05112  241 RPEDR 245
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
549-754 3.30e-09

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: 58.45  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 549 QLQDFRCLAVLGRGHFGKVLLVQYKGTGkyYAIKALKKqevlgrDEIDSLYCEKRILETVGRtgHPFLLSLLACIQTSSH 628
Cdd:cd05082    4 NMKELKLLQTIGKGEFGDVMLGDYRGNK--VAVKCIKN------DATAQAFLAEASVMTQLR--HSNLVQLLGVIVEEKG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACF-VTEFLPGGDLMMQIH---EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI 704
Cdd:cd05082   74 GLYiVTEYMAKGSLVDYLRsrgRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEAS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564339933 705 GFGDRTSTfcgTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFP 754
Cdd:cd05082  154 STQDTGKL---PVKWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYP 201
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
559-795 3.49e-09

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 58.93  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYyAIKALKKqevlGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIqTSSHACFVTEFLPG 638
Cdd:cd05070   17 LGNGQFGEVWMGTWNGNTKV-AIKTLKP----GTMSPESFLEEAQIMK---KLKHDKLVQLYAVV-SEEPIYIVTEYMSK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHED---VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEgigFGDRTSTFCG 715
Cdd:cd05070   88 GSLLDFLKDGegrALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARL---IEDNEYTARQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TPEF----LAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLELIQKLLQ 789
Cdd:cd05070  165 GAKFpikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPQDCPISLHELMIHCWK 244

                 ....*.
gi 564339933 790 KSPEKR 795
Cdd:cd05070  245 KDPEER 250
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
549-753 4.36e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 60.52  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  549 QLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKAL---------KKQEVLGRDEIDSLYcEKRILETVGRtghpFLlsl 619
Cdd:PTZ00266   11 RLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAIsyrglkereKSQLVIEVNVMRELK-HKNIVRYIDR----FL--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  620 lacIQTSSHACFVTEFLPGGDLMMQIhedvfpepQACFYL-------ACVVLGLQFLHE-------------KRIIYR-- 677
Cdd:PTZ00266   83 ---NKANQKLYILMEFCDAGDLSRNI--------QKCYKMfgkieehAIVDITRQLLHAlaychnlkdgpngERVLHRdl 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933  678 ---------------DLKLDNLLLDAQGFLKIADFGLCKEgIGFGDRTSTFCGTPEFLAPEVLTQE--AYTRAVDWWGLG 740
Cdd:PTZ00266  152 kpqniflstgirhigKITAQANNLNGRPIAKIGDFGLSKN-IGIESMAHSCVGTPYYWSPELLLHEtkSYDDKSDMWALG 230
                         250
                  ....*....|...
gi 564339933  741 VLLYEMLVGECPF 753
Cdd:PTZ00266  231 CIIYELCSGKTPF 243
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
559-795 4.62e-09

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 58.20  E-value: 4.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlgrdEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd05052   14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTM----EVEEFLKEAAVMKEIK---HPNLVQLLGVCTREPPFYIITEFMPY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIHEDVFPE--PQACFYLAC-VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKegIGFGDRTSTFCG 715
Cdd:cd05052   87 GNLLDYLRECNREElnAVVLLYMATqIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSR--LMTGDTYTAHAG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TP---EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLELIQKLLQK 790
Cdd:cd05052  165 AKfpiKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYELLEKGyRMERPEGCPPKVYELMRACWQW 244

                 ....*
gi 564339933 791 SPEKR 795
Cdd:cd05052  245 NPSDR 249
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
551-800 4.68e-09

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 58.01  E-value: 4.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKAL-----KKQEVLgrdeidslycekRILETVGRTGHPFLLSLLACIQT 625
Cdd:cd14110    3 KTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIpykpeDKQLVL------------REYQVLRRLSHPRIAQLHSAYLS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG----LC 700
Cdd:cd14110   71 PRHLVLIEELCSGPELLYNLAErNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGnaqpFN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 KEGIGFGDRTSTFCgtpEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP---CPHFLS 777
Cdd:cd14110  151 QGKVLMTDKKGDYV---ETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQlsrCYAGLS 227
                        250       260
                 ....*....|....*....|...
gi 564339933 778 AQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd14110  228 GGAVNFLKSTLCAKPWGRPTASE 250
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
551-754 4.73e-09

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: 58.91  E-value: 4.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQ-EVLGRDEIdslyceKRILETVGRTGHPFLLSLLACIQTSSHA 629
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEiKPAIRNQI------IRELQVLHECNSPYIVGFYGAFYSDGEI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEK-RIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGfg 707
Cdd:cd06649   79 SICMEHMDGGSLDQVLKEaKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID-- 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564339933 708 DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFP 754
Cdd:cd06649  157 SMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIP 203
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
553-811 5.34e-09

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: 58.81  E-value: 5.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKK---QEVLGRdeidSLYCEKRILEtvgRTGHPFLLSLLACIQTSSHA 629
Cdd:cd07880   17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRpfqSELFAK----RAYRELRLLK---HMKHENVIGLLDVFTPDLSL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEF---LP--GGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGi 704
Cdd:cd07880   90 DRFHDFylvMPfmGTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQT- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 705 gfGDRTSTFCGTPEFLAPEV-LTQEAYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECIVNADVPCPHFL------ 776
Cdd:cd07880  169 --DSEMTGYVVTRWYRAPEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGhDHLDQLMEIMKVTGTPSKEFVqklqse 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 777 ------------------------SAQGLELIQKLLQKSPEKRLGAGE----------RDAE-EIKVQPF 811
Cdd:cd07880  247 daknyvkklprfrkkdfrsllpnaNPLAVNVLEKMLVLDAESRITAAEalahpyfeefHDPEdETEAPPY 316
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
559-763 5.98e-09

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: 58.10  E-value: 5.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYY--AIKALKKQeVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLA-CIQTSSHACF---- 631
Cdd:cd05075    8 LGEGEFGSVMEGQLNQDDSVLkvAVKTMKIA-ICTRSEMEDFLSEAVCMKEFD---HPNVMRLIGvCLQNTESEGYpspv 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 -VTEFLPGGDLMMQI------HEDVF-PEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEg 703
Cdd:cd05075   84 vILPFMKHGDLHSFLlysrlgDCPVYlPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKK- 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933 704 IGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFE 763
Cdd:cd05075  163 IYNGDyyRQGRISKMPvKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYD 226
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
550-795 6.30e-09

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: 58.10  E-value: 6.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVllvqYKG--------TGKYYAIKALKkqEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLA 621
Cdd:cd05090    4 LSAVRFMEELGECAFGKI----YKGhlylpgmdHAQLVAIKTLK--DYNNPQQWNEFQQEASLMTELH---HPNIVCLLG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 CIQTSSHACFVTEFLPGGDL-----MMQIHEDVfpepqAC-----------------FYLAC-VVLGLQFLHEKRIIYRD 678
Cdd:cd05090   75 VVTQEQPVCMLFEFMNQGDLhefliMRSPHSDV-----GCssdedgtvkssldhgdfLHIAIqIAAGMEYLSSHFFVHKD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 679 LKLDNLLLDAQGFLKIADFGLCKEGIGfgdrTSTFCGTPE------FLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGEC 751
Cdd:cd05090  150 LAARNILVGEQLHVKISDLGLSREIYS----SDYYRVQNKsllpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQ 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564339933 752 PFPGDTEDEVFECIVNAD-VPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05090  226 PYYGFSNQEVIEMVRKRQlLPCSEDCPPRMYSLMTECWQEIPSRR 270
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
556-811 6.83e-09

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: 57.99  E-value: 6.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTgkyyAIKALKKQEVLGRDE--IDSLYCEKRILETVgrTGHPFLLSLL-ACIQTSSHACFV 632
Cdd:cd14131    6 LKQLGKGGSSKVYKVLNPKK----KIYALKRVDLEGADEqtLQSYKNEIELLKKL--KGSDRIIQLYdYEVTDEDDYLYM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDL--MMQIHED-VFPEPQACFY----LACVvlglQFLHEKRIIYRDLKLdnllldA-----QGFLKIADFGLC 700
Cdd:cd14131   80 VMECGEIDLatILKKKRPkPIDPNFIRYYwkqmLEAV----HTIHEEGIVHSDLKP------AnfllvKGRLKLIDFGIA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 KeGIGfGDRTS----TFCGTPEFLAPEVLTQEAYT----------RAVDWWGLGVLLYEMLVGECPFPGDTED-EVFECI 765
Cdd:cd14131  150 K-AIQ-NDTTSivrdSQVGTLNYMSPEAIKDTSASgegkpkskigRPSDVWSLGCILYQMVYGKTPFQHITNPiAKLQAI 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 564339933 766 VNAD--VPCPHFLSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPF 811
Cdd:cd14131  228 IDPNheIEFPDIPNPDLIDVMKRCLQRDPKKRP-----SIPELLNHPF 270
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
658-814 7.27e-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: 58.08  E-value: 7.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 658 YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEA-YTRAVDW 736
Cdd:cd07872  109 FLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSSeYSTQIDM 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 737 WGLGVLLYEMLVGECPFPGDT-EDEVFECIVNADVPC------------------PHF-----------LSAQGLELIQK 786
Cdd:cd07872  189 WGVGCIFFEMASGRPLFPGSTvEDELHLIFRLLGTPTeetwpgissndefknynfPKYkpqplinhaprLDTEGIELLTK 268
                        170       180
                 ....*....|....*....|....*...
gi 564339933 787 LLQKSPEKRLgagerDAEEIKVQPFFRT 814
Cdd:cd07872  269 FLQYESKKRI-----SAEEAMKHAYFRS 291
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
559-796 7.71e-09

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: 57.81  E-value: 7.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGTGK----------YYAIKALKKQEVlgrDEIDSLYCEKRILetVGRTGHPFLLSLLA-CIQTSS 627
Cdd:cd05044    3 LGSGAFGEV----FEGTAKdilgdgsgetKVAVKTLRKGAT---DQEKAEFLKEAHL--MSNFKHPNILKLLGvCLDNDP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HAcFVTEFLPGGDLMMQIHEDVFPEPQACfYLA-------C--VVLGLQFLHEKRIIYRDLKLDNLLLDAQGF----LKI 694
Cdd:cd05044   74 QY-IILELMEGGDLLSYLRAARPTAFTPP-LLTlkdllsiCvdVAKGCVYLEDMHFVHRDLAARNCLVSSKDYrervVKI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLC----------KEGIGFgdrtstfcgTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVF 762
Cdd:cd05044  152 GDFGLArdiykndyyrKEGEGL---------LPvRWMAPESLVDGVFTTQSDVWAFGVLMWEILtLGQQPYPARNNLEVL 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564339933 763 ECIVNA---DVP--CPHFLsaqgLELIQKLLQKSPEKRL 796
Cdd:cd05044  223 HFVRAGgrlDQPdnCPDDL----YELMLRCWSTDPEERP 257
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
556-766 8.03e-09

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: 57.94  E-value: 8.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALK-----KQEVLgrdeidslyCEKRILETV---GRTGHPFLLSLLACIQTSS 627
Cdd:cd14210   18 LSVLGKGSFGQVVKCLDHKTGQLVAIKIIRnkkrfHQQAL---------VEVKILKHLndnDPDDKHNIVRYKDSFIFRG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 628 HACFVTEFLpgG----DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIY----------RDLKLDNllldaqgfLK 693
Cdd:cd14210   89 HLCIVFELL--SinlyELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHcdlkpenillKQPSKSS--------IK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 694 IADFGL-CKEG------IgfgdrTSTFcgtpeFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIV 766
Cdd:cd14210  159 VIDFGSsCFEGekvytyI-----QSRF-----YRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIM 228
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
551-795 8.57e-09

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: 8.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGkvlLVQY-KGTGKY-YAIKALKKqevlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSH 628
Cdd:cd05113    4 KDLTFLKELGTGQFG---VVKYgKWRGQYdVAIKMIKE----GSMSEDEFIEEAKVMMNLS---HEKLVQLYGVCTKQRP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLPGGDLMMQIHEDV-FPEPQACFYLaC--VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIg 705
Cdd:cd05113   74 IFIITEYMANGCLLNYLREMRkRFQTQQLLEM-CkdVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVL- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 fGDRTSTFCGTP---EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNA-DVPCPHFLSAQG 780
Cdd:cd05113  152 -DDEYTSSVGSKfpvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYsLGKMPYERFTNSETVEHVSQGlRLYRPHLASEKV 230
                        250
                 ....*....|....*
gi 564339933 781 LELIQKLLQKSPEKR 795
Cdd:cd05113  231 YTIMYSCWHEKADER 245
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
550-795 8.62e-09

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 57.72  E-value: 8.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTG-----KYYAIKALK-KQEVLGRDEidslYCEKRILETvgRTGHPFLLSLLACI 623
Cdd:cd05091    5 LSAVRFMEELGEDRFGKVYKGHLFGTApgeqtQAVAIKTLKdKAEGPLREE----FRHEAMLRS--RLQHPNIVCLLGVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 624 QTSSHACFVTEFLPGGDL-----MMQIHEDVFP-----------EPQACFYLAC-VVLGLQFLHEKRIIYRDLKLDNLLL 686
Cdd:cd05091   79 TKEQPMSMIFSYCSHGDLheflvMRSPHSDVGStdddktvkstlEPADFLHIVTqIAAGMEYLSSHHVVHKDLATRNVLV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 687 DAQGFLKIADFGLCKEgIGFGDRTSTFCGTP---EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVF 762
Cdd:cd05091  159 FDKLNVKISDLGLFRE-VYAADYYKLMGNSLlpiRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFsYGLQPYCGYSNQDVI 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564339933 763 ECIVNADV-PCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05091  238 EMIRNRQVlPCPDDCPAWVYTLMLECWNEFPSRR 271
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
543-795 8.62e-09

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: 57.77  E-value: 8.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 543 STRNPPQLQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKqevlgrdeIDSLYCEKRIL---ETVGRTgH--PFLL 617
Cdd:cd06618    7 GKKYKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRR--------SGNKEENKRILmdlDVVLKS-HdcPYIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 618 SllaciqtsSHACFVTEF--LPGGDLMMQIHEDV-------FPEPQACFYLACVVLGLQFLHEKR-IIYRDLKLDNLLLD 687
Cdd:cd06618   78 K--------CYGYFITDSdvFICMELMSTCLDKLlkriqgpIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 688 AQGFLKIADFGLCKEGIGFGDRTSTfCGTPEFLAPEVLTQE---AYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFE 763
Cdd:cd06618  150 ESGNVKLCDFGISGRLVDSKAKTRS-AGCAAYMAPERIDPPdnpKYDIRADVWSLGISLVELATGQFPYRNcKTEFEVLT 228
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564339933 764 CIVNADVPCPHF---LSAQGLELIQKLLQKSPEKR 795
Cdd:cd06618  229 KILNEEPPSLPPnegFSPDFCSFVDLCLTKDHRYR 263
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
559-770 8.90e-09

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 57.22  E-value: 8.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIK-----ALKKQevlgrdeidslyCEKRILETVGRTGHPFLLSLLACIQTSSHACFVT 633
Cdd:cd14108   10 IGRGAFSYLRRVKEKSSDLSFAAKfipvrAKKKT------------SARRELALLAELDHKSIVRFHDAFEKRRVVIIVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EfLPGGDLMmqihEDVFPEPQAC-----FYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF--LKIADFGLCKEgigF 706
Cdd:cd14108   78 E-LCHEELL----ERITKRPTVCesevrSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQE---L 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 707 GDRTSTFC--GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADV 770
Cdd:cd14108  150 TPNEPQYCkyGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNV 215
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
657-776 9.23e-09

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: 58.13  E-value: 9.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 657 FYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGigfgdrTSTFCGTPE-----FLAPEVLTQEAYT 731
Cdd:cd07875  130 YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA------GTSFMMTPYvvtryYRAPEVILGMGYK 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 732 RAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECIVNADVPCPHFL 776
Cdd:cd07875  204 ENVDIWSVGCIMGEMIKGGVLFPGtDHIDQWNKVIEQLGTPCPEFM 249
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
537-746 1.11e-08

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: 57.73  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 537 PPLAALSTRNPPQlQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILEtvgRTGHPFL 616
Cdd:cd06634    2 PEVAELFFKDDPE-KLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQ---KLRHPNT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 617 LSLLACIQTSSHACFVTEF-LPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIA 695
Cdd:cd06634   78 IEYRGCYLREHTAWLVMEYcLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 696 DFGlckeGIGFGDRTSTFCGTPEFLAPEV---LTQEAYTRAVDWWGLGVLLYEM 746
Cdd:cd06634  158 DFG----SASIMAPANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIEL 207
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
559-797 1.22e-08

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: 56.88  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKY--YAIKALKKQ-EVLGRDEIdslyceKRILETVGRTGHPFLLSLLACIQTSShACFVTEF 635
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRKKQidVAIKVLKQGnEKAVRDEM------MREAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDL--MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeGIGFGD---RT 710
Cdd:cd05115   85 ASGGPLnkFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSK-ALGADDsyyKA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 711 STFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIV-NADVPCPHFLSAQGLELIQKL 787
Cdd:cd05115  164 RSAGKWPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFsYGQKPYKKMKGPEVMSFIEqGKRMDCPAECPPEMYALMSDC 243
                        250
                 ....*....|
gi 564339933 788 LQKSPEKRLG 797
Cdd:cd05115  244 WIYKWEDRPN 253
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
552-795 1.27e-08

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 57.34  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVllvqYKG----TGKY----YAIKALKkqevlgrdEIDSLYCEKRILE---TVGRTGHPFLLSLL 620
Cdd:cd05108    8 EFKKIKVLGSGAFGTV----YKGlwipEGEKvkipVAIKELR--------EATSPKANKEILDeayVMASVDNPHVCRLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 621 ACIQTSShACFVTEFLPGGDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG 698
Cdd:cd05108   76 GICLTST-VQLITQLMPFGCLLdyVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 LCKEgIGFGDRTSTFCG--TP-EFLAPEVLTQEAYTRAVDWWGLGVLLYE-MLVGECPFPGDTEDEVFECIVNAD-VPCP 773
Cdd:cd05108  155 LAKL-LGAEEKEYHAEGgkVPiKWMALESILHRIYTHQSDVWSYGVTVWElMTFGSKPYDGIPASEISSILEKGErLPQP 233
                        250       260
                 ....*....|....*....|..
gi 564339933 774 HFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05108  234 PICTIDVYMIMVKCWMIDADSR 255
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
559-753 1.73e-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: 56.73  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGT---GKYYAIKALKkqevlGRDEIDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACFVTEF 635
Cdd:cd14664    1 IGRGGAGTV----YKGVmpnGTLVAVKRLK-----GEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHEDVFPEPQ---ACFYLACV--VLGLQFLHEK---RIIYRDLKLDNLLLDAQGFLKIADFGLCKegigFG 707
Cdd:cd14664   72 MPNGSLGELLHSRPESQPPldwETRQRIALgsARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAK----LM 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564339933 708 DRTSTFC-----GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14664  148 DDKDSHVmssvaGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
553-746 2.20e-08

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: 56.30  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALK---KQEVLGRDEIDSlycEKRILETVGrtgHPFLLSLLACIQTSSHA 629
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSysgKQSTEKWQDIIK---EVKFLRQLR---HPNTIEYKGCYLREHTA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLPG--GDlMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGlckeGIGFG 707
Cdd:cd06607   77 WLVMEYCLGsaSD-IVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG----SASLV 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564339933 708 DRTSTFCGTPEFLAPEV---LTQEAYTRAVDWWGLGVLLYEM 746
Cdd:cd06607  152 CPANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIEL 193
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
558-812 2.21e-08

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: 56.36  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKalkkqEVLgrdeIDSLYCEkRILETVGRTGHPFLLSLLACIQTSS------HACF 631
Cdd:cd14137   11 VIGSGSFGVVYQAKLLETGEVVAIK-----KVL----QDKRYKN-RELQIMRRLKHPNIVKLKYFFYSSGekkdevYLNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPG--GDLMMQIHEDVFPEP---------QACfylacvvLGLQFLHEKRIIYRDLKLD-NLLLDAQGFLKIADFGL 699
Cdd:cd14137   81 VMEYMPEtlYRVIRHYSKNKQTIPiiyvklysyQLF-------RGLAYLHSLGICHRDIKPQnLLVDPETGVLKLCDFGS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 CKEGIGFGDRTSTFCgTPEFLAPE-VLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA-------DV- 770
Cdd:cd14137  154 AKRLVPGEPNVSYIC-SRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVlgtptreQIk 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 771 ---------------PCP------HFLSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14137  233 amnpnytefkfpqikPHPwekvfpKRTPPDAIDLLSKILVYNPSKRL-----TALEALAHPFF 290
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
179-227 2.28e-08

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 51.04  E-value: 2.28e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564339933   179 EELQHRLRIEAAVAAGAKNVVKLLGgqriQDRKALAEAQAQLQESSQKL 227
Cdd:smart00742   4 EDLRRKIEKELKVKEGAENMRKLTS----NDRKVLSEAQSMLRESNQKL 48
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
558-767 2.29e-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: 56.39  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVL---LVQYKGTGKYYAIKALKkQEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLA-CIQTSSHACF-- 631
Cdd:cd05035    6 ILGEGEFGSVMeaqLKQDDGSQLKVAVKTMK-VDIHTYSEIEEFLSEAACMKDFD---HPNVMRLIGvCFTASDLNKPps 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 ---VTEFLPGGDL-----MMQIHEDV--FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK 701
Cdd:cd05035   82 pmvILPFMKHGDLhsyllYSRLGGLPekLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSR 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 EgIGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVN 767
Cdd:cd05035  162 K-IYSGDyyRQGRISKMPvKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRN 230
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
657-776 2.62e-08

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: 57.02  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 657 FYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGiGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDW 736
Cdd:cd07874  123 YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA-GTSFMMTPYVVTRYYRAPEVILGMGYKENVDI 201
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564339933 737 WGLGVLLYEMLVGECPFPG-DTEDEVFECIVNADVPCPHFL 776
Cdd:cd07874  202 WSVGCIMGEMVRHKILFPGrDYIDQWNKVIEQLGTPCPEFM 242
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
545-746 2.90e-08

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: 55.81  E-value: 2.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 545 RNPPQlQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVlgrdeiDSLYCEKRILETVGRTGHPFLLSLLACIQ 624
Cdd:cd06646    4 RRNPQ-HDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPG------DDFSLIQQEIFMVKECKHCNIVAYFGSYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHACFVTEFLPGGDLMMQIH-EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEG 703
Cdd:cd06646   77 SREKLWICMEYCGGGSLQDIYHvTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKI 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 704 IGFGDRTSTFCGTPEFLAPEVLTQE---AYTRAVDWWGLGVLLYEM 746
Cdd:cd06646  157 TATIAKRKSFIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIEL 202
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
662-795 3.52e-08

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 56.57  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 662 VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI---GFGDRTSTFCGTpEFLAPEVLTQEAYTRAVDWWG 738
Cdd:cd05105  246 VARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMhdsNYVSKGSTFLPV-KWMAPESIFDNLYTTLSDVWS 324
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 739 LGVLLYEML-VGECPFPGDTEDEVFECIVNAD--VPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05105  325 YGILLWEIFsLGGTPYPGMIVDSTFYNKIKSGyrMAKPDHATQEVYDIMVKCWNSEPEKR 384
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
545-753 3.81e-08

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: 55.88  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 545 RNPPQLqdFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALkkqEVLGrDEIDSLYCEKRILETVGRtgHPFLLSLLACI- 623
Cdd:cd06637    2 RDPAGI--FELVELVGNGTYGQVYKGRHVKTGQLAAIKVM---DVTG-DEEEEIKQEINMLKKYSH--HRNIATYYGAFi 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 624 -----QTSSHACFVTEFLPGG---DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIA 695
Cdd:cd06637   74 kknppGMDDQLWLVMEFCGAGsvtDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLV 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 696 DFGLCKEGIGFGDRTSTFCGTPEFLAPEVLT-----QEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd06637  154 DFGVSAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPL 216
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
550-773 4.17e-08

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 55.46  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVllvqYKG--TGKY-------YAIKALKKQ-EVLGRDEIdslyceKRILETVGRTGHPFLLSL 619
Cdd:cd05048    4 LSAVRFLEELGEGAFGKV----YKGelLGPSseesaisVAIKTLKENaSPKTQQDF------RREAELMSDLQHPNIVCL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 620 LACIQTSSHACFVTEFLPGGDL-----MMQIHEDV--------FPEPQACFYLACVVL----GLQFLHEKRIIYRDLKLD 682
Cdd:cd05048   74 LGVCTKEQPQCMLFEYMAHGDLheflvRHSPHSDVgvssdddgTASSLDQSDFLHIAIqiaaGMEYLSSHHYVHRDLAAR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 683 NLLLDAQGFLKIADFGLCKEGIGfGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTE 758
Cdd:cd05048  154 NCLVGDGLTVKISDFGLSRDIYS-SDyyRVQSKSLLPvRWMPPEAILYGKFTTESDVWSFGVVLWEIFsYGLQPYYGYSN 232
                        250
                 ....*....|....*.
gi 564339933 759 DEVFECIVNADV-PCP 773
Cdd:cd05048  233 QEVIEMIRSRQLlPCP 248
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
559-800 4.29e-08

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: 55.21  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKkQEVLGRDEID--SLYCEKRILETVG--RTGhPFLLSLLaciqtsshacfvtE 634
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVR-LEVFRAEELMacAGLTSPRVVPLYGavREG-PWVNIFM-------------D 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG---FLkiADFGL--CKEGIGFGD 708
Cdd:cd13991   79 LKEGGSLGQLIKEqGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsdaFL--CDFGHaeCLDPDGLGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTST---FCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVP-------CPHFLSa 778
Cdd:cd13991  157 SLFTgdyIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPPlreippsCAPLTA- 235
                        250       260
                 ....*....|....*....|..
gi 564339933 779 qglELIQKLLQKSPEKRLGAGE 800
Cdd:cd13991  236 ---QAIQAGLRKEPVHRASAAE 254
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
556-753 4.45e-08

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: 55.76  E-value: 4.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGK--VLLVQYKGTGKYYAIKalkKQEVLGRDEIDSLYCEKRILeTVGRTGHPFLLSLLACIQTSSHACFVT 633
Cdd:cd08216    3 LYEIGKCFKGGgvVHLAKHKPTNTLVAVK---KINLESDSKEDLKFLQQEIL-TSRQLQHPNILPYVTSFVVDNDLYVVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGG---DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRT 710
Cdd:cd08216   79 PLMAYGscrDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQ 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339933 711 STFCGTPEF-------LAPEVLTQ--EAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd08216  159 RVVHDFPKSseknlpwLSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPF 210
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
548-774 6.89e-08

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: 55.56  E-value: 6.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 548 PQLQDFRclaVLGRGHFGKVLLVQYKGTGKYYAIK------------ALKKQEVLGRDEIDSLYcekRILETVGRTGHPf 615
Cdd:cd07854    5 SRYMDLR---PLGCGSNGLVFSAVDSDCDKRVAVKkivltdpqsvkhALREIKIIRRLDHDNIV---KVYEVLGPSGSD- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 616 lLSLLACIQTSSHACFVTEFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF-LKI 694
Cdd:cd07854   78 -LTEDVGSLTELNSVYIVQEYMETDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLvLKI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLCK-------------EGIgfgdrTSTFCGTPEFLapevLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEV 761
Cdd:cd07854  157 GDFGLARivdphyshkgylsEGL-----VTKWYRSPRLL----LSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQ 227
                        250
                 ....*....|...
gi 564339933 762 FECIVNAdVPCPH 774
Cdd:cd07854  228 MQLILES-VPVVR 239
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
559-747 8.82e-08

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 54.40  E-value: 8.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKkqevLGRDEIDSLycekRILETVGRTGHPFLLSLLA-CIQTSS-HAcfVTEFL 636
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMNT----LSSNRANML----REVQLMNRLSHPNILRFMGvCVHQGQlHA--LTEYI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHEDVFPEPQACFYLAC-VVLGLQFLHEKRIIYRDLKLD--NLLLDAQGFLKI-ADFGLCKEGIGFGDRTST 712
Cdd:cd14155   71 NGGNLEQLLDSNEPLSWTVRVKLALdIARGLSYLHSKGIFHRDLTSKncLIKRDENGYTAVvGDFGLAEKIPDYSDGKEK 150
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564339933 713 F--CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML 747
Cdd:cd14155  151 LavVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII 187
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
559-753 1.04e-07

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: 53.98  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGT--GKYYAIKalkkqevlgrdEIDSLYCEKRI---LETVGRTGHPFLLSLLACIQTSSHACFVT 633
Cdd:cd14058    1 VGRGSFGVV----CKARwrNQIVAVK-----------IIESESEKKAFeveVRQLSRVDHPNIIKLYGACSNQKPVCLVM 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHEDVfPEPQ------ACFYLACVVlGLQFLH---EKRIIYRDLKLDNLLLDAQG-FLKIADFGLCKEg 703
Cdd:cd14058   66 EYAEGGSLYNVLHGKE-PKPIytaahaMSWALQCAK-GVAYLHsmkPKALIHRDLKPPNLLLTNGGtVLKICDFGTACD- 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339933 704 igFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14058  143 --ISTHMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
647-764 1.05e-07

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 54.99  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 647 EDVFPEPQACFYLAC----VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD--RTSTFCGTPEFL 720
Cdd:cd05103  169 EDLYKDFLTLEDLICysfqVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDyvRKGDARLPLKWM 248
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564339933 721 APEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFEC 764
Cdd:cd05103  249 APETIFDRVYTIQSDVWSFGVLLWEIFsLGASPYPGVKIDEEFCR 293
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
553-755 1.21e-07

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: 54.79  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALkkqevlgRDEIDSLYCEKRILETVG---RTGHPFLLSLLACIQTSSHA 629
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKI-------NDVFEHVSDATRILREIKllrLLRHPDIVEIKHIMLPPSRR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CF----VTEFLPGGDLMMQI--HEDVFPEPQAcFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKeg 703
Cdd:cd07859   75 EFkdiyVVFELMESDLHQVIkaNDDLTPEHHQ-FFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLAR-- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 704 IGFGDRTST-----FCGTPEFLAPEVLTQ--EAYTRAVDWWGLGVLLYEMLVGECPFPG 755
Cdd:cd07859  152 VAFNDTPTAifwtdYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPG 210
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
556-753 1.30e-07

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: 54.15  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETvGRTGHpfLLSLLACIQTSSHACFVTEF 635
Cdd:cd14026    2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHK-ARFSY--ILPILGICNEPEFLGIVTEY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHE-DVFPEPQACFYLAC---VVLGLQFLHEKR--IIYRDLKLDNLLLDAQGFLKIADFGLCKEGI----- 704
Cdd:cd14026   79 MTNGSLNELLHEkDIYPDVAWPLRLRIlyeIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKWRQlsisq 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339933 705 GFGDRTSTFCGTPEFLAPEVLTQEAYTRAV---DWWGLGVLLYEMLVGECPF 753
Cdd:cd14026  159 SRSSKSAPEGGTIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKIPF 210
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
553-778 1.66e-07

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: 54.33  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRiLETVGRTGHPFLLSLlACIQTSSHACFV 632
Cdd:cd14227   17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILAR-LSTESADDYNFVRAY-ECFQHKNHTCLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIY---RDLKLDNLLLDAQGF-LKIADFGLCKEGIGf 706
Cdd:cd14227   95 FEMLEQNlyDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHadlKPENIMLVDPSRQPYrVKVIDFGSASHVSK- 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 707 gDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVPCPHFLSA 778
Cdd:cd14227  174 -AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEyDQIRYISQTQGLPAEYLLSA 245
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
559-763 1.69e-07

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 53.84  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKG----TGKYYAIKALKKQEVL----------GRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIQ 624
Cdd:cd05095   13 LGEGQFGEVHLCEAEGmekfMDKDFALEVSENQPVLvavkmlradaNKNARNDFLKEIKIMS---RLKDPNIIRLLAVCI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHACFVTEFLPGGDLMMQIHEDVFPEPQA-------------CFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGF 691
Cdd:cd05095   90 TDDPLCMITEYMENGDLNQFLSRQQPEGQLAlpsnaltvsysdlRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 692 LKIADFGLCKEgIGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV--GECPFPGDTEDEVFE 763
Cdd:cd05095  170 IKIADFGMSRN-LYSGDyyRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWETLTfcREQPYSQLSDEQVIE 245
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
558-762 1.90e-07

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 53.81  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVL---LVQYKGTGKY--YAIKALKKQEvlGRDEIDSLYCEKRILETVGrtgHPFLLSLLACIQTSSHACFV 632
Cdd:cd05045    7 TLGEGEFGKVVkatAFRLKGRAGYttVAVKMLKENA--SSSELRDLLSEFNLLKQVN---HPHVIKLYGACSQDGPLLLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDVFPEPQACFYLAC-------------------------VVLGLQFLHEKRIIYRDLKLDNLLLD 687
Cdd:cd05045   82 VEYAKYGSLRSFLRESRKVGPSYLGSDGNrnssyldnpderaltmgdlisfawqISRGMQYLAEMKLVHRDLAARNVLVA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 688 AQGFLKIADFGLCK---EGIGFGDRTSTFCGTpEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVF 762
Cdd:cd05045  162 EGRKMKISDFGLSRdvyEEDSYVKRSKGRIPV-KWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIAPERLF 239
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
666-800 2.12e-07

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: 53.72  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 666 LQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK------EGIGFGDRTStFCGTPEFLAPEVL-TQEAYTRAVDWWG 738
Cdd:cd07852  120 LKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARslsqleEDDENPVLTD-YVATRWYRAPEILlGSTRYTKGVDMWS 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 739 LGVLLYEMLVGECPFPG----DTEDEVFECI----------------------------VNADVPCPHfLSAQGLELIQK 786
Cdd:cd07852  199 VGCILGEMLLGKPLFPGtstlNQLEKIIEVIgrpsaediesiqspfaatmleslppsrpKSLDELFPK-ASPDALDLLKK 277
                        170
                 ....*....|....
gi 564339933 787 LLQKSPEKRLGAGE 800
Cdd:cd07852  278 LLVFNPNKRLTAEE 291
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
551-795 2.21e-07

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: 53.15  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYyAIKALKKqevlGRDEIDSLYCEKRILEtvgRTGHPFLLSLLACIqTSSHAC 630
Cdd:cd05071    9 ESLRLEVKLGQGCFGEVWMGTWNGTTRV-AIKTLKP----GTMSPEAFLQEAQVMK---KLRHEKLVQLYAVV-SEEPIY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQI---HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK--EGIG 705
Cdd:cd05071   80 IVTEYMSKGSLLDFLkgeMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARliEDNE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCGTpEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNA-DVPCPHFLSAQGLEL 783
Cdd:cd05071  160 YTARQGAKFPI-KWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERGyRMPCPPECPESLHDL 238
                        250
                 ....*....|..
gi 564339933 784 IQKLLQKSPEKR 795
Cdd:cd05071  239 MCQCWRKEPEER 250
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
559-797 2.28e-07

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: 53.04  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVL--LVQYKGTGKYYAIKALKKQEvlgRDEI--DSLYCEKRILETVGrtgHPFLLSLLACIQTSSHAcFVTE 634
Cdd:cd05116    3 LGSGNFGTVKkgYYQMKKVVKTVAVKILKNEA---NDPAlkDELLREANVMQQLD---NPYIVRMIGICEAESWM-LVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDL--MMQIHEDVfPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK---EGIGFGDR 709
Cdd:cd05116   76 MAELGPLnkFLQKNRHV-TEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKalrADENYYKA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNAD-VPCPHFLSAQGLELIQKL 787
Cdd:cd05116  155 QTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFsYGQKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLMKLC 234
                        250
                 ....*....|
gi 564339933 788 LQKSPEKRLG 797
Cdd:cd05116  235 WTYDVDERPG 244
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
553-778 2.30e-07

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: 53.88  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRiLETVGRTGHPFLLSLlACIQTSSHACFV 632
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILAR-LSNENADEFNFVRAY-ECFQHRNHTCLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIY---RDLKLDNLLLDAQGF-LKIADFGlckeGIGF 706
Cdd:cd14229   80 FEMLEQNlyDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHadlKPENIMLVDPVRQPYrVKVIDFG----SASH 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 707 GDRT--STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVPCPHFLSA 778
Cdd:cd14229  156 VSKTvcSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEyDQIRYISQTQGLPGEQLLNV 230
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
581-753 2.31e-07

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: 52.88  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 581 IKALKKQEVLGR--DEIDSLYCEKRILEtvgrtgHPFLLSLLACIQTSSHACFVTEFLPGGDLMMQIHED---VFPEPQA 655
Cdd:cd14057   23 AKILKVRDVTTRisRDFNEEYPRLRIFS------HPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHEGtgvVVDQSQA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 656 CFYLACVVLGLQFLHE-KRIIYRDLKLDNLLLDAQGFlkIADFGLCKEGIGFGDRTSTFcgTPEFLAPEVLT---QEAYT 731
Cdd:cd14057   97 VKFALDIARGMAFLHTlEPLIPRHHLNSKHVMIDEDM--TARINMADVKFSFQEPGKMY--NPAWMAPEALQkkpEDINR 172
                        170       180
                 ....*....|....*....|..
gi 564339933 732 RAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14057  173 RSADMWSFAILLWELVTREVPF 194
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
665-777 2.62e-07

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: 53.57  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 665 GLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC-KEGIGFgdRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLL 743
Cdd:cd07850  114 GIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLArTAGTSF--MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIM 191
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564339933 744 YEMLVGECPFPG-DTEDEVFECIVNADVPCPHFLS 777
Cdd:cd07850  192 GEMIRGTVLFPGtDHIDQWNKIIEQLGTPSDEFMS 226
HR1_Ste20-like cd11627
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of ...
100-166 2.83e-07

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Schizosaccharomyces pombe Ste20-like proteins; This group is composed of predominantly uncharacterized fungal proteins, which contain two known domains: HR1 at the N-terminal region and REM (Ras exchanger motif) at the C-terminal region. One member protein from Schizosaccharomyces pombe is named Ste16 while its gene is called ste20 (a target of rapamycin complex 2 subunit). It is a subunit in the protein kinase TOR complexes in fission yeast. The REM domain is usually found in nucleotide exchange factors for Ras-like small GTPases. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212017 [Multi-domain]  Cd Length: 71  Bit Score: 48.53  E-value: 2.83e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 100 SRARLLEALHRQLEVELKVKQGAENMIHTCASGTPKERKLL-AAAQQMLKDSQLKVALLRmkiSGLEA 166
Cdd:cd11627    2 VSEQRLEELRGKLEIETKIKDGAENLLQVLDSKNAKEKKDQrARVESELNSSNRKIAQLT---SQLEE 66
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
558-800 3.40e-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: 52.90  E-value: 3.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILetvgrTGHPFLLSLLACI----QTSSHAC--- 630
Cdd:cd14036    7 VIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKL-----SGHPNIVQFCSAAsigkEESDQGQaey 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 -FVTEFLPGG--DLMMQIHEdvfPEPQAC------FYLACvvLGLQFLHEKR--IIYRDLKLDNLLLDAQGFLKIADFGL 699
Cdd:cd14036   82 lLLTELCKGQlvDFVKKVEA---PGPFSPdtvlkiFYQTC--RAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 CKEGIGFGDRT------------STFCGTPEFLAPEVL---TQEAYTRAVDWWGLGVLLYEMLVGECPFpgdtEDEVFEC 764
Cdd:cd14036  157 ATTEAHYPDYSwsaqkrslvedeITRNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPF----EDGAKLR 232
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564339933 765 IVNADVPCPHFLSAQGL--ELIQKLLQKSPEKRLGAGE 800
Cdd:cd14036  233 IINAKYTIPPNDTQYTVfhDLIRSTLKVNPEERLSITE 270
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
556-753 3.92e-07

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: 52.33  E-value: 3.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTgkyYAIKALKKQEVLGrDEIDSLYCEKRILEtvgRTGHPFLLsLLACIQTSSHACFVTEF 635
Cdd:cd14150    5 LKRIGTGSFGTVFRGKWHGD---VAVKILKVTEPTP-EQLQAFKNEMQVLR---KTRHVNIL-LFMGFMTRPNFAIITQW 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIH--EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC--KEGIGFGDRTS 711
Cdd:cd14150   77 CEGSSLYRHLHvtETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAtvKTRWSGSQQVE 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564339933 712 TFCGTPEFLAPEVLTQE---AYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14150  157 QPSGSILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPY 201
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
632-798 3.97e-07

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 52.51  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLpggDLMMQIHEDVFPE----PQAC-FYLACVVLGLQFLHEKRIIYRDLKLDNLLL-DAQGFLKIADFGLCKegiG 705
Cdd:PLN00009  79 VFEYL---DLDLKKHMDSSPDfaknPRLIkTYLYQILRGIAYCHSHRVLHRDLKPQNLLIdRRTNALKLADFGLAR---A 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCG---TPEFLAPEVLT-QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVP--------- 771
Cdd:PLN00009 153 FGIPVRTFTHevvTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEiDELFKIFRILGTPneetwpgvt 232
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 772 -CPHFLSA------------------QGLELIQKLLQKSPEKRLGA 798
Cdd:PLN00009 233 sLPDYKSAfpkwppkdlatvvptlepAGVDLLSKMLRLDPSKRITA 278
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
665-812 4.77e-07

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 52.44  E-value: 4.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 665 GLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKegiGFGDRTSTFCG---TPEFLAPEVLT-QEAYTRAVDWWGLG 740
Cdd:cd07839  111 GLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR---AFGIPVRCYSAevvTLWYRPPDVLFgAKLYSTSIDMWSAG 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 741 VLLYEMLVGECP-FPG-DTEDE---VFECI-------------VNADVPCPHF------------LSAQGLELIQKLLQK 790
Cdd:cd07839  188 CIFAELANAGRPlFPGnDVDDQlkrIFRLLgtpteeswpgvskLPDYKPYPMYpattslvnvvpkLNSTGRDLLQNLLVC 267
                        170       180
                 ....*....|....*....|..
gi 564339933 791 SPEKRLgagerDAEEIKVQPFF 812
Cdd:cd07839  268 NPVQRI-----SAEEALQHPYF 284
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
558-795 5.16e-07

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 52.09  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVL---LVQYKGTGKYYAIKALKKQEVLGrdEIDSLYCEKRILETVGrtgHPFLLSLLA-CIQTSSHACFVT 633
Cdd:cd05058    2 VIGKGHFGCVYhgtLIDSDGQKIHCAVKSLNRITDIE--EVEQFLKEGIIMKDFS---HPNVLSLLGiCLPSEGSPLVVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIH-EDVFPEPQAC--FYLAcVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIG---FG 707
Cdd:cd05058   77 PYMKHGDLRNFIRsETHNPTVKDLigFGLQ-VAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDkeyYS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPG-DTEDEVFECIVNADVPCPHFLSAQGLELI 784
Cdd:cd05058  156 VHNHTGAKLPvKWMALESLQTQKFTTKSDVWSFGVLLWELMTrGAPPYPDvDSFDITVYLLQGRRLLQPEYCPDPLYEVM 235
                        250
                 ....*....|.
gi 564339933 785 QKLLQKSPEKR 795
Cdd:cd05058  236 LSCWHPKPEMR 246
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
559-773 5.35e-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: 52.01  E-value: 5.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGTGKYY---------AIKAL----KKQevlgrDEIDSLYcEKRILetvGRTGHPFLLSLLA-CIQ 624
Cdd:cd05036   14 LGQGAFGEV----YEGTVSGMpgdpsplqvAVKTLpelcSEQ-----DEMDFLM-EALIM---SKFNHPNIVRCIGvCFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHAcFVTEFLPGGDLMMQIHED----VFPEPQACFYLAC----VVLGLQFLHEKRIIYRDLKLDNLLLDAQG---FLK 693
Cdd:cd05036   81 RLPRF-ILLELMAGGDLKSFLRENrprpEQPSSLTMLDLLQlaqdVAKGCRYLEENHFIHRDIAARNCLLTCKGpgrVAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 694 IADFGLCKEgIGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYE-MLVGECPFPGDTEDEVFECIVNA- 768
Cdd:cd05036  160 IGDFGMARD-IYRADyyRKGGKAMLPvKWMPPEAFLDGIFTSKTDVWSFGVLLWEiFSLGYMPYPGKSNQEVMEFVTSGg 238

                 ....*....
gi 564339933 769 --DVP--CP 773
Cdd:cd05036  239 rmDPPknCP 247
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
556-798 5.58e-07

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: 52.37  E-value: 5.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKyyaIKALKKQEVLGRDE---IDSLYcEKRILETVGrtgHPFLLSLLACIQTSSHAC-- 630
Cdd:cd07865   17 LAKIGQGTFGEVFKARHRKTGQ---IVALKKVLMENEKEgfpITALR-EIKILQLLK---HENVVNLIEICRTKATPYnr 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 ------FVTEF----LPGgdLMMQIHEDvFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC 700
Cdd:cd07865   90 ykgsiyLVFEFcehdLAG--LLSNKNVK-FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 701 K----EGIGFGDRTSTFCGTPEFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIV--------- 766
Cdd:cd07865  167 RafslAKNSQPNRYTNRVVTLWYRPPELLLGERdYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISqlcgsitpe 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 767 ------------NADVP-----------CPHFLSAQGLELIQKLLQKSPEKRLGA 798
Cdd:cd07865  247 vwpgvdklelfkKMELPqgqkrkvkerlKPYVKDPYALDLIDKLLVLDPAKRIDA 301
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
556-777 5.80e-07

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: 52.40  E-value: 5.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIdslyCEKRILETVGRTGHPFLLSLLACIQT---SSHACFV 632
Cdd:cd14225   48 LEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQAL----VEVKILDALRRKDRDNSHNVIHMKEYfyfRNHLCIT 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLpGGDLMMQIHEDVFpepQAcFYLACV-------VLGLQFLHEKRIIY--RDLKLDNLLLDAQGFLKIADFGL-CKE 702
Cdd:cd14225  124 FELL-GMNLYELIKKNNF---QG-FSLSLIrrfaislLQCLRLLYRERIIHcdLKPENILLRQRGQSSIKVIDFGSsCYE 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 703 GigfgDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNA-DVPCPHFLS 777
Cdd:cd14225  199 H----QRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVlGLPPPELIE 270
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
558-756 6.70e-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: 51.58  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVllvqYKGtgKYYAIKALKKQEVLGRDEiDSLYCEKRILETVGRTGHPFLLSLLACIQTSSHACFVTEFLP 637
Cdd:cd14063    7 VIGKGRFGRV----HRG--RWHGDVAIKLLNIDYLNE-EQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 638 GGDLMMQIHE--DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLlldaqgFLK-----IADFGLCK-EGIGFGDR 709
Cdd:cd14063   80 GRTLYSLIHErkEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNI------FLEngrvvITDFGLFSlSGLLQPGR 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564339933 710 TSTFCGTPE----FLAPEVLT----------QEAYTRAVDWWGLGVLLYEMLVGECPFPGD 756
Cdd:cd14063  154 REDTLVIPNgwlcYLAPEIIRalspdldfeeSLPFTKASDVYAFGTVWYELLAGRWPFKEQ 214
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
650-800 6.98e-07

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: 52.11  E-value: 6.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 650 FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK-----EGIGFGDRTSTFCGTPeflaPEV 724
Cdd:cd07864  113 FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARlynseESRPYTNKVITLWYRP----PEL 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 725 LT-QEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVN-ADVPCP----------------------------- 773
Cdd:cd07864  189 LLgEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRlCGSPCPavwpdviklpyfntmkpkkqyrrrlreef 268
                        170       180
                 ....*....|....*....|....*..
gi 564339933 774 HFLSAQGLELIQKLLQKSPEKRLGAGE 800
Cdd:cd07864  269 SFIPTPALDLLDHMLTLDPSKRCTAEQ 295
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
174-226 7.79e-07

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


Pssm-ID: 212008 [Multi-domain]  Cd Length: 68  Bit Score: 47.32  E-value: 7.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564339933 174 PDLLAEELQHRLRIEAAVAAGAKNVVKLLGGQriQDRKALAEAQAQLQESSQK 226
Cdd:cd00089    3 LQQRLEELRRKLEKELKIREGAENLLKLYSNP--KVKKDLAEVQLNLKESKEK 53
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
662-762 7.83e-07

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 52.31  E-value: 7.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 662 VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD--RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGL 739
Cdd:cd14207  189 VARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDyvRKGDARLPLKWMAPESIFDKIYSTKSDVWSY 268
                         90       100
                 ....*....|....*....|....
gi 564339933 740 GVLLYEML-VGECPFPGDTEDEVF 762
Cdd:cd14207  269 GVLLWEIFsLGASPYPGVQIDEDF 292
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
553-759 9.05e-07

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: 51.80  E-value: 9.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrDEIDSLYCEKRILETVGR---TGHPFLLSLLACIQTSSHA 629
Cdd:cd14134   14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVE----KYREAAKIEIDVLETLAEkdpNGKSHCVQLRDWFDYRGHM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEFLpgG----DLMMQIHEDVFPepqacfyLACVV-------LGLQFLHEKRII-------------------YRDL 679
Cdd:cd14134   90 CIVFELL--GpslyDFLKKNNYGPFP-------LEHVQhiakqllEAVAFLHDLKLThtdlkpenillvdsdyvkvYNPK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 680 KLDNLLLDAQGFLKIADFGlckeGIGFgDRT--STFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFpgDT 757
Cdd:cd14134  161 KKRQIRVPKSTDIKLIDFG----SATF-DDEyhSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLF--QT 233

                 ..
gi 564339933 758 ED 759
Cdd:cd14134  234 HD 235
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
558-795 9.07e-07

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 51.12  E-value: 9.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVllvqYKGT----GKYYAIKALKKQEVLGRDEIDS---LYCEKRILETVGrTGHPFLLSLLACIQTSSHAC 630
Cdd:cd14100    7 LLGSGGFGSV----YSGIrvadGAPVAIKHVEKDRVSEWGELPNgtrVPMEIVLLKKVG-SGFRGVIRLLDWFERPDSFV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEF-LPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLL-DAQGFLKIADFGlckEGIGFG 707
Cdd:cd14100   82 LVLERpEPVQDLFDFITERgALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIdLNTGELKLIDFG---SGALLK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 708 DRTST-FCGTPEFLAPEVLTQEAY-TRAVDWWGLGVLLYEMLVGECPFPGDTEdevfecIVNADVPCPHFLSAQGLELIQ 785
Cdd:cd14100  159 DTVYTdFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHDEE------IIRGQVFFRQRVSSECQHLIK 232
                        250
                 ....*....|
gi 564339933 786 KLLQKSPEKR 795
Cdd:cd14100  233 WCLALRPSDR 242
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
647-762 1.03e-06

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 51.90  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 647 EDVFPEPQACFYLAC----VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGD--RTSTFCGTPEFL 720
Cdd:cd05102  162 DDLWQSPLTMEDLICysfqVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDyvRKGSARLPLKWM 241
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 564339933 721 APEVLTQEAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVF 762
Cdd:cd05102  242 APESIFDKVYTTQSDVWSFGVLLWEIFsLGASPYPGVQINEEF 284
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
558-799 1.19e-06

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: 51.29  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVllvqYKGTGKYYAIkALKkqeVLGRDEIDSLYCEKRILETVGRTgHPFLLSLLACIQTSSHAC----FVT 633
Cdd:cd13998    2 VIGKGRFGEV----WKASLKNEPV-AVK---IFSSRDKQSWFREKEIYRTPMLK-HENILQFIAADERDTALRtelwLVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEK---------RIIYRDLKLDNLLLDAQGFLKIADFGLC---K 701
Cdd:cd13998   73 AFHPNGSL*DYLSLHTIDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGLAvrlS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 EGIGFGDR-TSTFCGTPEFLAPEVL-------TQEAYTRaVDWWGLGVLLYEM--------------------LVGECPF 753
Cdd:cd13998  153 PSTGEEDNaNNGQVGTKRYMAPEVLegainlrDFESFKR-VDIYAMGLVLWEMasrctdlfgiveeykppfysEVPNHPS 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339933 754 PGDTEDEVFECIVNADVPcPHFLSAQGLELIQKLLQKS----PEKRLGAG 799
Cdd:cd13998  232 FEDMQEVVVRDKQRPNIP-NRWLSHPGLQSLAETIEECwdhdAEARLTAQ 280
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
662-747 1.21e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 51.80  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 662 VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTStFCGTPEFLAPEVLTQEAYTRAVDWWGLGV 741
Cdd:PHA03209 166 ILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLG-LAGTVETNAPEVLARDKYNSKADIWSAGI 244

                 ....*.
gi 564339933 742 LLYEML 747
Cdd:PHA03209 245 VLFEML 250
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
666-812 1.33e-06

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 51.96  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 666 LQFLHEKRIIYRDLKLDNLLLDAQGF-LKIADFGLCKEGIGfGDRTSTFCGTPEFLAPEV-LTQEAYTRAVDWWGLGVLL 743
Cdd:PTZ00036 183 LAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLLA-GQRSVSYICSRFYRAPELmLGATNYTTHIDLWSLGCII 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 744 YEMLVGECPFPGD----------------TEDEVFECIVN-ADVPCPHFLSA------------QGLELIQKLLQKSPEK 794
Cdd:PTZ00036 262 AEMILGYPIFSGQssvdqlvriiqvlgtpTEDQLKEMNPNyADIKFPDVKPKdlkkvfpkgtpdDAINFISQFLKYEPLK 341
                        170
                 ....*....|....*...
gi 564339933 795 RLGAGERDAEeikvqPFF 812
Cdd:PTZ00036 342 RLNPIEALAD-----PFF 354
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
546-816 1.41e-06

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: 51.21  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 546 NPPQLQDFRCLAVLGRGHFGKVllvqYKGTGKY---YAIKALKKQEVLGRDEIDSLY----C-EKRILETVGrtgHPFLL 617
Cdd:cd14040    1 HPTLNERYLLLHLLGRGGFSEV----YKAFDLYeqrYAAVKIHQLNKSWRDEKKENYhkhaCrEYRIHKELD---HPRIV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 618 SLLACIQTSSHA-CFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKR--IIY---RDLKLDNLLLDAQG 690
Cdd:cd14040   74 KLYDYFSLDTDTfCTVLEYCEGNDLDFYLKQhKLMSEKEARSIVMQIVNALRYLNEIKppIIHydlKPGNILLVDGTACG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 691 FLKIADFGLCK------EGIGFGDRTSTFCGTPEFLAPE--VLTQE--AYTRAVDWWGLGVLLYEMLVGECPFP-GDTED 759
Cdd:cd14040  154 EIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGhNQSQQ 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933 760 EVFE--CIVNA---DVPCPHFLSAQGLELIQKLLQKSPEKRLGAGERdAEEIKVQPFFRTTN 816
Cdd:cd14040  234 DILQenTILKAtevQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQL-ASDPYLLPHMRRSN 294
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
613-755 1.44e-06

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 50.73  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 613 HPFLLSLLACIQTSSHACFVTEFLPGgDLM--MQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQG 690
Cdd:cd07870   57 HANIVLLHDIIHTKETLTFVFEYMHT-DLAqyMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLG 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 691 FLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPG 755
Cdd:cd07870  136 ELKLADFGLARAKSIPSQTYSSEVVTLWYRPPDVLLGATdYSSALDIWGAGCIFIEMLQGQPAFPG 201
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
556-778 1.55e-06

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: 51.30  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRD---EIDSLYCekriLETVGRTGHPFLLSlLACIQTSSHACFV 632
Cdd:cd14211    4 LEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQgqiEVSILSR----LSQENADEFNFVRA-YECFQHKNHTCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDLMMQIHEDVFPEPQACF--YLACVVLGLQFLHEKRIIY---RDLKLDNLLLDAQGF-LKIADFG-------- 698
Cdd:cd14211   79 FEMLEQNLYDFLKQNKFSPLPLKYIrpILQQVLTALLKLKSLGLIHadlKPENIMLVDPVRQPYrVKVIDFGsashvska 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 LCkegigfgdrtSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVPCPHFLS 777
Cdd:cd14211  159 VC----------STYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEyDQIRYISQTQGLPAEHLLN 228

                 .
gi 564339933 778 A 778
Cdd:cd14211  229 A 229
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
662-753 1.93e-06

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


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 50.39  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 662 VVLGLQFLHEKR--IIYRDLKLDNLLLDA-QGFLKIADFGLCKegIGFGDRTSTFCGTPEFLAPEvLTQEAYTRAVDWWG 738
Cdd:cd14033  113 ILKGLHFLHSRCppILHRDLKCDNIFITGpTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPE-MYEEKYDEAVDVYA 189
                         90
                 ....*....|....*
gi 564339933 739 LGVLLYEMLVGECPF 753
Cdd:cd14033  190 FGMCILEMATSEYPY 204
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
595-750 2.09e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 51.15  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 595 IDSLYCEKRILETVGRTG------------HPFLLSLLACIQTSSHACFVtefLPGGDLMMQIHEDVFPEPQACFYLA-- 660
Cdd:PHA03212 112 IDNKTCEHVVIKAGQRGGtateahilrainHPSIIQLKGTFTYNKFTCLI---LPRYKTDLYCYLAAKRNIAICDILAie 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 661 -CVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG-LCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWG 738
Cdd:PHA03212 189 rSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGaACFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWS 268
                        170
                 ....*....|..
gi 564339933 739 LGVLLYEMLVGE 750
Cdd:PHA03212 269 AGIVLFEMATCH 280
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
556-800 2.24e-06

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 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: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 50.37  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLL--VQYKGTGKYYAIKALKKQEVLgRDEIDSLYCEK--RILEtvgrtgHPFLLSLLA-CIQTSSHaC 630
Cdd:cd05087    2 LKEIGHGWFGKVFLgeVNSGLSSTQVVVKELKASASV-QDQMQFLEEAQpyRALQ------HTNLLQCLAqCAEVTPY-L 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLM-----MQIHEDVFPEPQACFYLAC-VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL--CKE 702
Cdd:cd05087   74 LVMEFCPLGDLKgylrsCRAAESMAPDPLTLQRMACeVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLshCKY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 703 GIGFGDRTSTFCGTPEFLAPEvLTQEAY--------TRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIVNAD---V 770
Cdd:cd05087  154 KEDYFVTADQLWVPLRWIAPE-LVDEVHgnllvvdqTKQSNVWSLGVTIWELFeLGNQPYRHYSDRQVLTYTVREQqlkL 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564339933 771 PCPHF---LSAQGLELIQKL-LQksPEKRLGAGE 800
Cdd:cd05087  233 PKPQLklsLAERWYEVMQFCwLQ--PEQRPTAEE 264
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
561-805 2.40e-06

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 50.01  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 561 RGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRD-EIDSLYCEKRILETVG-----RTGHPFLlsllaciqtsshacfvtE 634
Cdd:cd13995   14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDvEIQACFRHENIAELYGallweETVHLFM-----------------E 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLMMQIhEDVFP--EPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLkIADFGLC---KEGIGFgdr 709
Cdd:cd13995   77 AGEGGSVLEKL-ESCGPmrEFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSvqmTEDVYV--- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECP----FPgDTEDEVFECIVNADVP----CPHFLSAQGL 781
Cdd:cd13995  152 PKDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPwvrrYP-RSAYPSYLYIIHKQAPpledIAQDCSPAMR 230
                        250       260
                 ....*....|....*....|....
gi 564339933 782 ELIQKLLQKSPEKRLGAGERDAEE 805
Cdd:cd13995  231 ELLEAALERNPNHRSSAAELLKHE 254
HR1_PKN_3 cd11625
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
100-159 2.56e-06

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that 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 cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212015  Cd Length: 74  Bit Score: 45.74  E-value: 2.56e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 100 SRARLLEALHRqLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRM 159
Cdd:cd11625    7 LELRIEELRHH-LRVETAVVEGAKNVIKLLQNAKKDDKKALQEAQKSLSESSQKLDLLRL 65
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
559-753 2.66e-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: 50.27  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVL---GRDEIdslycekRILETVgRTGHPFLLSLLACIQ----------T 625
Cdd:cd14136   18 LGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYteaALDEI-------KLLKCV-READPKDPGREHVVQllddfkhtgpN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 626 SSHACFVTEFLpGGDLMMQIhedvfpepQACFY----LACV------VL-GLQFLHEK-RIIYRDLKLDNLLLDAQGF-L 692
Cdd:cd14136   90 GTHVCMVFEVL-GPNLLKLI--------KRYNYrgipLPLVkkiarqVLqGLDYLHTKcGIIHTDIKPENVLLCISKIeV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933 693 KIADFG-LCKEGIGFGDRTStfcgTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14136  161 KIADLGnACWTDKHFTEDIQ----TRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLF 218
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
556-758 2.71e-06

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: 50.06  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEvlgrdeiDSLYCEK---RILETVGRTGHPFLLSLLACIQTSSHACFV 632
Cdd:cd07847    6 LSKIGEGSYGVVFKCRNRETGQIVAIKKFVESE-------DDPVIKKialREIRMLKQLKHPNLVNLIEVFRRKRKLHLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGGDL-MMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTS 711
Cdd:cd07847   79 FEYCDHTVLnELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYT 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339933 712 TFCGTPEFLAPEVL---TQeaYTRAVDWWGLGVLLYEMLVGECPFPGDTE 758
Cdd:cd07847  159 DYVATRWYRAPELLvgdTQ--YGPPVDVWAIGCVFAELLTGQPLWPGKSD 206
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
551-763 2.82e-06

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: 49.97  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVLLVQYKGTGKYY--------------AIKALKKqEVLGRDEIDSLycekRILETVGRTGHPFL 616
Cdd:cd05097    5 QQLRLKEKLGEGQFGEVHLCEAEGLAEFLgegapefdgqpvlvAVKMLRA-DVTKTARNDFL----KEIKIMSRLKNPNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 617 LSLLACIQTSSHACFVTEFLPGGDLMMQI----------HEDVFP--EPQACFYLAC-VVLGLQFLHEKRIIYRDLKLDN 683
Cdd:cd05097   80 IRLLGVCVSDDPLCMITEYMENGDLNQFLsqreiestftHANNIPsvSIANLLYMAVqIASGMKYLASLNFVHRDLATRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 684 LLLDAQGFLKIADFGLCKEgIGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEM--LVGECPFPGDTE 758
Cdd:cd05097  160 CLVGNHYTIKIADFGMSRN-LYSGDyyRIQGRAVLPiRWMAWESILLGKFTTASDVWAFGVTLWEMftLCKEQPYSLLSD 238

                 ....*
gi 564339933 759 DEVFE 763
Cdd:cd05097  239 EQVIE 243
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
559-756 3.17e-06

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: 49.82  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTgkYYAIKALKKQEVLGRDEI-DSLYCEkriLETVGRTGHPFLLSLLA-CIQTSSHaCFVTEFL 636
Cdd:cd14159    1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSELDWSVVkNSFLTE---VEKLSRFRHPNIVDLAGySAQQGNY-CLIYVYL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIHEDV----FPEPQACFYLACVVLGLQFLHEKR--IIYRDLKLDNLLLDAQGFLKIADFGL---CKEGIGFG 707
Cdd:cd14159   75 PNGSLEDRLHCQVscpcLSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLarfSRRPKQPG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 708 D-----RTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGD 756
Cdd:cd14159  155 MsstlaRTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVD 208
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
548-753 3.27e-06

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 50.06  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 548 PQLQD-FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKaLKKQEVLGRDEIDSLY----C-EKRILETVGrtgHPFLLSLLA 621
Cdd:cd14041    2 PTLNDrYLLLHLLGRGGFSEVYKAFDLTEQRYVAVK-IHQLNKNWRDEKKENYhkhaCrEYRIHKELD---HPRIVKLYD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 622 CIQTSSHA-CFVTEFLPGGDLMMQIHE-DVFPEPQACFYLACVVLGLQFLHEKR--IIY---RDLKLDNLLLDAQGFLKI 694
Cdd:cd14041   78 YFSLDTDSfCTVLEYCEGNDLDFYLKQhKLMSEKEARSIIMQIVNALKYLNEIKppIIHydlKPGNILLVNGTACGEIKI 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 695 ADFGLCK-------EGIGFGDRTSTFCGTPEFLAPE--VLTQE--AYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14041  158 TDFGLSKimdddsyNSVDGMELTSQGAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFYQCLYGRKPF 227
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
662-795 3.45e-06

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 50.39  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 662 VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGI---GFGDRTSTFCGTpEFLAPEVLTQEAYTRAVDWWG 738
Cdd:cd05107  248 VANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMrdsNYISKGSTFLPL-KWMAPESIFNNLYTTLSDVWS 326
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 739 LGVLLYEML-VGECPFPGDTEDEVFECIVNAD--VPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05107  327 FGILLWEIFtLGGTPYPELPMNEQFYNAIKRGyrMAKPAHASDEIYEIMQKCWEEKFEIR 386
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
665-755 4.01e-06

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: 49.68  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 665 GLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEV-LTQEAYTRAVDWWGLGVLL 743
Cdd:cd07858  120 GLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDFMTEYVVTRWYRAPELlLNCSEYTTAIDVWSVGCIF 199
                         90
                 ....*....|..
gi 564339933 744 YEMLVGECPFPG 755
Cdd:cd07858  200 AELLGRKPLFPG 211
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
550-795 4.25e-06

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: 49.43  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLycekRILETVGRTGHPFL----------LSL 619
Cdd:cd14049    5 LNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVL----REVKVLAGLQHPNIvgyhtawmehVQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 620 LACIQT--------------SSHACF-VTEFLPGGDLMMQIHEDVFPEpqacfylacVVLGLQFLHEKRIIYRDLKLDNL 684
Cdd:cd14049   81 MLYIQMqlcelslwdwiverNKRPCEeEFKSAPYTPVDVDVTTKILQQ---------LLEGVTYIHSMGIVHRDLKPRNI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 685 LLDAQGF-LKIADFGL-CKEGIGFG------DRTSTF-----CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVgec 751
Cdd:cd14049  152 FLHGSDIhVRIGDFGLaCPDILQDGndsttmSRLNGLthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ--- 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 752 PFPGDTED-EVFECIVNADVPCPHFLSAQGL-ELIQKLLQKSPEKR 795
Cdd:cd14049  229 PFGTEMERaEVLTQLRNGQIPKSLCKRWPVQaKYIKLLTSTEPSER 274
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
550-814 4.44e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 49.29  E-value: 4.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDfrcLAVLGRGHFGKVLLVQYKGTGKYYAIKalkkqevlgrdeidslycekRILETVGRTGHPFLLSLLACIQTSSHA 629
Cdd:cd06616    8 LKD---LGEIGRGAFGTVNKMLHKPSGTIMAVK--------------------RIRSTVDEKEQKRLLMDLDVVMRSSDC 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 630 CFVTEF----LPGGD------LM--------MQIHE---DVFPEPQACFYLACVVLGLQFLHEK-RIIYRDLKLDNLLLD 687
Cdd:cd06616   65 PYIVKFygalFREGDcwicmeLMdisldkfyKYVYEvldSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 688 AQGFLKIADFGLCKEGIGFGDRTSTfCGTPEFLAPEVLT----QEAYTRAVDWWGLGVLLYEMLVGECPFPGdtEDEVFE 763
Cdd:cd06616  145 RNGNIKLCDFGISGQLVDSIAKTRD-AGCRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPK--WNSVFD 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 764 CI---VNADVP------CPHFlSAQGLELIQKLLQKSPEKRLGAGerdaeEIKVQPFFRT 814
Cdd:cd06616  222 QLtqvVKGDPPilsnseEREF-SPSFVNFVNLCLIKDESKRPKYK-----ELLKHPFIKM 275
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
559-755 4.69e-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: 48.93  E-value: 4.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGtgKYYAIKALKKQEVLGRDEIDsLYCEKRILETVGRTGHPFLLSLLACIqTSSHACFVTEFLPG 638
Cdd:cd14062    1 IGSGSFGTV----YKG--RWHGDVAVKKLNVTDPTPSQ-LQAFKNEVAVLRKTRHVNILLFMGYM-TKPQLAIVTQWCEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIH--EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC--KEGIGFGDRTSTFC 714
Cdd:cd14062   73 SSLYKHLHvlETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKTRWSGSQQFEQPT 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564339933 715 GTPEFLAPEVL---TQEAYTRAVDWWGLGVLLYEMLVGECPFPG 755
Cdd:cd14062  153 GSILWMAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPYSH 196
HR1_Ste20-like cd11627
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of ...
17-77 5.62e-06

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Schizosaccharomyces pombe Ste20-like proteins; This group is composed of predominantly uncharacterized fungal proteins, which contain two known domains: HR1 at the N-terminal region and REM (Ras exchanger motif) at the C-terminal region. One member protein from Schizosaccharomyces pombe is named Ste16 while its gene is called ste20 (a target of rapamycin complex 2 subunit). It is a subunit in the protein kinase TOR complexes in fission yeast. The REM domain is usually found in nucleotide exchange factors for Ras-like small GTPases. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212017 [Multi-domain]  Cd Length: 71  Bit Score: 44.67  E-value: 5.62e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933  17 PEDEKEMIRRAIQKELKIKEGMENMRRV-----ATDRRHL-GHVQQLLRASNRRLEQLHGELRELHA 77
Cdd:cd11627    3 SEQRLEELRGKLEIETKIKDGAENLLQVldsknAKEKKDQrARVESELNSSNRKIAQLTSQLEEEIQ 69
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
550-800 6.05e-06

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: 49.10  E-value: 6.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 550 LQDFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALK-KQEVLGRDEIdslyceKRILETVGRTGHPFLLSLLACIQTSSH 628
Cdd:cd14048    5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRlPNNELAREKV------LREVRALAKLDHPGIVRYFNAWLERPP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTE----FLPggdLMMQ----------IHEDVFPEPQACFYLACVVL----GLQFLHEKRIIYRDLKLDNLLLDAQG 690
Cdd:cd14048   79 EGWQEKmdevYLY---IQMQlcrkenlkdwMNRRCTMESRELFVCLNIFKqiasAVEYLHSKGLIHRDLKPSNVFFSLDD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 691 FLKIADFGLCKEgIGFGDRTSTF-------------CGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVgecPFP--- 754
Cdd:cd14048  156 VVKVGDFGLVTA-MDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIY---SFStqm 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339933 755 ------GDTEDEVFECIVNADVPCPHflsaqglELIQKLLQKSPEKRLGAGE 800
Cdd:cd14048  232 erirtlTDVRKLKFPALFTNKYPEER-------DMVQQMLSPSPSERPEAHE 276
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
632-795 6.84e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 49.79  E-value: 6.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRdlkldnllldaQGFLKIADFGLCkegigfgdR- 709
Cdd:NF033483  85 VMEYVDGRTLKDYIREHgPLSPEEAVEIMIQILSALEHAHRNGIVHRdikpqnilitkDGRVKVTDFGIA--------Ra 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 --------TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDT----------EDEVFECIVNADVP 771
Cdd:NF033483 157 lssttmtqTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSpvsvaykhvqEDPPPPSELNPGIP 236
                        170       180
                 ....*....|....*....|....*
gi 564339933 772 cphflsaQGLE-LIQKLLQKSPEKR 795
Cdd:NF033483 237 -------QSLDaVVLKATAKDPDDR 254
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
553-778 6.85e-06

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: 49.32  E-value: 6.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRiLETVGRTGHPFLLSLlACIQTSSHACFV 632
Cdd:cd14228   17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSR-LSSENADEYNFVRSY-ECFQHKNHTCLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLPGG--DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIY---RDLKLDNLLLDAQGF-LKIADFGLCKEGIGf 706
Cdd:cd14228   95 FEMLEQNlyDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHadlKPENIMLVDPVRQPYrVKVIDFGSASHVSK- 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 707 gDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE-DEVFECIVNADVPCPHFLSA 778
Cdd:cd14228  174 -AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEyDQIRYISQTQGLPAEYLLSA 245
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
559-765 6.96e-06

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: 48.52  E-value: 6.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGtgKYYAIKALKKQEVLGRDEiDSLYCEKRILETVGRTGHPFLLsLLACIQTSSHACFVTEFLPG 638
Cdd:cd14151   16 IGSGSFGTV----YKG--KWHGDVAVKMLNVTAPTP-QQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLMMQIH--EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC--KEGIGFGDRTSTFC 714
Cdd:cd14151   88 SSLYHHLHiiETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLS 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 715 GTPEFLAPEVLTQE---AYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECI 765
Cdd:cd14151  168 GSILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMV 222
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
662-769 7.21e-06

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: 48.64  E-value: 7.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 662 VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK-EGIGFGdrtsTFCGTPEFLAPEVLTQEaYTRAVDWWGLG 740
Cdd:cd13975  111 VVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFSGK-YDNSVDVYAFG 185
                         90       100
                 ....*....|....*....|....*....
gi 564339933 741 VLLYEMLVGECPFPgdtedEVFECIVNAD 769
Cdd:cd13975  186 ILFWYLCAGHVKLP-----EAFEQCASKD 209
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
636-793 7.62e-06

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: 49.26  E-value: 7.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 636 LPGGDLMMQIHEDVFPEpQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGigfgdrTSTFCG 715
Cdd:cd07876  107 LMDANLCQVIHMELDHE-RMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA------CTNFMM 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 716 TP-----EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPG-DTEDEVFECIVNADVPCPHFLSAQgLELIQKLLQ 789
Cdd:cd07876  180 TPyvvtrYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGtDHIDQWNKVIEQLGTPSAEFMNRL-QPTVRNYVE 258

                 ....
gi 564339933 790 KSPE 793
Cdd:cd07876  259 NRPQ 262
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
631-761 8.69e-06

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 48.71  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDlMMQIHEDVFPEPQA--CFYLAcVVLGLQFLHEKRIIYRDLKL---DNLLLDAQGFLKIADFGLCKEGIG 705
Cdd:cd13977  112 FVMEFCDGGD-MNEYLLSRRPDRQTntSFMLQ-LSSALAFLHRNQIVHRDLKPdniLISHKRGEPILKVADFGLSKVCSG 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 706 FGDRT-----------STFCGTPEFLAPEVLtQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEV 761
Cdd:cd13977  190 SGLNPeepanvnkhflSSACGSDFYMAPEVW-EGHYTAKADIFALGIIIWAMVERITFRDGETKKEL 255
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
665-792 8.88e-06

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: 48.94  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 665 GLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL---CKEGIGFGDRTST-FCGTPEFLAPEV-LTQEAYTRAVDWWGL 739
Cdd:cd07857  117 GLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLargFSENPGENAGFMTeYVATRWYRAPEImLSFQSYTKAIDVWSV 196
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 740 GVLLYEMLVGECPFPG-DTEDEVFECIVNADVPCPHFLSAQGLELIQKLLQKSP 792
Cdd:cd07857  197 GCILAELLGRKPVFKGkDYVDQLNQILQVLGTPDEETLSRIGSPKAQNYIRSLP 250
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
558-747 9.05e-06

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 48.42  E-value: 9.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYKGtgKYYAIKALKKqevlgRDEiDSLYCEKRILETVgRTGHPFLLSLLACIQTSSHAC----FVT 633
Cdd:cd14056    2 TIGKGRYGEVWLGKYRG--EKVAVKIFSS-----RDE-DSWFRETEIYQTV-MLRHENILGFIAADIKSTGSWtqlwLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDL--MMQIHEDVFPEPQACFYLACVvlGLQFLH-----EKR---IIYRDLKLDNLLLDAQGFLKIADFGLckeG 703
Cdd:cd14056   73 EYHEHGSLydYLQRNTLDTEEALRLAYSAAS--GLAHLHteivgTQGkpaIAHRDLKSKNILVKRDGTCCIADLGL---A 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 704 IGFGDRTSTF-------CGTPEFLAPEVLTQ-------EAYTRAvDWWGLGVLLYEML 747
Cdd:cd14056  148 VRYDSDTNTIdippnprVGTKRYMAPEVLDDsinpksfESFKMA-DIYSFGLVLWEIA 204
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
559-759 1.06e-05

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 47.90  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKalkkqevLGRDEIDSLYCEKRIlETVGRTGHPFLLSLLACIQTSSHACFVTEFLPG 638
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVK-------IYKNDVDQHKIVREI-SLLQKLSHPNIVRYLGICVKDEKLHPILEYVSG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 639 GDLM-MQIHEDVFPEPQACFYLAC-VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLK---IADFGLCKEGIGF----GDR 709
Cdd:cd14156   73 GCLEeLLAREELPLSWREKVELACdISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVGEMpandPER 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339933 710 TSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLvgeCPFPGDTED 759
Cdd:cd14156  153 KLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL---ARIPADPEV 199
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
631-753 1.08e-05

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: 48.18  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHEDVFPEPQAC-FYLACVVLGLQFLHEKR--IIYRDLKLDNLLLDA-QGFLKIADFGLCKEGigf 706
Cdd:cd14031   90 LVTELMTSGTLKTYLKRFKVMKPKVLrSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATLM--- 166
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339933 707 gdRTS---TFCGTPEFLAPEvLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14031  167 --RTSfakSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPY 213
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
552-761 1.20e-05

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 48.14  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVllvqYKGT----GKYYAIKALKK--QEVLGRDEIDSLYCEKRILETVGrtgHPFLLSLLA-CIQ 624
Cdd:cd05110    8 ELKRVKVLGSGAFGTV----YKGIwvpeGETVKIPVAIKilNETTGPKANVEFMDEALIMASMD---HPHLVRLLGvCLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHacFVTEFLPGGDLMMQIHE--DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKE 702
Cdd:cd05110   81 PTIQ--LVTQLMPHGCLLDYVHEhkDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933 703 GIGFGDRTSTFCGTP--EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEV 761
Cdd:cd05110  159 LEGDEKEYNADGGKMpiKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDGIPTREI 220
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
552-795 1.29e-05

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 48.10  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVllvqYKGT----GKY----YAIKALKkqevlgrdEIDSLYCEKRILE---TVGRTGHPFLLSLL 620
Cdd:cd05109    8 ELKKVKVLGSGAFGTV----YKGIwipdGENvkipVAIKVLR--------ENTSPKANKEILDeayVMAGVGSPYVCRLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 621 ACIQTSShACFVTEFLPGGDLMMQIHE--DVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG 698
Cdd:cd05109   76 GICLTST-VQLVTQLMPYGCLLDYVREnkDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 699 LC-------KEGIGFGDRTSTfcgtpEFLAPEVLTQEAYTRAVDWWGLGVLLYE-MLVGECPFPGDTEDEVFECIVNAD- 769
Cdd:cd05109  155 LArlldideTEYHADGGKVPI-----KWMALESILHRRFTHQSDVWSYGVTVWElMTFGAKPYDGIPAREIPDLLEKGEr 229
                        250       260
                 ....*....|....*....|....*.
gi 564339933 770 VPCPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd05109  230 LPQPPICTIDVYMIMVKCWMIDSECR 255
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
557-758 1.44e-05

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: 47.64  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 557 AVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYC--EKRILETVGrTGHPFLLSLLACIQTSSHACFVTE 634
Cdd:cd14102    6 SVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVplEIVLLKKVG-SGFRGVIKLLDWYERPDGFLIVME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 F-LPGGDLMMQIHED-VFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQ-GFLKIADFGlckEGIGFGDRTS 711
Cdd:cd14102   85 RpEPVKDLFDFITEKgALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRtGELKLIDFG---SGALLKDTVY 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564339933 712 T-FCGTPEFLAPEVLTQEAY-TRAVDWWGLGVLLYEMLVGECPFPGDTE 758
Cdd:cd14102  162 TdFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQDEE 210
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
552-795 1.45e-05

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: 47.71  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYcEKRILETVGRtgHPFLLSLLACIQTSSHACF 631
Cdd:cd14138    6 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALR-EVYAHAVLGQ--HSHVVRYYSAWAEDDHMLI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGGDLMMQIHED-----VFPEPQACFYLACVVLGLQFLHEKRI---------IYRDLKLDNLLLDAQGF------ 691
Cdd:cd14138   83 QNEYCNGGSLADAISENyrimsYFTEPELKDLLLQVARGLKYIHSMSLvhmdikpsnIFISRTSIPNAASEEGDedewas 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 692 ----LKIADFG----LCKEGIGFGDRtstfcgtpEFLAPEVLtQEAYT--RAVDWWGLGVLLYEMlVGECPFPgdTEDEV 761
Cdd:cd14138  163 nkviFKIGDLGhvtrVSSPQVEEGDS--------RFLANEVL-QENYThlPKADIFALALTVVCA-AGAEPLP--TNGDQ 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564339933 762 FECIVNADVP-CPHFLSAQGLELIQKLLQKSPEKR 795
Cdd:cd14138  231 WHEIRQGKLPrIPQVLSQEFLDLLKVMIHPDPERR 265
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
559-753 1.64e-05

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 47.72  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVllvqYKGtgKYYAIKALKKQEVLGR--DEIDSLYCEKRILEtvgRTGHPFLLsLLACIQTSSHACFVTEFL 636
Cdd:cd14149   20 IGSGSFGTV----YKG--KWHGDVAVKILKVVDPtpEQFQAFRNEVAVLR---KTRHVNIL-LFMGYMTKDNLAIVTQWC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 637 PGGDLMMQIH--EDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLC--KEGIGFGDRTST 712
Cdd:cd14149   90 EGSSLYKHLHvqETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQ 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564339933 713 FCGTPEFLAPEVLTQE---AYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14149  170 PTGSILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPY 213
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
559-800 1.73e-05

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk 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: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 47.58  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQ-YKGTGKYYAI-KALKKQ-EVLGRDEIDSLYCEKRILEtvgrtgHPFLLSLLA-CIQTSSHaCFVTE 634
Cdd:cd05042    3 IGNGWFGKVLLGEiYSGTSVAQVVvKELKASaNPKEQDTFLKEGQPYRILQ------HPNILQCLGqCVEAIPY-LLVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDL-----MMQIHEDVFPEPQACFYLAC-VVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLckegiGFGD 708
Cdd:cd05042   76 FCDLGDLkaylrSEREHERGDSDTRTLQRMACeVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGL-----AHSR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 709 RTSTFCGTPE-------FLAPEVLTQ-------EAYTRAVDWWGLGVLLYEML-VGECPFPGDTEDEVFECIV---NADV 770
Cdd:cd05042  151 YKEDYIETDDklwfplrWTAPELVTEfhdrllvVDQTKYSNIWSLGVTLWELFeNGAQPYSNLSDLDVLAQVVreqDTKL 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564339933 771 PCPHF---LSAQGLELIQkLLQKSPEKRLGAGE 800
Cdd:cd05042  231 PKPQLelpYSDRWYEVLQ-FCWLSPEQRPAAED 262
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
553-758 1.74e-05

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: 47.63  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQEVL---GRDEIDSLycekRILET-VGRTGHPFLLSLLACIQTSSH 628
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYfrqAMLEIAIL----TLLNTkYDPEDKHHIVRLLDHFMHHGH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 629 ACFVTEFLpGGDLMMQIHEDVF---PEPQACFYLACVVLGLQFLHEKRIIY-----------RDLKLDnllldaqgfLKI 694
Cdd:cd14212   77 LCIVFELL-GVNLYELLKQNQFrglSLQLIRKFLQQLLDALSVLKDARIIHcdlkpenillvNLDSPE---------IKL 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564339933 695 ADFG-LCkegigFGDRT------STFcgtpeFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTE 758
Cdd:cd14212  147 IDFGsAC-----FENYTlytyiqSRF-----YRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSE 207
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
559-698 1.80e-05

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 45.13  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSlycEKRILETVGRTG--HPFLLSllACIQTSSHAcFVTEFL 636
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLES---EMDILRRLKGLElnIPKVLV--TEDVDGPNI-LLMELV 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339933 637 PGGDLMMQIHEDVFPE--PQACFYLacVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFG 698
Cdd:cd13968   75 KGGTLIAYTQEEELDEkdVESIMYQ--LAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
556-772 2.53e-05

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


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 47.24  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRG--HFGKVLLVQYKGTGKYYAIKALKkQEVLGRDEIDSLYCEkriLETVGRTGHPFLLSLLACIQTSSHACFVT 633
Cdd:cd08227    3 LTVIGRGfeDLMTVNLARYKPTGEYVTVRRIN-LEACTNEMVTFLQGE---LHVSKLFNHPNIVPYRATFIADNELWVVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGG---DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRT 710
Cdd:cd08227   79 SFMAYGsakDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564339933 711 STFCGTPEF-------LAPEVLTQ--EAYTRAVDWWGLGVLLYEMLVGECPFPGDTEDEVFECIVNADVPC 772
Cdd:cd08227  159 RVVHDFPKYsvkvlpwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPC 229
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
558-751 2.75e-05

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 46.95  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 558 VLGRGHFGKVLLVQYkgTGKYYAIKALKKQEVLgrdeidSLYCEKRILETVGRTgHPFLLSLLACIQTSSHA----CFVT 633
Cdd:cd14140    2 IKARGRFGCVWKAQL--MNEYVAVKIFPIQDKQ------SWQSEREIFSTPGMK-HENLLQFIAAEKRGSNLemelWLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDLMMQIHEDVFPEPQACFYLACVVLGLQFLHEK-----------RIIYRDLKLDNLLLDAQGFLKIADFGLC-- 700
Cdd:cd14140   73 AFHDKGSLTDYLKGNIVSWNELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLTAVLADFGLAvr 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564339933 701 -KEGIGFGDrTSTFCGTPEFLAPEVL------TQEAYTRaVDWWGLGVLLYEmLVGEC 751
Cdd:cd14140  153 fEPGKPPGD-THGQVGTRRYMAPEVLegainfQRDSFLR-IDMYAMGLVLWE-LVSRC 207
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
559-812 6.12e-05

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: 46.00  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGKYYAIKALK--KQEVLGRdEIdslycekRILETVgrTGHPFLLSLLACIQT--SSHACFVTE 634
Cdd:cd14132   26 IGRGKYSEVFEGINIGNNEKVVIKVLKpvKKKKIKR-EI-------KILQNL--RGGPNIVKLLDVVKDpqSKTPSLIFE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 635 FLPGGDLmmqihEDVFP---EPQACFYLACVVLGLQFLHEKRIIYR----------DLKLDnllldaqgfLKIADFGLCK 701
Cdd:cd14132   96 YVNNTDF-----KTLYPtltDYDIRYYMYELLKALDYCHSKGIMHRdvkphnimidHEKRK---------LRLIDWGLAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 702 egigF---GDRTSTFCGTPEFLAPEVLTQ-EAYTRAVDWWGLGVLLYEMLVGECP-FPGDTEDEVFECIV---------- 766
Cdd:cd14132  162 ----FyhpGQEYNVRVASRYYKGPELLVDyQYYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVKIAkvlgtddlya 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339933 767 -------------NADVPC--------------PHFLSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFF 812
Cdd:cd14132  238 yldkygielpprlNDILGRhskkpwerfvnsenQHLVTPEALDLLDKLLRYDHQERI-----TAKEAMQHPYF 305
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
553-717 6.64e-05

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: 45.53  E-value: 6.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 553 FRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKqevlgRDEIDSLYCEKRILETVGrtGHPFLLSLLACIQTSSHACFV 632
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKK-----DSKHPQLEYEAKVYKLLQ--GGPGIPRLYWFGQEGDYNVMV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 633 TEFLpGGDLmmqihEDVFpepQAC---FYLACVVL-------GLQFLHEKRIIYRDlkldnllldaqgfLK--------- 693
Cdd:cd14016   75 MDLL-GPSL-----EDLF---NKCgrkFSLKTVLMladqmisRLEYLHSKGYIHRD-------------IKpenflmglg 132
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564339933 694 -------IADFGLCK--------EGIGFGDRTStFCGTP 717
Cdd:cd14016  133 knsnkvyLIDFGLAKkyrdprtgKHIPYREGKS-LTGTA 170
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
551-761 8.07e-05

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 45.33  E-value: 8.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 551 QDFRCLAVLGRGHFGKVllvqYKGT----GKYYAIKALKK--QEVLGRDEIDSLYCEkriLETVGRTGHPFLLSLLAcIQ 624
Cdd:cd05111    7 TELRKLKVLGSGVFGTV----HKGIwipeGDSIKIPVAIKviQDRSGRQSFQAVTDH---MLAIGSLDHAYIVRLLG-IC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 625 TSSHACFVTEFLPGGDLMMQI--HEDVFpEPQACF-YLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCK 701
Cdd:cd05111   79 PGASLQLVTQLLPLGSLLDHVrqHRGSL-GPQLLLnWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVAD 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339933 702 egIGFGDRTSTF---CGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEV 761
Cdd:cd05111  158 --LLYPDDKKYFyseAKTPiKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPYAGMRLAEV 220
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
559-796 1.24e-04

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: 45.03  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQYKGTGK-----YYAIKALKKQEVLGRDEIdslyceKRILETVGRTGHPFLLSLLACIQTSSHACFVT 633
Cdd:cd05093   13 LGEGAFGKVFLAECYNLCPeqdkiLVAVKTLKDASDNARKDF------HREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 634 EFLPGGDL-------------MMQIHEDV-FPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGL 699
Cdd:cd05093   87 EYMKHGDLnkflrahgpdavlMAEGNRPAeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 700 CKEgIGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV-GECPFPGDTEDEVFECIVNADV-PCPH 774
Cdd:cd05093  167 SRD-VYSTDyyRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlQRPR 245
                        250       260
                 ....*....|....*....|..
gi 564339933 775 FLSAQGLELIQKLLQKSPEKRL 796
Cdd:cd05093  246 TCPKEVYDLMLGCWQREPHMRL 267
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
631-753 1.33e-04

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 44.68  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 631 FVTEFLPGGDLMMQIHEDVFPEPQAC-FYLACVVLGLQFLHEKR--IIYRDLKLDNLLLDA-QGFLKIADFGLCKegIGF 706
Cdd:cd14032   81 LVTELMTSGTLKTYLKRFKVMKPKVLrSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLAT--LKR 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564339933 707 GDRTSTFCGTPEFLAPEvLTQEAYTRAVDWWGLGVLLYEMLVGECPF 753
Cdd:cd14032  159 ASFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPY 204
PHA03378 PHA03378
EBNA-3B; Provisional
461-549 1.71e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 461 PPCSSPSTVSPPKGCPSAAaceTSSSASPSNFRPVKTLPGEDMKPPPKPPRLYLQEPAPGTPCTKRPHMDPRTGVAPPLA 540
Cdd:PHA03378 716 RPAAATGRARPPAAAPGRA---RPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRG 792

                 ....*....
gi 564339933 541 ALSTRNPPQ 549
Cdd:PHA03378 793 APTPQPPPQ 801
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
613-755 1.75e-04

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: 44.57  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 613 HPFLLSLlacIQTSSHA-CFVTEFLPGGDL---MMQIHEDVFPEP---QACFYLAC-VVLGLQFLHEKRIIYRDLKLD-- 682
Cdd:cd14067   69 HPCIVYL---IGISIHPlCFALELAPLGSLntvLEENHKGSSFMPlghMLTFKIAYqIAAGLAYLHKKNIIFCDLKSDni 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 683 ---NLLLDAQGFLKIADFGLCKEGigFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPG 755
Cdd:cd14067  146 lvwSLDVQEHINIKLSDYGISRQS--FHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLG 219
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
556-812 1.89e-04

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 44.44  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 556 LAVLGRGHFGKVLLVQYKGTGKyyaIKALKKQEVLGRDE-IDSLYC-EKRILETVGRTGHPFLLSLLACIQTSSHACF-- 631
Cdd:cd07837    6 LEKIGEGTYGKVYKARDKNTGK---LVALKKTRLEMEEEgVPSTALrEVSLLQMLSQSIYIVRLLDVEHVEENGKPLLyl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPGG-----DLMMQIHEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLL-DAQGFLKIADFGLckeGIG 705
Cdd:cd07837   83 VFEYLDTDlkkfiDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVdKQKGLLKIADLGL---GRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 706 FGDRTSTFCG---TPEFLAPEVLTQEA-YTRAVDWWGLGVLLYEMLVGECPFPGDTE---------------DEVFECIV 766
Cdd:cd07837  160 FTIPIKSYTHeivTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFPGDSElqqllhifrllgtpnEEVWPGVS 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339933 767 N----------------ADVPCphfLSAQGLELIQKLLQKSPEKRLGAgeRDAEEikvQPFF 812
Cdd:cd07837  240 KlrdwheypqwkpqdlsRAVPD---LEPEGVDLLTKMLAYDPAKRISA--KAALQ---HPYF 293
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
552-835 1.96e-04

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: 44.34  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 552 DFRCLAVLGRGHFGKVLLVQYKGTGKYYAIKALKKQeVLGRDEidslyceKRILetvgrtghpflLSLLACIQTSShaCF 631
Cdd:cd06617    2 DLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRAT-VNSQEQ-------KRLL-----------MDLDISMRSVD--CP 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 632 VTEFLPG-----GDL-----MMQIHEDVF-----------PEPQACFYLACVVLGLQFLHEK-RIIYRDLKLDNLLLDAQ 689
Cdd:cd06617   61 YTVTFYGalfreGDVwicmeVMDTSLDKFykkvydkgltiPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 690 GFLKIADFGLCKEGIGFGDRTSTfCGTPEFLAPE----VLTQEAYTRAVDWWGLGVLLYEMLVGEcpFPGDTEDEVFECI 765
Cdd:cd06617  141 GQVKLCDFGISGYLVDSVAKTID-AGCKPYMAPErinpELNQKGYDVKSDVWSLGITMIELATGR--FPYDSWKTPFQQL 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339933 766 --VNADvPCPHF----LSAQGLELIQKLLQKSPEKRLgagerDAEEIKVQPFFRttnwQALLARTVQPPFVPTLCG 835
Cdd:cd06617  218 kqVVEE-PSPQLpaekFSPEFQDFVNKCLKKNYKERP-----NYPELLQHPFFE----LHLSKNTDVASFVSLILG 283
HR1_PKN2_2 cd11631
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
181-226 2.40e-04

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2; PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the second HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation.


Pssm-ID: 212021  Cd Length: 74  Bit Score: 40.45  E-value: 2.40e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 564339933 181 LQHRLRIEAAVAAGAKNVVKLLGGQRIQDRKALAEAQAQLQESSQK 226
Cdd:cd11631   14 LKKQLDIELKVKQGAENMIQMYSNGSSKDRKLLATAQQMLQDSKTK 59
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
559-763 2.57e-04

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 44.15  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 559 LGRGHFGKVLLVQY----------------KGTGKYYAIKALKKQEvlGRDEIDSLYCEKRILEtvgRTGHPFLLSLLAC 622
Cdd:cd05096   13 LGEGQFGEVHLCEVvnpqdlptlqfpfnvrKGRPLLVAVKILRPDA--NKNARNDFLKEVKILS---RLKDPNIIRLLGV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 623 IQTSSHACFVTEFLPGGDL-------------------MMQIHEDVFPEPQACFYLAC-VVLGLQFLHEKRIIYRDLKLD 682
Cdd:cd05096   88 CVDEDPLCMITEYMENGDLnqflsshhlddkeengndaVPPAHCLPAISYSSLLHVALqIASGMKYLSSLNFVHRDLATR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339933 683 NLLLDAQGFLKIADFGLCKEgIGFGD--RTSTFCGTP-EFLAPEVLTQEAYTRAVDWWGLGVLLYEMLV--GECPFPGDT 757
Cdd:cd05096  168 NCLVGENLTIKIADFGMSRN-LYAGDyyRIQGRAVLPiRWMAWECILMGKFTTASDVWAFGVTLWEILMlcKEQPYGELT 246

                 ....*.
gi 564339933 758 EDEVFE 763
Cdd:cd05096  247 DEQVIE 252
HR1_PKN1_3 cd11636
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
105-158 2.82e-04

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


Pssm-ID: 212026  Cd Length: 74  Bit Score: 39.96  E-value: 2.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339933 105 LEALHRQLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLR 158
Cdd:cd11636   11 IEELRHHFRVEHAVAEGAKNVLRLLGAGKAQDRKAISEAQSKLSESSQKLDLLR 64
HR1_PKN3_3 cd11637
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
103-161 1.50e-03

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3; PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the third HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC.


Pssm-ID: 212027  Cd Length: 74  Bit Score: 37.92  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339933 103 RLLEALHRqLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKI 161
Cdd:cd11637   10 RVEELRHH-LRIEAAVAEGAKNVVKLLGGRRFQDRKILAEAQARLQESSQKIDLLRLSL 67
HR1_PKN2_3 cd11635
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
105-161 1.66e-03

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2; PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the third HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation.


Pssm-ID: 212025  Cd Length: 74  Bit Score: 38.10  E-value: 1.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564339933 105 LEALHRQLEVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKI 161
Cdd:cd11635   11 MEELRHHFRIESAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSL 67
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH