NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|28467003|ref|NP_787062|]
View 

serine/threonine-protein kinase Kist isoform 1 [Homo sapiens]

Protein Classification

RNA-binding protein( domain architecture ID 10197111)

RNA-binding protein recognizes RNA via an RNA recognition motif (RRM); similar to Plasmodium falciparum clustered-asparagine-rich protein (CARP)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
22-308 0e+00

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 585.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  22 LWQVQSRLGSGSSASVYRVRCCGNPGSPPGALKQFLPPGTTGAAASaaEYGFRKERAALEQLQGHRNIVTLYGVFTIHFS 101
Cdd:cd14020   1 LWEVQSRLGQGSSASVYRVSSGRGADQPTSALKEFQLDHQGSQESG--DYGFAKERAALEQLQGHRNIVTLYGVFTNHYS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 PNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLS 181
Cdd:cd14020  79 ANVPSRCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDECFKLIDFGLS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 182 FKEGNQDVKYIQTDGYRAPEAELQNCLAQAGLQSDTECTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKANSSAIIDHI 261
Cdd:cd14020 159 FKEGNQDVKYIQTDGYRAPEAELQNCLAQAGLQSETECTSAVDLWSLGIVLLEMFSGMKLKHTVRSQEWKDNSSAIIDHI 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 28467003 262 FASKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFFSIPF 308
Cdd:cd14020 239 FASNAVVNPAIPAYHLRDLIKSMLHNDPGKRATAEAALCSPFFSIPF 285
RRM_SF super family cl17169
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
318-405 2.20e-51

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


The actual alignment was detected with superfamily member cd12465:

Pssm-ID: 473069 [Multi-domain]  Cd Length: 88  Bit Score: 167.44  E-value: 2.20e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 318 LPTPVLRLLNVLDDDYLENEEEYEDVVEDVKEECQKYGPVVSLLVPKENPGRGQVFVEYANAGDSKAAQKLLTGRMFDGK 397
Cdd:cd12465   1 LPTPVLRLLNVIDDSYLQSEEEYEDIVEDVREECQKYGPVVSLLIPKENPGKGQVFVEYANAGDSKAAQKMLTGRMFDGK 80

                ....*...
gi 28467003 398 FVVATFYP 405
Cdd:cd12465  81 FVVATFYP 88
 
Name Accession Description Interval E-value
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
22-308 0e+00

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 585.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  22 LWQVQSRLGSGSSASVYRVRCCGNPGSPPGALKQFLPPGTTGAAASaaEYGFRKERAALEQLQGHRNIVTLYGVFTIHFS 101
Cdd:cd14020   1 LWEVQSRLGQGSSASVYRVSSGRGADQPTSALKEFQLDHQGSQESG--DYGFAKERAALEQLQGHRNIVTLYGVFTNHYS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 PNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLS 181
Cdd:cd14020  79 ANVPSRCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDECFKLIDFGLS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 182 FKEGNQDVKYIQTDGYRAPEAELQNCLAQAGLQSDTECTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKANSSAIIDHI 261
Cdd:cd14020 159 FKEGNQDVKYIQTDGYRAPEAELQNCLAQAGLQSETECTSAVDLWSLGIVLLEMFSGMKLKHTVRSQEWKDNSSAIIDHI 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 28467003 262 FASKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFFSIPF 308
Cdd:cd14020 239 FASNAVVNPAIPAYHLRDLIKSMLHNDPGKRATAEAALCSPFFSIPF 285
RRM_UHMK1 cd12465
RNA recognition motif (RRM) found in U2AF homology motif kinase 1 (UHMK1) and similar proteins; ...
318-405 2.20e-51

RNA recognition motif (RRM) found in U2AF homology motif kinase 1 (UHMK1) and similar proteins; This subgroup corresponds to the RRM of UHMK1. UHMK1, also termed kinase interacting with stathmin (KIS) or P-CIP2, is a serine/threonine protein kinase functionally related to RNA metabolism and neurite outgrowth. It contains an N-terminal kinase domain and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), with high homology to the corresponding motif of the mammalian U2 small nuclear ribonucleoprotein auxiliary factor U2AF 65 kDa subunit (U2AF65 or U2AF2). UHMK1 targets two key regulators of cell proliferation and migration, the cyclin-dependent kinase (CDK) inhibitor p27Kip1 and the microtubule-destabilizing protein stathmin. It plays a critical role during vascular wound repair by preventing excessive vascular smooth muscle cell (VSMC) migration into the vascular lesion. Moreover, UHMK1 may control cell migration and neurite outgrowth by interacting with and phosphorylating the splicing factor SF1, thereby probably contributing to the control of protein expression. Furthermore, UHMK1 may be functionally related to microtubule dynamics and axon development. It localizes to RNA granules, interacts with three proteins found in RNA granules (KIF3A, NonO, and eEF1A), and further enhances the local translation. UHMK1 is highly expressed in regions of the brain implicated in schizophrenia and may play a role in susceptibility to schizophrenia.


Pssm-ID: 409898 [Multi-domain]  Cd Length: 88  Bit Score: 167.44  E-value: 2.20e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 318 LPTPVLRLLNVLDDDYLENEEEYEDVVEDVKEECQKYGPVVSLLVPKENPGRGQVFVEYANAGDSKAAQKLLTGRMFDGK 397
Cdd:cd12465   1 LPTPVLRLLNVIDDSYLQSEEEYEDIVEDVREECQKYGPVVSLLIPKENPGKGQVFVEYANAGDSKAAQKMLTGRMFDGK 80

                ....*...
gi 28467003 398 FVVATFYP 405
Cdd:cd12465  81 FVVATFYP 88
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
23-304 3.36e-41

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 146.52  E-value: 3.36e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003     23 WQVQSRLGSGSSASVYRVRCCGNpgsppG---ALKQFLPPGTTGAAASaaeygFRKERAALEQLQgHRNIVTLYGVFtiH 99
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKT-----GklvAIKVIKKKKIKKDRER-----ILREIKILKKLK-HPNIVRLYDVF--E 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    100 FSPNVpsrCLLLELLD-VSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDF 178
Cdd:smart00220  68 DEDKL---YLVMEYCEgGDLFDLL--KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHV-KLADF 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    179 GLS--FKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG----------MKLKHTVR 246
Cdd:smart00220 142 GLArqLDPGEKLTTFVGTPEYMAPE-----------VLLGKGYGKAVDIWSLGVILYELLTGkppfpgddqlLELFKKIG 210
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003    247 sqewKANSSAIIDHIFASKAvvnaaipayhLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:smart00220 211 ----KPKPPFPPPEWDISPE----------AKDLIRKLLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
19-298 1.77e-33

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 130.90  E-value: 1.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  19 FGRlWQVQSRLGSGSSASVYRVRCCGNpgSPPGALKQFLPPGTTGAAASAAeygFRKERAALEQLQgHRNIVTLYGVFTI 98
Cdd:COG0515   6 LGR-YRILRLLGRGGMGVVYLARDLRL--GRPVALKVLRPELAADPEARER---FRREARALARLN-HPNIVRVYDVGEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  99 HFSPnvpsrCLLLELLD-VSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLID 177
Cdd:COG0515  79 DGRP-----YLVMEYVEgESLADLL--RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRV-KLID 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 178 FGLSFKEGNQDVKY----IQTDGYRAPEaelqnclaQAglqSDTECTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKAn 253
Cdd:COG0515 151 FGIARALGGATLTQtgtvVGTPGYMAPE--------QA---RGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLR- 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 28467003 254 ssAIIDHIFASKAVVNAAIPAyHLRDLIKSMLHDDPSRRIP--AEMA 298
Cdd:COG0515 219 --AHLREPPPPPSELRPDLPP-ALDAIVLRALAKDPEERYQsaAELA 262
Pkinase pfam00069
Protein kinase domain;
23-304 1.27e-19

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 86.91  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    23 WQVQSRLGSGSSASVYRvrCCGNPGSPPGALKQFLPPGTTgaaaSAAEYGFRKERAALEQLQgHRNIVTLYGVFTIHfsp 102
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYK--AKHRDTGKIVAIKKIKKEKIK----KKKDKNILREIKILKKLN-HPNIVRLYDAFEDK--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   103 nvPSRCLLLELldVSVSELLLYSSHQGC-SMWMIQHCARDVLEALaflhhegyvhadlKPRNILWSaenecfklidfgls 181
Cdd:pfam00069  71 --DNLYLVLEY--VEGGSLFDLLSEKGAfSEREAKFIMKQILEGL-------------ESGSSLTT-------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   182 fkegnqdvkYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG-MKLKHTVRSQEWKANSSAIIDH 260
Cdd:pfam00069 120 ---------FVGTPWYMAPE-----------VLGGNPYGPKVDVWSLGCILYELLTGkPPFPGINGNEIYELIIDQPYAF 179
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 28467003   261 IFASKAVVNAAIpayhlrDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:pfam00069 180 PELPSNLSEEAK------DLLKKLLKKDPSKRLTATQALQHPWF 217
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
319-412 3.58e-16

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 80.32  E-value: 3.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   319 PTPVLRLLNVLDDDYLENEEEYEDVVEDVKEECQKYGPVVSLLVPKEN------PGRGQVFVEYANAGDSKAAQKLLTGR 392
Cdd:TIGR01642 408 PTKVVQLTNLVTGDDLMDDEEYEEIYEDVKTEFSKYGPLINIVIPRPNgdrnstPGVGKVFLEYADVRSAEKAMEGMNGR 487
                          90       100
                  ....*....|....*....|
gi 28467003   393 MFDGKFVVATFYPLSAYKRG 412
Cdd:TIGR01642 488 KFNDRVVVAAFYGEDCYKAG 507
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
21-304 1.32e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 75.07  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   21 RLWQVQSRLGSGSSASVYRVRCCGNpgSPPGALKQFLppgttgaaasaAEYGFRKERAALEQLQGHRNIVTLYGVF-TIH 99
Cdd:PTZ00036  66 KSYKLGNIIGNGSFGVVYEAICIDT--SEKVAIKKVL-----------QDPQYKNRELLIMKNLNHINIIFLKDYYyTEC 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  100 FSPNVPSRCL--LLELLDVSVSELLLYSS--HQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKL 175
Cdd:PTZ00036 133 FKKNEKNIFLnvVMEFIPQTVHKYMKHYArnNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLKL 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  176 IDFGlSFKE---GNQDVKYIQTDGYRAPEAELqnclaqaglqSDTECTSAVDLWSLGIILLEM------FSG-------- 238
Cdd:PTZ00036 213 CDFG-SAKNllaGQRSVSYICSRFYRAPELML----------GATNYTTHIDLWSLGCIIAEMilgypiFSGqssvdqlv 281
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003  239 --MKLKHTVRSQEWKANSSAIIDHIFAS------KAVVNAAIPAYHLrDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:PTZ00036 282 riIQVLGTPTEDQLKEMNPNYADIKFPDvkpkdlKKVFPKGTPDDAI-NFISQFLKYEPLKRLNPIEALADPFF 354
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
348-399 2.03e-06

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 44.92  E-value: 2.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28467003   348 KEECQKYGPVVSLLVPKENPG--RGQVFVEYANAGDSKAAQKLLTGRMFDGKFV 399
Cdd:pfam00076  16 KDLFSKFGPIKSIRLVRDETGrsKGFAFVEFEDEEDAEKAIEALNGKELGGREL 69
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
139-183 3.80e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 47.20  E-value: 3.80e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 28467003   139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENECFklIDFGLSFK 183
Cdd:TIGR03724  96 AREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVYL--IDFGLGKY 138
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
133-238 1.62e-05

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 47.10  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  133 WMIQhcardVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGlsfkegnqdvkyI----------QTDG------ 196
Cdd:NF033483 112 IMIQ-----ILSALEHAHRNGIVHRDIKPQNILIT-KDGRVKVTDFG------------IaralssttmtQTNSvlgtvh 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 28467003  197 YRAPEaelqnclaQA-GLQSDTEctsaVDLWSLGIILLEMFSG 238
Cdd:NF033483 174 YLSPE--------QArGGTVDAR----SDIYSLGIVLYEMLTG 204
 
Name Accession Description Interval E-value
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
22-308 0e+00

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 585.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  22 LWQVQSRLGSGSSASVYRVRCCGNPGSPPGALKQFLPPGTTGAAASaaEYGFRKERAALEQLQGHRNIVTLYGVFTIHFS 101
Cdd:cd14020   1 LWEVQSRLGQGSSASVYRVSSGRGADQPTSALKEFQLDHQGSQESG--DYGFAKERAALEQLQGHRNIVTLYGVFTNHYS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 PNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLS 181
Cdd:cd14020  79 ANVPSRCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDECFKLIDFGLS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 182 FKEGNQDVKYIQTDGYRAPEAELQNCLAQAGLQSDTECTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKANSSAIIDHI 261
Cdd:cd14020 159 FKEGNQDVKYIQTDGYRAPEAELQNCLAQAGLQSETECTSAVDLWSLGIVLLEMFSGMKLKHTVRSQEWKDNSSAIIDHI 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 28467003 262 FASKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFFSIPF 308
Cdd:cd14020 239 FASNAVVNPAIPAYHLRDLIKSMLHNDPGKRATAEAALCSPFFSIPF 285
RRM_UHMK1 cd12465
RNA recognition motif (RRM) found in U2AF homology motif kinase 1 (UHMK1) and similar proteins; ...
318-405 2.20e-51

RNA recognition motif (RRM) found in U2AF homology motif kinase 1 (UHMK1) and similar proteins; This subgroup corresponds to the RRM of UHMK1. UHMK1, also termed kinase interacting with stathmin (KIS) or P-CIP2, is a serine/threonine protein kinase functionally related to RNA metabolism and neurite outgrowth. It contains an N-terminal kinase domain and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), with high homology to the corresponding motif of the mammalian U2 small nuclear ribonucleoprotein auxiliary factor U2AF 65 kDa subunit (U2AF65 or U2AF2). UHMK1 targets two key regulators of cell proliferation and migration, the cyclin-dependent kinase (CDK) inhibitor p27Kip1 and the microtubule-destabilizing protein stathmin. It plays a critical role during vascular wound repair by preventing excessive vascular smooth muscle cell (VSMC) migration into the vascular lesion. Moreover, UHMK1 may control cell migration and neurite outgrowth by interacting with and phosphorylating the splicing factor SF1, thereby probably contributing to the control of protein expression. Furthermore, UHMK1 may be functionally related to microtubule dynamics and axon development. It localizes to RNA granules, interacts with three proteins found in RNA granules (KIF3A, NonO, and eEF1A), and further enhances the local translation. UHMK1 is highly expressed in regions of the brain implicated in schizophrenia and may play a role in susceptibility to schizophrenia.


Pssm-ID: 409898 [Multi-domain]  Cd Length: 88  Bit Score: 167.44  E-value: 2.20e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 318 LPTPVLRLLNVLDDDYLENEEEYEDVVEDVKEECQKYGPVVSLLVPKENPGRGQVFVEYANAGDSKAAQKLLTGRMFDGK 397
Cdd:cd12465   1 LPTPVLRLLNVIDDSYLQSEEEYEDIVEDVREECQKYGPVVSLLIPKENPGKGQVFVEYANAGDSKAAQKMLTGRMFDGK 80

                ....*...
gi 28467003 398 FVVATFYP 405
Cdd:cd12465  81 FVVATFYP 88
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
29-302 2.33e-41

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 145.49  E-value: 2.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCCGNpgSPPGALKQFLPPGTTGAAASaaeygFRKERAALEQLQgHRNIVTLYGVFTIHfspnvPSRC 108
Cdd:cd00180   1 LGKGSFGKVYKARDKET--GKKVAVKVIPKEKLKKLLEE-----LLREIEILKKLN-HPNIVKLYDVFETE-----NFLY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 109 LLLELLD-VSVSELLlYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENeCFKLIDFGLSFKEGNQ 187
Cdd:cd00180  68 LVMEYCEgGSLKDLL-KENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDG-TVKLADFGLAKDLDSD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 188 DVKYIQTDGYRAPEAelqnclAQAGLQSDTECTSAVDLWSLGIILLEMfsgmklkhtvrsqewkanssaiidhifaskav 267
Cdd:cd00180 146 DSLLKTTGGTTPPYY------APPELLGGRYYGPKVDIWSLGVILYEL-------------------------------- 187
                       250       260       270
                ....*....|....*....|....*....|....*
gi 28467003 268 vnaaipaYHLRDLIKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd00180 188 -------EELKDLIRRMLQYDPKKRPSAKELLEHL 215
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
23-304 3.36e-41

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 146.52  E-value: 3.36e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003     23 WQVQSRLGSGSSASVYRVRCCGNpgsppG---ALKQFLPPGTTGAAASaaeygFRKERAALEQLQgHRNIVTLYGVFtiH 99
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKT-----GklvAIKVIKKKKIKKDRER-----ILREIKILKKLK-HPNIVRLYDVF--E 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    100 FSPNVpsrCLLLELLD-VSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDF 178
Cdd:smart00220  68 DEDKL---YLVMEYCEgGDLFDLL--KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHV-KLADF 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    179 GLS--FKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG----------MKLKHTVR 246
Cdd:smart00220 142 GLArqLDPGEKLTTFVGTPEYMAPE-----------VLLGKGYGKAVDIWSLGVILYELLTGkppfpgddqlLELFKKIG 210
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003    247 sqewKANSSAIIDHIFASKAvvnaaipayhLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:smart00220 211 ----KPKPPFPPPEWDISPE----------AKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
24-304 1.42e-33

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: 125.81  E-value: 1.42e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRCCGNpgsppG---ALKQFLPPgttgaaASAAEYGFRkERAALEQL---QGHRNIVTLYGVFT 97
Cdd:cd05118   2 EVLRKIGEGAFGTVWLARDKVT-----GekvAIKKIKND------FRHPKAALR-EIKLLKHLndvEGHPNIVKLLDVFE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  98 IHFSPNVpsrCLLLELLDVSVSELL-LYSshQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLI 176
Cdd:cd05118  70 HRGGNHL---CLVFELMGMNLYELIkDYP--RGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLKLA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 177 DFGLSfKEGNQD--VKYIQTDGYRAPEAELQnclaqaglqsDTECTSAVDLWSLGIILLEMFSGMKLkhtvrsqeWKANS 254
Cdd:cd05118 145 DFGLA-RSFTSPpyTPYVATRWYRAPEVLLG----------AKPYGSSIDIWSLGCILAELLTGRPL--------FPGDS 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 28467003 255 SaiIDHIFASKAVvnaaIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd05118 206 E--VDQLAKIVRL----LGTPEALDLLSKMLKYDPAKRITASQALAHPYF 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
19-298 1.77e-33

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 130.90  E-value: 1.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  19 FGRlWQVQSRLGSGSSASVYRVRCCGNpgSPPGALKQFLPPGTTGAAASAAeygFRKERAALEQLQgHRNIVTLYGVFTI 98
Cdd:COG0515   6 LGR-YRILRLLGRGGMGVVYLARDLRL--GRPVALKVLRPELAADPEARER---FRREARALARLN-HPNIVRVYDVGEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  99 HFSPnvpsrCLLLELLD-VSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLID 177
Cdd:COG0515  79 DGRP-----YLVMEYVEgESLADLL--RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRV-KLID 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 178 FGLSFKEGNQDVKY----IQTDGYRAPEaelqnclaQAglqSDTECTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKAn 253
Cdd:COG0515 151 FGIARALGGATLTQtgtvVGTPGYMAPE--------QA---RGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLR- 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 28467003 254 ssAIIDHIFASKAVVNAAIPAyHLRDLIKSMLHDDPSRRIP--AEMA 298
Cdd:COG0515 219 --AHLREPPPPPSELRPDLPP-ALDAIVLRALAKDPEERYQsaAELA 262
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
86-304 8.33e-31

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: 118.91  E-value: 8.33e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTI--HFspnvpsrCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRN 163
Cdd:cd14133  60 KYHIVRLKDVFYFknHL-------CIVFELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPEN 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 164 ILWSAENEC-FKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqaGLQSDTectsAVDLWSLGIILLEMFSGMKLK 242
Cdd:cd14133 133 ILLASYSRCqIKIIDFGSSCFLTQRLYSYIQSRYYRAPEVIL-------GLPYDE----KIDMWSLGCILAELYTGEPLF 201
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28467003 243 HTVRSQEWKANSSAIIDhIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14133 202 PGASEVDQLARIIGTIG-IPPAHMLDQGKADDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
23-298 4.22e-30

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: 116.92  E-value: 4.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVRCCGNpgSPPGALKQFLPPGTTGAAASAAeygFRKERAALEQLQgHRNIVTLYGVFtihFSP 102
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLL--GRPVAIKVLRPELAEDEEFRER---FLREARALARLS-HPNIVRVYDVG---EDD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 103 NVPsrCLLLELLD-VSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLS 181
Cdd:cd14014  73 GRP--YIVMEYVEgGSLADLL--RERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRV-KLTDFGIA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 182 FKEG----NQDVKYIQTDGYRAPEaelqnclaQAglqSDTECTSAVDLWSLGIILLEMFSGmklKHTVRSQEWKANSSAI 257
Cdd:cd14014 148 RALGdsglTQTGSVLGTPAYMAPE--------QA---RGGPVDPRSDIYSLGVVLYELLTG---RPPFDGDSPAAVLAKH 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 28467003 258 IDHIFASKAVVNAAIPAyHLRDLIKSMLHDDPSRRIP--AEMA 298
Cdd:cd14014 214 LQEAPPPPSPLNPDVPP-ALDAIILRALAKDPEERPQsaAELL 255
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
80-304 5.65e-27

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: 109.56  E-value: 5.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  80 LEQLQ-----GHRNIVTLYGVFTI--HFspnvpsrCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14210  63 LKHLNdndpdDKHNIVRYKDSFIFrgHL-------CIVFELLSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKL 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAENE-CFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqaGLQSDTectsAVDLWSLGII 231
Cdd:cd14210 136 NIIHCDLKPENILLKQPSKsSIKVIDFGSSCFEGEKVYTYIQSRFYRAPEVIL-------GLPYDT----AIDMWSLGCI 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 232 LLEMFSGMKL---------------------KHTV----RSQE-----WKAN---SSAIIDHIFASK---AVVNAAIPay 275
Cdd:cd14210 205 LAELYTGYPLfpgeneeeqlacimevlgvppKSLIdkasRRKKffdsnGKPRpttNSKGKKRRPGSKslaQVLKCDDP-- 282
                       250       260
                ....*....|....*....|....*....
gi 28467003 276 HLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14210 283 SFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
23-303 1.76e-25

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: 104.10  E-value: 1.76e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVRccgNPGSppG---ALKQFLppgTTGAAASAAEYgFRKERAALEQLQgHRNIVTLYGVF--- 96
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAV---HKKT--GeeyAVKIID---KKKLKSEDEEM-LRREIEILKRLD-HPNIVKLYEVFedd 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  97 -TIHFspnVPSRCLLLELLDVSVSELLLysSHQGCSMWMIQhcardVLEALAFLHHEGYVHADLKPRNILWSAENECF-- 173
Cdd:cd05117  72 kNLYL---VMELCTGGELFDRIVKKGSF--SEREAAKIMKQ-----ILSAVAYLHSQGIVHRDLKPENILLASKDPDSpi 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 174 KLIDFGLS--FKEGNQDVKYIQTDGYRAPEaelqnCLAQAGLqsdtecTSAVDLWSLGIILLEMFSG---------MKLK 242
Cdd:cd05117 142 KIIDFGLAkiFEEGEKLKTVCGTPYYVAPE-----VLKGKGY------GKKCDIWSLGVILYILLCGyppfygeteQELF 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28467003 243 HTVRSQEWKANSSaIIDHIfaSKAVvnaaipayhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd05117 211 EKILKGKYSFDSP-EWKNV--SEEA----------KDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
135-304 1.53e-24

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: 101.53  E-value: 1.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLSfkEGNQDVKYIQ-----TDGYRAPEAeLQNCLA 209
Cdd:cd14019 103 IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGVLVDFGLA--QREEDRPEQRapragTRGFRAPEV-LFKCPH 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 210 QaglqsdtecTSAVDLWSLGIILLEMFSGmKLKHTVRSQEwkANSSAIIDHIFASKAVVnaaipayhlrDLIKSMLHDDP 289
Cdd:cd14019 180 Q---------TTAIDIWSAGVILLSILSG-RFPFFFSSDD--IDALAEIATIFGSDEAY----------DLLDKLLELDP 237
                       170
                ....*....|....*
gi 28467003 290 SRRIPAEMALCSPFF 304
Cdd:cd14019 238 SKRITAEEALKHPFF 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
73-304 1.59e-24

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: 101.86  E-value: 1.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfSPNVPSRCLLLELLDV-SVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHH 151
Cdd:cd14008  51 VRREIAIMKKLD-HPNIVRLYEVID---DPESDKLYLVLEYCEGgPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHE 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EGYVHADLKPRNILWSAENECfKLIDFGLS--FKEGNQDVKYIQ-TDGYRAPEAelqnCLAQAGLQSdtecTSAVDLWSL 228
Cdd:cd14008 127 NGIVHRDIKPENLLLTADGTV-KISDFGVSemFEDGNDTLQKTAgTPAFLAPEL----CDGDSKTYS----GKAADIWAL 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 229 GIILLEMF---------SGMKLKHTVRSQEWKANSSAIIDHifaskavvnaaipayHLRDLIKSMLHDDPSRRIPAEMAL 299
Cdd:cd14008 198 GVTLYCLVfgrlpfngdNILELYEAIQNQNDEFPIPPELSP---------------ELKDLLRRMLEKDPEKRITLKEIK 262

                ....*
gi 28467003 300 CSPFF 304
Cdd:cd14008 263 EHPWV 267
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
22-304 2.95e-24

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 100.74  E-value: 2.95e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  22 LWQVQSRLGSGSSASVYRVRCcgNPGSPPGALKQfLPPGTtgaAASAAEYgfRKERAALEQLQgHRNIVTLYGVFtihFS 101
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARH--KKTGQIVAIKK-INLES---KEKKESI--LNEIAILKKCK-HPNIVKYYGSY---LK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 PNVPSrcLLLELLDV-SVSELLLySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL 180
Cdd:cd05122  69 KDELW--IVMEFCSGgSLKDLLK-NTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGE-VKLIDFGL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 181 S--FKEGNQDVKYIQTDGYRAPEAELQnclaqaglqsdTECTSAVDLWSLGIILLEMFSG---------MK-LKHTVRSQ 248
Cdd:cd05122 145 SaqLSDGKTRNTFVGTPYWMAPEVIQG-----------KPYGFKADIWSLGITAIEMAEGkppyselppMKaLFLIATNG 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 249 ----EWKANSSAIidhifaskavvnaaipayhLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd05122 214 ppglRNPKKWSKE-------------------FKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
29-292 3.22e-24

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: 100.30  E-value: 3.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCCGNPGsppgALKQFLPPGTTGAAASAaeygFRKERAALEQLQgHRNIVTLYGVFTihfspNVPSRC 108
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTDV----AIKKLKVEDDNDELLKE----FRREVSILSKLR-HPNIVQFIGACL-----SPPPLC 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 109 LLLELLDV-SVSELLLYSSHQGcSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS-FKEGN 186
Cdd:cd13999  67 IVTEYMPGgSLYDLLHKKKIPL-SWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLD-ENFTVKIADFGLSrIKNST 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 187 QDVKYIQ--TDGYRAPEAelqnclaqagLQSDtECTSAVDLWSLGIILLEMFSGmklkhtvrsqEW---KANSSAIIDhi 261
Cdd:cd13999 145 TEKMTGVvgTPRWMAPEV----------LRGE-PYTEKADVYSFGIVLWELLTG----------EVpfkELSPIQIAA-- 201
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 28467003 262 faskAVVNA----AIPAY---HLRDLIKSMLHDDPSRR 292
Cdd:cd13999 202 ----AVVQKglrpPIPPDcppELSKLIKRCWNEDPEKR 235
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
75-292 3.94e-24

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: 101.61  E-value: 3.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQGHRNIVTLYGVF--TIHFSpnvpsrcLLLELLdvSVSELL-------LYSSHQGCSMWmiqhcaRDVLEA 145
Cdd:cd14092  47 REVQLLRLCQGHPNIVKLHEVFqdELHTY-------LVMELL--RGGELLerirkkkRFTESEASRIM------RQLVSA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 146 LAFLHHEGYVHADLKPRNILWSAENE--CFKLIDFGLS-FKEGNQDVKY-IQTDGYRAPEAelqncLAQAGlqSDTECTS 221
Cdd:cd14092 112 VSFMHSKGVVHRDLKPENLLFTDEDDdaEIKIVDFGFArLKPENQPLKTpCFTLPYAAPEV-----LKQAL--STQGYDE 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 222 AVDLWSLGIILLEMFSGMKLKHTvRSQEWkaNSSAIIDHI------FASKAVVNAAIPAyhlRDLIKSMLHDDPSRR 292
Cdd:cd14092 185 SCDLWSLGVILYTMLSGQVPFQS-PSRNE--SAAEIMKRIksgdfsFDGEEWKNVSSEA---KSLIQGLLTVDPSKR 255
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
86-304 8.38e-24

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: 100.27  E-value: 8.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIHfSPNVPSRCLLL--ELLDVSVSELLLYSSHQGCSMWMI-------QhcardVLEALAFLHHEGYVH 156
Cdd:cd14137  56 HPNIVKLKYFFYSS-GEKKDEVYLNLvmEYMPETLYRVIRHYSKNKQTIPIIyvklysyQ-----LFRGLAYLHSLGICH 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 157 ADLKPRNILWSAENECFKLIDFGlSFKE---GNQDVKYIQTDGYRAPEaelqnCLAQAglqsdTECTSAVDLWSLGIILL 233
Cdd:cd14137 130 RDIKPQNLLVDPETGVLKLCDFG-SAKRlvpGEPNVSYICSRYYRAPE-----LIFGA-----TDYTTAIDIWSAGCVLA 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 234 EM------FSGMK----LKHTV-------RSQ--EWKANSSAI-IDHIFA--SKAVVNAAIPAyHLRDLIKSMLHDDPSR 291
Cdd:cd14137 199 ELllgqplFPGESsvdqLVEIIkvlgtptREQikAMNPNYTEFkFPQIKPhpWEKVFPKRTPP-DAIDLLSKILVYNPSK 277
                       250
                ....*....|...
gi 28467003 292 RIPAEMALCSPFF 304
Cdd:cd14137 278 RLTALEALAHPFF 290
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
75-304 8.64e-24

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: 100.04  E-value: 8.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQ--GHRNIVTLYGVFTIHFSPNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd07838  47 REIALLKQLEsfEHPNVVRLLDVCHGPRTDRELKLTLVFEHVDQDLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSH 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQD--VKYIQTDGYRAPEAELQNCLAqaglqsdtectSAVDLWSLGI 230
Cdd:cd07838 127 RIVHRDLKPQNILVTSDGQ-VKLADFGLARIYSFEMalTSVVVTLWYRAPEVLLQSSYA-----------TPVDMWSVGC 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 231 ILLEMFS----------GMKLKHTVR------SQEWKANSSAIIDHiFAS------KAVVNAAIPAYHlrDLIKSMLHDD 288
Cdd:cd07838 195 IFAELFNrrplfrgsseADQLGKIFDviglpsEEEWPRNSALPRSS-FPSytprpfKSFVPEIDEEGL--DLLKKMLTFN 271
                       250
                ....*....|....*.
gi 28467003 289 PSRRIPAEMALCSPFF 304
Cdd:cd07838 272 PHKRISAFEALQHPYF 287
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
76-304 1.62e-23

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 98.36  E-value: 1.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQgHRNIVTLYgvFTIHFSPNVpsrCLLLELldVSVSELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHEGY 154
Cdd:cd05123  43 ERNILERVN-HPFIVKLH--YAFQTEEKL---YLVLDY--VPGGELFSHLSKEGRfPEERARFYAAEIVLALEYLHSLGI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNILWSAENECfKLIDFGLSfKEGNQDVKYIQTD----GYRAPEAelqnclaqagLQSdTECTSAVDLWSLGI 230
Cdd:cd05123 115 IYRDLKPENILLDSDGHI-KLTDFGLA-KELSSDGDRTYTFcgtpEYLAPEV----------LLG-KGYGKAVDWWSLGV 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 231 ILLEMFSGMKLkhtvrsqeWKANSSAIIDHIFASKAVVnaaIPAY---HLRDLIKSMLHDDPSRRI---PAEMALCSPFF 304
Cdd:cd05123 182 LLYEMLTGKPP--------FYAENRKEIYEKILKSPLK---FPEYvspEAKSLISGLLQKDPTKRLgsgGAEEIKAHPFF 250
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
24-304 2.89e-23

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: 98.71  E-value: 2.89e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRCcgNPGSPPGALKQFLppgttgaaASAAEYGF-----RkERAALEQLQgHRNIVTLYGVftI 98
Cdd:cd07829   2 EKLEKLGEGTYGVVYKAKD--KKTGEIVALKKIR--------LDNEEEGIpstalR-EISLLKELK-HPNIVKLLDV--I 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  99 HFSPNVpsrCLLLELLDVSVSELLlYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENeCFKLIDF 178
Cdd:cd07829  68 HTENKL---YLVFEYCDQDLKKYL-DKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDG-VLKLADF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 179 GLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEM------FSG----------- 238
Cdd:cd07829 143 GLARAFGIPLRTYtheVVTLWYRAPEI----------LLGSKHYSTAVDIWSVGCIFAELitgkplFPGdseidqlfkif 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 239 --------------MKLKH-TVRSQEWKANSSAIIDHIFASKAVvnaaipayhlrDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd07829 213 qilgtpteeswpgvTKLPDyKPTFPKWPKNDLEKVLPRLDPEGI-----------DLLSKMLQYNPAKRISAKEALKHPY 281

                .
gi 28467003 304 F 304
Cdd:cd07829 282 F 282
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
75-304 3.30e-23

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: 98.37  E-value: 3.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQGHRNIVTLYGVF----TIHFSpnvpsrcllLELLDVSVSELllYSSHQGCSM-------WMIQhcardVL 143
Cdd:cd07830  46 REVKSLRKLNEHPNIVKLKEVFrendELYFV---------FEYMEGNLYQL--MKDRKGKPFsesvirsIIYQ-----IL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 144 EALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDV--KYIQTDGYRAPEAELQnclaqaglqsDTECTS 221
Cdd:cd07830 110 QGLAHIHKHGFFHRDLKPENLLVS-GPEVVKIADFGLAREIRSRPPytDYVSTRWYRAPEILLR----------STSYSS 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 222 AVDLWSLGIILLEMFSG----------------MKLKHTVRSQEWK-----ANSSAI---------IDHIFASkaVVNAA 271
Cdd:cd07830 179 PVDIWALGCIMAELYTLrplfpgsseidqlykiCSVLGTPTKQDWPegyklASKLGFrfpqfaptsLHQLIPN--ASPEA 256
                       250       260       270
                ....*....|....*....|....*....|...
gi 28467003 272 IpayhlrDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07830 257 I------DLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
23-304 3.57e-23

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: 97.59  E-value: 3.57e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRvrcCGNPGSppG---ALKQFLPPGTTGAAASAaeygFRKERAALEQLQgHRNIVTLYGVftiH 99
Cdd:cd06606   2 WKKGELLGKGSFGSVYL---ALNLDT--GelmAVKEVELSGDSEEELEA----LEREIRILSSLK-HPNIVRYLGT---E 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 100 FSPNvpSRCLLLELldV---SVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLI 176
Cdd:cd06606  69 RTEN--TLNIFLEY--VpggSLASLL--KKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVV-KLA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 177 DFGLSFK-----EGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGmklKHTvrsqeW- 250
Cdd:cd06606 142 DFGCAKRlaeiaTGEGTKSLRGTPYWMAPE-----------VIRGEGYGRAADIWSLGCTVIEMATG---KPP-----Ws 202
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 251 -KANSSAIIDHIFASKAVVNaaIPAY---HLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd06606 203 eLGNPVAALFKIGSSGEPPP--IPEHlseEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
108-304 1.20e-22

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: 97.64  E-value: 1.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNIL------------------WSAE 169
Cdd:cd14134  90 CIVFELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlvdsdyvkvynpkkkrqiRVPK 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 170 NECFKLIDFG-LSFKEGNQ-DVkyIQTDGYRAPEAELqnclaqaGLQSDTECtsavDLWSLGIILLEMFSGMKLKHT--- 244
Cdd:cd14134 170 STDIKLIDFGsATFDDEYHsSI--VSTRHYRAPEVIL-------GLGWSYPC----DVWSIGCILVELYTGELLFQThdn 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 245 ------------------------VRSQE--------WKANSSAI--IDHIFASKAVVNAAIPAYH--LRDLIKSMLHDD 288
Cdd:cd14134 237 lehlammerilgplpkrmirrakkGAKYFyfyhgrldWPEGSSSGrsIKRVCKPLKRLMLLVDPEHrlLFDLIRKMLEYD 316
                       250
                ....*....|....*.
gi 28467003 289 PSRRIPAEMALCSPFF 304
Cdd:cd14134 317 PSKRITAKEALKHPFF 332
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
29-304 6.00e-22

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: 94.68  E-value: 6.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVrccgNPGSPPG----ALKQFLPPGTTGAAASAAEYgFRKERAALEQLQgHRNIVTLYGVFtIHFSPnv 104
Cdd:cd13994   1 IGKGATSVVRIV----TKKNPRSgvlyAVKEYRRRDDESKRKDYVKR-LTSEYIISSKLH-HPNIVKVLDLC-QDLHG-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 105 pSRCLLLELL---DVS--VSELLLYSSHQGCSMWmiqhcaRDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFG 179
Cdd:cd13994  72 -KWCLVMEYCpggDLFtlIEKADSLSLEEKDCFF------KQILRGVAYLHSHGIAHRDLKPENILLDEDGVL-KLTDFG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 180 LSFKEGN-QDVKYIQTDG------YRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGmklkhtvrSQEWKA 252
Cdd:cd13994 144 TAEVFGMpAEKESPMSAGlcgsepYMAPEV----------FTSGSYDGRAVDVWSCGIVLFALFTG--------RFPWRS 205
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28467003 253 NSSAiiDHIFAS-----KAVVNAAIPA-----YHLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd13994 206 AKKS--DSAYKAyeksgDFTNGPYEPIenllpSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
80-306 1.28e-21

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: 94.78  E-value: 1.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  80 LEQLQGHRNIVTLYGVfTIHFSPNVPSRCLLLELLDVSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADL 159
Cdd:cd07857  55 LRHFRGHKNITCLYDM-DIVFPGNFNELYLYEELMEADLHQII--RSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDL 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 160 KPRNILWSAeNECFKLIDFGLS------FKEGNQDVK-YIQTDGYRAPEAELqnclaqaglqSDTECTSAVDLWSLGIIL 232
Cdd:cd07857 132 KPGNLLVNA-DCELKICDFGLArgfsenPGENAGFMTeYVATRWYRAPEIML----------SFQSYTKAIDVWSVGCIL 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 233 LE------MFSGMKLKH---------------TVRsqewKANSSAIIDHIFASKAVVNAAIP-----AYHLR-DLIKSML 285
Cdd:cd07857 201 AEllgrkpVFKGKDYVDqlnqilqvlgtpdeeTLS----RIGSPKAQNYIRSLPNIPKKPFEsifpnANPLAlDLLEKLL 276
                       250       260
                ....*....|....*....|.
gi 28467003 286 HDDPSRRIPAEMALCSPFFSI 306
Cdd:cd07857 277 AFDPTKRISVEEALEHPYLAI 297
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
86-332 1.53e-21

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: 94.51  E-value: 1.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTihfsPNVPSRC----LLLELLDvsvSEL--LLYS----SHQGCSMWMIQhcardVLEALAFLHHEGYV 155
Cdd:cd07834  58 HENIIGLLDILR----PPSPEEFndvyIVTELME---TDLhkVIKSpqplTDDHIQYFLYQ-----ILRGLKYLHSAGVI 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 156 HADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKYIQTDG-----YRAPEAELqnclaqaglqSDTECTSAVDLWSLGI 230
Cdd:cd07834 126 HRDLKPSNILVNSNCD-LKICDFGLARGVDPDEDKGFLTEYvvtrwYRAPELLL----------SSKKYTKAIDIWSVGC 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 231 ILLEM------FSGM----KLKHTVR-----SQE---WKANSSAI--IDHIFASKAVVNAAIP--AYHL-RDLIKSMLHD 287
Cdd:cd07834 195 IFAELltrkplFPGRdyidQLNLIVEvlgtpSEEdlkFISSEKARnyLKSLPKKPKKPLSEVFpgASPEaIDLLEKMLVF 274
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 28467003 288 DPSRRIPAEMALCSPFFSIPFAPHIEdlvMLPTPVLRLLNVLDDD 332
Cdd:cd07834 275 NPKKRITADEALAHPYLAQLHDPEDE---PVAKPPFDFPFFDDEE 316
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
88-304 2.36e-21

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 94.31  E-value: 2.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  88 NIVTLYGVFTI--HFspnvpsrCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE--GYVHADLKPRN 163
Cdd:cd14226  76 YIVRLKRHFMFrnHL-------CLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPEN 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 164 ILW-SAENECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqaGLQSDTectsAVDLWSLGIILLEM------F 236
Cdd:cd14226 149 ILLcNPKRSAIKIIDFGSSCQLGQRIYQYIQSRFYRSPEVLL-------GLPYDL----AIDMWSLGCILVEMhtgeplF 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 237 SG-------MKL-----------------------KHTVRSQEWKANSSAIIDHIFASKAV-----VNAAIPAYH----- 276
Cdd:cd14226 218 SGanevdqmNKIvevlgmppvhmldqapkarkffeKLPDGTYYLKKTKDGKKYKPPGSRKLheilgVETGGPGGRragep 297
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 28467003 277 ---------LRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14226 298 ghtvedylkFKDLILRMLDYDPKTRITPAEALQHSFF 334
RRM3_U2AF65 cd12232
RNA recognition motif 3 (RRM3) found in U2 large nuclear ribonucleoprotein auxiliary factor ...
320-402 7.20e-21

RNA recognition motif 3 (RRM3) found in U2 large nuclear ribonucleoprotein auxiliary factor U2AF 65 kDa subunit (U2AF65) and similar proteins; This subfamily corresponds to the RRM3 of U2AF65 and dU2AF50. U2AF65, also termed U2AF2, is the large subunit of U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF), which has been implicated in the recruitment of U2 snRNP to pre-mRNAs and is a highly conserved heterodimer composed of large and small subunits. U2AF65 specifically recognizes the intron polypyrimidine tract upstream of the 3' splice site and promotes binding of U2 snRNP to the pre-mRNA branchpoint. U2AF65 also plays an important role in the nuclear export of mRNA. It facilitates the formation of a messenger ribonucleoprotein export complex, containing both the NXF1 receptor and the RNA substrate. Moreover, U2AF65 interacts directly and specifically with expanded CAG RNA, and serves as an adaptor to link expanded CAG RNA to NXF1 for RNA export. U2AF65 contains an N-terminal RS domain rich in arginine and serine, followed by a proline-rich segment and three C-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The N-terminal RS domain stabilizes the interaction of U2 snRNP with the branch point (BP) by contacting the branch region, and further promotes base pair interactions between U2 snRNA and the BP. The proline-rich segment mediates protein-protein interactions with the RRM domain of the small U2AF subunit (U2AF35 or U2AF1). The RRM1 and RRM2 are sufficient for specific RNA binding, while RRM3 is responsible for protein-protein interactions. The family also includes Splicing factor U2AF 50 kDa subunit (dU2AF50), the Drosophila ortholog of U2AF65. dU2AF50 functions as an essential pre-mRNA splicing factor in flies. It associates with intronless mRNAs and plays a significant and unexpected role in the nuclear export of a large number of intronless mRNAs.


Pssm-ID: 409679 [Multi-domain]  Cd Length: 89  Bit Score: 86.49  E-value: 7.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 320 TPVLRLLNVLDDDYLENEEEYEDVVEDVKEECQKYGPVVSLLVPK------ENPGRGQVFVEYANAGDSKAAQKLLTGRM 393
Cdd:cd12232   1 SRVLCLLNMVTPEELEDDEEYEEILEDVKEECSKYGKVLSVVIPRpeaegvDVPGVGKVFVEFEDVEDAQKAQKALAGRK 80

                ....*....
gi 28467003 394 FDGKFVVAT 402
Cdd:cd12232  81 FDGRTVVAS 89
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
24-304 7.79e-21

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: 91.86  E-value: 7.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRCcGNPGSPPgALKQFLppgttgaaASAAEYGF-----RkERAALEQLQgHRNIVTLYGVFTI 98
Cdd:cd07840   2 EKIAQIGEGTYGQVYKARN-KKTGELV-ALKKIR--------MENEKEGFpitaiR-EIKLLQKLD-HPNVVRLKEIVTS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  99 HFSPNVPSRC-LLLELLDVSVSELLLYSSHQgCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLID 177
Cdd:cd07840  70 KGSAKYKGSIyMVFEYMDHDLTGLLDNPEVK-FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGV-LKLAD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 178 FGLS-FKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG--------------- 238
Cdd:cd07840 148 FGLArPYTKENNADYtnrVITLWYRPPEL----------LLGATRYGPEVDMWSVGCILAELFTGkpifqgkteleqlek 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 239 ------------------MKLKHTVRSQEWKANssaIIDHIFASKavvnaaIPAYHLrDLIKSMLHDDPSRRIPAEMALC 300
Cdd:cd07840 218 ifelcgspteenwpgvsdLPWFENLKPKKPYKR---RLREVFKNV------IDPSAL-DLLDKLLTLDPKKRISADQALQ 287

                ....
gi 28467003 301 SPFF 304
Cdd:cd07840 288 HEYF 291
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
29-303 1.11e-20

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: 91.12  E-value: 1.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRccgNPGSPPGALKQFlppGTTGAAASAAEyGFRKERAALEQLQGHRNIVTLYGvFTIHFSPNVPSrc 108
Cdd:cd14131   9 LGKGGSSKVYKVL---NPKKKIYALKRV---DLEGADEQTLQ-SYKNEIELLKKLKGSDRIIQLYD-YEVTDEDDYLY-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 109 LLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILwSAENEcFKLIDFGLSfkegnqd 188
Cdd:cd14131  79 MVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFL-LVKGR-LKLIDFGIA------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 189 vKYIQTD-------------GYRAPEAeLQNCLAQAGLQSDTECTSAVDLWSLGIILLEMFSGmklkHTVRSQEWKANS- 254
Cdd:cd14131 150 -KAIQNDttsivrdsqvgtlNYMSPEA-IKDTSASGEGKPKSKIGRPSDVWSLGCILYQMVYG----KTPFQHITNPIAk 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 28467003 255 -SAIID--HIFASKAVVNAAipayhLRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14131 224 lQAIIDpnHEIEFPDIPNPD-----LIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
74-304 1.36e-20

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: 90.88  E-value: 1.36e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQGHRNIVTLYGVF-TIHFSPNVPSRCLLLELLDVSVSELLLysSHQGCSMWMiqhcaRDVLEALAFLHHE 152
Cdd:cd14093  56 RREIEILRQVSGHPNIIELHDVFeSPTFIFLVFELCRKGELFDYLTEVVTL--SEKKTRRIM-----RQLFEAVEFLHSL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSaENECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSDTECTSA-----VDL 225
Cdd:cd14093 129 NIVHRDLKPENILLD-DNLNVKISDFGFAtrLDEGEKLRELCGTPGYLAPEV----------LKCSMYDNAPgygkeVDM 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 226 WSLGIILLEMFSG----------------MKLKHTVRSQEWKANSSAIidhifaskavvnaaipayhlRDLIKSMLHDDP 289
Cdd:cd14093 198 WACGVIMYTLLAGcppfwhrkqmvmlrniMEGKYEFGSPEWDDISDTA--------------------KDLISKLLVVDP 257
                       250
                ....*....|....*
gi 28467003 290 SRRIPAEMALCSPFF 304
Cdd:cd14093 258 KKRLTAEEALEHPFF 272
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
108-241 1.81e-20

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 91.69  E-value: 1.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEC-FKLIDFGLSFKEGN 186
Cdd:cd14225 121 CITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSsIKVIDFGSSCYEHQ 200
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 187 QDVKYIQTDGYRAPEAELqnclaqaGLQSDTectsAVDLWSLGIILLEMFSGMKL 241
Cdd:cd14225 201 RVYTYIQSRFYRSPEVIL-------GLPYSM----AIDMWSLGCILAELYTGYPL 244
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
24-302 2.04e-20

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: 89.75  E-value: 2.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRV--RCCGNPGSPPGALKQFlppgttgaaasaaeYGFrKERA-------ALEQLQGHRNIVTLY- 93
Cdd:cd13997   3 HELEQIGSGSFSEVFKVrsKVDGCLYAVKKSKKPF--------------RGP-KERAralreveAHAALGQHPNIVRYYs 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  94 -----GVFTIHFSP-NVPSRCLLLELL--DVSVSELLLysshqgcsmWMIqhcARDVLEALAFLHHEGYVHADLKPRNIL 165
Cdd:cd13997  68 sweegGHLYIQMELcENGSLQDALEELspISKLSEAEV---------WDL---LLQVALGLAFIHSKGIVHLDIKPDNIF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 166 WSAENECfKLIDFGLS--------FKEGNQdvkyiqtdGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd13997 136 ISNKGTC-KIGDFGLAtrletsgdVEEGDS--------RYLAPEL----------LNENYTHLPKADIFSLGVTVYEAAT 196
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 238 GMKLKHTvrSQEWKANSSAIIdhIFASKAVVNAAipayhLRDLIKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd13997 197 GEPLPRN--GQQWQQLRQGKL--PLPPGLVLSQE-----LTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
80-305 2.99e-20

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: 90.32  E-value: 2.99e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  80 LEQLQgHRNIVTLYGVFTiHFSpNVpsrCLLLELL--DVSV----SELLLYSSHQGCSMWMIqhcardvLEALAFLHHEG 153
Cdd:cd07841  56 LQELK-HPNIIGLLDVFG-HKS-NI---NLVFEFMetDLEKvikdKSIVLTPADIKSYMLMT-------LRGLEYLHSNW 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGI 230
Cdd:cd07841 123 ILHRDLKPNNLLIASDGVL-KLADFGLARSFGSPNRKMthqVVTRWYRAPEL----------LFGARHYGVGVDMWSVGC 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 231 ILLEM------FSGM----KLKHTVR------SQEWKANSS-----------AI-IDHIFasKAVVNAAIpayhlrDLIK 282
Cdd:cd07841 192 IFAELllrvpfLPGDsdidQLGKIFEalgtptEENWPGVTSlpdyvefkpfpPTpLKQIF--PAASDDAL------DLLQ 263
                       250       260
                ....*....|....*....|...
gi 28467003 283 SMLHDDPSRRIPAEMALCSPFFS 305
Cdd:cd07841 264 RLLTLNPNKRITARQALEHPYFS 286
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
73-305 6.79e-20

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 89.92  E-value: 6.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRkERAALEQLQGHRNIVTLYGVftiHFSPNVPSRCLLLELLDVSVSEL----LLYSSHqgcsmwmIQHCARDVLEALAF 148
Cdd:cd07852  54 FR-EIMFLQELNDHPNIIKLLNV---IRAENDKDIYLVFEYMETDLHAViranILEDIH-------KQYIMYQLLKALKY 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAenECF-KLIDFGL--SFKEGNQDVK------YIQTDGYRAPEAelqnclaqagLQSDTEC 219
Cdd:cd07852 123 LHSGGVIHRDLKPSNILLNS--DCRvKLADFGLarSLSQLEEDDEnpvltdYVATRWYRAPEI----------LLGSTRY 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 220 TSAVDLWSLGIILLEMFSGMKLkhtvrsqewKANSSAI--IDHI------------------FASKAVVNAAIP---AYH 276
Cdd:cd07852 191 TKGVDMWSVGCILGEMLLGKPL---------FPGTSTLnqLEKIievigrpsaediesiqspFAATMLESLPPSrpkSLD 261
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 28467003 277 LR---------DLIKSMLHDDPSRRIPAEMALCSPFFS 305
Cdd:cd07852 262 ELfpkaspdalDLLKKLLVFNPNKRLTAEEALRHPYVA 299
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
79-304 7.30e-20

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: 88.87  E-value: 7.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  79 ALEQLQGHRNIVTLYGVftiHFSPNVPSRCLLLELLDVSVSELL----LYSSHQGCSMWMIQhcardVLEALAFLHHEGY 154
Cdd:cd07831  50 ALRRLSPHPNILRLIEV---LFDRKTGRLALVFELMDMNLYELIkgrkRPLPEKRVKNYMYQ-----LLKSLDHMHRNGI 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNILwsAENECFKLIDFG--------LSFKEgnqdvkYIQTDGYRAPEaelqnCLAQAGLQSdtectSAVDLW 226
Cdd:cd07831 122 FHRDIKPENIL--IKDDILKLADFGscrgiyskPPYTE------YISTRWYRAPE-----CLLTDGYYG-----PKMDIW 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 227 SLGIILLEM------FSG------MKLKHTV-----RSQEWKANSSAIIDHIFASKA-------VVNAAIPAyhlRDLIK 282
Cdd:cd07831 184 AVGCVFFEIlslfplFPGtneldqIAKIHDVlgtpdAEVLKKFRKSRHMNYNFPSKKgtglrklLPNASAEG---LDLLK 260
                       250       260
                ....*....|....*....|..
gi 28467003 283 SMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07831 261 KLLAYDPDERITAKQALRHPYF 282
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
84-241 1.13e-19

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: 89.23  E-value: 1.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  84 QGHRNIVTLYGVFTIHfspnvPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRN 163
Cdd:cd14212  59 EDKHHIVRLLDHFMHH-----GHLCIVFELLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPEN 133
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 164 ILWSAENEC-FKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqaGLQSDTectsAVDLWSLGIILLEMFSGMKL 241
Cdd:cd14212 134 ILLVNLDSPeIKLIDFGSACFENYTLYTYIQSRFYRSPEVLL-------GLPYST----AIDMWSLGCIAAELFLGLPL 201
Pkinase pfam00069
Protein kinase domain;
23-304 1.27e-19

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 86.91  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    23 WQVQSRLGSGSSASVYRvrCCGNPGSPPGALKQFLPPGTTgaaaSAAEYGFRKERAALEQLQgHRNIVTLYGVFTIHfsp 102
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYK--AKHRDTGKIVAIKKIKKEKIK----KKKDKNILREIKILKKLN-HPNIVRLYDAFEDK--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   103 nvPSRCLLLELldVSVSELLLYSSHQGC-SMWMIQHCARDVLEALaflhhegyvhadlKPRNILWSaenecfklidfgls 181
Cdd:pfam00069  71 --DNLYLVLEY--VEGGSLFDLLSEKGAfSEREAKFIMKQILEGL-------------ESGSSLTT-------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   182 fkegnqdvkYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG-MKLKHTVRSQEWKANSSAIIDH 260
Cdd:pfam00069 120 ---------FVGTPWYMAPE-----------VLGGNPYGPKVDVWSLGCILYELLTGkPPFPGINGNEIYELIIDQPYAF 179
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 28467003   261 IFASKAVVNAAIpayhlrDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:pfam00069 180 PELPSNLSEEAK------DLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
139-302 1.88e-19

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: 87.45  E-value: 1.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENE--CFKLIDFGLSFKEGNQDV--KYIQTDGYRAPEAelqncLAQAGlq 214
Cdd:cd14084 117 FYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEecLIKITDFGLSKILGETSLmkTLCGTPTYLAPEV-----LRSFG-- 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 sDTECTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKANSSAIIDHIFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIP 294
Cdd:cd14084 190 -TEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEQILSGKYTFIPKAWKNVSEEA---KDLVKKMLVVDPSRRPS 265

                ....*...
gi 28467003 295 AEMALCSP 302
Cdd:cd14084 266 IEEALEHP 273
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
74-293 2.16e-19

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: 88.00  E-value: 2.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQGHRNIVTLYGVFTIHFSPNvpsrcLLLELLDVSvsELL-LYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14180  48 QREVAALRLCQSHPNIVALHEVLHDQYHTY-----LVMELLRGG--ELLdRIKKKARFSESEASQLMRSLVSAVSFMHEA 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAENE--CFKLIDFGLS--FKEGNQDVKY-IQTDGYRAPEaelqnCLAQAGLqsDTECtsavDLWS 227
Cdd:cd14180 121 GVVHRDLKPENILYADESDgaVLKVIDFGFArlRPQGSRPLQTpCFTLQYAAPE-----LFSNQGY--DESC----DLWS 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28467003 228 LGIILLEMFSGMKLKHTVRSQEWKANSSAIIDHI------FASKAVVNAAIPAyhlRDLIKSMLHDDPSRRI 293
Cdd:cd14180 190 LGVILYTMLSGQVPFQSKRGKMFHNHAADIMHKIkegdfsLEGEAWKGVSEEA---KDLVRGLLTVDPAKRL 258
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
75-304 2.99e-19

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: 87.38  E-value: 2.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQGHRNIVTLYGVFtihfspNVPSRC-LLLELLDVSVSELLlYSSHQGCSMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd07832  48 REIKALQACQGHPYVVKLRDVF------PHGTGFvLVFEYMLSSLSEVL-RDEERPLTEAQVKRYMRMLLKGVAYMHANR 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWSAeNECFKLIDFGLS--FKEGNQDVKYIQ--TDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLG 229
Cdd:cd07832 121 IMHRDLKPANLLISS-TGVLKIADFGLArlFSEEDPRLYSHQvaTRWYRAPEL----------LYGSRKYDEGVDLWAVG 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 230 IILLEMFSGMKL--------------KH--TVRSQEWKANSSaIIDhifASKaVVNAAIPAYHLR-----------DLIK 282
Cdd:cd07832 190 CIFAELLNGSPLfpgendieqlaivlRTlgTPNEKTWPELTS-LPD---YNK-ITFPESKGIRLEeifpdcspeaiDLLK 264
                       250       260
                ....*....|....*....|..
gi 28467003 283 SMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07832 265 GLLVYNPKKRLSAEEALRHPYF 286
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
73-237 3.21e-19

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: 86.45  E-value: 3.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003     73 FRKERAALEQLQgHRNIVTLYGVFTIhfspnVPSRCLLLELLDV-SVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHH 151
Cdd:smart00221  48 FLREARIMRKLD-HPNIVKLLGVCTE-----EEPLMIVMEYMPGgDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLES 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    152 EGYVHADLKPRNILWSAENECfKLIDFGLSfKEGNQDVKYIQTDG---YR--APEAeLQNClaqaglqsdtECTSAVDLW 226
Cdd:smart00221 122 KNFIHRDLAARNCLVGENLVV-KISDFGLS-RDLYDDDYYKVKGGklpIRwmAPES-LKEG----------KFTSKSDVW 188
                          170
                   ....*....|.
gi 28467003    227 SLGIILLEMFS 237
Cdd:smart00221 189 SFGVLLWEIFT 199
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
23-303 3.57e-19

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: 86.76  E-value: 3.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRvrCCGNPGSPPGALKQF------LPPGTTGaaasaaeyGFRKERAALEQLQgHRNIVTLYGVF 96
Cdd:cd14098   2 YQIIDRLGSGTFAEVKK--AVEVETGKMRAIKQIvkrkvaGNDKNLQ--------LFQREINILKSLE-HPGIVRLIDWY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  97 TihfspNVPSRCLLLELldVSVSELLLYSSHQGCsmwmI--QHCA---RDVLEALAFLHHEGYVHADLKPRNILWSAENE 171
Cdd:cd14098  71 E-----DDQHIYLVMEY--VEGGDLMDFIMAWGA----IpeQHAReltKQILEAMAYTHSMGITHRDLKPENILITQDDP 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 172 CF-KLIDFGLSFKEGNQD--VKYIQTDGYRAPEAelqncLAQAGLQSDTECTSAVDLWSLGIILLEMFSGmKLKHTVRSQ 248
Cdd:cd14098 140 VIvKISDFGLAKVIHTGTflVTFCGTMAYLAPEI-----LMSKEQNLQGGYSNLVDMWSVGCLVYVMLTG-ALPFDGSSQ 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 249 EwkanssAIIDHI----FASKAVVNAAIpAYHLRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14098 214 L------PVEKRIrkgrYTQPPLVDFNI-SEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
76-293 9.33e-19

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: 85.73  E-value: 9.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLqGHRNIVTLYgvFTIHFSpnvpsRCL--LLELLdvSVSELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHE 152
Cdd:cd05581  51 EKEVLSRL-AHPGIVKLY--YTFQDE-----SKLyfVLEYA--PNGDLLEYIRKYGSlDEKCTRFYTAEIVLALEYLHSK 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQnclAQAG------------LQSDTECT 220
Cdd:cd05581 121 GIIHRDLKPENILLD-EDMHIKITDFGTAKVLGPDSSPESTKGDADSQIAYNQ---ARAAsfvgtaeyvspeLLNEKPAG 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 221 SAVDLWSLGIILLEMFSGmklKHTVR-SQEWkanssaiidHIFasKAVVNAA------IPAyHLRDLIKSMLHDDPSRRI 293
Cdd:cd05581 197 KSSDLWALGCIIYQMLTG---KPPFRgSNEY---------LTF--QKIVKLEyefpenFPP-DAKDLIQKLLVLDPSKRL 261
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
24-303 1.09e-18

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: 85.34  E-value: 1.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRccGNPGSPPGALKQFLPPGTTGaaasaaeygFRKE-RAALEQLQ--GHRNIVTLYGVFtihF 100
Cdd:cd06623   4 ERVKVLGQGSSGVVYKVR--HKPTGKIYALKKIHVDGDEE---------FRKQlLRELKTLRscESPYVVKCYGAF---Y 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 101 SPNvpSRCLLLELLDV-SVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGY-VHADLKPRNILWSAENEcFKLIDF 178
Cdd:cd06623  70 KEG--EISIVLEYMDGgSLADLL--KKVGKIPEPVLAYIARQILKGLDYLHTKRHiIHRDIKPSNLLINSKGE-VKIADF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 179 GLS-FKEGNQDVK--YIQTDGYRAPEAelqnclaqagLQSDTECTSAvDLWSLGIILLEMFSGmklKHTVRSQEwKANSS 255
Cdd:cd06623 145 GISkVLENTLDQCntFVGTVTYMSPER----------IQGESYSYAA-DIWSLGLTLLECALG---KFPFLPPG-QPSFF 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 28467003 256 AIIDHI--FASKAVVNAAIPAyHLRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd06623 210 ELMQAIcdGPPPSLPAEEFSP-EFRDFISACLQKDPKKRPSAAELLQHPF 258
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
74-304 1.26e-18

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: 85.41  E-value: 1.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQGHRNIVTLYGVF-TIHFSPNVPSRCLLLELLDVSVSELLLYSSHQGCSMwmiqhcaRDVLEALAFLHHE 152
Cdd:cd14181  63 LKEIHILRQVSGHPSIITLIDSYeSSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIM-------RSLLEAVSYLHAN 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSaENECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPeaELQNCLAQaglQSDTECTSAVDLWSLGI 230
Cdd:cd14181 136 NIVHRDLKPENILLD-DQLHIKLSDFGFSchLEPGEKLRELCGTPGYLAP--EILKCSMD---ETHPGYGKEVDLWACGV 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 231 ILLEMFSG----------------MKLKHTVRSQEWKANSSAIidhifaskavvnaaipayhlRDLIKSMLHDDPSRRIP 294
Cdd:cd14181 210 ILFTLLAGsppfwhrrqmlmlrmiMEGRYQFSSPEWDDRSSTV--------------------KDLISRLLVVDPEIRLT 269
                       250
                ....*....|
gi 28467003 295 AEMALCSPFF 304
Cdd:cd14181 270 AEQALQHPFF 279
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
73-237 1.28e-18

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 84.89  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003     73 FRKERAALEQLQgHRNIVTLYGVFTIhfspnVPSRCLLLELLD--------------VSVSELLLYsshqgcsmwmiqhc 138
Cdd:smart00219  48 FLREARIMRKLD-HPNVVKLLGVCTE-----EEPLYIVMEYMEggdllsylrknrpkLSLSDLLSF-------------- 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfKEGNQDVKYIQTDG---YR--APEAeLQNClaqagl 213
Cdd:smart00219 108 ALQIARGMEYLESKNFIHRDLAARNCLVGENLVV-KISDFGLS-RDLYDDDYYRKRGGklpIRwmAPES-LKEG------ 178
                          170       180
                   ....*....|....*....|....
gi 28467003    214 qsdtECTSAVDLWSLGIILLEMFS 237
Cdd:smart00219 179 ----KFTSKSDVWSFGVLLWEIFT 198
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
73-293 1.44e-18

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: 84.49  E-value: 1.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfSPNvpSRCLLLELldVSVSELLLY-SSHQGCS-------MWMIqhcardvLE 144
Cdd:cd14003  46 IKREIEIMKLLN-HPNIIKLYEVIE---TEN--KIYLVMEY--ASGGELFDYiVNNGRLSedearrfFQQL-------IS 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSDTECTSA 222
Cdd:cd14003 111 AVDYCHSNGIVHRDLKLENILLD-KNGNLKIIDFGLSneFRGGSLLKTFCGTPAYAAPEV----------LLGRKYDGPK 179
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 223 VDLWSLGIILLEMFSGmKL---KHTVRSQEWKANSSAIIDHIFASKAvvnaaipayhLRDLIKSMLHDDPSRRI 293
Cdd:cd14003 180 ADVWSLGVILYAMLTG-YLpfdDDNDSKLFRKILKGKYPIPSHLSPD----------ARDLIRRMLVVDPSKRI 242
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
75-334 1.89e-18

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: 85.99  E-value: 1.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTIHFSPN---------VPSRCLLLELLDVSVSELL----LYSSHqgCSMWMIQhcard 141
Cdd:cd07854  51 REIKIIRRLD-HDNIVKVYEVLGPSGSDLtedvgslteLNSVYIVQEYMETDLANVLeqgpLSEEH--ARLFMYQ----- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLS------------FKEGnqdvkyIQTDGYRAPEAelqncla 209
Cdd:cd07854 123 LLRGLKYIHSANVLHRDLKPANVFINTEDLVLKIGDFGLArivdphyshkgyLSEG------LVTKWYRSPRL------- 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 210 qagLQSDTECTSAVDLWSLGIILLEMFSGMKL---KHTVRSQEWKANSSAIIDH--------IFASKAVVNAAIPAYHLR 278
Cdd:cd07854 190 ---LLSPNNYTKAIDMWAAGCIFAEMLTGKPLfagAHELEQMQLILESVPVVREedrnellnVIPSFVRNDGGEPRRPLR 266
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 279 -----------DLIKSMLHDDPSRRIPAEMALCSPFFSIPFAPHIEDLVMLPtpvLRLLNVLDDDYL 334
Cdd:cd07854 267 dllpgvnpealDFLEQILTFNPMDRLTAEEALMHPYMSCYSCPFDEPVSLHP---FHIEDELDDILL 330
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-303 4.89e-18

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 84.11  E-value: 4.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  19 FGRLWQVQSRLGSGSSASVYRVRCCGNpgSPPGALKQFlppgttgaAASAAEYGFRKERAALEQLQgHRNIVTLYGVFTI 98
Cdd:cd14085   1 LEDFFEIESELGRGATSVVYRCRQKGT--QKPYAVKKL--------KKTVDKKIVRTEIGVLLRLS-HPNIIKLKEIFET 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  99 HFSPNvpsrcLLLELldVSVSELL-------LYSSHQGCSmwmiqhCARDVLEALAFLHHEGYVHADLKPRNILW--SAE 169
Cdd:cd14085  70 PTEIS-----LVLEL--VTGGELFdrivekgYYSERDAAD------AVKQILEAVAYLHENGIVHRDLKPENLLYatPAP 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 170 NECFKLIDFGLSfKEGNQDV---KYIQTDGYRAPEAelqnclaqagLQSDTECTsAVDLWSLGIILLEMFSGMKLKHTVR 246
Cdd:cd14085 137 DAPLKIADFGLS-KIVDQQVtmkTVCGTPGYCAPEI----------LRGCAYGP-EVDMWSVGVITYILLCGFEPFYDER 204
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 247 SQEWKANSSAIIDHIFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14085 205 GDQYMFKRILNCDYDFVSPWWDDVSLNA---KDLVKKLIVLDPKKRLTTQQALQHPW 258
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
75-304 7.22e-18

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 83.81  E-value: 7.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQGH-----RNIVTLYGVFTI--HFspnvpsrCLLLELLDVSVSELL-LYSSHQGCSMWMIQHCARDVLEAL 146
Cdd:cd14135  46 KELEILKKLNDAdpddkKHCIRLLRHFEHknHL-------CLVFESLSMNLREVLkKYGKNVGLNIKAVRSYAQQLFLAL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 147 AFLHHEGYVHADLKPRNILWSAENECFKLIDFG-LSFKEGNQDVKYIQTDGYRAPEAELqnclaqaGLQSDTectsAVDL 225
Cdd:cd14135 119 KHLKKCNILHADIKPDNILVNEKKNTLKLCDFGsASDIGENEITPYLVSRFYRAPEIIL-------GLPYDY----PIDM 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 226 WSLGIILLEMFSG------------MKL--------------KHTVRSQEWKANSSAI---IDHI--------------- 261
Cdd:cd14135 188 WSVGCTLYELYTGkilfpgktnnhmLKLmmdlkgkfpkkmlrKGQFKDQHFDENLNFIyreVDKVtkkevrrvmsdikpt 267
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 28467003 262 --FASKAVVNAAIPAY------HLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14135 268 kdLKTLLIGKQRLPDEdrkkllQLKDLLDKCLMLDPEKRITPNEALQHPFI 318
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
14-292 8.48e-18

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: 82.73  E-value: 8.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  14 RFLEAFgrlwQVQSRLGSGSSASVYRVRccGNPGSPPGALKQFLppgtTGAAASAAEYGFRkERAALEQLQgHRNIVTLY 93
Cdd:cd13996   3 RYLNDF----EEIELLGSGGFGSVYKVR--NKVDGVTYAIKKIR----LTEKSSASEKVLR-EVKALAKLN-HPNIVRYY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  94 GVFtihfspnVPSRCLLL--ELLD-VSVSELLLYSSHQGCSM-WMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAE 169
Cdd:cd13996  71 TAW-------VEEPPLYIqmELCEgGTLRDWIDRRNSSSKNDrKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDND 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 170 NECFKLIDFGLSFKEGNQDVKY-----------------IQTDGYRAPEAElqnclaqaglqSDTECTSAVDLWSLGIIL 232
Cdd:cd13996 144 DLQVKIGDFGLATSIGNQKRELnnlnnnnngntsnnsvgIGTPLYASPEQL-----------DGENYNEKADIYSLGIIL 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 233 LEMFSGMKLKHTvRSQEWKANSSAIIDHIFASKAVVNAaipayhlrDLIKSMLHDDPSRR 292
Cdd:cd13996 213 FEMLHPFKTAME-RSTILTDLRNGILPESFKAKHPKEA--------DLIQSLLSKNPEER 263
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
28-237 1.21e-17

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: 82.16  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    28 RLGSGSSASVYRVRCCGNPGSPPG--ALKQfLPPGTTGAAASAaeygFRKERAALEQLQgHRNIVTLYGVFTIHfspnvP 105
Cdd:pfam07714   6 KLGEGAFGEVYKGTLKGEGENTKIkvAVKT-LKEGADEEERED----FLEEASIMKKLD-HPNIVKLLGVCTQG-----E 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   106 SRCLLLE------LLD--------VSVSELLLYsshqgcsmwmiqhcARDVLEALAFLHHEGYVHADLKPRNILWSaENE 171
Cdd:pfam07714  75 PLYIVTEympggdLLDflrkhkrkLTLKDLLSM--------------ALQIAKGMEYLESKNFVHRDLAARNCLVS-ENL 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28467003   172 CFKLIDFGLSfKEGNQDVKYIQTDG------YRAPEAeLQNClaqaglqsdtECTSAVDLWSLGIILLEMFS 237
Cdd:pfam07714 140 VVKISDFGLS-RDIYDDDYYRKRGGgklpikWMAPES-LKDG----------KFTSKSDVWSFGVLLWEIFT 199
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
86-303 1.35e-17

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: 82.08  E-value: 1.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIHfspnvPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNIL 165
Cdd:cd14074  61 HPNVVRLYEVIDTQ-----TKLYLILELGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVV 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 166 WSAENECFKLIDFGLS--FKEGNQdvkyIQTD----GYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGm 239
Cdd:cd14074 136 FFEKQGLVKLTDFGFSnkFQPGEK----LETScgslAYSAPEI----------LLGDEYDAPAVDIWSLGVILYMLVCG- 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 240 klkhtvRSQEWKANSSAIIDHIFASKAVVNAAIPAyHLRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14074 201 ------QPPFQEANDSETLTMIMDCKYTVPAHVSP-ECKDLIRRMLIRDPKKRASLEEIENHPW 257
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
23-303 1.44e-17

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: 81.97  E-value: 1.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRvrCCGNPGSPPGALKQF-LPPGTTGAAASAAEygfrkERAALEQLQgHRNIVTLYGVfTIHfs 101
Cdd:cd06626   2 WQRGNKIGEGTFGKVYT--AVNLDTGELMAMKEIrFQDNDPKTIKEIAD-----EMKVLEGLD-HPNLVRYYGV-EVH-- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 pnvpsR---CLLLELLDV-SVSELLLYSSHQgcSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAeNECFKLID 177
Cdd:cd06626  71 -----ReevYIFMEYCQEgTLEELLRHGRIL--DEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDS-NGLIKLGD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 178 FGLSFKEGNQDVKYIQ--------TDGYRAPEAELQNCLAQAGlqsdtectSAVDLWSLGIILLEMFSGMKLKHTVrSQE 249
Cdd:cd06626 143 FGSAVKLKNNTTTMAPgevnslvgTPAYMAPEVITGNKGEGHG--------RAADIWSLGCVVLEMATGKRPWSEL-DNE 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 250 WkanssAIIDHIfASKAVvnAAIPAyHL------RDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd06626 214 W-----AIMYHV-GMGHK--PPIPD-SLqlspegKDFLSRCLESDPKKRPTASELLDHPF 264
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
70-293 1.45e-17

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: 82.78  E-value: 1.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  70 EYGFRKERAALEQLQGHRNIVTLYGVF--TIHfspnvpsRCLLLELLdvSVSELL-LYSSHQGCSMWMIQHCARDVLEAL 146
Cdd:cd14179  45 EANTQREIAALKLCEGHPNIVKLHEVYhdQLH-------TFLVMELL--KGGELLeRIKKKQHFSETEASHIMRKLVSAV 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 147 AFLHHEGYVHADLKPRNILWSAENEC--FKLIDFGLSFKE--GNQDVKY-IQTDGYRAPEaelqnCLAQAGLqsDTECts 221
Cdd:cd14179 116 SHMHDVGVVHRDLKPENLLFTDESDNseIKIIDFGFARLKppDNQPLKTpCFTLHYAAPE-----LLNYNGY--DESC-- 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 222 avDLWSLGIILLEMFSGmKLKHTVRSQEWKANSSAII-------DHIFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRI 293
Cdd:cd14179 187 --DLWSLGVILYTMLSG-QVPFQCHDKSLTCTSAEEImkkikqgDFSFEGEAWKNVSQEA---KDLIQGLLTVDPNKRI 259
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
75-241 1.51e-17

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: 83.64  E-value: 1.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQ-----GHRNIVTLYGVFTihFSPNVpsrCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFL 149
Cdd:cd14224 110 EEIRILEHLKkqdkdNTMNVIHMLESFT--FRNHI---CMTFELLSMNLYELIKKNKFQGFSLQLVRKFAHSILQCLDAL 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 150 HHEGYVHADLKPRNILWSAENEC-FKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQnclAQAGLqsdtectsAVDLWSL 228
Cdd:cd14224 185 HRNKIIHCDLKPENILLKQQGRSgIKVIDFGSSCYEHQRIYTYIQSRFYRAPEVILG---ARYGM--------PIDMWSF 253
                       170
                ....*....|...
gi 28467003 229 GIILLEMFSGMKL 241
Cdd:cd14224 254 GCILAELLTGYPL 266
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
24-293 2.14e-17

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: 81.61  E-value: 2.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRccgNPGSPPG-ALKQFLppgttgAAASAAEYGFRKERAALEQLQGHRNIVTLYGVfTIHFSP 102
Cdd:cd13985   3 QVTKQLGEGGFSYVYLAH---DVNTGRRyALKRMY------FNDEEQLRVAIKEIEIMKRLCGHPNIVQYYDS-AILSSE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 103 NVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEG--YVHADLKPRNILWSAENEcFKLIDFG- 179
Cdd:cd13985  73 GRKEVLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR-FKLCDFGs 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 180 ----LSFKEGNQDVKYIQ-------TDGYRAPEAelqnclaqAGLQSDTECTSAVDLWSLGIILLEMfsgMKLKHTVrsq 248
Cdd:cd13985 152 atteHYPLERAEEVNIIEeeiqkntTPMYRAPEM--------IDLYSKKPIGEKADIWALGCLLYKL---CFFKLPF--- 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 28467003 249 ewkaNSSAIIDHIFAskavvNAAIPAYH-----LRDLIKSMLHDDPSRRI 293
Cdd:cd13985 218 ----DESSKLAIVAG-----KYSIPEQPryspeLHDLIRHMLTPDPAERP 258
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
24-302 3.10e-17

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: 80.82  E-value: 3.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRCCGNpgSPPGALKQFLPPgTTGAAASAAEYGfrkERAALEQLQGHRNIVTLY------GVFT 97
Cdd:cd14050   4 TILSKLGEGSFGEVFKVRSRED--GKLYAVKRSRSR-FRGEKDRKRKLE---EVERHEKLGEHPNCVRFIkaweekGILY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  98 IHfspnvpsrcllLELLDVSvseLLLYSS-HQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLI 176
Cdd:cd14050  78 IQ-----------TELCDTS---LQQYCEeTHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVC-KLG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 177 DFGLSFKEGNQDVKYIQtDG---YRAPEAelqnclaqagLQSDTecTSAVDLWSLGIILLEMFSGMKLKHTvrSQEWKAN 253
Cdd:cd14050 143 DFGLVVELDKEDIHDAQ-EGdprYMAPEL----------LQGSF--TKAADIFSLGITILELACNLELPSG--GDGWHQL 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 28467003 254 SSAIIDHIFASKAvvnaaipAYHLRDLIKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd14050 208 RQGYLPEEFTAGL-------SPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
29-303 3.45e-17

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: 81.19  E-value: 3.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRV--RCCGNPGsppgALKqflppgTTGAAASAAEYGFRKERAALEQLQgHRNIVTLYGVF--TIHFSpnv 104
Cdd:cd14166  11 LGSGAFSEVYLVkqRSTGKLY----ALK------CIKKSPLSRDSSLENEIAVLKRIK-HENIVTLEDIYesTTHYY--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 105 psrcLLLELldVSVSELL-------LYSSHQGCSMwmiqhcARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLI- 176
Cdd:cd14166  77 ----LVMQL--VSGGELFdrilergVYTEKDASRV------INQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMi 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 177 -DFGLSFKEGNQDVKY-IQTDGYRAPEAelqncLAQAGLqsdtecTSAVDLWSLGIILLEMFSGM---------KLKHTV 245
Cdd:cd14166 145 tDFGLSKMEQNGIMSTaCGTPGYVAPEV-----LAQKPY------SKAVDCWSIGVITYILLCGYppfyeetesRLFEKI 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 246 RSQEWkANSSAIIDHIFASKavvnaaipayhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14166 214 KEGYY-EFESPFWDDISESA------------KDFIRHLLEKNPSKRYTCEKALSHPW 258
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
76-304 3.78e-17

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: 80.86  E-value: 3.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQGHRNIVTLYGVFtihfspNVPSRCLLL-------ELLDVSVSELLLYSSHqgcsmwmIQHCARDVLEALAF 148
Cdd:cd14106  57 EIAVLELCKDCPRVVNLHEVY------ETRSELILIlelaaggELQTLLDEEECLTEAD-------VRRLMRQILEGVQY 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAENEC--FKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSDTECTsAVD 224
Cdd:cd14106 124 LHERNIVHLDLKPQNILLTSEFPLgdIKLCDFGISrvIGEGEEIREILGTPDYVAPEI----------LSYEPISL-ATD 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 225 LWSLGIILLEMFSGMKLKHTVRSQEWKANSSAII----DHIFasKAVVNAAIpayhlrDLIKSMLHDDPSRRIPAEMALC 300
Cdd:cd14106 193 MWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNldfpEELF--KDVSPLAI------DFIKRLLVKDPEKRLTAKECLE 264

                ....
gi 28467003 301 SPFF 304
Cdd:cd14106 265 HPWL 268
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
108-304 6.76e-17

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 81.21  E-value: 6.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILW------------------SAE 169
Cdd:cd14214  92 CIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFvnsefdtlynesksceekSVK 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 170 NECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQNCLAQAglqsdteCtsavDLWSLGIILLEMFSGMKL-------- 241
Cdd:cd14214 172 NTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQP-------C----DVWSLGCILFEYYRGFTLfqthenre 240
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 242 ----------------KHTVRSQE--------WKANSSaiiDHIFASKA-------VVNAAIPAYHLRDLIKSMLHDDPS 290
Cdd:cd14214 241 hlvmmekilgpipshmIHRTRKQKyfykgslvWDENSS---DGRYVSENckplmsyMLGDSLEHTQLFDLLRRMLEFDPA 317
                       250
                ....*....|....
gi 28467003 291 RRIPAEMALCSPFF 304
Cdd:cd14214 318 LRITLKEALLHPFF 331
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
75-304 9.74e-17

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: 80.05  E-value: 9.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFT----IHfspnvpsrcLLLELLDVSVSELLlYSSHQGCSMWMIQHCARDVLEALAFLH 150
Cdd:cd07833  49 REVKVLRQLR-HENIVNLKEAFRrkgrLY---------LVFEYVERTLLELL-EASPGGLPPDAVRSYIWQLLQAIAYCH 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSaENECFKLIDFG----LSFKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLW 226
Cdd:cd07833 118 SHNIIHRDIKPENILVS-ESGVLKLCDFGfaraLTARPASPLTDYVATRWYRAPEL----------LVGDTNYGKPVDVW 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 227 SLGIILLEMFSG----------------MKLKHTVRSQEWKANSSaiiDHIFASKAVVN-----------AAIPAYHLRD 279
Cdd:cd07833 187 AIGCIMAELLDGeplfpgdsdidqlyliQKCLGPLPPSHQELFSS---NPRFAGVAFPEpsqpeslerryPGKVSSPALD 263
                       250       260
                ....*....|....*....|....*
gi 28467003 280 LIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07833 264 FLKACLRMDPKERLTCDELLQHPYF 288
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
135-326 1.07e-16

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: 80.43  E-value: 1.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEneC-FKLIDFGLS------FKEGNQDVKYIQTDGYRAPEAELqnc 207
Cdd:cd07849 108 IQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTN--CdLKICDFGLAriadpeHDHTGFLTEYVATRWYRAPEIML--- 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 208 laqaglqSDTECTSAVDLWSLGIILLEMFSGMKL---KHtVRSQEW----------KANSSAII-----DHI----FASK 265
Cdd:cd07849 183 -------NSKGYTKAIDIWSVGCILAEMLSNRPLfpgKD-YLHQLNlilgilgtpsQEDLNCIIslkarNYIkslpFKPK 254
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 266 AVVNAAIPAYHLR--DLIKSMLHDDPSRRIPAEMALCSPFFS------------IPFAPHIEDLVMLPTPVLRLL 326
Cdd:cd07849 255 VPWNKLFPNADPKalDLLDKMLTFNPHKRITVEEALAHPYLEqyhdpsdepvaeEPFPFDMELFDDLPKEKLKEL 329
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
134-305 1.11e-16

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: 79.57  E-value: 1.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSF------------------KEGNQDVKYIQTD 195
Cdd:cd05579  94 VARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGH-LKLTDFGLSKvglvrrqiklsiqkksngAPEKEDRRIVGTP 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 196 GYRAPEAELqnclaqagLQSDtecTSAVDLWSLGIILLEMFSGMKLKHTVRSQEwkanssaIIDHIFASKavvnaaIP-- 273
Cdd:cd05579 173 DYLAPEILL--------GQGH---GKTVDWWSLGVILYEFLVGIPPFHAETPEE-------IFQNILNGK------IEwp 228
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 28467003 274 -----AYHLRDLIKSMLHDDPSRRIPAEMA---LCSPFFS 305
Cdd:cd05579 229 edpevSDEAKDLISKLLTPDPEKRLGAKGIeeiKNHPFFK 268
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
26-292 1.17e-16

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: 79.35  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  26 QSRLGSGSSASVYRVRCCGNPGsppgALKQFlppgTTGAAASAAEYGFRKERAALeQLQgHRNIVTL-----------YG 94
Cdd:cd13979   8 QEPLGSGGFGSVYKATYKGETV----AVKIV----RRRRKNRASRQSFWAELNAA-RLR-HENIVRVlaaetgtdfasLG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  95 VFTIHFSPNVPsrclLLELLDVSVSELLLYsshqgcsmwmiqHCAR---DVLEALAFLHHEGYVHADLKPRNILWSAENE 171
Cdd:cd13979  78 LIIMEYCGNGT----LQQLIYEGSEPLPLA------------HRILislDIARALRFCHSHGIVHLDVKPANILISEQGV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 172 CfKLIDFGLSFK--EGN---QDVKYIQ-TDGYRAPEAelqnclaqagLQSDTeCTSAVDLWSLGIILLEMFSG----MKL 241
Cdd:cd13979 142 C-KLCDFGCSVKlgEGNevgTPRSHIGgTYTYRAPEL----------LKGER-VTPKADIYSFGITLWQMLTRelpyAGL 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 28467003 242 KHTVRSQEWKANSSAIIDHIFASKavvnaaiPAYHLRDLIKSMLHDDPSRR 292
Cdd:cd13979 210 RQHVLYAVVAKDLRPDLSGLEDSE-------FGQRLRSLISRCWSAQPAER 253
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
75-304 1.66e-16

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: 79.31  E-value: 1.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQG--HRNIVTLYGVFTIHFSPNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd07862  50 REVAVLRHLETfeHPNVVRLFDVCTVSRTDRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSH 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAENEcFKLIDFGL----SFKEGNQDVkyIQTDGYRAPEAELQNCLAqaglqsdtectSAVDLWSL 228
Cdd:cd07862 130 RVVHRDLKPQNILVTSSGQ-IKLADFGLariySFQMALTSV--VVTLWYRAPEVLLQSSYA-----------TPVDLWSV 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 229 GIILLEMFSGMKLKH---------------TVRSQEWKANSSAIIDHIFASKAV--VNAAIPAYHL--RDLIKSMLHDDP 289
Cdd:cd07862 196 GCIFAEMFRRKPLFRgssdvdqlgkildviGLPGEEDWPRDVALPRQAFHSKSAqpIEKFVTDIDElgKDLLLKCLTFNP 275
                       250
                ....*....|....*
gi 28467003 290 SRRIPAEMALCSPFF 304
Cdd:cd07862 276 AKRISAYSALSHPYF 290
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
84-238 1.91e-16

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: 79.54  E-value: 1.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  84 QGHRNIVTLYGVFTiHFSPNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE-GYVHADLKPR 162
Cdd:cd14136  71 PGREHVVQLLDDFK-HTGPNGTHVCMVFEVLGPNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPE 149
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 163 NILWSAENECFKLIDFGLS---FKEGNQDvkyIQTDGYRAPEAELqnclaqaGLQSDTectsAVDLWSLGIILLEMFSG 238
Cdd:cd14136 150 NVLLCISKIEVKIADLGNAcwtDKHFTED---IQTRQYRSPEVIL-------GAGYGT----PADIWSTACMAFELATG 214
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
86-305 2.11e-16

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 79.64  E-value: 2.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTihfsPNVPSR-----CLLLELLDVSVSELLlysSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLK 160
Cdd:cd07851  73 HENVIGLLDVFT----PASSLEdfqdvYLVTHLMGADLNNIV---KCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLK 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 161 PRNIlwsAENE-C-FKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqaglqSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd07851 146 PSNL---AVNEdCeLKILDFGLARHTDDEMTGYVATRWYRAPEIML----------NWMHYNQTVDIWSVGCIMAELLTG 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 239 ----------------MKLKHTvRSQEW--KANSSAIIDHI----------FasKAVVNAAIPayHLRDLIKSMLHDDPS 290
Cdd:cd07851 213 ktlfpgsdhidqlkriMNLVGT-PDEELlkKISSESARNYIqslpqmpkkdF--KEVFSGANP--LAIDLLEKMLVLDPD 287
                       250
                ....*....|....*
gi 28467003 291 RRIPAEMALCSPFFS 305
Cdd:cd07851 288 KRITAAEALAHPYLA 302
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
19-305 3.04e-16

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: 79.15  E-value: 3.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  19 FGRLWQVQSR------LGSGSSASVYRVRccGNPGSPPGALKQFLPPGTTgaaASAAEYGFRkERAALEQLQgHRNIVTL 92
Cdd:cd07856   2 FGTVFEITTRysdlqpVGMGAFGLVCSAR--DQLTGQNVAVKKIMKPFST---PVLAKRTYR-ELKLLKHLR-HENIISL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  93 YGVFtihFSPnVPSRCLLLELLDVSVSELLlysSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENEC 172
Cdd:cd07856  75 SDIF---ISP-LEDIYFVTELLGTDLHRLL---TSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVN-ENCD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 173 FKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqaglqSDTECTSAVDLWSLGIILLEMFSGMKL---KHTVrsqe 249
Cdd:cd07856 147 LKICDFGLARIQDPQMTGYVSTRYYRAPEIML----------TWQKYDVEVDIWSAGCIFAEMLEGKPLfpgKDHV---- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 250 wkaNSSAIIDHIFAS--KAVVNAAIPAYHLR-------------------------DLIKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd07856 213 ---NQFSIITELLGTppDDVINTICSENTLRfvqslpkrervpfsekfknadpdaiDLLEKMLVFDPKKRISAAEALAHP 289

                ...
gi 28467003 303 FFS 305
Cdd:cd07856 290 YLA 292
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
319-412 3.58e-16

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 80.32  E-value: 3.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   319 PTPVLRLLNVLDDDYLENEEEYEDVVEDVKEECQKYGPVVSLLVPKEN------PGRGQVFVEYANAGDSKAAQKLLTGR 392
Cdd:TIGR01642 408 PTKVVQLTNLVTGDDLMDDEEYEEIYEDVKTEFSKYGPLINIVIPRPNgdrnstPGVGKVFLEYADVRSAEKAMEGMNGR 487
                          90       100
                  ....*....|....*....|
gi 28467003   393 MFDGKFVVATFYPLSAYKRG 412
Cdd:TIGR01642 488 KFNDRVVVAAFYGEDCYKAG 507
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
80-310 3.80e-16

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: 79.00  E-value: 3.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  80 LEQLQGHRNIVTLYGVFTihfspnvPSRC--------LLLELLDVS---VSELLLysSHQGCSMWMIQhcardVLEALAF 148
Cdd:cd07850  52 LMKLVNHKNIIGLLNVFT-------PQKSleefqdvyLVMELMDANlcqVIQMDL--DHERMSYLLYQ-----MLCGIKH 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILwsAENEC-FKLIDFGLSFKEGNQDV--KYIQTDGYRAPEAELqnclaQAGLQSDtectsaVDL 225
Cdd:cd07850 118 LHSAGIIHRDLKPSNIV--VKSDCtLKILDFGLARTAGTSFMmtPYVVTRYYRAPEVIL-----GMGYKEN------VDI 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 226 WSLGIILLEMFSG----------------------------MKLKHTVRS-------QEWKANSSAIIDHIFASKAVVNA 270
Cdd:cd07850 185 WSVGCIMGEMIRGtvlfpgtdhidqwnkiieqlgtpsdefmSRLQPTVRNyvenrpkYAGYSFEELFPDVLFPPDSEEHN 264
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 28467003 271 AIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFFSIPFAP 310
Cdd:cd07850 265 KLKASQARDLLSKMLVIDPEKRISVDDALQHPYINVWYDP 304
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
86-305 5.23e-16

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: 77.86  E-value: 5.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIHfspnvPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNIL 165
Cdd:cd06611  61 HPNIVGLYEAYFYE-----NKLWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNIL 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 166 WSAENEcFKLIDFGLSFKEGNQDVK---YIQTDGYRAPeaELQNCLAqaglQSDTECTSAVDLWSLGIILLEMFSGMKLK 242
Cdd:cd06611 136 LTLDGD-VKLADFGVSAKNKSTLQKrdtFIGTPYWMAP--EVVACET----FKDNPYDYKADIWSLGITLIELAQMEPPH 208
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 243 HTVrsqewkaNSSAIIDHIFASK--AVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFFS 305
Cdd:cd06611 209 HEL-------NPMRVLLKILKSEppTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
22-304 5.33e-16

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 78.10  E-value: 5.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  22 LWQVQSRLGSGSSASVYRVRCCGNPGSPPGALKQFLPPGTTGAAASAAEYgfrKERAALEQLQgHRNIVTLYGVFtihfs 101
Cdd:cd07842   1 KYEIEGCIGRGTYGRVYKAKRKNGKDGKEYAIKKFKGDKEQYTGISQSAC---REIALLRELK-HENVVSLVEVF----- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 pnvpsrcllLELLDVSVSELLLYSSHqgcSMWMIQHCARD-----------------VLEALAFLHHEGYVHADLKPRNI 164
Cdd:cd07842  72 ---------LEHADKSVYLLFDYAEH---DLWQIIKFHRQakrvsippsmvksllwqILNGIHYLHSNWVLHRDLKPANI 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 165 LWSAENE---CFKLIDFGL---------SFKEGNqdvKYIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIIL 232
Cdd:cd07842 140 LVMGEGPergVVKIGDLGLarlfnaplkPLADLD---PVVVTIWYRAPEL----------LLGARHYTKAIDIWAIGCIF 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 233 LEM------FSGM--KLKHTV---RSQ-----------------------EWKANSSaiidHIFASKAVVNAAIPAYHLR 278
Cdd:cd07842 207 AELltlepiFKGReaKIKKSNpfqRDQlerifevlgtptekdwpdikkmpEYDTLKS----DTKASTYPNSLLAKWMHKH 282
                       330       340       350
                ....*....|....*....|....*....|....
gi 28467003 279 --------DLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07842 283 kkpdsqgfDLLRKLLEYDPTKRITAEEALEHPYF 316
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
75-304 5.72e-16

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: 77.54  E-value: 5.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVftIHfspNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGY 154
Cdd:cd07860  48 REISLLKELN-HPNIVKLLDV--IH---TENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAeLQNCLAQaglqsdtecTSAVDLWSLGII 231
Cdd:cd07860 122 LHRDLKPQNLLINTEGA-IKLADFGLARAFGVPVRTYtheVVTLWYRAPEI-LLGCKYY---------STAVDIWSLGCI 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 232 LLEMFSgmklkhtvRSQEWKANSSaiIDHIFASKAVVN----------AAIPAYHL---------------------RDL 280
Cdd:cd07860 191 FAEMVT--------RRALFPGDSE--IDQLFRIFRTLGtpdevvwpgvTSMPDYKPsfpkwarqdfskvvppldedgRDL 260
                       250       260
                ....*....|....*....|....
gi 28467003 281 IKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07860 261 LSQMLHYDPNKRISAKAALAHPFF 284
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
75-304 1.03e-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: 76.95  E-value: 1.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVftIHfspnVPSRC-LLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd07835  47 REISLLKELN-HPNIVRLLDV--VH----SENKLyLVFEFLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHR 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGI 230
Cdd:cd07835 120 VLHRDLKPQNLLIDTEGA-LKLADFGLARAFGVPVRTYtheVVTLWYRAPEI----------LLGSKHYSTPVDIWSVGC 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 231 ILLEM------FSG----------MKLKHTVRSQEWKANSSAIID-HIFASKAVVN--AAIPAY--HLRDLIKSMLHDDP 289
Cdd:cd07835 189 IFAEMvtrrplFPGdseidqlfriFRTLGTPDEDVWPGVTSLPDYkPTFPKWARQDlsKVVPSLdeDGLDLLSQMLVYDP 268
                       250
                ....*....|....*
gi 28467003 290 SRRIPAEMALCSPFF 304
Cdd:cd07835 269 AKRISAKAALQHPYF 283
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
86-305 1.26e-15

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 77.40  E-value: 1.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIHFS-PNVPSRCLLLELLDVSVSELLLYsshQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNI 164
Cdd:cd07878  73 HENVIGLLDVFTPATSiENFNEVYLVTNLMGADLNNIVKC---QKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 165 lwsAENE-C-FKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqNCLaqaglqsdtECTSAVDLWSLGIILLEMFSG---- 238
Cdd:cd07878 150 ---AVNEdCeLRILDFGLARQADDEMTGYVATRWYRAPEIML-NWM---------HYNQTVDIWSVGCIMAELLKGkalf 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 239 ------------MKLKHTVRSQEWKANSSAIIDHIFAS---------KAVVNAAIPAyhLRDLIKSMLHDDPSRRIPAEM 297
Cdd:cd07878 217 pgndyidqlkriMEVVGTPSPEVLKKISSEHARKYIQSlphmpqqdlKKIFRGANPL--AIDLLEKMLVLDSDKRISASE 294

                ....*...
gi 28467003 298 ALCSPFFS 305
Cdd:cd07878 295 ALAHPYFS 302
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
24-238 1.33e-15

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: 76.23  E-value: 1.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYR-----------VRCcgnpgsppgaLKQFLPPGTTGAAASAAEygFRKERAALEQLQGHRNIVTL 92
Cdd:cd13993   3 QLISPIGEGAYGVVYLavdlrtgrkyaIKC----------LYKSGPNSKDGNDFQKLP--QLREIDLHRRVSRHPNIITL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  93 YGVFTIH-FSPNVPSRCLLLELLDVSVSelllySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENE 171
Cdd:cd13993  71 HDVFETEvAIYIVLEYCPNGDLFEAITE-----NRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEG 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 172 CFKLIDFGLSFKEgnqDVKY---IQTDGYRAPEaelqnCLAQAGLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd13993 146 TVKLCDFGLATTE---KISMdfgVGSEFYMAPE-----CFDEVGRSLKGYPCAAGDIWSLGIILLNLTFG 207
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
29-237 1.43e-15

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: 76.04  E-value: 1.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCCGNPGSP-PGALKQfLPPGTTGAAASAaeygFRKERAALEQLqGHRNIVTLYGVFTIHFSPnvpsr 107
Cdd:cd00192   3 LGEGAFGEVYKGKLKGGDGKTvDVAVKT-LKEDASESERKD----FLKEARVMKKL-GHPNVVRLLGVCTEEEPL----- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLD--------VSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFG 179
Cdd:cd00192  72 YLVMEYMEggdlldflRKSRPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVV-KISDFG 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 180 LSfKEGNQDVKYIQTDGYR------APEAeLQnclaqaglqsDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd00192 151 LS-RDIYDDDYYRKKTGGKlpirwmAPES-LK----------DGIFTSKSDVWSFGVLLWEIFT 202
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
23-304 1.66e-15

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: 76.24  E-value: 1.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVRCCgnPGSPPGALKqflppgTTGAAASAAEYGF-RKERAALEQLQgHRNIVTLYGVFTIhfs 101
Cdd:cd06610   3 YELIEVIGSGATAVVYAAYCL--PKKEKVAIK------RIDLEKCQTSMDElRKEIQAMSQCN-HPNVVSYYTSFVV--- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 pnvpSRCL--LLELLDV-SVSELLLYS-SHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWsAENECFKLID 177
Cdd:cd06610  71 ----GDELwlVMPLLSGgSLLDIMKSSyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILL-GEDGSVKIAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 178 FGLS---FKEGNQDVK----YIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG------------ 238
Cdd:cd06610 146 FGVSaslATGGDRTRKvrktFVGTPCWMAPEV----------MEQVRGYDFKADIWSFGITAIELATGaapyskyppmkv 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 239 --MKLKHTVRSQEWKANSSAIidhifaSKAvvnaaipayhLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd06610 216 lmLTLQNDPPSLETGADYKKY------SKS----------FRKMISLCLQKDPSKRPTAEELLKHKFF 267
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
108-304 1.66e-15

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 77.20  E-value: 1.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILW------------------SAE 169
Cdd:cd14213  91 CIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFvqsdyvvkynpkmkrderTLK 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 170 NECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQnclaqagLQSDTECtsavDLWSLGIILLEMFSGMKLKHTVRSQE 249
Cdd:cd14213 171 NPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILA-------LGWSQPC----DVWSIGCILIEYYLGFTVFQTHDSKE 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 250 WKANSSAII-------------------------DHIFASKAVVNAAIPA-----------YHLRDLIKSMLHDDPSRRI 293
Cdd:cd14213 240 HLAMMERILgplpkhmiqktrkrkyfhhdqldwdEHSSAGRYVRRRCKPLkefmlsqdvdhEQLFDLIQKMLEYDPAKRI 319
                       250
                ....*....|.
gi 28467003 294 PAEMALCSPFF 304
Cdd:cd14213 320 TLDEALKHPFF 330
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
75-304 1.91e-15

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: 76.20  E-value: 1.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVftIHfspnvPSRCLLL--ELLDvsvSELLLYSSHqgCSMWMIQHCAR----DVLEALAF 148
Cdd:cd07871  52 REVSLLKNLK-HANIVTLHDI--IH-----TERCLTLvfEYLD---SDLKQYLDN--CGNLMSMHNVKifmfQLLRGLSY 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDL 225
Cdd:cd07871 119 CHKRKILHRDLKPQNLLINEKGE-LKLADFGLARAKSVPTKTYsneVVTLWYRPPDV----------LLGSTEYSTPIDM 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 226 WSLGIILLEMFSG----------------MKLKHTVRSQEWKAnssaiidhIFASKAVVNAAIPAYHLR----------- 278
Cdd:cd07871 188 WGVGCILYEMATGrpmfpgstvkeelhliFRLLGTPTEETWPG--------VTSNEEFRSYLFPQYRAQplinhaprldt 259
                       250       260
                ....*....|....*....|....*....
gi 28467003 279 ---DLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07871 260 dgiDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
135-303 4.07e-15

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: 75.02  E-value: 4.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVKYIQTDG------------------ 196
Cdd:cd14010  96 VRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLD-GNGTLKLSDFGLARREGEILKELFGQFSdegnvnkvskkqakrgtp 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 197 -YRAPEaelqncLAQAGLQSdtectSAVDLWSLGIILLEMFSGmKLKHTVRSQEWKANSsaIIDHIFASKAVVNAAIPAY 275
Cdd:cd14010 175 yYMAPE------LFQGGVHS-----FASDLWALGCVLYEMFTG-KPPFVAESFTELVEK--ILNEDPPPPPPKVSSKPSP 240
                       170       180
                ....*....|....*....|....*...
gi 28467003 276 HLRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14010 241 DFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
85-302 5.20e-15

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: 74.98  E-value: 5.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  85 GHRNIVTLYGVF----TIHfspnvpsrcLLLELLdvSVSELLLYSSHQGCsmwMIQHCARDVL----EALAFLHHEGYVH 156
Cdd:cd14091  52 QHPNIITLRDVYddgnSVY---------LVTELL--RGGELLDRILRQKF---FSEREASAVMktltKTVEYLHSQGVVH 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 157 ADLKPRNILWSAEN---ECFKLIDFGLSfKEGNQDVKYIQTDGYR----APEAelqncLAQAGLqsDTECtsavDLWSLG 229
Cdd:cd14091 118 RDLKPSNILYADESgdpESLRICDFGFA-KQLRAENGLLMTPCYTanfvAPEV-----LKKQGY--DAAC----DIWSLG 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 230 IILLEMFSGmklkHTVRSQEWKANSSAIIDHIFASKAVVNAaiPAYHL-----RDLIKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd14091 186 VLLYTMLAG----YTPFASGPNDTPEVILARIGSGKIDLSG--GNWDHvsdsaKDLVRKMLHVDPSQRPTAAQVLQHP 257
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
75-305 5.29e-15

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: 75.76  E-value: 5.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTIHFS-PNVPSRCLLLELLDVSVSELLlysSHQGCSMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd07880  63 RELRLLKHMK-HENVIGLLDVFTPDLSlDRFHDFYLVMPFMGTDLGKLM---KHEKLSEDRIQFLVYQMLKGLKYIHAAG 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqaglqSDTECTSAVDLWSLGIILL 233
Cdd:cd07880 139 IIHRDLKPGNLAVNEDCE-LKILDFGLARQTDSEMTGYVVTRWYRAPEVIL----------NWMHYTQTVDIWSVGCIMA 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 234 EMFSG----------------MKLKHTvRSQEW--KANSSAIIDHIfaskavvnAAIPAYHLRD--------------LI 281
Cdd:cd07880 208 EMLTGkplfkghdhldqlmeiMKVTGT-PSKEFvqKLQSEDAKNYV--------KKLPRFRKKDfrsllpnanplavnVL 278
                       250       260
                ....*....|....*....|....
gi 28467003 282 KSMLHDDPSRRIPAEMALCSPFFS 305
Cdd:cd07880 279 EKMLVLDAESRITAAEALAHPYFE 302
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
75-304 5.34e-15

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: 74.95  E-value: 5.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQGHRNIVTL---YGVFTIHFspnvpsrcLLLELLdvSVSELLLYSSHQ-GCSMWMIQHCARDVLEALAFLH 150
Cdd:cd14182  58 KEIDILRKVSGHPNIIQLkdtYETNTFFF--------LVFDLM--KKGELFDYLTEKvTLSEKETRKIMRALLEVICALH 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSaENECFKLIDFGLSFK--EGNQDVKYIQTDGYRAPEaelqncLAQAGLQSDTE-CTSAVDLWS 227
Cdd:cd14182 128 KLNIVHRDLKPENILLD-DDMNIKLTDFGFSCQldPGEKLREVCGTPGYLAPE------IIECSMDDNHPgYGKEVDMWS 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 228 LGIILLEMFSG----------------MKLKHTVRSQEWKANSSAIidhifaskavvnaaipayhlRDLIKSMLHDDPSR 291
Cdd:cd14182 201 TGVIMYTLLAGsppfwhrkqmlmlrmiMSGNYQFGSPEWDDRSDTV--------------------KDLISRFLVVQPQK 260
                       250
                ....*....|...
gi 28467003 292 RIPAEMALCSPFF 304
Cdd:cd14182 261 RYTAEEALAHPFF 273
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
70-305 5.39e-15

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: 75.08  E-value: 5.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  70 EYGFRKERAALEQLQgHRNIVTLYGVFTihfSPNVPSRCLLL----ELLDvSVSELLLYSSHQGCSMwmiqhcARDVLEA 145
Cdd:cd14168  52 ESSIENEIAVLRKIK-HENIVALEDIYE---SPNHLYLVMQLvsggELFD-RIVEKGFYTEKDASTL------IRQVLDA 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 146 LAFLHHEGYVHADLKPRNILWSAENECFKLI--DFGLSFKEGNQDVKYIQ--TDGYRAPEAelqncLAQAGLqsdtecTS 221
Cdd:cd14168 121 VYYLHRMGIVHRDLKPENLLYFSQDEESKIMisDFGLSKMEGKGDVMSTAcgTPGYVAPEV-----LAQKPY------SK 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 222 AVDLWSLGIILLEMFSGMklkhtvrSQEWKANSSAIIDHIFASKAVVNAaiPAY-----HLRDLIKSMLHDDPSRRIPAE 296
Cdd:cd14168 190 AVDCWSIGVIAYILLCGY-------PPFYDENDSKLFEQILKADYEFDS--PYWddisdSAKDFIRNLMEKDPNKRYTCE 260

                ....*....
gi 28467003 297 MALCSPFFS 305
Cdd:cd14168 261 QALRHPWIA 269
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
28-320 5.58e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 75.10  E-value: 5.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  28 RLGSGSSASVYRVRCCgnpgsppgalkqflppgTTGAAASAAEYGFRKER-----------AALEQLQgHRNIVTLYGVF 96
Cdd:cd07845  14 RIGEGTYGIVYRARDT-----------------TSGEIVALKKVRMDNERdgipisslreiTLLLNLR-HPNIVELKEVV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  97 TihfSPNVPSRCLLLELLDVSVSELLlYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLI 176
Cdd:cd07845  76 V---GKHLDSIFLVMEYCEQDLASLL-DNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLT-DKGCLKIA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 177 DFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGMKLkhtvrsqeWKAN 253
Cdd:cd07845 151 DFGLARTYGLPAKPMtpkVVTLWYRAPEL----------LLGCTTYTTAIDMWAVGCILAELLAHKPL--------LPGK 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 254 SS-AIIDHIFASKAVVNAAI-------PA---YHLR-------------------DLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd07845 213 SEiEQLDLIIQLLGTPNESIwpgfsdlPLvgkFTLPkqpynnlkhkfpwlseaglRLLNFLLMYDPKKRATAEEALESSY 292
                       330
                ....*....|....*..
gi 28467003 304 FSIPfaPHIEDLVMLPT 320
Cdd:cd07845 293 FKEK--PLPCEPEMMPT 307
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
75-293 5.81e-15

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: 74.70  E-value: 5.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTihfSPNVPSRCLLLELLD----VSVSELLLYSSHQGCSMWmiqhcaRDVLEALAFLH 150
Cdd:cd14118  63 REIAILKKLD-HPNVVKLVEVLD---DPNEDNLYMVFELVDkgavMEVPTDNPLSEETARSYF------RDIVLGIEYLH 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSAENEcFKLIDFGLSFK-EGNQDV--KYIQTDGYRAPEAELQNclaqaglqSDTECTSAVDLWS 227
Cdd:cd14118 133 YQKIIHRDIKPSNLLLGDDGH-VKIADFGVSNEfEGDDALlsSTAGTPAFMAPEALSES--------RKKFSGKALDIWA 203
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 228 LGIILLEMFSG---------MKLKHTVRSQEWKanssaiidhiFASKAVVNAAipayhLRDLIKSMLHDDPSRRI 293
Cdd:cd14118 204 MGVTLYCFVFGrcpfeddhiLGLHEKIKTDPVV----------FPDDPVVSEQ-----LKDLILRMLDKNPSERI 263
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
74-302 6.64e-15

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: 73.84  E-value: 6.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELldVSVSELLLYSSHQG-CSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14006  37 LREISILNQLQ-HPRIIQLHEAYE-----SPTELVLILEL--CSGGELLDRLAERGsLSEEEVRTYMRQLLEGLQYLHNH 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNIL-WSAENECFKLIDFGLSFKEGNQDVKYIQTDG--YRAPEAELQNCLaqaglqsdtecTSAVDLWSLG 229
Cdd:cd14006 109 HILHLDLKPENILlADRPSPQIKIIDFGLARKLNPGEELKEIFGTpeFVAPEIVNGEPV-----------SLATDMWSIG 177
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 230 IILLEMFSGMKLKHTVRSQEWKANSSAI---IDHIFASkAVVNAAipayhlRDLIKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd14006 178 VLTYVLLSGLSPFLGEDDQETLANISACrvdFSEEYFS-SVSQEA------KDFIRKLLVKEPRKRPTAQEALQHP 246
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
25-292 6.78e-15

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 74.63  E-value: 6.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  25 VQSRLGSGSSASVYRVRCcgNPGSPPGALKQFLPPGTTGAAasaaeyGFRKERAALEQLQGHRNIVTLYGVFTIHFSPNV 104
Cdd:cd14037   7 IEKYLAEGGFAHVYLVKT--SNGGNRAALKRVYVNDEHDLN------VCKREIEIMKRLSGHKNIVGYIDSSANRSGNGV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 105 PSRCLLLELL-DVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHH--EGYVHADLKPRNILWSAENEcFKLIDFG-L 180
Cdd:cd14037  79 YEVLLLMEYCkGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYlkPPLIHRDLKVENVLISDSGN-YKLCDFGsA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 181 SFK----EGNQDVKYIQTD-------GYRAPE-AELQNCLaqaglqsdtECTSAVDLWSLGIILlemfsgMKLKHTVRSQ 248
Cdd:cd14037 158 TTKilppQTKQGVTYVEEDikkyttlQYRAPEmIDLYRGK---------PITEKSDIWALGCLL------YKLCFYTTPF 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 28467003 249 EwKANSSAIIDhifaskavVNAAIPAYH-----LRDLIKSMLHDDPSRR 292
Cdd:cd14037 223 E-ESGQLAILN--------GNFTFPDNSryskrLHKLIRYMLEEDPEKR 262
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
29-308 8.00e-15

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: 73.80  E-value: 8.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCCGNPGspPGALKQFLPPGTTGAAASAAEYgfrkERAALEQLQgHRNIVTLYGV----FTIHfspnv 104
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGE--VVAIKEISRKKLNKKLQENLES----EIAILKSIK-HPNIVRLYDVqkteDFIY----- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 105 psrcLLLELLDV-SVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSA--ENECFKLIDFGLS 181
Cdd:cd14009  69 ----LVLEYCAGgDLSQYI--RKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTsgDDPVLKIADFGFA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 182 fkegnqdvKYIQTDG----------YRAPEA-ELQNCLAQAglqsdtectsavDLWSLGIILLEM------FSGmklkht 244
Cdd:cd14009 143 --------RSLQPASmaetlcgsplYMAPEIlQFQKYDAKA------------DLWSVGAILFEMlvgkppFRG------ 196
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 245 vrsqewkANSSAIIDHIFASKAVVNAAIPAY---HLRDLIKSMLHDDPSRRIPAEmalcsPFFSIPF 308
Cdd:cd14009 197 -------SNHVQLLRNIERSDAVIPFPIAAQlspDCKDLLRRLLRRDPAERISFE-----EFFAHPF 251
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
28-237 8.01e-15

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 74.36  E-value: 8.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  28 RLGSGSSASVYRVRCCGNPGS--PPGALKQFLPPGTTGAAASaaeYGFR--KERAALEQLQgHRNIVTlYGVFTihfSPN 103
Cdd:cd14001   6 KLGYGTGVNVYLMKRSPRGGSsrSPWAVKKINSKCDKGQRSL---YQERlkEEAKILKSLN-HPNIVG-FRAFT---KSE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 104 VPSRCLLLELLDVSVSELL---LYSSHQGCSMWMIQHCARDVLEALAFLHHEGYV-HADLKPRNILWSAENECFKLIDFG 179
Cdd:cd14001  78 DGSLCLAMEYGGKSLNDLIeerYEAGLGPFPAATILKVALSIARALEYLHNEKKIlHGDIKSGNVLIKGDFESVKLCDFG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 180 LSFK-------EGNQDVKYIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd14001 158 VSLPltenlevDSDPKAQYVGTEPWKAKEA----------LEEGGVITDKADIFAYGLVLWEMMT 212
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
137-303 8.91e-15

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: 74.38  E-value: 8.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 137 HCARDVLEALAFLHHEGYVHADLKPRNILWS--AENECFKLIDFGLSFK-EGNQDVKY--IQTDGYRAPEAelqnclaqa 211
Cdd:cd14086 104 HCIQQILESVNHCHQNGIVHRDLKPENLLLAskSKGAAVKLADFGLAIEvQGDQQAWFgfAGTPGYLSPEV--------- 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 212 gLQSDTECTsAVDLWSLGIILLEMFSGM---------KL-------KHTVRSQEWKAnssaiidhifaskaVVNAAipay 275
Cdd:cd14086 175 -LRKDPYGK-PVDIWACGVILYILLVGYppfwdedqhRLyaqikagAYDYPSPEWDT--------------VTPEA---- 234
                       170       180
                ....*....|....*....|....*...
gi 28467003 276 hlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14086 235 --KDLINQMLTVNPAKRITAAEALKHPW 260
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
27-304 1.15e-14

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: 73.84  E-value: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  27 SRLGSGSSASVYRVRccgNPGSPPG-ALKQF-LPPGTTGAAASAAeygfrKERAALEQLQG--HRNIVTLYGVFTIHFSP 102
Cdd:cd07863   6 AEIGVGAYGTVYKAR---DPHSGHFvALKSVrVQTNEDGLPLSTV-----REVALLKRLEAfdHPNIVRLMDVCATSRTD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 103 NVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGL-- 180
Cdd:cd07863  78 RETKVTLVFEHVDQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQV-KLADFGLar 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 181 --SFKEGNQDVkyIQTDGYRAPEAELQNCLAqaglqsdtectSAVDLWSLGIILLEMFSGMKL--KHTVRSQ-------- 248
Cdd:cd07863 157 iySCQMALTPV--VVTLWYRAPEVLLQSTYA-----------TPVDMWSVGCIFAEMFRRKPLfcGNSEADQlgkifdli 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 249 ------EWKANSSaIIDHIFASKAV--VNAAIPAYHLR--DLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07863 224 glppedDWPRDVT-LPRGAFSPRGPrpVQSVVPEIEESgaQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
140-304 1.23e-14

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: 73.46  E-value: 1.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENEC----FKLIDFGLSfKEGNQDVKYIQ-------TDGYRAPEAELQNCL 208
Cdd:cd13982 106 RQIASGLAHLHSLNIVHRDLKPQNILISTPNAHgnvrAMISDFGLC-KKLDVGRSSFSrrsgvagTSGWIAPEMLSGSTK 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 209 AQAglqsdtecTSAVDLWSLGIILLEMFSGMklKHTV-RSQEWKANssaIIDHIFASKAVVNAAIPAYHLRDLIKSMLHD 287
Cdd:cd13982 185 RRQ--------TRAVDIFSLGCVFYYVLSGG--SHPFgDKLEREAN---ILKGKYSLDKLLSLGEHGPEAQDLIERMIDF 251
                       170
                ....*....|....*..
gi 28467003 288 DPSRRIPAEMALCSPFF 304
Cdd:cd13982 252 DPEKRPSAEEVLNHPFF 268
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
86-310 1.24e-14

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: 74.74  E-value: 1.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIHFS-PNVPSRCLLLELLDVSVSELL-LYSSHQGCSMWMIQhcardVLEALAFLHHEGYVHADLKPRN 163
Cdd:cd07874  75 HKNIISLLNVFTPQKSlEEFQDVYLVMELMDANLCQVIqMELDHERMSYLLYQ-----MLCGIKHLHSAGIIHRDLKPSN 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 164 ILwsAENEC-FKLIDFGLSFKEGNQDV--KYIQTDGYRAPEAELqnclaQAGLQSDtectsaVDLWSLGIILLEM----- 235
Cdd:cd07874 150 IV--VKSDCtLKILDFGLARTAGTSFMmtPYVVTRYYRAPEVIL-----GMGYKEN------VDIWSVGCIMGEMvrhki 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 236 -FSG----------------------MKLKHTVRSQ-EWKANSSAII------DHIFASKAVVNaAIPAYHLRDLIKSML 285
Cdd:cd07874 217 lFPGrdyidqwnkvieqlgtpcpefmKKLQPTVRNYvENRPKYAGLTfpklfpDSLFPADSEHN-KLKASQARDLLSKML 295
                       250       260
                ....*....|....*....|....*
gi 28467003 286 HDDPSRRIPAEMALCSPFFSIPFAP 310
Cdd:cd07874 296 VIDPAKRISVDEALQHPYINVWYDP 320
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
21-304 1.32e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 75.07  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   21 RLWQVQSRLGSGSSASVYRVRCCGNpgSPPGALKQFLppgttgaaasaAEYGFRKERAALEQLQGHRNIVTLYGVF-TIH 99
Cdd:PTZ00036  66 KSYKLGNIIGNGSFGVVYEAICIDT--SEKVAIKKVL-----------QDPQYKNRELLIMKNLNHINIIFLKDYYyTEC 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  100 FSPNVPSRCL--LLELLDVSVSELLLYSS--HQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKL 175
Cdd:PTZ00036 133 FKKNEKNIFLnvVMEFIPQTVHKYMKHYArnNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLKL 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  176 IDFGlSFKE---GNQDVKYIQTDGYRAPEAELqnclaqaglqSDTECTSAVDLWSLGIILLEM------FSG-------- 238
Cdd:PTZ00036 213 CDFG-SAKNllaGQRSVSYICSRFYRAPELML----------GATNYTTHIDLWSLGCIIAEMilgypiFSGqssvdqlv 281
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003  239 --MKLKHTVRSQEWKANSSAIIDHIFAS------KAVVNAAIPAYHLrDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:PTZ00036 282 riIQVLGTPTEDQLKEMNPNYADIKFPDvkpkdlKKVFPKGTPDDAI-NFISQFLKYEPLKRLNPIEALADPFF 354
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
86-304 1.37e-14

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: 73.57  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGvfTIHFSPnvpSRCLLLELLDvsvSELLLYSSHQGCSMWMiqHCAR----DVLEALAFLHHEGYVHADLKP 161
Cdd:cd07844  57 HANIVTLHD--IIHTKK---TLTLVFEYLD---TDLKQYMDDCGGGLSM--HNVRlflfQLLRGLAYCHQRRVLHRDLKP 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 162 RNILWSAENEcFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd07844 127 QNLLISERGE-LKLADFGLARAKSVPSKTYsneVVTLWYRPPDV----------LLGSTEYSTSLDMWGVGCIFYEMATG 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 239 M-----------------KLKHTVRSQEWKANSS-----AIIDHIFASKAVVNAA-----IPayHLRDLIKSMLHDDPSR 291
Cdd:cd07844 196 RplfpgstdvedqlhkifRVLGTPTEETWPGVSSnpefkPYSFPFYPPRPLINHAprldrIP--HGEELALKFLQYEPKK 273
                       250
                ....*....|...
gi 28467003 292 RIPAEMALCSPFF 304
Cdd:cd07844 274 RISAAEAMKHPYF 286
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
27-237 1.44e-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: 73.57  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  27 SRLGSGSSASVYRvrCC-GNPGSPPG---ALKQFLPPGTTGAAAsaaeyGFRKERAALEQLQgHRNIVTLYGVFTihfSP 102
Cdd:cd05038  10 KQLGEGHFGSVEL--CRyDPLGDNTGeqvAVKSLQPSGEEQHMS-----DFKREIEILRTLD-HEYIVKYKGVCE---SP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 103 NVPSRCLLLELLDV-SVSELLLYSSHQGCSMWMIQHcARDVLEALAFLHHEGYVHADLKPRNILWSAENeCFKLIDFGLS 181
Cdd:cd05038  79 GRRSLRLIMEYLPSgSLRDYLQRHRDQIDLKRLLLF-ASQICKGMEYLGSQRYIHRDLAARNILVESED-LVKISDFGLA 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28467003 182 -FKEGNQDVKYIQTDG-----YRAPEaelqnCLaqaglqSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05038 157 kVLPEDKEYYYVKEPGespifWYAPE-----CL------RESRFSSASDVWSFGVTLYELFT 207
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
23-303 1.79e-14

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: 72.82  E-value: 1.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVRCCGNpgsppG---ALKQfLPPGTTGAAASAAEYGFRKERAALEQLQgHRNIVTLYGVFTIH 99
Cdd:cd06632   2 WQKGQLLGSGSFGSVYEGFNGDT-----GdffAVKE-VSLVDDDKKSRESVKQLEQEIALLSKLR-HPNIVQYYGTEREE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 100 fspnvPSRCLLLELldVSVSELL-LYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDF 178
Cdd:cd06632  75 -----DNLYIFLEY--VPGGSIHkLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGV-VKLADF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 179 GLSFK-EGNQDVKYIQTDGY-RAPEAeLQNCLAQAGLqsdtectsAVDLWSLGIILLEMFSGmklkhtvrSQEWKANSS- 255
Cdd:cd06632 147 GMAKHvEAFSFAKSFKGSPYwMAPEV-IMQKNSGYGL--------AVDIWSLGCTVLEMATG--------KPPWSQYEGv 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 28467003 256 AIIDHIFASKAVvnAAIPAyHL----RDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd06632 210 AAIFKIGNSGEL--PPIPD-HLspdaKDFIRLCLQRDPEDRPTASQLLEHPF 258
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
134-238 1.93e-14

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: 73.18  E-value: 1.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKE----GNQDVKYIQ-TDGYRAPEAelqncl 208
Cdd:cd06629 109 LVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGIC-KISDFGISKKSddiyGNNGATSMQgSVFWMAPEV------ 181
                        90       100       110
                ....*....|....*....|....*....|.
gi 28467003 209 aqagLQSDTECTSA-VDLWSLGIILLEMFSG 238
Cdd:cd06629 182 ----IHSQGQGYSAkVDIWSLGCVVLEMLAG 208
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
29-292 1.98e-14

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


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 73.08  E-value: 1.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCcgNPGSPpGALKQFlppGTTGAAASAAEygFRKERAALEQLQgHRNIVTLYGvftIHFSPNvpSRC 108
Cdd:cd14066   1 IGSGGFGTVYKGVL--ENGTV-VAVKRL---NEMNCAASKKE--FLTELEMLGRLR-HPNLVRLLG---YCLESD--EKL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 109 LLLELLDV-SVSELLlySSHQGCSM--W-MIQHCARDVLEALAFLHHEGY---VHADLKPRNILWSAENECfKLIDFGLS 181
Cdd:cd14066  67 LVYEYMPNgSLEDRL--HCHKGSPPlpWpQRLKIAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEP-KLTDFGLA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 182 -----FKEGNQDVKYIQTDGYRAPEAELQNCLaqaglqsdtecTSAVDLWSLGIILLEMFSGMKLKHTVRS--------- 247
Cdd:cd14066 144 rlippSESVSKTSAVKGTIGYLAPEYIRTGRV-----------STKSDVYSFGVVLLELLTGKPAVDENREnasrkdlve 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 248 ---QEWKANSSAIIDhIFASKAVVnaaipayHLRDLIKSML-------HDDPSRR 292
Cdd:cd14066 213 wveSKGKEELEDILD-KRLVDDDG-------VEEEEVEALLrlallctRSDPSLR 259
RRM3_RBM39_like cd12285
RNA recognition motif 3 (RRM3) found in vertebrate RNA-binding protein 39 (RBM39) and similar ...
348-405 2.26e-14

RNA recognition motif 3 (RRM3) found in vertebrate RNA-binding protein 39 (RBM39) and similar proteins; This subfamily corresponds to the RRM3 of RBM39, also termed hepatocellular carcinoma protein 1, or RNA-binding region-containing protein 2, or splicing factor HCC1, ia nuclear autoantigen that contains an N-terminal arginine/serine rich (RS) motif and three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). An octapeptide sequence called the RS-ERK motif is repeated six times in the RS region of RBM39. Based on the specific domain composition, RBM39 has been classified into a family of non-snRNP (small nuclear ribonucleoprotein) splicing factors that are usually not complexed to snRNAs.


Pssm-ID: 409727 [Multi-domain]  Cd Length: 85  Bit Score: 67.96  E-value: 2.26e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 348 KEECQKYGPVVSLLVPKENPgRGQVFVEYANAGDSKAAQKLLTGRMFDGKFVVATFYP 405
Cdd:cd12285  29 IEECSKYGPVLHIYVDKNSP-QGNVYVKFKTIEAAQKCVQAMNGRWFDGRQITAAYVP 85
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
140-302 2.37e-14

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: 72.42  E-value: 2.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFK-EGNQDvKYIQT----DGYRAPEAelqnclaqagLQ 214
Cdd:cd14078 108 RQIVSAVAYVHSQGYAHRDLKPENLLLD-EDQNLKLIDFGLCAKpKGGMD-HHLETccgsPAYAAPEL----------IQ 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 SDTECTSAVDLWSLGIILLEMFSG---------MKLKHTVRS-----QEWKANSSaiidhifaskavvnaaipayhlRDL 280
Cdd:cd14078 176 GKPYIGSEADVWSMGVLLYALLCGflpfdddnvMALYRKIQSgkyeePEWLSPSS----------------------KLL 233
                       170       180
                ....*....|....*....|..
gi 28467003 281 IKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd14078 234 LDQMLQVDPKKRITVKELLNHP 255
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
75-304 2.44e-14

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 72.95  E-value: 2.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQGHRNIVTLYGVFTIHFSPNvPSRCLLLELLDVSVSELL-LY--SSHQGCSMWMIQHCARDVLEALAFLHH 151
Cdd:cd07837  49 REVSLLQMLSQSIYIVRLLDVEHVEENGK-PLLYLVFEYLDTDLKKFIdSYgrGPHNPLPAKTIQSFMYQLCKGVAHCHS 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EGYVHADLKPRNILWSAENECFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSL 228
Cdd:cd07837 128 HGVMHRDLKPQNLLVDKQKGLLKIADLGLGRAFTIPIKSYtheIVTLWYRAPEV----------LLGSTHYSTPVDMWSV 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 229 GIILLEM------FSG----------MKLKHTVRSQEWKANSSAIIDHIFAS--KAVVNAAIPAY--HLRDLIKSMLHDD 288
Cdd:cd07837 198 GCIFAEMsrkqplFPGdselqqllhiFRLLGTPNEEVWPGVSKLRDWHEYPQwkPQDLSRAVPDLepEGVDLLTKMLAYD 277
                       250
                ....*....|....*.
gi 28467003 289 PSRRIPAEMALCSPFF 304
Cdd:cd07837 278 PAKRISAKAALQHPYF 293
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
108-304 2.44e-14

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 73.51  E-value: 2.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILW------------------SAE 169
Cdd:cd14215  91 CISFELLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekkrderSVK 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 170 NECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQnclaqagLQSDTECtsavDLWSLGIILLEMFSGMKLKHT----- 244
Cdd:cd14215 171 STAIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILE-------LGWSQPC----DVWSIGCIIFEYYVGFTLFQThdnre 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 245 -------------------VRSQ--------EWKANSSA---IIDHIFASKAVVNAAIPAYH-LRDLIKSMLHDDPSRRI 293
Cdd:cd14215 240 hlammerilgpipsrmirkTRKQkyfyhgrlDWDENTSAgryVRENCKPLRRYLTSEAEEHHqLFDLIESMLEYEPSKRL 319
                       250
                ....*....|.
gi 28467003 294 PAEMALCSPFF 304
Cdd:cd14215 320 TLAAALKHPFF 330
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
86-305 2.47e-14

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: 73.55  E-value: 2.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFtihfSPNVPsrclLLELLDVSV------SEL--LLYSShQGCSMWMIQHCARDVLEALAFLHHEGYVHA 157
Cdd:cd07855  63 HDNIIAIRDIL----RPKVP----YADFKDVYVvldlmeSDLhhIIHSD-QPLTLEHIRYFLYQLLRGLKYIHSANVIHR 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 158 DLKPRNILWSaENECFKLIDFGL-----SFKEGNQD--VKYIQTDGYRAPEAELqnclaqaglqSDTECTSAVDLWSLGI 230
Cdd:cd07855 134 DLKPSNLLVN-ENCELKIGDFGMarglcTSPEEHKYfmTEYVATRWYRAPELML----------SLPEYTQAIDMWSVGC 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 231 ILLEM------FSG------MKLKHTVRSQEwkanSSAIIDHI-----------FASKAVV--NAAIPAY--HLRDLIKS 283
Cdd:cd07855 203 IFAEMlgrrqlFPGknyvhqLQLILTVLGTP----SQAVINAIgadrvrryiqnLPNKQPVpwETLYPKAdqQALDLLSQ 278
                       250       260
                ....*....|....*....|..
gi 28467003 284 MLHDDPSRRIPAEMALCSPFFS 305
Cdd:cd07855 279 MLRFDPSERITVAEALQHPFLA 300
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
86-304 2.89e-14

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: 72.20  E-value: 2.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFtiHFSPNVpsrCLLLELL-DVSVSELLL---YSSHQGCSMWMIQhcardVLEALAFLHHEGYVHADLKP 161
Cdd:cd14099  60 HPNIVKFHDCF--EDEENV---YILLELCsNGSLMELLKrrkALTEPEVRYFMRQ-----ILSGVKYLHSNRIIHRDLKL 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 162 RNILWSAENEcFKLIDFGLSFKegnqdvkyIQTDG-----------YRAPEAelqnclaqagLQSDTECTSAVDLWSLGI 230
Cdd:cd14099 130 GNLFLDENMN-VKIGDFGLAAR--------LEYDGerkktlcgtpnYIAPEV----------LEKKKGHSFEVDIWSLGV 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 231 ILLEM------FSGMKLKHTVRsqEWKANSSAIIDHIFASKAvvnaaipayhLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14099 191 ILYTLlvgkppFETSDVKETYK--RIKKNEYSFPSHLSISDE----------AKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
80-304 3.26e-14

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: 72.40  E-value: 3.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  80 LEQLQgHRNIVTLYGVF----TIHfspnvpsrcLLLELLDVSV-SELLLYSshQGCSMWMIQHCARDVLEALAFLHHEGY 154
Cdd:cd07847  54 LKQLK-HPNLVNLIEVFrrkrKLH---------LVFEYCDHTVlNELEKNP--RGVPEHLIKKIIWQTLQAVNFCHKHNC 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNILWSAENEcFKLIDFG----LSFKEGNQDvKYIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGI 230
Cdd:cd07847 122 IHRDVKPENILITKQGQ-IKLCDFGfariLTGPGDDYT-DYVATRWYRAPEL----------LVGDTQYGPPVDVWAIGC 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 231 ILLEMFSGMKLkhtvrsqeWKANSSaiIDHIFASKAVVNAAIP---------------------------------AYHL 277
Cdd:cd07847 190 VFAELLTGQPL--------WPGKSD--VDQLYLIRKTLGDLIPrhqqifstnqffkglsipepetrepleskfpniSSPA 259
                       250       260
                ....*....|....*....|....*..
gi 28467003 278 RDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07847 260 LSFLKGCLQMDPTERLSCEELLEHPYF 286
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
75-303 3.32e-14

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: 72.36  E-value: 3.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELldVSVSELLLY-SSHQGCSMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd14194  57 REVSILKEIQ-HPNVITLHEVYE-----NKTDVILILEL--VAGGELFDFlAEKESLTEEEATEFLKQILNGVYYLHSLQ 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWSAEN---ECFKLIDFGLSFK--EGNQDVKYIQTDGYRAPEAELQNCLaqaGLQSdtectsavDLWSL 228
Cdd:cd14194 129 IAHFDLKPENIMLLDRNvpkPRIKIIDFGLAHKidFGNEFKNIFGTPEFVAPEIVNYEPL---GLEA--------DMWSI 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 229 GIILLEMFSGMKLKHTVRSQEWKANSSAiIDHIFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14194 198 GVITYILLSGASPFLGDTKQETLANVSA-VNYEFEDEYFSNTSALA---KDFIRRLLVKDPKKRMTIQDSLQHPW 268
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
70-305 3.75e-14

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: 71.98  E-value: 3.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  70 EYGFRKERAALEQLQgHRNIVTLYGVFTI--HFSpnvpsrcLLLELldVSVSELL-------LYSSHQGCSMwmiqhcAR 140
Cdd:cd14167  45 ETSIENEIAVLHKIK-HPNIVALDDIYESggHLY-------LIMQL--VSGGELFdrivekgFYTERDASKL------IF 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSAENECFKLI--DFGLSFKEGNQDVKYIQ--TDGYRAPEAelqncLAQAGLqsd 216
Cdd:cd14167 109 QILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMisDFGLSKIEGSGSVMSTAcgTPGYVAPEV-----LAQKPY--- 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 tecTSAVDLWSLGIILLEMFSG---------MKLKHTVRSQEWKANSSAIIDhifaskaVVNAAipayhlRDLIKSMLHD 287
Cdd:cd14167 181 ---SKAVDCWSIGVIAYILLCGyppfydendAKLFEQILKAEYEFDSPYWDD-------ISDSA------KDFIQHLMEK 244
                       250
                ....*....|....*...
gi 28467003 288 DPSRRIPAEMALCSPFFS 305
Cdd:cd14167 245 DPEKRFTCEQALQHPWIA 262
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
75-303 4.33e-14

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: 72.45  E-value: 4.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQGHRNIVTLygvftIHFSPNVPSRCLLLELLdvSVSELLLYSSHQGCsmwMIQHCA----RDVLEALAFLH 150
Cdd:cd14090  48 REVETLHQCQGHPNILQL-----IEYFEDDERFYLVFEKM--RGGPLLSHIEKRVH---FTEQEAslvvRDIASALDFLH 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSAENEC--FKLIDFGLS--FKEGNQDVKYIQTDG---------YRAPEAeLQNCLAQAgLQSDT 217
Cdd:cd14090 118 DKGIAHRDLKPENILCESMDKVspVKICDFDLGsgIKLSSTSMTPVTTPElltpvgsaeYMAPEV-VDAFVGEA-LSYDK 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 218 ECtsavDLWSLGIILLEMFSGMK--LKHTVRSQEWK--ANSSAIIDHIFAS-------------KAVVNAAipayhlRDL 280
Cdd:cd14090 196 RC----DLWSLGVILYIMLCGYPpfYGRCGEDCGWDrgEACQDCQELLFHSiqegeyefpekewSHISAEA------KDL 265
                       250       260
                ....*....|....*....|...
gi 28467003 281 IKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14090 266 ISHLLVRDASQRYTAEQVLQHPW 288
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
86-305 4.44e-14

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: 71.47  E-value: 4.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIhfspnvpSRCLLL--ELLDV-SVSELLLYSSHQgCSMWMIQHCARDVLEALAFLHHEGYVHADLKPR 162
Cdd:cd06614  55 HPNIVDYYDSYLV-------GDELWVvmEYMDGgSLTDIITQNPVR-MNESQIAYVCREVLQGLEYLHSQNVIHRDIKSD 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 163 NILWSAENECfKLIDFG----LSfKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEM--- 235
Cdd:cd06614 127 NILLSKDGSV-KLADFGfaaqLT-KEKSKRNSVVGTPYWMAPE-----------VIKRKDYGPKVDIWSLGIMCIEMaeg 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 236 ------FSGMKlkhtvrsqewkanssaiidhifASKAVVNAAIPAYH--------LRDLIKSMLHDDPSRRIPAEMALCS 301
Cdd:cd06614 194 eppyleEPPLR----------------------ALFLITTKGIPPLKnpekwspeFKDFLNKCLVKDPEKRPSAEELLQH 251

                ....
gi 28467003 302 PFFS 305
Cdd:cd06614 252 PFLK 255
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
134-304 4.54e-14

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: 72.26  E-value: 4.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQhcardVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKYIQ---TDGYRAPEAelqnclaq 210
Cdd:cd07843 112 MLQ-----LLSGVAHLHDNWILHRDLKTSNLLLNNRGI-LKICDFGLAREYGSPLKPYTQlvvTLWYRAPEL-------- 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 211 agLQSDTECTSAVDLWSLGIILLEM------FSG----------MKLKHTVRSQEWKANSS--AIIDHIFASKAVVN--A 270
Cdd:cd07843 178 --LLGAKEYSTAIDMWSVGCIFAELltkkplFPGkseidqlnkiFKLLGTPTEKIWPGFSElpGAKKKTFTKYPYNQlrK 255
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 28467003 271 AIPAYHLR----DLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07843 256 KFPALSLSdngfDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
86-304 4.72e-14

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: 72.13  E-value: 4.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVftIHFSPNVpsrCLLLELLDVSVSELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHEGYVHADLKPRNI 164
Cdd:cd07836  57 HENIVRLHDV--IHTENKL---MLVFEYMDKDLKKYMDTHGVRGAlDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNL 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 165 LWSAENEcFKLIDFGLSFKEG---NQDVKYIQTDGYRAPEAElqnclaqagLQSDTECTSaVDLWSLGIILLEMFSG--- 238
Cdd:cd07836 132 LINKRGE-LKLADFGLARAFGipvNTFSNEVVTLWYRAPDVL---------LGSRTYSTS-IDIWSVGCIMAEMITGrpl 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 239 -------------MKLKHTVRSQEWK--ANSSAI-IDHIFASKAVVNAAIPAYH--LRDLIKSMLHDDPSRRIPAEMALC 300
Cdd:cd07836 201 fpgtnnedqllkiFRIMGTPTESTWPgiSQLPEYkPTFPRYPPQDLQQLFPHADplGIDLLHRLLQLNPELRISAHDALQ 280

                ....
gi 28467003 301 SPFF 304
Cdd:cd07836 281 HPWF 284
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
140-303 5.52e-14

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: 71.35  E-value: 5.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVK-YIQTDGYRAPEaelqnclaqagLQSDTE 218
Cdd:cd14007 107 YQLALALDYLHSKNIIHRDIKPENILLGSNGEL-KLADFGWSVHAPSNRRKtFCGTLDYLPPE-----------MVEGKE 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 219 CTSAVDLWSLGIILLEMFSG---------MKLKHTVRSQEWKanssaIIDHIfaSKAvvnaaipayhLRDLIKSMLHDDP 289
Cdd:cd14007 175 YDYKVDIWSLGVLCYELLVGkppfeskshQETYKRIQNVDIK-----FPSSV--SPE----------AKDLISKLLQKDP 237
                       170
                ....*....|....
gi 28467003 290 SRRIPAEMALCSPF 303
Cdd:cd14007 238 SKRLSLEQVLNHPW 251
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
75-303 5.61e-14

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 71.57  E-value: 5.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELldVSVSELL-LYSSHQGCSMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd14195  57 REVNILREIQ-HPNIITLHDIFE-----NKTDVVLILEL--VSGGELFdFLAEKESLTEEEATQFLKQILDGVHYLHSKR 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILW---SAENECFKLIDFGLSFK--EGNQDVKYIQTDGYRAPEAELQNCLaqaGLQSdtectsavDLWSL 228
Cdd:cd14195 129 IAHFDLKPENIMLldkNVPNPRIKLIDFGIAHKieAGNEFKNIFGTPEFVAPEIVNYEPL---GLEA--------DMWSI 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 229 GIILLEMFSGMKLKHTVRSQEWKANSSAiIDHIFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14195 198 GVITYILLSGASPFLGETKQETLTNISA-VNYDFDEEYFSNTSELA---KDFIRRLLVKDPKKRMTIAQSLEHSW 268
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-302 6.86e-14

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: 71.25  E-value: 6.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQgHRNIVTLYGVFtihfspNVPSRC-LLLELldVSVSELLLYSSHQGC------SmwmiqHCARDVLEALAF 148
Cdd:cd14083  51 EIAVLRKIK-HPNIVQLLDIY------ESKSHLyLVMEL--VTGGELFDRIVEKGSytekdaS-----HLIRQVLEAVDY 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAENECFKLI--DFGLSFKEGNQDVKY-IQTDGYRAPEAelqncLAQAGLqsdtecTSAVDL 225
Cdd:cd14083 117 LHSLGIVHRDLKPENLLYYSPDEDSKIMisDFGLSKMEDSGVMSTaCGTPGYVAPEV-----LAQKPY------GKAVDC 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 226 WSLGI---ILL------------EMFSG-MKLKHTVRSQEWkanssaiiDHIFASKavvnaaipayhlRDLIKSMLHDDP 289
Cdd:cd14083 186 WSIGVisyILLcgyppfydendsKLFAQiLKAEYEFDSPYW--------DDISDSA------------KDFIRHLMEKDP 245
                       250
                ....*....|...
gi 28467003 290 SRRIPAEMALCSP 302
Cdd:cd14083 246 NKRYTCEQALEHP 258
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
29-240 7.53e-14

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: 71.53  E-value: 7.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASV-YRVRCCGNPGsppgALKQF----LPPGTTGAAASAAEY-----------GFRKERAALEQLQgHRNIVTL 92
Cdd:cd14067   1 LGQGGSGTViYRARYQGQPV----AVKRFhikkCKKRTDGSADTMLKHlraadamknfsEFRQEASMLHSLQ-HPCIVYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  93 YGVftihfspNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQH-----CARDVLEALAFLHHEGYVHADLKPRNIL-W 166
Cdd:cd14067  76 IGI-------SIHPLCFALELAPLGSLNTVLEENHKGSSFMPLGHmltfkIAYQIAAGLAYLHKKNIIFCDLKSDNILvW 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 167 S---AENECFKLIDFGL---SFKEGNQDVKyiQTDGYRAPEaelqnclAQAGLQSDTEctsaVDLWSLGIILLEMFSGMK 240
Cdd:cd14067 149 SldvQEHINIKLSDYGIsrqSFHEGALGVE--GTPGYQAPE-------IRPRIVYDEK----VDMFSYGMVLYELLSGQR 215
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
52-239 7.72e-14

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: 71.20  E-value: 7.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  52 ALKQFLPPGTTgaaasaaEYGFRKERAALEQLQGHRNIVTLYG---------VFTIHFSP------NVPSRclllelldV 116
Cdd:cd13987  22 ALKFVPKPSTK-------LKDFLREYNISLELSVHPHIIKTYDvafetedyyVFAQEYAPygdlfsIIPPQ--------V 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 117 SVSELllysshqgcsmwMIQHCARDVLEALAFLHHEGYVHADLKPRNILWsAENEC--FKLIDFGLSFKEGNQdVKYIQ- 193
Cdd:cd13987  87 GLPEE------------RVKRCAAQLASALDFMHSKNLVHRDIKPENVLL-FDKDCrrVKLCDFGLTRRVGST-VKRVSg 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 28467003 194 TDGYRAPEaelqncLAQAGLQSDTECTSAVDLWSLGIILLEMFSGM 239
Cdd:cd13987 153 TIPYTAPE------VCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGN 192
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
72-303 8.50e-14

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


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 70.85  E-value: 8.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  72 GFRKE----RAALEQLQG--HRNIVTLYGvFTI--HFSPNVPSRCLLLELLDV-SVSELLlyssHQGCS-------MWMI 135
Cdd:cd14012  37 NGKKQiqllEKELESLKKlrHPNLVSYLA-FSIerRGRSDGWKVYLLTEYAPGgSLSELL----DSVGSvpldtarRWTL 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 136 QhcardVLEALAFLHHEGYVHADLKPRNILWSAENECF--KLIDFGLSFK----EGNQDVKYIQTDGYRAPEaelqncLA 209
Cdd:cd14012 112 Q-----LLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGivKLTDYSLGKTlldmCSRGSLDEFKQTYWLPPE------LA 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 210 QAGLqSDTECTsavDLWSLGIILLEMFSGmklKHTVrsqEWKANSSAIIdhifaskavVNAAIPAyHLRDLIKSMLHDDP 289
Cdd:cd14012 181 QGSK-SPTRKT---DVWDLGLLFLQMLFG---LDVL---EKYTSPNPVL---------VSLDLSA-SLQDFLSKCLSLDP 240
                       250
                ....*....|....
gi 28467003 290 SRRIPAEMALCSPF 303
Cdd:cd14012 241 KKRPTALELLPHEF 254
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
29-292 8.74e-14

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: 71.11  E-value: 8.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCCGNPGsppgALKQF--LPPGTTGAAASAAEYG-------------FRKERAALEQLQgHRNIVTLY 93
Cdd:cd14000   2 LGDGGFGSVYRASYKGEPV----AVKIFnkHTSSNFANVPADTMLRhlratdamknfrlLRQELTVLSHLH-HPSIVYLL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  94 GVfTIHfspnvpSRCLLLELLDV-SVSELLLYSSHQGCSMW-MIQH-CARDVLEALAFLHHEGYVHADLKPRNIL-WS-- 167
Cdd:cd14000  77 GI-GIH------PLMLVLELAPLgSLDHLLQQDSRSFASLGrTLQQrIALQVADGLRYLHSAMIIYRDLKSHNVLvWTly 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 168 -AENECFKLIDFGLS---FKEGNQDVKyiQTDGYRAPEAELQNclaqaglqsdTECTSAVDLWSLGIILLEMFSGMK--L 241
Cdd:cd14000 150 pNSAIIIKIADYGISrqcCRMGAKGSE--GTPGFRAPEIARGN----------VIYNEKVDVFSFGMLLYEILSGGApmV 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 28467003 242 KHtVRSQEWKANSSAIIDHIFASKAVvnaaiPAYHLRDLIKSMLHDDPSRR 292
Cdd:cd14000 218 GH-LKFPNEFDIHGGLRPPLKQYECA-----PWPEVEVLMKKCWKENPQQR 262
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
20-305 1.04e-13

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: 71.22  E-value: 1.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  20 GRLWQVQSRLGSGSSASVYRVRccgnpGSPPGALkqflppGTTGAAASAAEYGFRKERAALEQLQ--GHRNIVTLYGVF- 96
Cdd:cd06644  11 NEVWEIIGELGDGAFGKVYKAK-----NKETGAL------AAAKVIETKSEEELEDYMVEIEILAtcNHPYIVKLLGAFy 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  97 -------TIHFSPNVPSRCLLLELldvsvselllyssHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAE 169
Cdd:cd06644  80 wdgklwiMIEFCPGGAVDAIMLEL-------------DRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 170 NEcFKLIDFGLSFKEGNQDVK---YIQTDGYRAPEAELQNCLaqaglqSDTECTSAVDLWSLGIILLEMFSGMKLKHTVr 246
Cdd:cd06644 147 GD-IKLADFGVSAKNVKTLQRrdsFIGTPYWMAPEVVMCETM------KDTPYDYKADIWSLGITLIEMAQIEPPHHEL- 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28467003 247 sqewkaNSSAIIDHIFASK--AVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFFS 305
Cdd:cd06644 219 ------NPMRVLLKIAKSEppTLSQPSKWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVS 273
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
75-304 1.16e-13

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: 71.15  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVftIHFSPNVpsrCLLLELLDVSVSELLlySSHQG------CSMWMIQhcardVLEALAF 148
Cdd:cd07870  47 REASLLKGLK-HANIVLLHDI--IHTKETL---TFVFEYMHTDLAQYM--IQHPGglhpynVRLFMFQ-----LLRGLAY 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDL 225
Cdd:cd07870 114 IHGQHILHRDLKPQNLLISYLGE-LKLADFGLARAKSIPSQTYsseVVTLWYRPPDV----------LLGATDYSSALDI 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 226 WSLGIILLEMFSGMKLKHTVRS------------------------------QEWKANSSAIIDHIfaskaVVNAAIPAY 275
Cdd:cd07870 183 WGAGCIFIEMLQGQPAFPGVSDvfeqlekiwtvlgvptedtwpgvsklpnykPEWFLPCKPQQLRV-----VWKRLSRPP 257
                       250       260
                ....*....|....*....|....*....
gi 28467003 276 HLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07870 258 KAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
75-304 1.18e-13

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 70.91  E-value: 1.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFT----IHfspnvpsrcLLLELLDVSV-SELLLYSShqGCSMWMIQHCARDVLEALAFL 149
Cdd:cd07846  49 REIKMLKQLR-HENLVNLIEVFRrkkrWY---------LVFEFVDHTVlDDLEKYPN--GLDESRVRKYLFQILRGIDFC 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 150 HHEGYVHADLKPRNILWSaENECFKLIDFGLS-FKEGNQDV--KYIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLW 226
Cdd:cd07846 117 HSHNIIHRDIKPENILVS-QSGVVKLCDFGFArTLAAPGEVytDYVATRWYRAPEL----------LVGDTKYGKAVDVW 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 227 SLGIILLEMFSGM----------KLKHTVRSQewkANSSAIIDHIFASKAV--------VNAAIPAYH--------LRDL 280
Cdd:cd07846 186 AVGCLVTEMLTGEplfpgdsdidQLYHIIKCL---GNLIPRHQELFQKNPLfagvrlpeVKEVEPLERrypklsgvVIDL 262
                       250       260
                ....*....|....*....|....
gi 28467003 281 IKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07846 263 AKKCLHIDPDKRPSCSELLHHEFF 286
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
86-310 1.29e-13

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: 71.60  E-value: 1.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIHFS-PNVPSRCLLLELLDVSVSELL-LYSSHQGCSMWMIQhcardVLEALAFLHHEGYVHADLKPRN 163
Cdd:cd07876  79 HKNIISLLNVFTPQKSlEEFQDVYLVMELMDANLCQVIhMELDHERMSYLLYQ-----MLCGIKHLHSAGIIHRDLKPSN 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 164 ILwsAENEC-FKLIDFGLSFKEGNQDV--KYIQTDGYRAPEAELqnclaqaGLQSDTEctsaVDLWSLGIILLEMFSG-M 239
Cdd:cd07876 154 IV--VKSDCtLKILDFGLARTACTNFMmtPYVVTRYYRAPEVIL-------GMGYKEN----VDIWSVGCIMGELVKGsV 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 240 KLKHTVRSQEWkansSAIIDHIFASKAVVNAAI-----------PAYH--------------------------LRDLIK 282
Cdd:cd07876 221 IFQGTDHIDQW----NKVIEQLGTPSAEFMNRLqptvrnyvenrPQYPgisfeelfpdwifpseserdklktsqARDLLS 296
                       250       260
                ....*....|....*....|....*...
gi 28467003 283 SMLHDDPSRRIPAEMALCSPFFSIPFAP 310
Cdd:cd07876 297 KMLVIDPDKRISVDEALRHPYITVWYDP 324
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
80-238 1.31e-13

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: 70.33  E-value: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  80 LEQLQgHRNIVTLYGVFTIHFSPNVpsrclLLE------LLDV-----SVSELLlysshqgCSMWMIQhcardVLEALAF 148
Cdd:cd06627  53 LKKLN-HPNIVKYIGSVKTKDSLYI-----ILEyvengsLASIikkfgKFPESL-------VAVYIYQ-----VLEGLAY 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAENECfKLIDFGLSFK---EGNQDVKYIQTDGYRAPEA-ELQNclaqaglqsdteCTSAVD 224
Cdd:cd06627 115 LHEQGVIHRDIKGANILTTKDGLV-KLADFGVATKlneVEKDENSVVGTPYWMAPEViEMSG------------VTTASD 181
                       170
                ....*....|....
gi 28467003 225 LWSLGIILLEMFSG 238
Cdd:cd06627 182 IWSVGCTVIELLTG 195
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
75-303 1.70e-13

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: 70.60  E-value: 1.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFT-----IHFSPNVPSRCLLLELLDVSV-----SELLLYSSHQGCSMWmiqhcaRDVLE 144
Cdd:cd07864  55 REIKILRQLN-HRSVVNLKEIVTdkqdaLDFKKDKGAFYLVFEYMDHDLmglleSGLVHFSEDHIKSFM------KQLLE 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLS-FKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECT 220
Cdd:cd07864 128 GLNYCHKKNFLHRDIKCSNILLNNKGQ-IKLADFGLArLYNSEESRPYtnkVITLWYRPPEL----------LLGEERYG 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 221 SAVDLWSLGIILLEMFsgmklkhtVRSQEWKANSS----AIIDHIFASKAVVN----AAIPAYH-----------LR--- 278
Cdd:cd07864 197 PAIDVWSCGCILGELF--------TKKPIFQANQElaqlELISRLCGSPCPAVwpdvIKLPYFNtmkpkkqyrrrLReef 268
                       250       260       270
                ....*....|....*....|....*....|...
gi 28467003 279 --------DLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd07864 269 sfiptpalDLLDHMLTLDPSKRCTAEQALNSPW 301
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
73-235 1.86e-13

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: 70.65  E-value: 1.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQGHRNIVTLYGVFTIHfSPNVPSrcLLLELLDvSVSELLLYSShqgCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14132  59 IKREIKILQNLRGGPNIVKLLDVVKDP-QSKTPS--LIFEYVN-NTDFKTLYPT---LTDYDIRYYMYELLKALDYCHSK 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAENECFKLIDFGLS-F----KEGNQDV--KYiqtdgYRAPEaelqnclaqagLQSDTEC-TSAVD 224
Cdd:cd14132 132 GIMHRDVKPHNIMIDHEKRKLRLIDWGLAeFyhpgQEYNVRVasRY-----YKGPE-----------LLVDYQYyDYSLD 195
                       170
                ....*....|.
gi 28467003 225 LWSLGIILLEM 235
Cdd:cd14132 196 MWSLGCMLASM 206
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
75-308 2.49e-13

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: 69.32  E-value: 2.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYgvftiHFSPNVPSRCLLLELLDVSvsELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd14120  41 KEIKILKELS-HENVVALL-----DCQETSSSVYLVMEYCNGG--DLADYLQAKGTlSEDTIRVFLQQIAAAMKALHSKG 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWSAENEC--------FKLIDFGLSfkegnqdvKYIQTDG----------YRAPEAelqnclaqagLQS 215
Cdd:cd14120 113 IVHRDLKPQNILLSHNSGRkpspndirLKIADFGFA--------RFLQDGMmaatlcgspmYMAPEV----------IMS 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 216 DTECTSAvDLWSLGIILLEMFSGmklkhtvrSQEWKANSSAIIDHIFASKAVVNAAIPAY---HLRDLIKSMLHDDPSRR 292
Cdd:cd14120 175 LQYDAKA-DLWSIGTIVYQCLTG--------KAPFQAQTPQELKAFYEKNANLRPNIPSGtspALKDLLLGLLKRNPKDR 245
                       250
                ....*....|....*.
gi 28467003 293 IPAEmalcsPFFSIPF 308
Cdd:cd14120 246 IDFE-----DFFSHPF 256
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
145-293 2.58e-13

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: 69.59  E-value: 2.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAelqncLAQAGLqsdtecTSA 222
Cdd:cd05578 112 ALDYLHSKNIIHRDIKPDNILLDEQGHV-HITDFNIAtkLTDGTLATSTSGTKPYMAPEV-----FMRAGY------SFA 179
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 223 VDLWSLGIILLEMFSGMKlkhtvrsqEWKANSSAIIDHIFASKAVVNAAIPAYH---LRDLIKSMLHDDPSRRI 293
Cdd:cd05578 180 VDWWSLGVTAYEMLRGKR--------PYEIHSRTSIEEIRAKFETASVLYPAGWseeAIDLINKLLERDPQKRL 245
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
134-292 2.92e-13

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: 69.44  E-value: 2.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL--SFKEGNQDVKYIQTDGYRAPEaelqnclaQA 211
Cdd:cd14047 118 LALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK-VKIGDFGLvtSLKNDGKRTKSKGTLSYMSPE--------QI 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 212 GLQS-DTEctsaVDLWSLGIILLEMFSGMKlKHTVRSQEWKANSSAIIDHIFASKavvnaaipaYHLRD-LIKSMLHDDP 289
Cdd:cd14047 189 SSQDyGKE----VDIYALGLILFELLHVCD-SAFEKSKFWTDLRNGILPDIFDKR---------YKIEKtIIKKMLSKKP 254

                ...
gi 28467003 290 SRR 292
Cdd:cd14047 255 EDR 257
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
75-304 3.00e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 69.85  E-value: 3.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   75 KERAALEQLQgHRNIVTLYGVftIHfspnvPSRCLLL--ELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:PLN00009  50 REISLLKEMQ-HGNIVRLQDV--VH-----SEKRLYLvfEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  153 GYVHADLKPRNILWSAENECFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAELQNClaqaglqsdtECTSAVDLWSLG 229
Cdd:PLN00009 122 RVLHRDLKPQNLLIDRRTNALKLADFGLARAFGIPVRTFtheVVTLWYRAPEILLGSR----------HYSTPVDIWSVG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  230 IILLEM------FSG----------MKLKHTVRSQEWkANSSAIIDHIFA----SKAVVNAAIPAYHLR--DLIKSMLHD 287
Cdd:PLN00009 192 CIFAEMvnqkplFPGdseidelfkiFRILGTPNEETW-PGVTSLPDYKSAfpkwPPKDLATVVPTLEPAgvDLLSKMLRL 270
                        250
                 ....*....|....*..
gi 28467003  288 DPSRRIPAEMALCSPFF 304
Cdd:PLN00009 271 DPSKRITARAALEHEYF 287
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-305 3.79e-13

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: 69.15  E-value: 3.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQgHRNIVTLYGVFtihfspNVPSRCLLL-------ELLDvSVSELLLYSSHQGcsmwmiQHCARDVLEALAF 148
Cdd:cd14169  51 EIAVLRRIN-HENIVSLEDIY------ESPTHLYLAmelvtggELFD-RIIERGSYTEKDA------SQLIGQVLQAVKY 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAENECFKLI--DFGLS-FKEGNQDVKYIQTDGYRAPEAELQNCLAQaglqsdtectsAVDL 225
Cdd:cd14169 117 LHQLGIVHRDLKPENLLYATPFEDSKIMisDFGLSkIEAQGMLSTACGTPGYVAPELLEQKPYGK-----------AVDV 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 226 WSLGIILLEMFSGMklkhtvrSQEWKANSSAIIDHIFasKAVVNAAIPAYH-----LRDLIKSMLHDDPSRRIPAEMALC 300
Cdd:cd14169 186 WAIGVISYILLCGY-------PPFYDENDSELFNQIL--KAEYEFDSPYWDdisesAKDFIRHLLERDPEKRFTCEQALQ 256

                ....*
gi 28467003 301 SPFFS 305
Cdd:cd14169 257 HPWIS 261
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
133-305 3.85e-13

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: 69.05  E-value: 3.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 WMIQHCArDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAELQNclaq 210
Cdd:cd05611  98 WAKQYIA-EVVLGVEDLHQRGIIHRDIKPENLLID-QTGHLKLTDFGLSrnGLEKRHNKKFVGTPDYLAPETILGV---- 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 211 aglqsdtECTSAVDLWSLGIILLEMFSGMKLKHtvrsqewkANS-SAIIDHIFA-----SKAVVNAAIPayHLRDLIKSM 284
Cdd:cd05611 172 -------GDDKMSDWWSLGCVIFEFLFGYPPFH--------AETpDAVFDNILSrrinwPEEVKEFCSP--EAVDLINRL 234
                       170       180
                ....*....|....*....|....
gi 28467003 285 LHDDPSRRIPA---EMALCSPFFS 305
Cdd:cd05611 235 LCMDPAKRLGAngyQEIKSHPFFK 258
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
142-305 4.24e-13

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: 69.29  E-value: 4.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILW---SAENECFKLIDFGLSfKEGNQDVKYIQTDGYR----APEAelqncLAQAGLq 214
Cdd:cd14175 104 ICKTVEYLHSQGVVHRDLKPSNILYvdeSGNPESLRICDFGFA-KQLRAENGLLMTPCYTanfvAPEV-----LKRQGY- 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 sDTECtsavDLWSLGIILLEMFSGmklkHTVRSQEWKANSSAIIDHIFASKAVVNAA---IPAYHLRDLIKSMLHDDPSR 291
Cdd:cd14175 177 -DEGC----DIWSLGILLYTMLAG----YTPFANGPSDTPEEILTRIGSGKFTLSGGnwnTVSDAAKDLVSKMLHVDPHQ 247
                       170
                ....*....|....
gi 28467003 292 RIPAEMALCSPFFS 305
Cdd:cd14175 248 RLTAKQVLQHPWIT 261
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
76-304 5.89e-13

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: 68.81  E-value: 5.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQGHRNIVTLYGVFtihfspNVPSRCLLL-------ELLDVSVSElllysSHQGCSMWMIQHCARDVLEALAF 148
Cdd:cd14197  58 EIAVLELAQANPWVINLHEVY------ETASEMILVleyaaggEIFNQCVAD-----REEAFKEKDVKRLMKQILEGVSF 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAENEC--FKLIDFGLS-FKEGNQDVKYIQ-TDGYRAPEaelqnclaqagLQSDTECTSAVD 224
Cdd:cd14197 127 LHNNNVVHLDLKPQNILLTSESPLgdIKIVDFGLSrILKNSEELREIMgTPEYVAPE-----------ILSYEPISTATD 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 225 LWSLGIILLEMFSGMKLKHTVRSQEWKANSSAI--------IDHIFASkavvnaAIpayhlrDLIKSMLHDDPSRRIPAE 296
Cdd:cd14197 196 MWSIGVLAYVMLTGISPFLGDDKQETFLNISQMnvsyseeeFEHLSES------AI------DFIKTLLIKKPENRATAE 263

                ....*...
gi 28467003 297 MALCSPFF 304
Cdd:cd14197 264 DCLKHPWL 271
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
86-305 6.89e-13

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 69.30  E-value: 6.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTihfspnvPSRCLLlELLDVSVSELLLysshqGCSMWMIQHCAR-----------DVLEALAFLHHEGY 154
Cdd:cd07877  75 HENVIGLLDVFT-------PARSLE-EFNDVYLVTHLM-----GADLNNIVKCQKltddhvqfliyQILRGLKYIHSADI 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNIlwSAENEC-FKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqNCLaqaglqsdtECTSAVDLWSLGIILL 233
Cdd:cd07877 142 IHRDLKPSNL--AVNEDCeLKILDFGLARHTDDEMTGYVATRWYRAPEIML-NWM---------HYNQTVDIWSVGCIMA 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 234 EMFSG----------------MKLKHTVRSQEWKANSSAIIDHIFAS------KAVVNAAIPAYHLR-DLIKSMLHDDPS 290
Cdd:cd07877 210 ELLTGrtlfpgtdhidqlkliLRLVGTPGAELLKKISSESARNYIQSltqmpkMNFANVFIGANPLAvDLLEKMLVLDSD 289
                       250
                ....*....|....*
gi 28467003 291 RRIPAEMALCSPFFS 305
Cdd:cd07877 290 KRITAAQALAHAYFA 304
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
86-310 6.98e-13

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: 69.30  E-value: 6.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIHFS-PNVPSRCLLLELLDVSVSELL-LYSSHQGCSMWMIQhcardVLEALAFLHHEGYVHADLKPRN 163
Cdd:cd07875  82 HKNIIGLLNVFTPQKSlEEFQDVYIVMELMDANLCQVIqMELDHERMSYLLYQ-----MLCGIKHLHSAGIIHRDLKPSN 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 164 ILwsAENEC-FKLIDFGLSFKEGNQDV--KYIQTDGYRAPEAELqnclaQAGLQSDtectsaVDLWSLGIILLEMFSG-- 238
Cdd:cd07875 157 IV--VKSDCtLKILDFGLARTAGTSFMmtPYVVTRYYRAPEVIL-----GMGYKEN------VDIWSVGCIMGEMIKGgv 223
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 239 --------------------------MKLKHTVRSQEWKANSSA-------IIDHIFASKAVVNaAIPAYHLRDLIKSML 285
Cdd:cd07875 224 lfpgtdhidqwnkvieqlgtpcpefmKKLQPTVRTYVENRPKYAgysfeklFPDVLFPADSEHN-KLKASQARDLLSKML 302
                       250       260
                ....*....|....*....|....*
gi 28467003 286 HDDPSRRIPAEMALCSPFFSIPFAP 310
Cdd:cd07875 303 VIDASKRISVDEALQHPYINVWYDP 327
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
74-293 8.78e-13

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: 67.67  E-value: 8.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTIHFSPNVpsrCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd14119  42 KREIQILRRLN-HRNVIKLVDVLYNEEKQKL---YMVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQG 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWSAEnECFKLIDFGLS-----FKEGNQDVKYIQTDGYRAPEaelqncLAqAGLqsDTECTSAVDLWSL 228
Cdd:cd14119 118 IIHKDIKPGNLLLTTD-GTLKISDFGVAealdlFAEDDTCTTSQGSPAFQPPE------IA-NGQ--DSFSGFKVDIWSA 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 229 GIILLEMFSG---------MKLKHTVRSQEWkanssAIIDHIFASkavvnaaipayhLRDLIKSMLHDDPSRRI 293
Cdd:cd14119 188 GVTLYNMTTGkypfegdniYKLFENIGKGEY-----TIPDDVDPD------------LQDLLRGMLEKDPEKRF 244
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
74-238 8.89e-13

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: 67.64  E-value: 8.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTihfSPNvpSRCLLLELldVSVSELL-------LYSSHQGCSMWMiqhcaRDVLEAL 146
Cdd:cd14103  38 RNEIEIMNQLR-HPRLLQLYDAFE---TPR--EMVLVMEY--VAGGELFervvdddFELTERDCILFM-----RQICEGV 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 147 AFLHHEGYVHADLKPRNILW-SAENECFKLIDFGLSFK-EGNQDVKYIQ-TDGYRAPEaelqnclaqagLQSDTECTSAV 223
Cdd:cd14103 105 QYMHKQGILHLDLKPENILCvSRTGNQIKIIDFGLARKyDPDKKLKVLFgTPEFVAPE-----------VVNYEPISYAT 173
                       170
                ....*....|....*
gi 28467003 224 DLWSLGIILLEMFSG 238
Cdd:cd14103 174 DMWSVGVICYVLLSG 188
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
80-238 9.50e-13

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: 68.10  E-value: 9.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  80 LEQLQGHRNIVTLYGVFTIHFSPNVPSRC-LLLELLDV-SVSELLLYSSHQGCSMW--MIQHCARDVLEALAFLHHEGYV 155
Cdd:cd06608  56 LRKFSNHPNIATFYGAFIKKDPPGGDDQLwLVMEYCGGgSVTDLVKGLRKKGKRLKeeWIAYILRETLRGLAYLHENKVI 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 156 HADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVK---YIQTDGYRAPEaelqncLAQAGLQSDTECTSAVDLWSLGIIL 232
Cdd:cd06608 136 HRDIKGQNILLTEEAE-VKLVDFGVSAQLDSTLGRrntFIGTPYWMAPE------VIACDQQPDASYDARCDVWSLGITA 208

                ....*.
gi 28467003 233 LEMFSG 238
Cdd:cd06608 209 IELADG 214
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
22-238 9.82e-13

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: 68.21  E-value: 9.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  22 LWQVQSRLGSGSSASVYRVRCCGNpgsppGALKQFLPPGTTGAAasaaEYGFRKERAALEQLQGHRNIVTLYGVFTIHFS 101
Cdd:cd06637   7 IFELVELVGNGTYGQVYKGRHVKT-----GQLAAIKVMDVTGDE----EEEIKQEINMLKKYSHHRNIATYYGAFIKKNP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 PNVPSRC-LLLELLDV-SVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFG 179
Cdd:cd06637  78 PGMDDQLwLVMEFCGAgSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT-ENAEVKLVDFG 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 180 LSFK----EGNQDVkYIQTDGYRAPEaelqncLAQAGLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd06637 157 VSAQldrtVGRRNT-FIGTPYWMAPE------VIACDENPDATYDFKSDLWSLGITAIEMAEG 212
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
73-237 1.44e-12

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: 67.37  E-value: 1.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTIHFSPNVPSRC---LLLELLDVSVSELLLYSSHQgcsmWMIQHCardvlEALAFL 149
Cdd:cd05040  45 FLKEVNAMHSLD-HPNLIRLYGVVLSSPLMMVTELAplgSLLDRLRKDQGHFLISTLCD----YAVQIA-----NGMAYL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 150 HHEGYVHADLKPRNILWSAeNECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAElqnClAQAGLQSDTeCTSAVDLWSLG 229
Cdd:cd05040 115 ESKRFIHRDLAARNILLAS-KDKVKIGDFGLMRALPQNEDHYVMQEHRKVPFAW---C-APESLKTRK-FSHASDVWMFG 188

                ....*...
gi 28467003 230 IILLEMFS 237
Cdd:cd05040 189 VTLWEMFT 196
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
140-303 1.47e-12

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: 67.50  E-value: 1.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL--SFKEGN-QDVKYIQTDGYRAPEAELQnclaqaGLQSD 216
Cdd:cd06917 108 REVLVALKFIHKDGIIHRDIKAANILVTNTGN-VKLCDFGVaaSLNQNSsKRSTFVGTPYWMAPEVITE------GKYYD 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 TEctsaVDLWSLGIILLEMFSGmklkHTVRSQEWKANSSAIIDHIFASKAVVNAAIPAyhLRDLIKSMLHDDPSRRIPAE 296
Cdd:cd06917 181 TK----ADIWSLGITTYEMATG----NPPYSDVDALRAVMLIPKSKPPRLEGNGYSPL--LKEFVAACLDEEPKDRLSAD 250

                ....*..
gi 28467003 297 MALCSPF 303
Cdd:cd06917 251 ELLKSKW 257
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
133-304 1.50e-12

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: 67.10  E-value: 1.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 WMIQhcardVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfKEGNQDVKYIQTD-G---YRAPEAelqncl 208
Cdd:cd08215 108 WFVQ-----ICLALKYLHSRKILHRDLKTQNIFLTKDGVV-KLGDFGIS-KVLESTTDLAKTVvGtpyYLSPEL------ 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 209 aqaglqsdteC-----TSAVDLWSLGIILLEMfsgMKLKHTVRSQEWKANSSAIIDHIFAskavvnaAIPAY---HLRDL 280
Cdd:cd08215 175 ----------CenkpyNYKSDIWALGCVLYEL---CTLKHPFEANNLPALVYKIVKGQYP-------PIPSQyssELRDL 234
                       170       180
                ....*....|....*....|....
gi 28467003 281 IKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd08215 235 VNSMLQKDPEKRPSANEILSSPFI 258
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
145-309 1.99e-12

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: 68.08  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEG-NQDVKYIQTDGYRAPEAELQNCLAQAGLQSDTECTSAV 223
Cdd:cd05573 113 ALDSLHKLGFIHRDIKPDNILLDADGH-IKLADFGLCTKMNkSGDRESYLNDSVNTLFQDNVLARRRPHKQRRVRAYSAV 191
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 224 --------------------DLWSLGIILLEM------FSGMKLKHTVRSqewkanssaIIDH----IFASKAVVNAaip 273
Cdd:cd05573 192 gtpdyiapevlrgtgygpecDWWSLGVILYEMlygfppFYSDSLVETYSK---------IMNWkeslVFPDDPDVSP--- 259
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 28467003 274 ayHLRDLIKSMLHDdPSRRI-PAEMALCSPFFS-IPFA 309
Cdd:cd05573 260 --EAIDLIRRLLCD-PEDRLgSAEEIKAHPFFKgIDWE 294
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
85-303 2.09e-12

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: 67.10  E-value: 2.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  85 GHRNIVTLYGVF--TIHF--SPNVPSRCLL-LELLDVSvsELLLY-SSHQGCSMWMIQHCARDVLEALAFLHHEGYVHAD 158
Cdd:cd14171  57 GHPNIVQIYDVYanSVQFpgESSPRARLLIvMELMEGG--ELFDRiSQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRD 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 159 LKPRNILW--SAENECFKLIDFGLSfKEGNQDVKYIQ-TDGYRAP---EAELQNCLAQAGL-QSDTECT--SAVDLWSLG 229
Cdd:cd14171 135 LKPENLLLkdNSEDAPIKLCDFGFA-KVDQGDLMTPQfTPYYVAPqvlEAQRRHRKERSGIpTSPTPYTydKSCDMWSLG 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 230 IILLEMFSG----------------MKLK-----HTVRSQEWKANSSAIidhifaskavvnaaipayhlRDLIKSMLHDD 288
Cdd:cd14171 214 VIIYIMLCGyppfysehpsrtitkdMKRKimtgsYEFPEEEWSQISEMA--------------------KDIVRKLLCVD 273
                       250
                ....*....|....*
gi 28467003 289 PSRRIPAEMALCSPF 303
Cdd:cd14171 274 PEERMTIEEVLHHPW 288
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
142-303 2.20e-12

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 67.85  E-value: 2.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILwsAENEC-FKLIDFGLSFKEGNQDVKYIQ----TDGYRAPEAelqnclaqagLQSD 216
Cdd:cd07853 112 ILRGLKYLHSAGILHRDIKPGNLL--VNSNCvLKICDFGLARVEEPDESKHMTqevvTQYYRAPEI----------LMGS 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 TECTSAVDLWSLGIILLEMFSG----------------MKLKHTVRSQEWKANSSAIIDHIFASK-------AVVNAAIP 273
Cdd:cd07853 180 RHYTSAVDIWSVGCIFAELLGRrilfqaqspiqqldliTDLLGTPSLEAMRSACEGARAHILRGPhkppslpVLYTLSSQ 259
                       170       180       190
                ....*....|....*....|....*....|.
gi 28467003 274 AYH-LRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd07853 260 ATHeAVHLLCRMLVFDPDKRISAADALAHPY 290
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
145-315 2.48e-12

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: 67.43  E-value: 2.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVK---YIQTDGYRAPEAelqncLAQAGLqsdtecTS 221
Cdd:cd05584 112 ALGHLHSLGIIYRDLKPENILLDAQGH-VKLTDFGLCKESIHDGTVthtFCGTIEYMAPEI-----LTRSGH------GK 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 222 AVDLWSLGIILLEMFSGmklkhtvrSQEWKA-NSSAIIDHIFASKAVvnaaIPAY---HLRDLIKSMLHDDPSRRIPAEM 297
Cdd:cd05584 180 AVDWWSLGALMYDMLTG--------APPFTAeNRKKTIDKILKGKLN----LPPYltnEARDLLKKLLKRNVSSRLGSGP 247
                       170       180
                ....*....|....*....|
gi 28467003 298 ALCSPFFSIPFAPHI--EDL 315
Cdd:cd05584 248 GDAEEIKAHPFFRHInwDDL 267
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
86-304 2.78e-12

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 67.48  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   86 HRNIVTLYGVFT----IhfspnvpsrCLLLELLD-----VSVSELLLYSSHQGCSMWMIqhcardvLEALAFLHHEGYVH 156
Cdd:PTZ00024  79 HENIMGLVDVYVegdfI---------NLVMDIMAsdlkkVVDRKIRLTESQVKCILLQI-------LNGLNVLHKWYFMH 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  157 ADLKPRNILWSAENECfKLIDFGLSFKEGN-------QDVKYIQ----------TDGYRAPEAelqnclaqagLQSDTEC 219
Cdd:PTZ00024 143 RDLSPANIFINSKGIC-KIADFGLARRYGYppysdtlSKDETMQrreemtskvvTLWYRAPEL----------LMGAEKY 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  220 TSAVDLWSLGIILLEMFSG----------------MKLKHTVRSQEW-------------KANSSAIIDHI-FASKAVVn 269
Cdd:PTZ00024 212 HFAVDMWSVGCIFAELLTGkplfpgeneidqlgriFELLGTPNEDNWpqakklplyteftPRKPKDLKTIFpNASDDAI- 290
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 28467003  270 aaipayhlrDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:PTZ00024 291 ---------DLLQSLLKLNPLERISAKEALKHEYF 316
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
85-293 2.86e-12

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: 66.54  E-value: 2.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  85 GHRNIVTLYGVFTIHFSPNvpsRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCA---RDVLEALAFLHHEGYVHADLKP 161
Cdd:cd14089  52 GCPHIVRIIDVYENTYQGR---KCLLVVMECMEGGELFSRIQERADSAFTEREAAeimRQIGSAVAHLHSMNIAHRDLKP 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 162 RNILWS--AENECFKLIDFGLSfKEGNQDvKYIQTDGYR----APE---AElqnclaqaglQSDTECtsavDLWSLGIIL 232
Cdd:cd14089 129 ENLLYSskGPNAILKLTDFGFA-KETTTK-KSLQTPCYTpyyvAPEvlgPE----------KYDKSC----DMWSLGVIM 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 233 ---------------LEMFSGMKLK-----HTVRSQEWKANSSAIidhifaskavvnaaipayhlRDLIKSMLHDDPSRR 292
Cdd:cd14089 193 yillcgyppfysnhgLAISPGMKKRirngqYEFPNPEWSNVSEEA--------------------KDLIRGLLKTDPSER 252

                .
gi 28467003 293 I 293
Cdd:cd14089 253 L 253
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
23-238 2.96e-12

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: 66.94  E-value: 2.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVrccGNPGSPPGALKQFLPPGTTGAAASAAEYGFrkeraaLEQLQGHRNIVTLYGVFTIHFSP 102
Cdd:cd06639  24 WDIIETIGKGTYGKVYKV---TNKKDGSLAAVKILDPISDVDEEIEAEYNI------LRSLPNHPNVVKFYGMFYKADQY 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 103 NVPSRCLLLELLDV-SVSELL--LYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFG 179
Cdd:cd06639  95 VGGQLWLVLELCNGgSVTELVkgLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV-KLVDFG 173
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28467003 180 LSFKEGNQDVK---YIQTDGYRAPeaELQNCLAQAGLQSDTECtsavDLWSLGIILLEMFSG 238
Cdd:cd06639 174 VSAQLTSARLRrntSVGTPFWMAP--EVIACEQQYDYSYDARC----DVWSLGITAIELADG 229
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
140-304 3.04e-12

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: 66.48  E-value: 3.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENEC--FKLIDFGLSFKEGNQ-DVKYIQ-TDGYRAPEAelqnclaqagLQS 215
Cdd:cd14198 117 RQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLgdIKIVDFGMSRKIGHAcELREIMgTPEYLAPEI----------LNY 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 216 DTeCTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKANSSAI-IDhiFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIP 294
Cdd:cd14198 187 DP-ITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVnVD--YSEETFSSVSQLA---TDFIQKLLVKNPEKRPT 260
                       170
                ....*....|
gi 28467003 295 AEMALCSPFF 304
Cdd:cd14198 261 AEICLSHSWL 270
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
140-301 3.09e-12

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: 66.62  E-value: 3.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfKEGNQDVKYIQTDG---YRAPEAELQNCLAQAG---- 212
Cdd:cd14046 111 RQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN-VKIGDFGLA-TSNKLNVELATQDInksTSAALGSSGDLTGNVGtaly 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 213 ----LQSDTECT--SAVDLWSLGIILLEM---FS-GMKLKHTVRS-QEWKANSSAIIDHIFASKAvvnaaipayhlRDLI 281
Cdd:cd14046 189 vapeVQSGTKSTynEKVDMYSLGIIFFEMcypFStGMERVQILTAlRSVSIEFPPDFDDNKHSKQ-----------AKLI 257
                       170       180
                ....*....|....*....|
gi 28467003 282 KSMLHDDPSRRIPAEMALCS 301
Cdd:cd14046 258 RWLLNHDPAKRPSAQELLKS 277
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
142-304 3.12e-12

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: 67.11  E-value: 3.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILwsAENEC-FKLIDFGL---SFKEGNQDV---KYIQTDGYRAPeaELQNCLAqaglq 214
Cdd:cd07859 112 LLRALKYIHTANVFHRDLKPKNIL--ANADCkLKICDFGLarvAFNDTPTAIfwtDYVATRWYRAP--ELCGSFF----- 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 sdTECTSAVDLWSLGIILLEMFSGMKL---KHTVRSQEWKAN-----SSAIIDHIFASKA-------VVNAAIPAYH--- 276
Cdd:cd07859 183 --SKYTPAIDIWSIGCIFAEVLTGKPLfpgKNVVHQLDLITDllgtpSPETISRVRNEKArrylssmRKKQPVPFSQkfp 260
                       170       180       190
                ....*....|....*....|....*....|...
gi 28467003 277 -----LRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07859 261 nadplALRLLERLLAFDPKDRPTAEEALADPYF 293
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
28-304 3.47e-12

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: 66.05  E-value: 3.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  28 RLGSGSSASVYRVRC--CGNPG-----------SPPGALKQFLPpgttgaaasaaeygfrKERAALEQLQgHRNIVTLYG 94
Cdd:cd14080   7 TIGEGSYSKVKLAEYtkSGLKEkvackiidkkkAPKDFLEKFLP----------------RELEILRKLR-HPNIIQVYS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  95 VFtiHFSPNVpsrCLLLELL---DvsvseLLLYSSHQGC------SMWMiqhcaRDVLEALAFLHHEGYVHADLKPRNIL 165
Cdd:cd14080  70 IF--ERGSKV---FIFMEYAehgD-----LLEYIQKRGAlsesqaRIWF-----RQLALAVQYLHSLDIAHRDLKCENIL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 166 WSAENEcFKLIDFGLSFKEGNQDVK-----YIQTDGYRAPEAeLQnclaqaGLQSDteCTSAvDLWSLGIILLEMFSGM- 239
Cdd:cd14080 135 LDSNNN-VKLSDFGFARLCPDDDGDvlsktFCGSAAYAAPEI-LQ------GIPYD--PKKY-DIWSLGVILYIMLCGSm 203
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 240 -----KLKHTVRSQ---EWkanssaiidHIFASKAVVNAAIpayhlRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14080 204 pfddsNIKKMLKDQqnrKV---------RFPSSVKKLSPEC-----KDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
108-241 3.76e-12

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: 67.09  E-value: 3.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEC---FKLIDFGlSFKE 184
Cdd:cd14211  76 CLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQpyrVKVIDFG-SASH 154
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 185 GNQDVK--YIQTDGYRAPEAELqnclaqaGLQSDtectSAVDLWSLGIILLEMFSGMKL 241
Cdd:cd14211 155 VSKAVCstYLQSRYYRAPEIIL-------GLPFC----EAIDMWSLGCVIAELFLGWPL 202
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
139-293 3.95e-12

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: 66.88  E-value: 3.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQD--VKYIQTDGYRAP---EAELQNCLAQAGL 213
Cdd:cd05574 109 AAEVLLALEYLHLLGFVYRDLKPENILLH-ESGHIMLTDFDLSKQSSVTPppVRKSLRKGSRRSsvkSIEKETFVAEPSA 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 214 QSD----TE------------CTSAVDLWSLGIILLEM------FSGMKLKHTVRSqewkanssaII--DHIFASKAVVN 269
Cdd:cd05574 188 RSNsfvgTEeyiapevikgdgHGSAVDWWTLGILLYEMlygttpFKGSNRDETFSN---------ILkkELTFPESPPVS 258
                       170       180
                ....*....|....*....|....
gi 28467003 270 AAipayhLRDLIKSMLHDDPSRRI 293
Cdd:cd05574 259 SE-----AKDLIRKLLVKDPSKRL 277
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
74-303 3.98e-12

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: 65.75  E-value: 3.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAA-----LEQLQgHRNIVTLYGVFTihfSPNvpSRCLLLELLDVSvsELLLY-SSHQGCSMWMIQHCARDVLEALA 147
Cdd:cd14115  32 KKEQAAheaalLQHLQ-HPQYITLHDTYE---SPT--SYILVLELMDDG--RLLDYlMNHDELMEEKVAFYIRDIMEALQ 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 148 FLHHEGYVHADLKPRNILWSAE--NECFKLIDFGlsfkegnqdvKYIQTDGYRAPEAELQNC-LAQAGLQSDTECTSAVD 224
Cdd:cd14115 104 YLHNCRVAHLDIKPENLLIDLRipVPRVKLIDLE----------DAVQISGHRHVHHLLGNPeFAAPEVIQGTPVSLATD 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 225 LWSLGIILLEMFSGMKlKHTVRSQEWKANSSAIIDHIFASK---AVVNAAipayhlRDLIKSMLHDDPSRRIPAEMALCS 301
Cdd:cd14115 174 IWSIGVLTYVMLSGVS-PFLDESKEETCINVCRVDFSFPDEyfgDVSQAA------RDFINVILQEDPRRRPTAATCLQH 246

                ..
gi 28467003 302 PF 303
Cdd:cd14115 247 PW 248
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
24-292 4.00e-12

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


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 66.29  E-value: 4.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRccgnPGSPPG---ALKQFLPPGTtgaaasaaeyGFR-KERAALE-------QLQGHRNIVTL 92
Cdd:cd14052   3 ANVELIGSGEFSQVYKVS----ERVPTGkvyAVKKLKPNYA----------GAKdRLRRLEEvsilrelTLDGHDNIVQL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  93 YGVFTIHfspnvPSRCLLLEL-----LDVSVSElllYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWS 167
Cdd:cd14052  69 IDSWEYH-----GHLYIQTELcengsLDVFLSE---LGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLIT 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 168 AENEcFKLIDFGL-------SFKEGNQDVKYIqtdgyrAPEAelqnclaqaglQSDTECTSAVDLWSLGIILLEMFSGMK 240
Cdd:cd14052 141 FEGT-LKIGDFGMatvwpliRGIEREGDREYI------APEI-----------LSEHMYDKPADIFSLGLILLEAAANVV 202
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 241 LK------HTVRSQE--------WKANSSAIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRR 292
Cdd:cd14052 203 LPdngdawQKLRSGDlsdaprlsSTDLHSASSPSSNPPPDPPNMPILSGSLDRVVRWMLSPEPDRR 268
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
135-304 4.91e-12

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: 66.85  E-value: 4.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNIlwsAENE-C-FKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqag 212
Cdd:cd07879 119 VQYLVYQMLCGLKYIHSAGIIHRDLKPGNL---AVNEdCeLKILDFGLARHADAEMTGYVVTRWYRAPEVIL-------- 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 213 lqSDTECTSAVDLWSLGIILLEMFSGMKLkhtVRSQEWKANSSAI--------------IDHIFASKAVvnAAIPAYHLR 278
Cdd:cd07879 188 --NWMHYNQTVDIWSVGCIMAEMLTGKTL---FKGKDYLDQLTQIlkvtgvpgpefvqkLEDKAAKSYI--KSLPKYPRK 260
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 28467003 279 --------------DLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07879 261 dfstlfpkaspqavDLLEKMLELDVDKRLTATEALEHPYF 300
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
134-312 5.40e-12

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: 66.57  E-value: 5.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFK-EGNQDVKY---IQTDGYRAPEAeLQncla 209
Cdd:cd05601 103 MARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGH-IKLADFGSAAKlSSDKTVTSkmpVGTPDYIAPEV-LT---- 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 210 qaGLQSDTECTSAV--DLWSLGIILLEM------FSGMKLKHTVrsqewkansSAIIDH-----IFASKAVVNAAIpayh 276
Cdd:cd05601 177 --SMNGGSKGTYGVecDWWSLGIVAYEMlygktpFTEDTVIKTY---------SNIMNFkkflkFPEDPKVSESAV---- 241
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 28467003 277 lrDLIKSMLhDDPSRRIPAEMALCSPFFS-----------IPFAPHI 312
Cdd:cd05601 242 --DLIKGLL-TDAKERLGYEGLCCHPFFSgidwnnlrqtvPPFVPTL 285
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
22-303 5.58e-12

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: 65.75  E-value: 5.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  22 LWQVQSRLGSGSSASVYRVR--CCGNPGSPPGALKQFLPPGTTGAAASAAEygfrKERAALEQLQgHRNIVTLYGVFTih 99
Cdd:cd14196   6 FYDIGEELGSGQFAIVKKCRekSTGLEYAAKFIKKRQSRASRRGVSREEIE----REVSILRQVL-HPNIITLHDVYE-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 100 fspNVPSRCLLLELldVSVSELL-LYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEN---ECFKL 175
Cdd:cd14196  79 ---NRTDVVLILEL--VSGGELFdFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipiPHIKL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 176 IDFGLSFK--EGNQDVKYIQTDGYRAPEAELQNCLaqaGLqsdtectsAVDLWSLGIILLEMFSGMKLKHTVRSQEWKAN 253
Cdd:cd14196 154 IDFGLAHEieDGVEFKNIFGTPEFVAPEIVNYEPL---GL--------EADMWSIGVITYILLSGASPFLGDTKQETLAN 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 28467003 254 SSAiIDHIFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14196 223 ITA-VSYDFDEEFFSHTSELA---KDFIRKLLVKETRKRLTIQEALRHPW 268
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
70-301 7.52e-12

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: 65.16  E-value: 7.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  70 EYGFRKERAALEQLQgHRNIVTLYGVFTIHfSPnvpsRCLLLELLDV-SVSELLLYSSHQGCSMWMIQHCaRDVLEALAF 148
Cdd:cd05059  43 EDDFIEEAKVMMKLS-HPKLVQLYGVCTKQ-RP----IFIVTEYMANgCLLNYLRERRGKFQTEQLLEMC-KDVCEAMEY 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSaENECFKLIDFGLSfkegnqdvKYIQTDGYRAPE-AELQNCLAQAGLQSDTECTSAVDLWS 227
Cdd:cd05059 116 LESNGFIHRDLAARNCLVG-EQNVVKVSDFGLA--------RYVLDDEYTSSVgTKFPVKWSPPEVFMYSKFSSKSDVWS 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 228 LGIILLEMFSGMKLKHTVRSqewkanSSAIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRRiPAEMALCS 301
Cdd:cd05059 187 FGVLMWEVFSEGKMPYERFS------NSEVVEHISQGYRLYRPHLAPTEVYTIMYSCWHEKPEER-PTFKILLS 253
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
145-308 7.63e-12

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: 65.00  E-value: 7.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWS-AENECFKLIDFGLSFKEGNQDVKYiQTDG---YRAPEAELQNclaqaglQSDtect 220
Cdd:cd14121 107 ALQFLREHNISHMDLKPQNLLLSsRYNPVLKLADFGFAQHLKPNDEAH-SLRGsplYMAPEMILKK-------KYD---- 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 221 SAVDLWSLGIILLEMFSGMKLKH--TVRSQEWKANSSAIIdhifasKAVVNAAIPAyHLRDLIKSMLHDDPSRRIPAEma 298
Cdd:cd14121 175 ARVDLWSVGVILYECLFGRAPFAsrSFEELEEKIRSSKPI------EIPTRPELSA-DCRDLLLRLLQRDPDRRISFE-- 245
                       170
                ....*....|
gi 28467003 299 lcsPFFSIPF 308
Cdd:cd14121 246 ---EFFAHPF 252
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
132-238 8.32e-12

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: 65.70  E-value: 8.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 132 MWMIQHCAR-----------DVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLS---FKEGNQDVKYIQTDGY 197
Cdd:cd05570  84 MFHIQRARRfteerarfyaaEICLALQFLHERGIIYRDLKLDNVLLDAEGHI-KIADFGMCkegIWGGNTTSTFCGTPDY 162
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 28467003 198 RAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd05570 163 IAPE-----------ILREQDYGFSVDWWALGVLLYEMLAG 192
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
76-292 8.40e-12

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: 65.29  E-value: 8.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQgHRNIVTLYGVFTihfspnvPSRCLLLELLDVSVSELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHEGY 154
Cdd:cd05580  51 EKRILSEVR-HPFIVNLLGSFQ-------DDRNLYMVMEYVPGGELFSLLRRSGRfPNDVAKFYAAEVVLALEYLHSLDI 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNILWSAENEcFKLIDFGLSfkegnqdvKYIQ--------TDGYRAPEaelqnclaqagLQSDTECTSAVDLW 226
Cdd:cd05580 123 VYRDLKPENLLLDSDGH-IKITDFGFA--------KRVKdrtytlcgTPEYLAPE-----------IILSKGHGKAVDWW 182
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 227 SLGIILLEMFSGMklkhtvrSQEWKANSSAIIDHIFASKAVVnaaiPAY---HLRDLIKSMLHDDPSRR 292
Cdd:cd05580 183 ALGILIYEMLAGY-------PPFFDENPMKIYEKILEGKIRF----PSFfdpDAKDLIKRLLVVDLTKR 240
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
86-304 1.00e-11

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: 64.84  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIhfspNVPSRCLLLEL----LDVSVselLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKP 161
Cdd:cd14109  55 HPNIVQMHDAYDD----EKLAVTVIDNLastiELVRD---NLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRP 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 162 RNILWSAENecFKLIDFGLSFK--EGNqdvkyIQTDGYRAPEAELQNCLAQAGLqsdtecTSAVDLWSLGIILLEMFSGM 239
Cdd:cd14109 128 EDILLQDDK--LKLADFGQSRRllRGK-----LTTLIYGSPEFVSPEIVNSYPV------TLATDMWSVGVLTYVLLGGI 194
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 240 KLKH---------TVRSQEWKANSSaIIDHIfaskavvnaaipAYHLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14109 195 SPFLgdndretltNVRSGKWSFDSS-PLGNI------------SDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
70-238 1.06e-11

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: 65.03  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  70 EYGFRKERAALEQLQGHRNIVTLYGVFTIHFSPNVPSRC-LLLELLDV-SVSELLLYSSHQGCSMWMIQHCARDVLEALA 147
Cdd:cd06636  56 EEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLwLVMEFCGAgSVTDLVKNTKGNALKEDWIAYICREILRGLA 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 148 FLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFK----EGNQDVkYIQTDGYRAPEaelqncLAQAGLQSDTECTSAV 223
Cdd:cd06636 136 HLHAHKVIHRDIKGQNVLLT-ENAEVKLVDFGVSAQldrtVGRRNT-FIGTPYWMAPE------VIACDENPDATYDYRS 207
                       170
                ....*....|....*
gi 28467003 224 DLWSLGIILLEMFSG 238
Cdd:cd06636 208 DIWSLGITAIEMAEG 222
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
23-238 1.10e-11

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: 65.03  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVRccgNPGSPPGALKQFLPPGTTGAAASAAEYGFrkeraaLEQLQGHRNIVTLYGVFTIHFSP 102
Cdd:cd06638  20 WEIIETIGKGTYGKVFKVL---NKKNGSKAAVKILDPIHDIDEEIEAEYNI------LKALSDHPNVVKFYGMYYKKDVK 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 103 NVPSRCLLLELLDV-SVSELLLYSSHQGCSM--WMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFG 179
Cdd:cd06638  91 NGDQLWLVLELCNGgSVTDLVKGFLKRGERMeePIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGG-VKLVDFG 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28467003 180 LSFKEGNQDVK---YIQTDGYRAPeaELQNCLAQAGLQSDTECtsavDLWSLGIILLEMFSG 238
Cdd:cd06638 170 VSAQLTSTRLRrntSVGTPFWMAP--EVIACEQQLDSTYDARC----DVWSLGITAIELGDG 225
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
140-301 1.21e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 64.84  E-value: 1.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLSFKEGNQD-VKYIQTDGYRAPE--AELQNCLAQAGLQ-S 215
Cdd:cd14049 127 QQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIHVRIGDFGLACPDILQDgNDSTTMSRLNGLThtSGVGTCLYAAPEQlE 206
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 216 DTECTSAVDLWSLGIILLEMFS--GMKLKhtvRSQEWKANSSAIIDHIFASKAVVNAaipayhlrDLIKSMLHDDPSRRI 293
Cdd:cd14049 207 GSHYDFKSDMYSIGVILLELFQpfGTEME---RAEVLTQLRNGQIPKSLCKRWPVQA--------KYIKLLTSTEPSERP 275

                ....*...
gi 28467003 294 PAEMALCS 301
Cdd:cd14049 276 SASQLLES 283
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
140-304 1.54e-11

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: 64.33  E-value: 1.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWsAENECFKLIDFGLS--FKEGNQDVkYIQTDGYRAPEAelqnclaqagLQSDT 217
Cdd:cd14004 116 RQVADAVKHLHDQGIVHRDIKDENVIL-DGNGTIKLIDFGSAayIKSGPFDT-FVGTIDYAAPEV----------LRGNP 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 218 ECTSAVDLWSLGIILlemfsgmklkHTVRSQEwkaNSSAIIDHIFASKAVVNAAIpAYHLRDLIKSMLHDDPSRRIPAEM 297
Cdd:cd14004 184 YGGKEQDIWALGVLL----------YTLVFKE---NPFYNIEEILEADLRIPYAV-SEDLIDLISRMLNRDVGDRPTIEE 249

                ....*..
gi 28467003 298 ALCSPFF 304
Cdd:cd14004 250 LLTDPWL 256
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
29-304 1.61e-11

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: 64.29  E-value: 1.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRccgnpGSPPG---ALKQFLPPGTTgaaasaaeygfRKERAALEQLQ-GHR----NIVTLYGVFtihF 100
Cdd:cd06605   9 LGEGNGGVVSKVR-----HRPSGqimAVKVIRLEIDE-----------ALQKQILRELDvLHKcnspYIVGFYGAF---Y 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 101 SPNVPSRCLllELLDVSvSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE-GYVHADLKPRNILWSAENEcFKLIDFG 179
Cdd:cd06605  70 SEGDISICM--EYMDGG-SLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQ-VKLCDFG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 180 LSFKEGNQDVK-YIQTDGYRAPEaELQNclAQAGLQSDtectsavdLWSLGIILLEMFSGmklkhtvR---SQEWKANSS 255
Cdd:cd06605 146 VSGQLVDSLAKtFVGTRSYMAPE-RISG--GKYTVKSD--------IWSLGLSLVELATG-------RfpyPPPNAKPSM 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 256 AIIDHIfasKAVVNAAIPAY-------HLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd06605 208 MIFELL---SYIVDEPPPLLpsgkfspDFQDFVSQCLQKDPTERPSYKELMEHPFI 260
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
73-237 1.78e-11

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: 64.00  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTIHFSPnvpsrCLLLELLDV-SVSELL-------LYSSHQGCSmWMIQhCArdvlE 144
Cdd:cd14058  33 FEVEVRQLSRVD-HPNIIKLYGACSNQKPV-----CLVMEYAEGgSLYNVLhgkepkpIYTAAHAMS-WALQ-CA----K 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHH---EGYVHADLKPRNILWSAENECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEaelqnclAQAGLQSDTECts 221
Cdd:cd14058 101 GVAYLHSmkpKALIHRDLKPPNLLLTNGGTVLKICDFGTACDISTHMTNNKGSAAWMAPE-------VFEGSKYSEKC-- 171
                       170
                ....*....|....*.
gi 28467003 222 avDLWSLGIILLEMFS 237
Cdd:cd14058 172 --DVFSWGIILWEVIT 185
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
75-303 1.78e-11

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: 64.66  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQGHRNIVTLygvftihfspnvpsrcllLELLDVSVSELLLYSSHQGCSMWMIQH------------CARDV 142
Cdd:cd14173  48 REVEMLYQCQGHRNVLEL------------------IEFFEEEDKFYLVFEKMRGGSILSHIHrrrhfneleasvVVQDI 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 143 LEALAFLHHEGYVHADLKPRNILWSAENEC--FKLIDFGL-SFKEGNQDVKYIQTD---------GYRAPeaELQNCLAQ 210
Cdd:cd14173 110 ASALDFLHNKGIAHRDLKPENILCEHPNQVspVKICDFDLgSGIKLNSDCSPISTPelltpcgsaEYMAP--EVVEAFNE 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 211 AGLQSDTECtsavDLWSLGIILLEMFSGMK--LKHTVRSQEWKANSS--AIIDHIFASKAVVNAAIP-------AYHLRD 279
Cdd:cd14173 188 EASIYDKRC----DLWSLGVILYIMLSGYPpfVGRCGSDCGWDRGEAcpACQNMLFESIQEGKYEFPekdwahiSCAAKD 263
                       250       260
                ....*....|....*....|....
gi 28467003 280 LIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14173 264 LISKLLVRDAKQRLSAAQVLQHPW 287
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
75-303 2.32e-11

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: 64.05  E-value: 2.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELldVSVSELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd14105  57 REVSILRQVL-HPNIITLHDVFE-----NKTDVVLILEL--VAGGELFDFLAEKESlSEEEATEFLKQILDGVNYLHTKN 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWSAENEC---FKLIDFGLSFK-EGNQDVKYI-QTDGYRAPEAELQNCLaqaGLQSdtectsavDLWSL 228
Cdd:cd14105 129 IAHFDLKPENIMLLDKNVPiprIKLIDFGLAHKiEDGNEFKNIfGTPEFVAPEIVNYEPL---GLEA--------DMWSI 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 229 GIILLEMFSGMKLKHTVRSQEWKANSSAiIDHIFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14105 198 GVITYILLSGASPFLGDTKQETLANITA-VNYDFDDEYFSNTSELA---KDFIRQLLVKDPRKRMTIQESLRHPW 268
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
28-239 2.82e-11

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: 63.67  E-value: 2.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  28 RLGSGSSASVYRvrccGNPGSPPGALKQFLPpgTTGAAASAAEYGFRKERAALEQLQgHRNIVTLYGvftihFSPNVPSR 107
Cdd:cd14158  22 KLGEGGFGVVFK----GYINDKNVAVKKLAA--MVDISTEDLTKQFEQEIQVMAKCQ-HENLVELLG-----YSCDGPQL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLE------LLD--VSVSELLLYSSHQGCsmWMIQHCARdvleALAFLHHEGYVHADLKPRNILWsaeNECF--KLID 177
Cdd:cd14158  90 CLVYTympngsLLDrlACLNDTPPLSWHMRC--KIAQGTAN----GINYLHENNHIHRDIKSANILL---DETFvpKISD 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 178 FGLSFKEGnQDVKYIQTD------GYRAPEAeLQNclaqaglqsdtECTSAVDLWSLGIILLEMFSGM 239
Cdd:cd14158 161 FGLARASE-KFSQTIMTErivgttAYMAPEA-LRG-----------EITPKSDIFSFGVVLLEIITGL 215
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
75-304 3.95e-11

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 63.48  E-value: 3.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVftIHFSPnvpSRCLLLELLDVSVSELLlysshQGCSMWMIQHCAR----DVLEALAFLH 150
Cdd:cd07873  49 REVSLLKDLK-HANIVTLHDI--IHTEK---SLTLVFEYLDKDLKQYL-----DDCGNSINMHNVKlflfQLLRGLAYCH 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWS 227
Cdd:cd07873 118 RRKVLHRDLKPQNLLINERGE-LKLADFGLARAKSIPTKTYsneVVTLWYRPPDI----------LLGSTDYSTQIDMWG 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 228 LGIILLEMFSG----------------MKLKHTVRSQEWKAnssaiidhIFASKAVVNAAIPAYHLR------------- 278
Cdd:cd07873 187 VGCIFYEMSTGrplfpgstveeqlhfiFRILGTPTEETWPG--------ILSNEEFKSYNYPKYRADalhnhaprldsdg 258
                       250       260
                ....*....|....*....|....*..
gi 28467003 279 -DLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07873 259 aDLLSKLLQFEGRKRISAEEAMKHPYF 285
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
140-238 4.29e-11

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: 63.05  E-value: 4.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVK---YIQTDGYRAPEAELQ---NCLAqagl 213
Cdd:cd06612 106 YQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQA-KLADFGVSGQLTDTMAKrntVIGTPFWMAPEVIQEigyNNKA---- 180
                        90       100
                ....*....|....*....|....*
gi 28467003 214 qsdtectsavDLWSLGIILLEMFSG 238
Cdd:cd06612 181 ----------DIWSLGITAIEMAEG 195
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
108-321 4.34e-11

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 63.31  E-value: 4.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQ-GCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLS--FKE 184
Cdd:cd05577  69 CLVLTLMNGGDLKYHIYNVGTrGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHV-RISDLGLAveFKG 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 185 GNQDVKYIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGmklkHTVRSQEWKANSSAIIDHIFAS 264
Cdd:cd05577 148 GKKIKGRVGTHGYMAPEV----------LQKEVAYDFSVDWFALGCMLYEMIAG----RSPFRQRKEKVDKEELKRRTLE 213
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 265 KAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALC-----SPFF-SIPFaPHIEdLVMLPTP 321
Cdd:cd05577 214 MAVEYPDSFSPEARSLCEGLLQKDPERRLGCRGGSAdevkeHPFFrSLNW-QRLE-AGMLEPP 274
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
132-313 4.50e-11

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: 63.77  E-value: 4.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 132 MWMIQHCAR-----------DVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfKEGNQDVK----YIQTDG 196
Cdd:cd05590  84 MFHIQKSRRfdeararfyaaEITSALMFLHDKGIIYRDLKLDNVLLDHEGHC-KLADFGMC-KEGIFNGKttstFCGTPD 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 197 YRAPEAeLQNCLAQAglqsdtectsAVDLWSLGIILLEMFSGmklkHTVRSQEwkaNSSAIIDHIFASKaVVNAAIPAYH 276
Cdd:cd05590 162 YIAPEI-LQEMLYGP----------SVDWWAMGVLLYEMLCG----HAPFEAE---NEDDLFEAILNDE-VVYPTWLSQD 222
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 277 LRDLIKSMLHDDPSRRIPA------EMALCSPFF-------------SIPFAPHIE 313
Cdd:cd05590 223 AVDILKAFMTKNPTMRLGSltlggeEAILRHPFFkeldweklnrrqiEPPFRPRIK 278
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
135-304 5.38e-11

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: 63.11  E-value: 5.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHE-GYVHADLKPRNILWSaENECFKLIDFGLSFK---EGNQDVKYIQTDGYRAPEAELQ-NCLA 209
Cdd:cd14011 116 IKYGLLQISEALSFLHNDvKLVHGNICPESVVIN-SNGEWKLAGFDFCISseqATDQFPYFREYDPNLPPLAQPNlNYLA 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 210 QAGLQSDTeCTSAVDLWSLGIILLEMFS-GMKLKHTVRSQ-EWKANSSAIIDHIFASKAVVNAAipayhLRDLIKSMLHD 287
Cdd:cd14011 195 PEYILSKT-CDPASDMFSLGVLIYAIYNkGKPLFDCVNNLlSYKKNSNQLRQLSLSLLEKVPEE-----LRDHVKTLLNV 268
                       170
                ....*....|....*..
gi 28467003 288 DPSRRIPAEMALCSPFF 304
Cdd:cd14011 269 TPEVRPDAEQLSKIPFF 285
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
139-237 5.39e-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: 62.75  E-value: 5.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSfkegnQDVKYIQTDG-----YRAPEAeLQNclaqagl 213
Cdd:cd05039 108 ALDVCEGMEYLESKKFVHRDLAARNVLVS-EDNVAKVSDFGLA-----KEASSNQDGGklpikWTAPEA-LRE------- 173
                        90       100
                ....*....|....*....|....
gi 28467003 214 qsdTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05039 174 ---KKFSTKSDVWSFGILLWEIYS 194
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
86-303 5.73e-11

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: 63.11  E-value: 5.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTihfspNVPSRCLLLELLdvSVSELLLYSSHQGCsmwMIQHCARDVL----EALAFLHHEGYVHADLKP 161
Cdd:cd14178  56 HPNIITLKDVYD-----DGKFVYLVMELM--RGGELLDRILRQKC---FSEREASAVLctitKTVEYLHSQGVVHRDLKP 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 162 RNILWSAEN---ECFKLIDFGLSfKEGNQDVKYIQTDGYR----APEAelqncLAQAGLqsDTECtsavDLWSLGIILLE 234
Cdd:cd14178 126 SNILYMDESgnpESIRICDFGFA-KQLRAENGLLMTPCYTanfvAPEV-----LKRQGY--DAAC----DIWSLGILLYT 193
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 235 MFSGMklkhTVRSQEWKANSSAIIDHIFASK---------AVVNAAipayhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14178 194 MLAGF----TPFANGPDDTPEEILARIGSGKyalsggnwdSISDAA------KDIVSKMLHVDPHQRLTAPQVLRHPW 261
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
129-238 5.88e-11

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: 62.65  E-value: 5.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 129 GCSMWMI-QHCA----------------------RDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEG 185
Cdd:cd06609  71 GSKLWIImEYCGggsvldllkpgpldetyiafilREVLLGLEYLHSEGKIHRDIKAANILLSEEGD-VKLADFGVSGQLT 149
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 186 NQDVK---YIQTDGYRAPEAELQNclaqaglQSDTECtsavDLWSLGIILLEMFSG 238
Cdd:cd06609 150 STMSKrntFVGTPFWMAPEVIKQS-------GYDEKA----DIWSLGITAIELAKG 194
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
2-303 6.10e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 63.30  E-value: 6.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003    2 AGSGCAWGAEPPrfleaFGRLWQVQsRLGSGSSASVYRVRccGNPGSPPGALKQFlppgttgaaasaaeYGfRKERAALE 81
Cdd:PLN00034  61 SASGSAPSAAKS-----LSELERVN-RIGSGAGGTVYKVI--HRPTGRLYALKVI--------------YG-NHEDTVRR 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   82 QLQghRNIVTLYGVFtihfSPNVpSRC-----------LLLELLDvsvselllYSSHQGCSMW---MIQHCARDVLEALA 147
Cdd:PLN00034 118 QIC--REIEILRDVN----HPNV-VKChdmfdhngeiqVLLEFMD--------GGSLEGTHIAdeqFLADVARQILSGIA 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  148 FLHHEGYVHADLKPRNILWSAENECfKLIDFGLS------FKEGNQDVKYIqtdGYRAPEaELQNCLAQAGLQSdtectS 221
Cdd:PLN00034 183 YLHRRHIVHRDIKPSNLLINSAKNV-KIADFGVSrilaqtMDPCNSSVGTI---AYMSPE-RINTDLNHGAYDG-----Y 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  222 AVDLWSLGIILLEMFSGMKLKHTVRSQEWKANSSAIIdhifASKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCS 301
Cdd:PLN00034 253 AGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAIC----MSQPPEAPATASREFRHFISCCLQREPAKRWSAMQLLQH 328

                 ..
gi 28467003  302 PF 303
Cdd:PLN00034 329 PF 330
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
76-239 7.23e-11

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: 62.24  E-value: 7.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQgHRNIVTLYGVFT----IHFSPNVpsrCLLLELLDVSVSELLLYSSHQgcsmwmiQHCARDVLEALAFLHH 151
Cdd:cd05572  43 EKEILEECN-SPFIVKLYRTFKdkkyLYMLMEY---CLGGELWTILRDRGLFDEYTA-------RFYTACVVLAFEYLHS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVKY--IQTDGYRAPEaelqNCLAQAGlqsdtecTSAVDLWSLG 229
Cdd:cd05572 112 RGIIYRDLKPENLLLD-SNGYVKLVDFGFAKKLGSGRKTWtfCGTPEYVAPE----IILNKGY-------DFSVDYWSLG 179
                       170
                ....*....|
gi 28467003 230 IILLEMFSGM 239
Cdd:cd05572 180 ILLYELLTGR 189
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
143-303 7.54e-11

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: 62.04  E-value: 7.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 143 LEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS-FKEGNQDVKYIQT----DGYRAPEAelqncLAQAGLQSdt 217
Cdd:cd14663 110 IDAVDYCHSRGVFHRDLKPENLLLD-EDGNLKISDFGLSaLSEQFRQDGLLHTtcgtPNYVAPEV-----LARRGYDG-- 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 218 ectSAVDLWSLGIILLEMFSG---------MKLKHTVRSQEWKANSSaiidhiFASKAvvnaaipayhlRDLIKSMLHDD 288
Cdd:cd14663 182 ---AKADIWSCGVILFVLLAGylpfddenlMALYRKIMKGEFEYPRW------FSPGA-----------KSLIKRILDPN 241
                       170
                ....*....|....*
gi 28467003 289 PSRRIPAEMALCSPF 303
Cdd:cd14663 242 PSTRITVEQIMASPW 256
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
75-304 7.56e-11

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: 62.45  E-value: 7.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVftIHFSPNVpsrCLLLELLDVSVSELLL----YSSHQGCSMWMIQhcardVLEALAFLH 150
Cdd:cd07839  48 REICLLKELK-HKNIVRLYDV--LHSDKKL---TLVFEYCDQDLKKYFDscngDIDPEIVKSFMFQ-----LLKGLAFCH 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqncLAQAGLQSdtectSAVDLWS 227
Cdd:cd07839 117 SHNVLHRDLKPQNLLINKNGE-LKLADFGLARAFGIPVRCYsaeVVTLWYRPPDV-----LFGAKLYS-----TSIDMWS 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 228 LGIILLEM-------FSG----------MKLKHTVRSQEWkANSSAIIDH----IFASKAVVNAAIPAYHL--RDLIKSM 284
Cdd:cd07839 186 AGCIFAELanagrplFPGndvddqlkriFRLLGTPTEESW-PGVSKLPDYkpypMYPATTSLVNVVPKLNStgRDLLQNL 264
                       250       260
                ....*....|....*....|
gi 28467003 285 LHDDPSRRIPAEMALCSPFF 304
Cdd:cd07839 265 LVCNPVQRISAEEALQHPYF 284
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
139-303 8.39e-11

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: 62.08  E-value: 8.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSD 216
Cdd:cd14077 119 ARQIASALDYLHRNSIVHRDLKIENILIS-KSGNIKIIDFGLSnlYDPRRLLRTFCGSLYFAAPEL----------LQAQ 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 TECTSAVDLWSLGIILLEMFSGmklKHTVRSQewkaNSSAIIDHIfaSKAVVNaaIPAYHLRD---LIKSMLHDDPSRRI 293
Cdd:cd14077 188 PYTGPEVDVWSFGVVLYVLVCG---KVPFDDE----NMPALHAKI--KKGKVE--YPSYLSSEcksLISRMLVVDPKKRA 256
                       170
                ....*....|
gi 28467003 294 PAEMALCSPF 303
Cdd:cd14077 257 TLEQVLNHPW 266
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
70-303 8.52e-11

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: 61.90  E-value: 8.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  70 EYGFRKERAALEQLQgHRNIVTLYGVFtiHFSPNVpsrCLLLELLDVSVsellLYSSHQGCSMWMIQHCA---RDVLEAL 146
Cdd:cd14116  49 EHQLRREVEIQSHLR-HPNILRLYGYF--HDATRV---YLILEYAPLGT----VYRELQKLSKFDEQRTAtyiTELANAL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 147 AFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKE-GNQDVKYIQTDGYRAPEaelqnclAQAGLQSDTEctsaVDL 225
Cdd:cd14116 119 SYCHSKRVIHRDIKPENLLLGSAGE-LKIADFGWSVHApSSRRTTLCGTLDYLPPE-------MIEGRMHDEK----VDL 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 226 WSLGIILLEMFSGMKLKHTVRSQEwkanssaiidhIFASKAVVNAAIPAY---HLRDLIKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd14116 187 WSLGVLCYEFLVGKPPFEANTYQE-----------TYKRISRVEFTFPDFvteGARDLISRLLKHNPSQRPMLREVLEHP 255

                .
gi 28467003 303 F 303
Cdd:cd14116 256 W 256
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
76-302 9.45e-11

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: 61.96  E-value: 9.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQgHRNIVTLYGVFtihFSPNvpSRCLLLELL---DV--SVSELLLYSSHQGCSMwmiqhcARDVLEALAFLH 150
Cdd:cd14095  48 EVAILRRVK-HPNIVQLIEEY---DTDT--ELYLVMELVkggDLfdAITSSTKFTERDASRM------VTDLAQALKYLH 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILwSAENE----CFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAelqncLAQAG--LQsdtectsaVD 224
Cdd:cd14095 116 SLSIVHRDIKPENLL-VVEHEdgskSLKLADFGLATEVKEPLFTVCGTPTYVAPEI-----LAETGygLK--------VD 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 225 LWSLGIILLEMFSGM-KLKHTVRSQEwkanssAIIDHI------FASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIPAEM 297
Cdd:cd14095 182 IWAAGVITYILLCGFpPFRSPDRDQE------ELFDLIlagefeFLSPYWDNISDSA---KDLISRMLVVDPEKRYSAGQ 252

                ....*
gi 28467003 298 ALCSP 302
Cdd:cd14095 253 VLDHP 257
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
75-304 9.78e-11

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: 62.05  E-value: 9.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTihfspnVPSRC-LLLELLDVSVSELL-LYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd07861  48 REISLLKELQ-HPNIVCLEDVLM------QENRLyLVFEFLSMDLKKYLdSLPKGKYMDAELVKSYLYQILQGILFCHSR 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLG 229
Cdd:cd07861 121 RVLHRDLKPQNLLID-NKGVIKLADFGLARAFGIPVRVYtheVVTLWYRAPEV----------LLGSPRYSTPVDIWSIG 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 230 IILLEMFSGMKLKH----------------TVRSQEWKANSSaIIDH--IFA--SKAVVNAAIPAYHLR--DLIKSMLHD 287
Cdd:cd07861 190 TIFAEMATKKPLFHgdseidqlfrifrilgTPTEDIWPGVTS-LPDYknTFPkwKKGSLRTAVKNLDEDglDLLEKMLIY 268
                       250
                ....*....|....*..
gi 28467003 288 DPSRRIPAEMALCSPFF 304
Cdd:cd07861 269 DPAKRISAKKALVHPYF 285
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
75-304 1.07e-10

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: 62.32  E-value: 1.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVftIHFSPnvpSRCLLLELLDVSVSELLlysshQGCSMWMIQHCAR----DVLEALAFLH 150
Cdd:cd07872  53 REVSLLKDLK-HANIVTLHDI--VHTDK---SLTLVFEYLDKDLKQYM-----DDCGNIMSMHNVKiflyQILRGLAYCH 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWS 227
Cdd:cd07872 122 RRKVLHRDLKPQNLLINERGE-LKLADFGLARAKSVPTKTYsneVVTLWYRPPDV----------LLGSSEYSTQIDMWG 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 228 LGIILLEMFSG----------------MKLKHTVRSQEWKANSSaiIDHI-------FASKAVVNAAiPAYHLR--DLIK 282
Cdd:cd07872 191 VGCIFFEMASGrplfpgstvedelhliFRLLGTPTEETWPGISS--NDEFknynfpkYKPQPLINHA-PRLDTEgiELLT 267
                       250       260
                ....*....|....*....|..
gi 28467003 283 SMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07872 268 KFLQYESKKRISAEEAMKHAYF 289
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-314 1.32e-10

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: 62.24  E-value: 1.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCCGNPGSPPGALKQFLPPGTTGAAASAAEYGfRKERAALEQLQGHRNIVTLygvftiHFSPNVPSRC 108
Cdd:cd05614   8 LGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQKAKTVEHT-RTERNVLEHVRQSPFLVTL------HYAFQTDAKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 109 LLLelLD-VSVSELL--LYSsHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFkLIDFGLS---- 181
Cdd:cd05614  81 HLI--LDyVSGGELFthLYQ-RDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVV-LTDFGLSkefl 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 182 FKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGMklkhTVRSQEWKANSSAIIdhi 261
Cdd:cd05614 157 TEEKERTYSFCGTIEYMAPEI----------IRGKSGHGKAVDWWSLGILMFELLTGA----SPFTLEGEKNTQSEV--- 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 262 faSKAVVNAAIP-----AYHLRDLIKSMLHDDPSRRI-----PAEMALCSPFF-------------SIPFAPHIED 314
Cdd:cd05614 220 --SRRILKCDPPfpsfiGPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFkgldwealalrkvNPPFRPSIRS 293
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
139-293 1.39e-10

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: 61.68  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSDTE 218
Cdd:cd05612 107 ASEIVCALEYLHSKEIVYRDLKPENILLDKEGH-IKLTDFGFAKKLRDRTWTLCGTPEYLAPEV----------IQSKGH 175
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 219 CTsAVDLWSLGIILLEMFSGMklkhtvrSQEWKANSSAIIDHIFASKAVVNAAIPaYHLRDLIKSMLHDDPSRRI 293
Cdd:cd05612 176 NK-AVDWWALGILIYEMLVGY-------PPFFDDNPFGIYEKILAGKLEFPRHLD-LYAKDLIKKLLVVDRTRRL 241
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
143-293 1.45e-10

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: 61.19  E-value: 1.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 143 LEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS--FKEGNQDV---KYIQTDGYRAPEAelqnclaqagLQSDT 217
Cdd:cd14069 110 MAGLKYLHSCGITHRDIKPENLLLD-ENDNLKISDFGLAtvFRYKGKERllnKMCGTLPYVAPEL----------LAKKK 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 218 ECTSAVDLWSLGIILLEMFSGmklkhtvrSQEW---KANSSAIIDHIFASKAVVN--AAIPAYHLRdLIKSMLHDDPSRR 292
Cdd:cd14069 179 YRAEPVDVWSCGIVLFAMLAG--------ELPWdqpSDSCQEYSDWKENKKTYLTpwKKIDTAALS-LLRKILTENPNKR 249

                .
gi 28467003 293 I 293
Cdd:cd14069 250 I 250
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
86-324 1.67e-10

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: 61.69  E-value: 1.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFtIHFSPNVpsrCLLLELLDVSvSELLLYSSHQGCSMWMIQHCARDVLEALAFL---HHegYVHADLKPR 162
Cdd:cd06620  62 SPYIVSFYGAF-LNENNNI---IICMEYMDCG-SLDKILKKKGPFPEEVLGKIAVAVLEGLTYLynvHR--IIHRDIKPS 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 163 NILWSAENEcFKLIDFGLSFKEGNQDVK-YIQTDGYRAPEAelqnclaqagLQSDtECTSAVDLWSLGIILLEMFSGmkl 241
Cdd:cd06620 135 NILVNSKGQ-IKLCDFGVSGELINSIADtFVGTSTYMSPER----------IQGG-KYSVKSDVWSLGLSIIELALG--- 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 242 KHTVRSQEWKANSSAIIDHIFaskavvnaaipayhlrDLIKSMLHdDPSRRIPAemalcspffSIPFAPHIEDLV---ML 318
Cdd:cd06620 200 EFPFAGSNDDDDGYNGPMGIL----------------DLLQRIVN-EPPPRLPK---------DRIFPKDLRDFVdrcLL 253

                ....*.
gi 28467003 319 PTPVLR 324
Cdd:cd06620 254 KDPRER 259
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
108-241 1.72e-10

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: 61.97  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILW---SAENECFKLIDFG-LSFK 183
Cdd:cd14229  77 CLVFEMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdpVRQPYRVKVIDFGsASHV 156
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 184 EGNQDVKYIQTDGYRAPEAELqnclaqaGLqsdtECTSAVDLWSLGIILLEMFSGMKL 241
Cdd:cd14229 157 SKTVCSTYLQSRYYRAPEIIL-------GL----PFCEAIDMWSLGCVIAELFLGWPL 203
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
75-308 1.89e-10

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: 61.18  E-value: 1.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTIhfspnvpSRCLLLELLDVSVSELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd14202  50 KEIKILKELK-HENIVALYDFQEI-------ANSVYLVMEYCNGGDLADYLHTMRTlSEDTIRLFLQQIAGAMKMLHSKG 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWS--------AENECFKLIDFGLSfkegnqdvKYIQTDG----------YRAPEAEL-QNCLAQAglq 214
Cdd:cd14202 122 IIHRDLKPQNILLSysggrksnPNNIRIKIADFGFA--------RYLQNNMmaatlcgspmYMAPEVIMsQHYDAKA--- 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 sdtectsavDLWSLGIILLEMFSGmklkhtvrSQEWKANSSAIIDHIFASKAVVNAAIP---AYHLRDLIKSMLHDDPSR 291
Cdd:cd14202 191 ---------DLWSIGTIIYQCLTG--------KAPFQASSPQDLRLFYEKNKSLSPNIPretSSHLRQLLLGLLQRNQKD 253
                       250
                ....*....|....*..
gi 28467003 292 RIPAEmalcsPFFSIPF 308
Cdd:cd14202 254 RMDFD-----EFFHHPF 265
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
74-238 2.10e-10

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: 60.89  E-value: 2.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFtihfspNVPSRC-LLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14082  50 RNEVAILQQLS-HPGVVNLECMF------ETPERVfVVMEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSK 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAENEC--FKLIDFGLSFKEGNQDVK--YIQTDGYRAPEAELQNCLAQaglqsdtectsAVDLWSL 228
Cdd:cd14082 123 NIVHCDLKPENVLLASAEPFpqVKLCDFGFARIIGEKSFRrsVVGTPAYLAPEVLRNKGYNR-----------SLDMWSV 191
                       170
                ....*....|
gi 28467003 229 GIILLEMFSG 238
Cdd:cd14082 192 GVIIYVSLSG 201
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
73-303 2.30e-10

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: 60.73  E-value: 2.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfSPNvpSRCLLLELLDVSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14002  47 LRQEIEILRKLN-HPNIIEMLDSFE---TKK--EFVVVTEYAQGELFQIL--EDDGTLPEEEVRSIAKQLVSALHYLHSN 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAENECfKLIDFGL--SFKEGNQDVKYIQ-TDGYRAPEaelqncLAQAGLQSDTectsaVDLWSLG 229
Cdd:cd14002 119 RIIHRDMKPQNILIGKGGVV-KLCDFGFarAMSCNTLVLTSIKgTPLYMAPE------LVQEQPYDHT-----ADLWSLG 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 230 IILLEMFSG--------------MKLKHTVRsqeWKANSSAiidhifaskavvnaaipayHLRDLIKSMLHDDPSRRIPA 295
Cdd:cd14002 187 CILYELFVGqppfytnsiyqlvqMIVKDPVK---WPSNMSP-------------------EFKSFLQGLLNKDPSKRLSW 244

                ....*...
gi 28467003 296 EMALCSPF 303
Cdd:cd14002 245 PDLLEHPF 252
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
139-238 2.37e-10

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: 61.35  E-value: 2.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfKEGNQDVKYIQ----TDGYRAPEAeLQnclaqaglq 214
Cdd:cd05591 102 AAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHC-KLADFGMC-KEGILNGKTTTtfcgTPDYIAPEI-LQ--------- 169
                        90       100
                ....*....|....*....|....
gi 28467003 215 sDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd05591 170 -ELEYGPSVDWWALGVLMYEMMAG 192
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
135-235 2.57e-10

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: 60.78  E-value: 2.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVK---YIQTDGYRAPEAELQNCLAqa 211
Cdd:cd06613  99 IAYVCRETLKGLAYLHSTGKIHRDIKGANILLT-EDGDVKLADFGVSAQLTATIAKrksFIGTPYWMAPEVAAVERKG-- 175
                        90       100
                ....*....|....*....|....
gi 28467003 212 glQSDTECtsavDLWSLGIILLEM 235
Cdd:cd06613 176 --GYDGKC----DIWALGITAIEL 193
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
142-303 2.86e-10

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: 61.19  E-value: 2.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAEN---ECFKLIDFGLSFK---EGNQDVKYIQTDGYRAPEAelqncLAQAGLqs 215
Cdd:cd14176 122 ITKTVEYLHAQGVVHRDLKPSNILYVDESgnpESIRICDFGFAKQlraENGLLMTPCYTANFVAPEV-----LERQGY-- 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 216 DTECtsavDLWSLGIILLEMFSGmklkHTVRSQEWKANSSAIIDHIFASKAVVNAAI---PAYHLRDLIKSMLHDDPSRR 292
Cdd:cd14176 195 DAAC----DIWSLGVLLYTMLTG----YTPFANGPDDTPEEILARIGSGKFSLSGGYwnsVSDTAKDLVSKMLHVDPHQR 266
                       170
                ....*....|.
gi 28467003 293 IPAEMALCSPF 303
Cdd:cd14176 267 LTAALVLRHPW 277
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
142-302 4.15e-10

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: 60.13  E-value: 4.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLSfKEGNQDVK---YIQTDGYRAPEAelqnCLAQAGLQSDte 218
Cdd:cd08220 110 ILLALHHVHSKQILHRDLKTQNILLNKKRTVVKIGDFGIS-KILSSKSKaytVVGTPCYISPEL----CEGKPYNQKS-- 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 219 ctsavDLWSLGIILLEMFSgmkLKhtvRSQEwKANSSAIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMA 298
Cdd:cd08220 183 -----DIWALGCVLYELAS---LK---RAFE-AANLPALVLKIMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEI 250

                ....
gi 28467003 299 LCSP 302
Cdd:cd08220 251 MAQP 254
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
72-237 6.88e-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: 59.31  E-value: 6.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  72 GFRKERAALEQLQgHRNIVTLYGVFTihfspnvPSRCLLL--ELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFL 149
Cdd:cd05033  51 DFLTEASIMGQFD-HPNVIRLEGVVT-------KSRPVMIvtEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYL 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 150 HHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVKYIQTDG-----YRAPEAelqnclaqaglQSDTECTSAVD 224
Cdd:cd05033 123 SEMNYVHRDLAARNILVNSDLVC-KVSDFGLSRRLEDSEATYTTKGGkipirWTAPEA-----------IAYRKFTSASD 190
                       170
                ....*....|...
gi 28467003 225 LWSLGIILLEMFS 237
Cdd:cd05033 191 VWSFGIVMWEVMS 203
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
75-304 7.17e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 59.69  E-value: 7.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVftIHFSPNVPSRC-----LLLELLDVSVSELLLYSSHQgCSMWMIQHCARDVLEALAFL 149
Cdd:cd07865  60 REIKILQLLK-HENVVNLIEI--CRTKATPYNRYkgsiyLVFEFCEHDLAGLLSNKNVK-FTLSEIKKVMKMLLNGLYYI 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 150 HHEGYVHADLKPRNILWSaENECFKLIDFGL----SFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTECTSA 222
Cdd:cd07865 136 HRNKILHRDMKAANILIT-KDGVLKLADFGLarafSLAKNSQPNRYtnrVVTLWYRPPEL----------LLGERDYGPP 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 223 VDLWSLGIILLEMFSgmklkhtvRSQEWKANSSA----IIDHIFAS------KAVVN------AAIPAYHLR-------- 278
Cdd:cd07865 205 IDMWGAGCIMAEMWT--------RSPIMQGNTEQhqltLISQLCGSitpevwPGVDKlelfkkMELPQGQKRkvkerlkp 276
                       250       260       270
                ....*....|....*....|....*....|....
gi 28467003 279 --------DLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07865 277 yvkdpyalDLIDKLLVLDPAKRIDADTALNHDFF 310
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
76-304 8.57e-10

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: 59.22  E-value: 8.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELLDVSvsELLLYSSHQG-CSMWMIQHCARDVLEALAFLHHEGY 154
Cdd:cd14113  53 ELGVLQSLQ-HPQLVGLLDTFE-----TPTSYILVLEMADQG--RLLDYVVRWGnLTEEKIRFYLREILEALQYLHNCRI 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNIL--WSAENECFKLIDFGLSFKEGNqdVKYIQ----TDGYRAPEAELQNCLAqagLQSdtectsavDLWSL 228
Cdd:cd14113 125 AHLDLKPENILvdQSLSKPTIKLADFGDAVQLNT--TYYIHqllgSPEFAAPEIILGNPVS---LTS--------DLWSI 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 229 GIILLEMFSGMK--LKHTVrsqEWKANSSAIIDHIFAS---KAVVNAAipayhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14113 192 GVLTYVLLSGVSpfLDESV---EETCLNICRLDFSFPDdyfKGVSQKA------KDFVCFLLQMDPAKRPSAALCLQEQW 262

                .
gi 28467003 304 F 304
Cdd:cd14113 263 L 263
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
134-321 1.01e-09

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 60.19  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFG----LSFKEGNQDVKYIQTDGYRAPE-------- 201
Cdd:PLN03225 256 IIQTIMRQILFALDGLHSTGIVHRDVKPQNIIFSEGSGSFKIIDLGaaadLRVGINYIPKEFLLDPRYAAPEqyimstqt 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  202 ---------AELQNCLAQAGLqsdtecTSAVDLWSLGIILLEM-FSGM-----------KLKHTVRS-QEWKANSSAiid 259
Cdd:PLN03225 336 psapsapvaTALSPVLWQLNL------PDRFDIYSAGLIFLQMaFPNLrsdsnliqfnrQLKRNDYDlVAWRKLVEP--- 406
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003  260 hifASKAVVNAAIPAYHLRD-----LIKSMLHDDPSRRIPAEMALCSPFFSI--PFAPHIEDLVMLPTP 321
Cdd:PLN03225 407 ---RASPDLRRGFEVLDLDGgagweLLKSMMRFKGRQRISAKAALAHPYFDRegLLGLSVMQNLRLQLF 472
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
21-304 1.04e-09

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: 59.02  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  21 RLWQVQSRLGSGSSASVYR-----------VRCCGNPGSPPGALKQFLPpgttgaaasaaeygfrKERAALEQLQgHRNI 89
Cdd:cd14165   1 RGYILGINLGEGSYAKVKSayserlkcnvaIKIIDKKKAPDDFVEKFLP----------------RELEILARLN-HKSI 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  90 VTLYGVFTIhfspnvpSRCLLLELLDVSVS-ELLLYSSHQGCsmwMIQHCARDVLEALA----FLHHEGYVHADLKPRNI 164
Cdd:cd14165  64 IKTYEIFET-------SDGKVYIVMELGVQgDLLEFIKLRGA---LPEDVARKMFHQLSsaikYCHELDIVHRDLKCENL 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 165 LWSAENEcFKLIDFGLS---FKEGNQDVKYIQT----DGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd14165 134 LLDKDFN-IKLTDFGFSkrcLRDENGRIVLSKTfcgsAAYAAPEV----------LQGIPYDPRIYDIWSLGVILYIMVC 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 238 G--------------MKLKHTVRSQEWKANSSaiidhifaskavvnaaipayHLRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14165 203 GsmpyddsnvkkmlkIQKEHRVRFPRSKNLTS--------------------ECKDLIYRLLQPDVSQRLCIDEVLSHPW 262

                .
gi 28467003 304 F 304
Cdd:cd14165 263 L 263
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
74-293 1.32e-09

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: 58.56  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQGHRNIVTLygvftiHFSPNVPSRCLLLelLD-VSVSELL--LYSSHQgcsmwMIQHCAR----DVLEAL 146
Cdd:cd05583  46 MTERQVLEAVRQSPFLVTL------HYAFQTDAKLHLI--LDyVNGGELFthLYQREH-----FTESEVRiyigEIVLAL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 147 AFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLS--FKEGNQDVKY--IQTDGYRAPEaelqncLAQAGlqsDTECTSA 222
Cdd:cd05583 113 EHLHKLGIIYRDIKLENILLDSEGH-VVLTDFGLSkeFLPGENDRAYsfCGTIEYMAPE------VVRGG---SDGHDKA 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 223 VDLWSLGIILLEMFSGMKlKHTVrsqEWKANSSAIIdhifaSKAVVNAAIPAYHL-----RDLIKSMLHDDPSRRI 293
Cdd:cd05583 183 VDWWSLGVLTYELLTGAS-PFTV---DGERNSQSEI-----SKRILKSHPPIPKTfsaeaKDFILKLLEKDPKKRL 249
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
108-241 1.40e-09

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: 59.33  E-value: 1.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILW---SAENECFKLIDFGlSFKE 184
Cdd:cd14227  92 CLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpSRQPYRVKVIDFG-SASH 170
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 185 GNQDV--KYIQTDGYRAPEAELqnclaqaGLqsdtECTSAVDLWSLGIILLEMFSGMKL 241
Cdd:cd14227 171 VSKAVcsTYLQSRYYRAPEIIL-------GL----PFCEAIDMWSLGCVIAELFLGWPL 218
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
145-238 1.41e-09

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: 59.17  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKY--IQTDGYRAPEAELQnclaqaglqsdTECTSA 222
Cdd:cd05599 113 AIESIHKLGYIHRDIKPDNLLLDARGH-IKLSDFGLCTGLKKSHLAYstVGTPDYIAPEVFLQ-----------KGYGKE 180
                        90
                ....*....|....*.
gi 28467003 223 VDLWSLGIILLEMFSG 238
Cdd:cd05599 181 CDWWSLGVIMYEMLIG 196
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
26-237 1.43e-09

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: 58.45  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  26 QSRLGSGSSASVYR--VRCCGNPGSPPgALKQfLPPGTTgaaaSAAEYGFRKERAALEQLqGHRNIVTLYGVFTiHFSPN 103
Cdd:cd05063  10 QKVIGAGEFGEVFRgiLKMPGRKEVAV-AIKT-LKPGYT----EKQRQDFLSEASIMGQF-SHHNIIRLEGVVT-KFKPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 104 VpsrcLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLS-F 182
Cdd:cd05063  82 M----IITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLEC-KVSDFGLSrV 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 183 KEGNQDVKYIQTDG-----YRAPEAelqnclaqaglQSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05063 157 LEDDPEGTYTTSGGkipirWTAPEA-----------IAYRKFTSASDVWSFGIVMWEVMS 205
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
142-304 1.45e-09

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: 58.85  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAeNECFKLIDFGLS--FKEGNQD--VKYIQTDGYRAPEAELQnclAQAGlqsdt 217
Cdd:cd07848 109 LIKAIHWCHKNDIVHRDIKPENLLISH-NDVLKLCDFGFArnLSEGSNAnyTEYVATRWYRSPELLLG---APYG----- 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 218 ectSAVDLWSLGIILLEMFSGMKLkhtvrsqeWKANSSaiIDHIFASKAVVNA----------AIPAYH----------- 276
Cdd:cd07848 180 ---KAVDMWSVGCILGELSDGQPL--------FPGESE--IDQLFTIQKVLGPlpaeqmklfySNPRFHglrfpavnhpq 246
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 28467003 277 -------------LRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07848 247 slerrylgilsgvLLDLMKNLLKLNPTDRYLTEQCLNHPAF 287
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
74-303 1.49e-09

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: 58.72  E-value: 1.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTIH--------FSPNVPsrclLLELLDVSVSELllysshqgcSMWMIQHCARDVLEA 145
Cdd:cd14104  44 KKEISILNIAR-HRNILRLHESFESHeelvmifeFISGVD----IFERITTARFEL---------NEREIVSYVRQVCEA 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 146 LAFLHHEGYVHADLKPRNILWSAE-NECFKLIDFGLS--FKEGNQ-DVKYIQTDgYRAPEAelqnclaqagLQSDTECTs 221
Cdd:cd14104 110 LEFLHSKNIGHFDIRPENIIYCTRrGSYIKIIEFGQSrqLKPGDKfRLQYTSAE-FYAPEV----------HQHESVST- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 222 AVDLWSLGIILLEMFSGM---------KLKHTVRSQEWKanssaiidhiFASKAVVNAAIPAYhlrDLIKSMLHDDPSRR 292
Cdd:cd14104 178 ATDMWSLGCLVYVLLSGInpfeaetnqQTIENIRNAEYA----------FDDEAFKNISIEAL---DFVDRLLVKERKSR 244
                       250
                ....*....|.
gi 28467003 293 IPAEMALCSPF 303
Cdd:cd14104 245 MTAQEALNHPW 255
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
86-240 1.51e-09

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: 58.48  E-value: 1.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIhfspNVPSRCLLLEL-----LDV------SVSELLLYSshqgcsmWMIQhcardVLEALAFL--HHE 152
Cdd:cd13990  63 HPRIVKLYDVFEI----DTDSFCTVLEYcdgndLDFylkqhkSIPEREARS-------IIMQ-----VVSALKYLneIKP 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAENEC--FKLIDFGLS--FKEGNQDVKYIQ-------TDGYRAPEAELQNclaqaglQSDTECTS 221
Cdd:cd13990 127 PIIHYDLKPGNILLHSGNVSgeIKITDFGLSkiMDDESYNSDGMEltsqgagTYWYLPPECFVVG-------KTPPKISS 199
                       170
                ....*....|....*....
gi 28467003 222 AVDLWSLGIILLEMFSGMK 240
Cdd:cd13990 200 KVDVWSVGVIFYQMLYGRK 218
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
140-304 1.52e-09

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: 58.22  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFG----LSfKEGNQDVKYIQTDGYRAPEAelqnclaQAGLQS 215
Cdd:cd06648 110 RAVLKALSFLHSQGVIHRDIKSDSILLTSDGRV-KLSDFGfcaqVS-KEVPRRKSLVGTPYWMAPEV-------ISRLPY 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 216 DTEctsaVDLWSLGIILLEM-------FSGMKLKHTVRSQEWKANSSAiiDHIFASKAvvnaaipayhLRDLIKSMLHDD 288
Cdd:cd06648 181 GTE----VDIWSLGIMVIEMvdgeppyFNEPPLQAMKRIRDNEPPKLK--NLHKVSPR----------LRSFLDRMLVRD 244
                       170
                ....*....|....*.
gi 28467003 289 PSRRIPAEMALCSPFF 304
Cdd:cd06648 245 PAQRATAAELLNHPFL 260
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
86-235 1.52e-09

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: 58.50  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFtiHFSPNVpsrCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNIL 165
Cdd:cd06643  61 HPNIVKLLDAF--YYENNL---WILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNIL 135
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 166 WSAENEcFKLIDFGLSFKEG---NQDVKYIQTDGYRAPEaelqncLAQAGLQSDTECTSAVDLWSLGIILLEM 235
Cdd:cd06643 136 FTLDGD-IKLADFGVSAKNTrtlQRRDSFIGTPYWMAPE------VVMCETSKDRPYDYKADVWSLGVTLIEM 201
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
29-240 1.52e-09

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: 58.28  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCcgnPGSPPGALKQFLPPGTTGAaasaaEYGFRKERAALEQLQgHRNIVTLYGvftihFSPNVPSRC 108
Cdd:cd14664   1 IGRGGAGTVYKGVM---PNGTLVAVKRLKGEGTQGG-----DHGFQAEIQTLGMIR-HRNIVRLRG-----YCSNPTTNL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 109 LLLELL-DVSVSELLLYSSHQGCSM-WMIQHcaRDVLEA---LAFLHHE---GYVHADLKPRNILWSAENECfKLIDFGL 180
Cdd:cd14664  67 LVYEYMpNGSLGELLHSRPESQPPLdWETRQ--RIALGSargLAYLHHDcspLIIHRDVKSNNILLDEEFEA-HVADFGL 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 181 S--FKEGNQDVKYI--QTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGMK 240
Cdd:cd14664 144 AklMDDKDSHVMSSvaGSYGYIAPE-----------YAYTGKVSEKSDVYSYGVVLLELITGKR 196
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
28-236 1.74e-09

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: 58.06  E-value: 1.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  28 RLGSGSSASVYRvrccG--NpGSPPGALKQfLPPGTTGAAAsaaeygFRKERAALEQLQgHRNIVTLYGVFT----IHFS 101
Cdd:cd05034   2 KLGAGQFGEVWM----GvwN-GTTKVAVKT-LKPGTMSPEA------FLQEAQIMKKLR-HDKLVQLYAVCSdeepIYIV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 PNVPSRCLLLELL-DVSVSELLLyssHQGCSMwmiqhcARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGL 180
Cdd:cd05034  69 TELMSKGSLLDYLrTGEGRALRL---PQLIDM------AAQIASGMAYLESRNYIHRDLAARNILVGENNVC-KVADFGL 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 181 SfkegnqdvKYIQTDGYR------------APEAELQNCLaqaglqsdtecTSAVDLWSLGIILLEMF 236
Cdd:cd05034 139 A--------RLIEDDEYTaregakfpikwtAPEAALYGRF-----------TIKSDVWSFGILLYEIV 187
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
73-237 1.83e-09

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: 57.96  E-value: 1.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFT---IHFSPNVPSRCLLLELLD------VSVSELLLYSshqgcsmwmiqhcaRDVL 143
Cdd:cd05083  46 FLEETAVMTKLQ-HKNLVRLLGVILhngLYIVMELMSKGNLVNFLRsrgralVPVIQLLQFS--------------LDVA 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 144 EALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVKYIQTDGYRAPEAeLQNclaqaglqsdTECTSAV 223
Cdd:cd05083 111 EGMEYLESKKLVHRDLAARNILVSEDGVA-KISDFGLAKVGSMGVDNSRLPVKWTAPEA-LKN----------KKFSSKS 178
                       170
                ....*....|....
gi 28467003 224 DLWSLGIILLEMFS 237
Cdd:cd05083 179 DVWSYGVLLWEVFS 192
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
86-303 1.84e-09

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: 58.04  E-value: 1.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIHFSPNvpsrcLLLE------LLDVsVSELLLYSSHQGCSMWMiqhcarDVLEALAFLHHEGYVHADL 159
Cdd:cd14185  57 HPNIVKLFEVYETEKEIY-----LILEyvrggdLFDA-IIESVKFTEHDAALMII------DLCEALVYIHSKHIVHRDL 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 160 KPRNILW---SAENECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEaelqnCLAQAGLQSDtectsaVDLWSLGIILLEMF 236
Cdd:cd14185 125 KPENLLVqhnPDKSTTLKLADFGLAKYVTGPIFTVCGTPTYVAPE-----ILSEKGYGLE------VDMWAAGVILYILL 193
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 237 SGM-KLKHTVRSQEWKANSSAIIDHIFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14185 194 CGFpPFRSPERDQEELFQIIQLGHYEFLPPYWDNISEAA---KDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-293 1.85e-09

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: 58.47  E-value: 1.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVR-CCGNPGSPPGALKqFLPPGTTGAAASAAEYGfRKERAALEQLQGHRNIVTLygvftiHFSPNVPSR 107
Cdd:cd05613   8 LGTGAYGKVFLVRkVSGHDAGKLYAMK-VLKKATIVQKAKTAEHT-RTERQVLEHIRQSPFLVTL------HYAFQTDTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLelLD-VSVSELLLY-SSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFkLIDFGLS---- 181
Cdd:cd05613  80 LHLI--LDyINGGELFTHlSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVV-LTDFGLSkefl 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 182 FKEGNQDVKYIQTDGYRAPEaelqncLAQAGlqsDTECTSAVDLWSLGIILLEMFSGMKlKHTVRSQEwkaNSSAIIdhi 261
Cdd:cd05613 157 LDENERAYSFCGTIEYMAPE------IVRGG---DSGHDKAVDWWSLGVLMYELLTGAS-PFTVDGEK---NSQAEI--- 220
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 28467003 262 faSKAVVNAAIP-----AYHLRDLIKSMLHDDPSRRI 293
Cdd:cd05613 221 --SRRILKSEPPypqemSALAKDIIQRLLMKDPKKRL 255
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
70-247 1.98e-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: 58.04  E-value: 1.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  70 EYGFRKERAALEQLQgHRNIVTLYGVFTihfsPNVPSrCLLLELLDVS-VSELLLYSSHQGCSMWMIQHCArDVLEALAF 148
Cdd:cd05112  43 EEDFIEEAEVMMKLS-HPKLVQLYGVCL----EQAPI-CLVFEFMEHGcLSDYLRTQRGLFSAETLLGMCL-DVCEGMAY 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSaENECFKLIDFGLSfkEGNQDVKYIQTDGYRAPEAelqncLAQAGLQSDTECTSAVDLWSL 228
Cdd:cd05112 116 LEEASVIHRDLAARNCLVG-ENQVVKVSDFGMT--RFVLDDQYTSSTGTKFPVK-----WSSPEVFSFSRYSSKSDVWSF 187
                       170
                ....*....|....*....
gi 28467003 229 GIILLEMFSGMKLKHTVRS 247
Cdd:cd05112 188 GVLMWEVFSEGKIPYENRS 206
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
24-238 2.07e-09

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: 57.89  E-value: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRvrCCGNPGSPPGALKQFLPPGTTGAAASAAEYGFRKeraaleQLQGHRNIVTLYGV-----FTI 98
Cdd:cd13975   3 KLGRELGRGQYGVVYA--CDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTR------SLPKHERIVSLHGSvidysYGG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  99 HFSPNVpsrCLLLELLDVSvsellLYSS-HQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLID 177
Cdd:cd13975  75 GSSIAV---LLIMERLHRD-----LYTGiKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRA-KITD 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28467003 178 FGLSFKEGNQDVKYIQTDGYRAPEAelqnclaqaglqSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd13975 146 LGFCKPEAMMSGSIVGTPIHMAPEL------------FSGKYDNSVDVYAFGILFWYLCAG 194
RRM_UHM_SPF45 cd12647
RNA recognition motif (RRM) found in UHM domain of 45 kDa-splicing factor (SPF45) and similar ...
348-411 2.23e-09

RNA recognition motif (RRM) found in UHM domain of 45 kDa-splicing factor (SPF45) and similar proteins; This subgroup corresponds to the RRM of SPF45, also termed RNA-binding motif protein 17 (RBM17), an RNA-binding protein consisting of an unstructured N-terminal region, followed by a G-patch motif and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and an Arg-Xaa-Phe sequence motif. SPF45 regulates alternative splicing of the apoptosis regulatory gene FAS (also known as CD95). It induces exon 6 skipping in FAS pre-mRNA through the UHM domain that binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) present in the 3' splice site-recognizing factors U2AF65, SF1 and SF3b155.


Pssm-ID: 410051 [Multi-domain]  Cd Length: 95  Bit Score: 54.21  E-value: 2.23e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 348 KEECQKYGPVVSLLVpKENPGRG-----QVFVEYANAGDSKAAQKLLTGRMFDGKFVVATFYPLSAYKR 411
Cdd:cd12647  25 KEECEKYGKVTKVVI-FEIPGAPddeavRIFVEFERVESAIKAVVDLNGRFFGGRTVKASFYDLDRFRR 92
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
133-303 2.44e-09

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: 57.82  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 WMIQhcardVLEALAFLHHEGYVHADLKPRNILwsAENECFKLIDFGLS-FKEGNQDV--KYIQTDGYRAPEAelqncLA 209
Cdd:cd08222 111 WFIQ-----LLLAVQYMHERRILHRDLKAKNIF--LKNNVIKVGDFGISrILMGTSDLatTFTGTPYYMSPEV-----LK 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 210 QAGLQSDTectsavDLWSLGIILLEMFSgmkLKHtvrsqewkanssAIIDHIFAS--KAVVNAAIPA------YHLRDLI 281
Cdd:cd08222 179 HEGYNSKS------DIWSLGCILYEMCC---LKH------------AFDGQNLLSvmYKIVEGETPSlpdkysKELNAIY 237
                       170       180
                ....*....|....*....|..
gi 28467003 282 KSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd08222 238 SRMLNKDPALRPSAAEILKIPF 259
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
74-293 2.74e-09

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: 57.66  E-value: 2.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALeQLQGHRNIVTLYGVFTihfspnVPSRC-LLLELldVSVSELLLYSSHQGcsmWMIQHCAR----DVLEALAF 148
Cdd:cd14079  50 RREIQIL-KLFRHPHIIRLYEVIE------TPTDIfMVMEY--VSGGELFDYIVQKG---RLSEDEARrffqQIISGVEY 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAeNECFKLIDFGLSfkegN--QDVKYIQTD----GYRAPEAelqnclaqagLQSDTECTSA 222
Cdd:cd14079 118 CHRHMVVHRDLKPENLLLDS-NMNVKIADFGLS----NimRDGEFLKTScgspNYAAPEV----------ISGKLYAGPE 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 223 VDLWSLGIILLEMFSGmKLKHTVRSqewkanssaiIDHIFASKAVVNAAIPAyHL----RDLIKSMLHDDPSRRI 293
Cdd:cd14079 183 VDVWSCGVILYALLCG-SLPFDDEH----------IPNLFKKIKSGIYTIPS-HLspgaRDLIKRMLVVDPLKRI 245
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
143-296 2.96e-09

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


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 57.65  E-value: 2.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 143 LEALAFLHHEGYVHADLKPRNILWSAENECFkLIDFGlSFK-----EGN-QDVKY-IQTDGYR----APE---AELQncL 208
Cdd:cd13980 107 LHALNQCHKRGVCHGDIKTENVLVTSWNWVY-LTDFA-SFKptylpEDNpADFSYfFDTSRRRtcyiAPErfvDALT--L 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 209 AQAGLQSDTECTSAVDLWSLGIILLEMFSGMKLKHTVrSQ--EWKANSSAIIDHIfaskavvnAAIPAYHLRDLIKSMLH 286
Cdd:cd13980 183 DAESERRDGELTPAMDIFSLGCVIAELFTEGRPLFDL-SQllAYRKGEFSPEQVL--------EKIEDPNIRELILHMIQ 253
                       170
                ....*....|
gi 28467003 287 DDPSRRIPAE 296
Cdd:cd13980 254 RDPSKRLSAE 263
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
139-299 3.50e-09

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 57.72  E-value: 3.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALA----FLHHEGYVHADLKPRNILW---SAENECFKLIDFGLSfKEGNQDVKYIQTDGYR----APEAelqnc 207
Cdd:cd14177 100 ASAVLYTITktvdYLHCQGVVHRDLKPSNILYmddSANADSIRICDFGFA-KQLRGENGLLLTPCYTanfvAPEV----- 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 208 LAQAGLQsdtectSAVDLWSLGIILLEMFSGmklkHTVRSQEWKANSSAIIDHIFASK---------AVVNAAipayhlR 278
Cdd:cd14177 174 LMRQGYD------AACDIWSLGVLLYTMLAG----YTPFANGPNDTPEEILLRIGSGKfslsggnwdTVSDAA------K 237
                       170       180
                ....*....|....*....|.
gi 28467003 279 DLIKSMLHDDPSRRIPAEMAL 299
Cdd:cd14177 238 DLLSHMLHVDPHQRYTAEQVL 258
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
142-304 3.56e-09

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 57.69  E-value: 3.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfKEGNQDV----KYIQTDGYRAPEaelqnclaqagLQSDT 217
Cdd:cd06659 126 VLQALAYLHSQGVIHRDIKSDSILLTLDGR-VKLSDFGFC-AQISKDVpkrkSLVGTPYWMAPE-----------VISRC 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 218 ECTSAVDLWSLGIILLEMFSG----------MKLKHTVRSQEWKANSSAIIDHIfaskavvnaaipayhLRDLIKSMLHD 287
Cdd:cd06659 193 PYGTEVDIWSLGIMVIEMVDGeppyfsdspvQAMKRLRDSPPPKLKNSHKASPV---------------LRDFLERMLVR 257
                       170
                ....*....|....*..
gi 28467003 288 DPSRRIPAEMALCSPFF 304
Cdd:cd06659 258 DPQERATAQELLDHPFL 274
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
23-304 3.59e-09

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: 57.21  E-value: 3.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRV--RCCGNpgsppGALKQFLPpgttgAAASAAEYGFRKERAALEQLQgHRNIVTLYGVFTihf 100
Cdd:cd14114   4 YDILEELGTGAFGVVHRCteRATGN-----NFAAKFIM-----TPHESDKETVRKEIQIMNQLH-HPKLINLHDAFE--- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 101 spNVPSRCLLLELLdvSVSELLLYSSHQGCSM-------WMIQHCardvlEALAFLHHEGYVHADLKPRNILWSAENEC- 172
Cdd:cd14114  70 --DDNEMVLILEFL--SGGELFERIAAEHYKMseaevinYMRQVC-----EGLCHMHENNIVHLDIKPENIMCTTKRSNe 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 173 FKLIDFGLSFK-EGNQDVKYIQ-TDGYRAPEAelqnclaqaglqSDTECTS-AVDLWSLGIILLEMFSGMK--------- 240
Cdd:cd14114 141 VKLIDFGLATHlDPKESVKVTTgTAEFAAPEI------------VEREPVGfYTDMWAVGVLSYVLLSGLSpfagendde 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 241 -LKHtVRSQEWKANSSAIidhifasKAVVNAAipayhlRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14114 209 tLRN-VKSCDWNFDDSAF-------SGISEEA------KDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
135-304 3.88e-09

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


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 57.83  E-value: 3.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLSF----------KEGNQDVKYIQTDGY------- 197
Cdd:cd14013 122 IKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQFKIIDLGAAAdlriginyipKEFLLDPRYAPPEQYimstqtp 201
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 198 RAP----EAELQNCLAQAGLqsdtecTSAVDLWSLGIILLEMF-------SGMKLKHTV------------RSQEWKANS 254
Cdd:cd14013 202 SAPpapvAAALSPVLWQMNL------PDRFDMYSAGVILLQMAfpnlrsdSNLIAFNRQlkqcdydlnawrMLVEPRASA 275
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 255 S-----AIIDhifaskavVNAAIPAyhlrDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14013 276 DlregfEILD--------LDDGAGW----DLVTKLIRYKPRGRLSASAALAHPYF 318
RRM_UHM_SPF45_PUF60 cd12374
RNA recognition motif (RRM) found in UHM domain of 45 kDa-splicing factor (SPF45) and similar ...
348-405 3.89e-09

RNA recognition motif (RRM) found in UHM domain of 45 kDa-splicing factor (SPF45) and similar proteins; This subfamily corresponds to the RRM found in UHM domain of 45 kDa-splicing factor (SPF45 or RBM17), poly(U)-binding-splicing factor PUF60 (FIR or Hfp or RoBP1 or Siah-BP1), and similar proteins. SPF45 is an RNA-binding protein consisting of an unstructured N-terminal region, followed by a G-patch motif and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and an Arg-Xaa-Phe sequence motif. SPF45 regulates alternative splicing of the apoptosis regulatory gene FAS (also known as CD95). It induces exon 6 skipping in FAS pre-mRNA through the UHM domain that binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) present in the 3' splice site-recognizing factors U2AF65, SF1 and SF3b155. PUF60 is an essential splicing factor that functions as a poly-U RNA-binding protein required to reconstitute splicing in depleted nuclear extracts. Its function is enhanced through interaction with U2 auxiliary factor U2AF65. PUF60 also controls human c-myc gene expression by binding and inhibiting the transcription factor far upstream sequence element (FUSE)-binding-protein (FBP), an activator of c-myc promoters. PUF60 contains two central RRMs and a C-terminal UHM domain.


Pssm-ID: 409809 [Multi-domain]  Cd Length: 85  Bit Score: 53.38  E-value: 3.89e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28467003 348 KEECQKYGPVVSLLV----PKENPGRGQVFVEYANAGDSKAAQKLLTGRMFDGKFVVATFYP 405
Cdd:cd12374  24 KEECSKYGKVLNVIIhevaSSEADDAVRVFVEFEDADEAIKAFRALNGRFFGGRKVKARFYD 85
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
75-238 3.99e-09

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: 57.35  E-value: 3.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQGHRNIVTLygvftIHFSPNVPSRCLLLELLdVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGY 154
Cdd:cd14174  48 REVETLYQCQGNKNILEL-----IEFFEDDTRFYLVFEKL-RGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGI 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNILWSAENEC--FKLIDFGL-SFKEGNQDVKYIQTD---------GYRAPeaELQNCLAQAGLQSDTECtsa 222
Cdd:cd14174 122 AHRDLKPENILCESPDKVspVKICDFDLgSGVKLNSACTPITTPelttpcgsaEYMAP--EVVEVFTDEATFYDKRC--- 196
                       170
                ....*....|....*.
gi 28467003 223 vDLWSLGIILLEMFSG 238
Cdd:cd14174 197 -DLWSLGVILYIMLSG 211
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
142-292 4.06e-09

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: 57.02  E-value: 4.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAeNECFKLIDFGLSfKEGNQDVKYIQ--TDGYRAPEaelqnclaqagLQSDTEC 219
Cdd:cd08530 112 MLRGLKALHDQKILHRDLKSANILLSA-GDLVKIGDLGIS-KVLKKNLAKTQigTPLYAAPE-----------VWKGRPY 178
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 220 TSAVDLWSLGIILLEMfsgMKLKHTVRSQEWKANSSAIIDHIFaskavvnAAIPAYHLRDL---IKSMLHDDPSRR 292
Cdd:cd08530 179 DYKSDIWSLGCLLYEM---ATFRPPFEARTMQELRYKVCRGKF-------PPIPPVYSQDLqqiIRSLLQVNPKKR 244
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
142-303 4.69e-09

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: 56.77  E-value: 4.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECFKLI--DFGL-SFKEGNQDVKYIQTDG---YRAPEAELQnclaqaglqs 215
Cdd:cd14087 106 VLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMitDFGLaSTRKKGPNCLMKTTCGtpeYIAPEILLR---------- 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 216 dTECTSAVDLWSLGIILLEMFSG-MKLKHTVRSQEW----KANSSAIIDHIfasKAVVNAAipayhlRDLIKSMLHDDPS 290
Cdd:cd14087 176 -KPYTQSVDMWAVGVIAYILLSGtMPFDDDNRTRLYrqilRAKYSYSGEPW---PSVSNLA------KDFIDRLLTVNPG 245
                       170
                ....*....|...
gi 28467003 291 RRIPAEMALCSPF 303
Cdd:cd14087 246 ERLSATQALKHPW 258
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
143-304 4.87e-09

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: 57.32  E-value: 4.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 143 LEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS-----------FKEGNQDVKY---IQTDGYRAPEAELQNCl 208
Cdd:cd07866 125 LEGINYLHENHILHRDIKAANILID-NQGILKIADFGLArpydgpppnpkGGGGGGTRKYtnlVVTRWYRPPELLLGER- 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 209 aqaglqsdtECTSAVDLWSLGIILLEMFSG----------------MKLKHTVRSQEWKANSS---AIIDHIFASKAVVN 269
Cdd:cd07866 203 ---------RYTTAVDIWGIGCVFAEMFTRrpilqgksdidqlhliFKLCGTPTEETWPGWRSlpgCEGVHSFTNYPRTL 273
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 28467003 270 AAIPAYHLR---DLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd07866 274 EERFGKLGPeglDLLSKLLSLDPYKRLTASDALEHPYF 311
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
73-237 4.92e-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: 56.91  E-value: 4.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTIHFSpnvpSRCLLLELLdvSVSELLLYSSHQGCSMW---MIQHCARDVLEALAFL 149
Cdd:cd05082  46 FLAEASVMTQLR-HSNLVQLLGVIVEEKG----GLYIVTEYM--AKGSLVDYLRSRGRSVLggdCLLKFSLDVCEAMEYL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 150 HHEGYVHADLKPRNILWSAENeCFKLIDFGLSfKEGN--QDVKYIQTDgYRAPEAelqnclaqagLQSDTECTSAvDLWS 227
Cdd:cd05082 119 EGNNFVHRDLAARNVLVSEDN-VAKVSDFGLT-KEASstQDTGKLPVK-WTAPEA----------LREKKFSTKS-DVWS 184
                       170
                ....*....|
gi 28467003 228 LGIILLEMFS 237
Cdd:cd05082 185 FGILLWEIYS 194
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
27-238 5.21e-09

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: 57.05  E-value: 5.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  27 SRLGSGSSASVYRVRCcgNPGSPPGALKQFL-PPGTTGAAASAAEYGFRKERAaleqlqgHRNIVTLYGVFTIHFSPNVP 105
Cdd:cd06621   7 SSLGEGAGGSVTKCRL--RNTKTIFALKTITtDPNPDVQKQILRELEINKSCA-------SPYIVKYYGAFLDEQDSSIG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 106 srcLLLEL-----LDVSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL 180
Cdd:cd06621  78 ---IAMEYceggsLDSIYKKVK--KKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ-VKLCDFGV 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 181 SFKEGNQ-DVKYIQTDGYRAPEAelqnclAQAGLQSDTEctsavDLWSLGIILLEMFSG 238
Cdd:cd06621 152 SGELVNSlAGTFTGTSYYMAPER------IQGGPYSITS-----DVWSLGLTLLEVAQN 199
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
74-238 5.67e-09

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: 56.77  E-value: 5.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVftihfspNVPSRCLLLELLDV---SVSELLlySSHQGCSMWMIQHCARDVLEALAFLH 150
Cdd:cd06628  54 QREIALLRELQ-HENIVQYLGS-------SSDANHLNIFLEYVpggSVATLL--NNYGAFEESLVRNFVRQILKGLNYLH 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILwsAENE-CFKLIDFGLSFK-EGNQDVkyIQTDGYR----------APEAELQnclaqaglqsdTE 218
Cdd:cd06628 124 NRGIIHRDIKGANIL--VDNKgGIKISDFGISKKlEANSLS--TKNNGARpslqgsvfwmAPEVVKQ-----------TS 188
                       170       180
                ....*....|....*....|
gi 28467003 219 CTSAVDLWSLGIILLEMFSG 238
Cdd:cd06628 189 YTRKADIWSLGCLVVEMLTG 208
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
23-181 6.44e-09

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: 56.31  E-value: 6.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVRCCGNpgsppG---ALKqfLPPGTTgaaasaAEYGFRKERAALEQLQGHRNIVTLYgvftiH 99
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDLKT-----GeevAIK--IEKKDS------KHPQLEYEAKVYKLLQGGPGIPRLY-----W 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 100 FSPNVPSRCLLLELLDVSVSELLLYSSHQGC----SMWMIQhcardVLEALAFLHHEGYVHADLKPRNIL---WSAENEC 172
Cdd:cd14016  64 FGQEGDYNVMVMDLLGPSLEDLFNKCGRKFSlktvLMLADQ-----MISRLEYLHSKGYIHRDIKPENFLmglGKNSNKV 138

                ....*....
gi 28467003 173 FkLIDFGLS 181
Cdd:cd14016 139 Y-LIDFGLA 146
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
73-237 6.89e-09

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: 56.20  E-value: 6.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfspnVPSRCLLLELL-------------DVSVSELLLysshqgcsmWMIQhca 139
Cdd:cd05060  43 FLREASVMAQLD-HPCIVRLIGVCK------GEPLMLVMELAplgpllkylkkrrEIPVSDLKE---------LAHQ--- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 rdVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVKYIQTDGYR------APEaelqnCLAQAGL 213
Cdd:cd05060 104 --VAMGMAYLESKHFVHRDLAARNVLLVNRHQA-KISDFGMSRALGAGSDYYRATTAGRwplkwyAPE-----CINYGKF 175
                       170       180
                ....*....|....*....|....
gi 28467003 214 qsdtecTSAVDLWSLGIILLEMFS 237
Cdd:cd05060 176 ------SSKSDVWSYGVTLWEAFS 193
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
80-258 6.91e-09

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 55.96  E-value: 6.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  80 LEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQhCARDVLEALAFLHHEGYVHADL 159
Cdd:cd14059  35 LRKLN-HPNIIKFKGVCT-----QAPCYCILMEYCPYGQLYEVLRAGREITPSLLVD-WSKQIASGMNYLHLHKIIHRDL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 160 KPRNILWSaENECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAeLQNclaqaglqsdTECTSAVDLWSLGIILLEMFS 237
Cdd:cd14059 108 KSPNVLVT-YNDVLKISDFGTSkeLSEKSTKMSFAGTVAWMAPEV-IRN----------EPCSEKVDIWSFGVVLWELLT 175
                       170       180
                ....*....|....*....|.
gi 28467003 238 GMKLKHTVrsqewkaNSSAII 258
Cdd:cd14059 176 GEIPYKDV-------DSSAII 189
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
73-249 7.26e-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: 56.56  E-value: 7.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELLDV-SVSE-LLLYSSHQ--GCSM------------WMIQ 136
Cdd:cd05090  54 FQQEASLMTELH-HPNIVCLLGVVT-----QEQPVCMLFEFMNQgDLHEfLIMRSPHSdvGCSSdedgtvkssldhGDFL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 137 HCARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSFKEGNQDVKYIQTDG-----YRAPEAelqncLAQA 211
Cdd:cd05090 128 HIAIQIAAGMEYLSSHFFVHKDLAARNIL-VGEQLHVKISDLGLSREIYSSDYYRVQNKSllpirWMPPEA-----IMYG 201
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 28467003 212 GLQSDTectsavDLWSLGIILLEMFS-GMKLKHTVRSQE 249
Cdd:cd05090 202 KFSSDS------DIWSFGVVLWEIFSfGLQPYYGFSNQE 234
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
236-409 7.53e-09

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 57.62  E-value: 7.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   236 FSGMKLKHTVRSQEWKANSSAIIDHIFASK---AVVNAAIPAYHLRDLI--KSMLHDDPSRRIPAEMALCSPFFSIPFAP 310
Cdd:TIGR01622 314 FSGAGLNTPARSQLMRKLARDNEKGTGGLAipgTDVGGVNMNNYSRDGLmrKLAPTDEPPAVIPETQILKPKAETSFVPV 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   311 HiedlVMLPTPVLRLLNVLDDDYLENEEEYEDVVEDVKEECQKYGPVVSLLVPKENpGRGQVFVEYANAGDSKAAQKLLT 390
Cdd:TIGR01622 394 N----VNLASRCLVLSNMFDPATEEEPNWDKEIEDDVREECSKYGGVVHIYVDDKN-SAGDIYLKFDSVQAAEAAIKALN 468
                         170
                  ....*....|....*....
gi 28467003   391 GRMFDGKFVVATFYPLSAY 409
Cdd:TIGR01622 469 GRYFGGKMITAAFVVDAVY 487
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
135-238 7.60e-09

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: 56.09  E-value: 7.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFK---EGNQDVKYIQTDGYRAPEAELQNclaQA 211
Cdd:cd06647 105 IAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSV-KLTDFGFCAQitpEQSKRSTMVGTPYWMAPEVVTRK---AY 180
                        90       100
                ....*....|....*....|....*..
gi 28467003 212 GlqsdtectSAVDLWSLGIILLEMFSG 238
Cdd:cd06647 181 G--------PKVDIWSLGIMAIEMVEG 199
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
142-305 8.69e-09

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: 56.62  E-value: 8.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKY---IQTDGYRAPEAelqnclaqagLQSDTE 218
Cdd:cd07869 112 LLRGLSYIHQRYILHRDLKPQNLLISDTGE-LKLADFGLARAKSVPSHTYsneVVTLWYRPPDV----------LLGSTE 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 219 CTSAVDLWSLGIILLEM------FSGMK-----------LKHTVRSQEWKANSSaiIDH-------IFASKAVV---NAA 271
Cdd:cd07869 181 YSTCLDMWGVGCIFVEMiqgvaaFPGMKdiqdqleriflVLGTPNEDTWPGVHS--LPHfkperftLYSPKNLRqawNKL 258
                       170       180       190
                ....*....|....*....|....*....|....
gi 28467003 272 IPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFFS 305
Cdd:cd07869 259 SYVNHAEDLASKLLQCFPKNRLSAQAALSHEYFS 292
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
139-238 9.15e-09

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: 56.26  E-value: 9.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLeALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLS----------FKEGN--------QDVKYIQTDGYRAP 200
Cdd:cd05609 107 AETVL-ALEYLHSYGIVHRDLKPDNLLITSMGH-IKLTDFGLSkiglmslttnLYEGHiekdtrefLDKQVCGTPEYIAP 184
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 28467003 201 EAELQNCLAQaglqsdtectsAVDLWSLGIILLEMFSG 238
Cdd:cd05609 185 EVILRQGYGK-----------PVDWWAMGIILYEFLVG 211
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
74-246 9.35e-09

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: 55.86  E-value: 9.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELldVSVSELLLY-SSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14073  49 RREIEIMSSLN-HPHIIRIYEVFE-----NKDKIVIVMEY--ASGGELYDYiSERRRLPEREARRIFRQIVSAVHYCHKN 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSaENECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPeaELQNCLAQAGLQsdtectsaVDLWSLGI 230
Cdd:cd14073 121 GVVHRDLKLENILLD-QNGNAKIADFGLSnlYSKDKLLQTFCGSPLYASP--EIVNGTPYQGPE--------VDCWSLGV 189
                       170       180
                ....*....|....*....|..
gi 28467003 231 ILLEM------FSGMKLKHTVR 246
Cdd:cd14073 190 LLYTLvygtmpFDGSDFKRLVK 211
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
137-293 1.02e-08

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 56.36  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  137 HCARDVLeALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSD 216
Cdd:PTZ00263 123 YHAELVL-AFEYLHSKDIIYRDLKPENLLLDNKGH-VKVTDFGFAKKVPDRTFTLCGTPEYLAPEV----------IQSK 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  217 TEcTSAVDLWSLGIILLEMFSGMKL---KHTVRSQEWKANSSAIIDHIFASKAvvnaaipayhlRDLIKSMLHDDPSRRI 293
Cdd:PTZ00263 191 GH-GKAVDWWTMGVLLYEFIAGYPPffdDTPFRIYEKILAGRLKFPNWFDGRA-----------RDLVKGLLQTDHTKRL 258
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
86-295 1.02e-08

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: 55.79  E-value: 1.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVF----TIHFSPNVPSRCLLLELLDvSVSELLLYSShqgcsMWMIQHcardVLEALAFLHHEGYVHADLKP 161
Cdd:cd13995  55 HENIAELYGALlweeTVHLFMEAGEGGSVLEKLE-SCGPMREFEI-----IWVTKH----VLKGLDFLHSKNIIHHDIKP 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 162 RNILWSAENECfkLIDFGLSFKEgNQDVKYIQ----TDGYRAPEAELqnCLAQaglqsdtecTSAVDLWSLGIILLEMFS 237
Cdd:cd13995 125 SNIVFMSTKAV--LVDFGLSVQM-TEDVYVPKdlrgTEIYMSPEVIL--CRGH---------NTKADIYSLGATIIHMQT 190
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28467003 238 GMklKHTVRSQEWKANSSAIidHIFASKAVVNAAIP---AYHLRDLIKSMLHDDPSRRIPA 295
Cdd:cd13995 191 GS--PPWVRRYPRSAYPSYL--YIIHKQAPPLEDIAqdcSPAMRELLEAALERNPNHRSSA 247
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
73-238 1.19e-08

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: 55.69  E-value: 1.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFtihFSPNVPSRCLLLELldVSVSELLLY-SSHQGCSMWMIQHCARDVLEALAFLHH 151
Cdd:cd13983  47 FKQEIEILKSLK-HPNIIKFYDSW---ESKSKKEVIFITEL--MTSGTLKQYlKRFKRLKLKVIKSWCRQILEGLNYLHT 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EGY--VHADLKPRNILWSAENECFKLIDFGLS-FKEGNQDVKYIQTDGYRAPEAELQNClaqaglqsdtecTSAVDLWSL 228
Cdd:cd13983 121 RDPpiIHRDLKCDNIFINGNTGEVKIGDLGLAtLLRQSFAKSVIGTPEFMAPEMYEEHY------------DEKVDIYAF 188
                       170
                ....*....|
gi 28467003 229 GIILLEMFSG 238
Cdd:cd13983 189 GMCLLEMATG 198
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
132-308 1.20e-08

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: 56.24  E-value: 1.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 132 MWMIQHCAR-----------DVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVK---YIQTDGY 197
Cdd:cd05592  84 MFHIQQSGRfdedrarfygaEIICGLQFLHSRGIIYRDLKLDNVLLDREGH-IKIADFGMCKENIYGENKastFCGTPDY 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 198 RAPEAeLQnclaqaGLQSDtectSAVDLWSLGIILLEMFSGMKLKHTvrSQEwkanssaiiDHIFASKAVVNAAIPAYHL 277
Cdd:cd05592 163 IAPEI-LK------GQKYN----QSVDWWSFGVLLYEMLIGQSPFHG--EDE---------DELFWSICNDTPHYPRWLT 220
                       170       180       190
                ....*....|....*....|....*....|....
gi 28467003 278 R---DLIKSMLHDDPSRRIPAEMALCSPFFSIPF 308
Cdd:cd05592 221 KeaaSCLSLLLERNPEKRLGVPECPAGDIRDHPF 254
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
140-238 1.23e-08

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 55.60  E-value: 1.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEaelqncLAQAGLQSDT 217
Cdd:cd14072 106 RQIVSAVQYCHQKRIVHRDLKAENLLLDADMN-IKIADFGFSneFTPGNKLDTFCGSPPYAAPE------LFQGKKYDGP 178
                        90       100
                ....*....|....*....|.
gi 28467003 218 EctsaVDLWSLGIILLEMFSG 238
Cdd:cd14072 179 E----VDVWSLGVILYTLVSG 195
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
108-241 1.30e-08

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: 56.25  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILW---SAENECFKLIDFGlSFKE 184
Cdd:cd14228  92 CLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpVRQPYRVKVIDFG-SASH 170
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 185 GNQDV--KYIQTDGYRAPEAELqnclaqaGLqsdtECTSAVDLWSLGIILLEMFSGMKL 241
Cdd:cd14228 171 VSKAVcsTYLQSRYYRAPEIIL-------GL----PFCEAIDMWSLGCVIAELFLGWPL 218
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
75-308 1.36e-08

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: 55.79  E-value: 1.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVftiHFSPNvpSRCLLLELLDVSvsELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHEG 153
Cdd:cd14201  54 KEIKILKELQ-HENIVALYDV---QEMPN--SVFLVMEYCNGG--DLADYLQAKGTlSEDTIRVFLQQIAAAMRILHSKG 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 154 YVHADLKPRNILWSAENEC--------FKLIDFGLSfkegnqdvKYIQTD----------GYRAPEAEL-QNCLAQAglq 214
Cdd:cd14201 126 IIHRDLKPQNILLSYASRKkssvsgirIKIADFGFA--------RYLQSNmmaatlcgspMYMAPEVIMsQHYDAKA--- 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 sdtectsavDLWSLGIILLEMFSGmklkhtvrSQEWKANSSAIIDHIFASKAVVNAAIP---AYHLRDLIKSMLHDDPSR 291
Cdd:cd14201 195 ---------DLWSIGTVIYQCLVG--------KPPFQANSPQDLRMFYEKNKNLQPSIPretSPYLADLLLGLLQRNQKD 257
                       250
                ....*....|....*..
gi 28467003 292 RIPAEmalcsPFFSIPF 308
Cdd:cd14201 258 RMDFE-----AFFSHPF 269
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
138-183 1.44e-08

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 53.81  E-value: 1.44e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28467003 138 CARDVLEALAFLHHEGYVHADLKPRNILWSAENecFKLIDFGLSFK 183
Cdd:COG3642  56 LLRELGRLLARLHRAGIVHGDLTTSNILVDDGG--VYLIDFGLARY 99
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
76-303 1.49e-08

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: 55.49  E-value: 1.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQGHRNIVTLYG------VFTIhFSPNVPSRclllelldvSVSELLLysshqgcSMW--------MIQHCARD 141
Cdd:cd06624  54 EEIALHSRLSHKNIVQYLGsvsedgFFKI-FMEQVPGG---------SLSALLR-------SKWgplkdnenTIGYYTKQ 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLSFKEGNQDV---KYIQTDGYRAPEAELQnclAQAGLqsdte 218
Cdd:cd06624 117 ILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVVKISDFGTSKRLAGINPcteTFTGTLQYMAPEVIDK---GQRGY----- 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 219 cTSAVDLWSLGIILLEMFSGMKLKHTVRSQEwkanssAIIDHIFASKavVNAAIP---AYHLRDLIKSMLHDDPSRRIPA 295
Cdd:cd06624 189 -GPPADIWSLGCTIIEMATGKPPFIELGEPQ------AAMFKVGMFK--IHPEIPeslSEEAKSFILRCFEPDPDKRATA 259

                ....*...
gi 28467003 296 EMALCSPF 303
Cdd:cd06624 260 SDLLQDPF 267
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
145-239 1.58e-08

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: 55.87  E-value: 1.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfKEGNQDVK----YIQTDGYRAPEAelqncLAQAGLqsdtecT 220
Cdd:cd05582 109 ALDHLHSLGIIYRDLKPENILLDEDGH-IKLTDFGLS-KESIDHEKkaysFCGTVEYMAPEV-----VNRRGH------T 175
                        90
                ....*....|....*....
gi 28467003 221 SAVDLWSLGIILLEMFSGM 239
Cdd:cd05582 176 QSADWWSFGVLMFEMLTGS 194
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
145-238 1.67e-08

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 55.79  E-value: 1.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL--SFKeGNQDVKYIQ------TDGYRAPEAelqncLAQAGLqsd 216
Cdd:cd05598 113 AIESVHKMGFIHRDIKPDNILIDRDGH-IKLTDFGLctGFR-WTHDSKYYLahslvgTPNYIAPEV-----LLRTGY--- 182
                        90       100
                ....*....|....*....|..
gi 28467003 217 tecTSAVDLWSLGIILLEMFSG 238
Cdd:cd05598 183 ---TQLCDWWSVGVILYEMLVG 201
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
134-304 1.72e-08

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: 55.24  E-value: 1.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCARD---------------VLEALAFLHHEGY-----VHADLKPRNILWSaENECFKLIDFGLSfKEGNQDVK--- 190
Cdd:cd08217  91 LIKKCKKEnqyipeefiwkiftqLLLALYECHNRSVgggkiLHRDLKPANIFLD-SDNNVKLGDFGLA-RVLSHDSSfak 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 191 -YIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSgmkLKHTVRSQEWKANSSAIidhifasKAVVN 269
Cdd:cd08217 169 tYVGTPYYMSPE-----------LLNEQSYDEKSDIWSLGCLIYELCA---LHPPFQAANQLELAKKI-------KEGKF 227
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 28467003 270 AAIPAY---HLRDLIKSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd08217 228 PRIPSRyssELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
130-295 1.98e-08

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: 55.27  E-value: 1.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 130 CSMWMIQhcardVLEALAFLHHEGYVHADLKPRNILWSAEnECFKLIDFGLSFKEGNQD---------------VKYIQT 194
Cdd:cd14048 120 CLNIFKQ-----IASAVEYLHSKGLIHRDLKPSNVFFSLD-DVVKVGDFGLVTAMDQGEpeqtvltpmpayakhTGQVGT 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 195 DGYRAPEaelqnclaQAGLQSDTEctsAVDLWSLGIILLEmfsgmkLKHTVRSQEWKAnssaiidHIFASkaVVNAAIPA 274
Cdd:cd14048 194 RLYMSPE--------QIHGNQYSE---KVDIFALGLILFE------LIYSFSTQMERI-------RTLTD--VRKLKFPA 247
                       170       180
                ....*....|....*....|....*..
gi 28467003 275 YHL------RDLIKSMLHDDPSRRIPA 295
Cdd:cd14048 248 LFTnkypeeRDMVQQMLSPSPSERPEA 274
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
139-238 2.04e-08

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: 54.87  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARD----VLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLS-FKEGNQDVK--YIQTDGYRAPEAELqnclaqa 211
Cdd:cd14164 102 ARDmfaqMVGAVNYLHDMNIVHRDLKCENILLSADDRKIKIADFGFArFVEDYPELSttFCGSRAYTPPEVIL------- 174
                        90       100
                ....*....|....*....|....*..
gi 28467003 212 GLQSDTEctsAVDLWSLGIILLEMFSG 238
Cdd:cd14164 175 GTPYDPK---KYDVWSLGVVLYVMVTG 198
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
131-303 2.10e-08

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: 55.24  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 131 SMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILW-SAENEC-FKLIDFGLSFKEGNQDVKY---IQTDGYRAPEA--- 202
Cdd:cd14094 107 SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSApVKLGGFGVAIQLGESGLVAggrVGTPHFMAPEVvkr 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 203 ELQNClaqaglqsdtectsAVDLWSLGIILLEMFSG---------------MKLKHTVRSQEWkanssaiiDHIFASKav 267
Cdd:cd14094 187 EPYGK--------------PVDVWGCGVILFILLSGclpfygtkerlfegiIKGKYKMNPRQW--------SHISESA-- 242
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 28467003 268 vnaaipayhlRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd14094 243 ----------KDLVRRMLMLDPAERITVYEALNHPW 268
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
73-238 2.14e-08

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 54.76  E-value: 2.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTiHFSPNVpsrcLLLELldVSVSELLLYSSHQGCSMWMIQ--HCARDVLEALAFLH 150
Cdd:cd05041  40 FLQEARILKQYD-HPNIVKLIGVCV-QKQPIM----IVMEL--VPGGSLLTFLRKKGARLTVKQllQMCLDAAAGMEYLE 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSaENECFKLIDFGLSFKEgnQDVKYIQTDGYR-------APEAELQNclaqaglqsdtECTSAV 223
Cdd:cd05041 112 SKNCIHRDLAARNCLVG-ENNVLKISDFGMSREE--EDGEYTVSDGLKqipikwtAPEALNYG-----------RYTSES 177
                       170
                ....*....|....*
gi 28467003 224 DLWSLGIILLEMFSG 238
Cdd:cd05041 178 DVWSFGILLWEIFSL 192
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
86-303 2.68e-08

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: 54.48  E-value: 2.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFtihfspNVPSRC-LLLELL-DVSVSELLLYSSH--QGCSMWMIQHCArdvlEALAFLHHEGYVHADLKP 161
Cdd:cd14097  59 HAHIIHLEEVF------ETPKRMyLVMELCeDGELKELLLRKGFfsENETRHIIQSLA----SAVAYLHKNDIVHRDLKL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 162 RNILWS------AENECFKLIDFGLSFKEGNQDVKYIQ----TDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGII 231
Cdd:cd14097 129 ENILVKssiidnNDKLNIKVTDFGLSVQKYGLGEDMLQetcgTPIYMAPE-----------VISAHGYSQQCDIWSIGVI 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 232 LLEMFSGM---------KLKHTVRSQEWKANSSAIidhifasKAVVNAAipayhlRDLIKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd14097 198 MYMLLCGEppfvakseeKLFEEIRKGDLTFTQSVW-------QSVSDAA------KNVLQQLLKVDPAHRMTASELLDNP 264

                .
gi 28467003 303 F 303
Cdd:cd14097 265 W 265
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
86-319 2.71e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 55.62  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   86 HRNIVTLygvftIHFSPNVPSRCLLLElldVSVSELLLYSSHQGC----SMWMIQhcaRDVLEALAFLHHEGYVHADLKP 161
Cdd:PHA03207 145 HRAIINL-----IHAYRWKSTVCMVMP---KYKCDLFTYVDRSGPlpleQAITIQ---RRLLEALAYLHGRGIIHRDVKT 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  162 RNILWSAENECFkLIDFGLSFKEGN-----QDVKYIQTDGYRAPEAelqnclaqagLQSDTECTSaVDLWSLGIILLEMF 236
Cdd:PHA03207 214 ENIFLDEPENAV-LGDFGAACKLDAhpdtpQCYGWSGTLETNSPEL----------LALDPYCAK-TDIWSAGLVLFEMS 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  237 -------------SGMKLKHTVRSQ-----EWKANSSAIIDHIFASKAVVNAaiPAYHLRDLI-KSMLHDDpsrripAEM 297
Cdd:PHA03207 282 vknvtlfgkqvksSSSQLRSIIRCMqvhplEFPQNGSTNLCKHFKQYAIVLR--PPYTIPPVIrKYGMHMD------VEY 353
                        250       260
                 ....*....|....*....|...
gi 28467003  298 ALCSPF-FSIPFAPHIEDLVMLP 319
Cdd:PHA03207 354 LIAKMLtFDQEFRPSAQDILSLP 376
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
73-237 3.02e-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: 54.69  E-value: 3.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfsPNVPsRCLLLELLDV-SVSE-LLLYSSHQGCSMWMIQHCARDVLEALAFL- 149
Cdd:cd05048  55 FRREAELMSDLQ-HPNIVCLLGVCT----KEQP-QCMLFEYMAHgDLHEfLVRHSPHSDVGVSSDDDGTASSLDQSDFLh 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 150 --------------HHegYVHADLKPRNILwSAENECFKLIDFGLSFKEGNQDVKYIQTDG-----YRAPEAELQNclaq 210
Cdd:cd05048 129 iaiqiaagmeylssHH--YVHRDLAARNCL-VGDGLTVKISDFGLSRDIYSSDYYRVQSKSllpvrWMPPEAILYG---- 201
                       170       180
                ....*....|....*....|....*..
gi 28467003 211 aglqsdtECTSAVDLWSLGIILLEMFS 237
Cdd:cd05048 202 -------KFTTESDVWSFGVVLWEIFS 221
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
79-304 3.02e-08

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: 54.18  E-value: 3.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  79 ALEQLQGHRNIVTLYGVFTihfspnvPSRCLLLELLDVSVSELLLY-SSHQGCSMWMIQHCARDVLEALAFLHHEGYVHA 157
Cdd:cd14081  53 AIMKLIEHPNVLKLYDVYE-------NKKYLYLVLEYVSGGELFDYlVKKGRLTEKEARKFFRQIISALDYCHSHSICHR 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 158 DLKPRNILWSAENEcFKLIDFGLSFKEGNQdvKYIQTD----GYRAPEaelqnclAQAGLQSDtecTSAVDLWSLGIILL 233
Cdd:cd14081 126 DLKPENLLLDEKNN-IKIADFGMASLQPEG--SLLETScgspHYACPE-------VIKGEKYD---GRKADIWSCGVILY 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 234 EMFSGM---------KLKHTVRSQEWkanssaiidhifaskavvnaAIPAYH---LRDLIKSMLHDDPSRRIPAEMALCS 301
Cdd:cd14081 193 ALLVGAlpfdddnlrQLLEKVKRGVF--------------------HIPHFIspdAQDLLRRMLEVNPEKRITIEEIKKH 252

                ...
gi 28467003 302 PFF 304
Cdd:cd14081 253 PWF 255
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
140-292 3.05e-08

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 54.44  E-value: 3.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS--FK-EGNQDVKYIQ--TDGYRAPEaelqnclaqagLQ 214
Cdd:cd14070 110 RQLVSAVEHLHRAGVVHRDLKIENLLLD-ENDNIKLIDFGLSncAGiLGYSDPFSTQcgSPAYAAPE-----------LL 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 SDTECTSAVDLWSLGIILLEMFSGmKLKHTVRSQEWKANSSAIIDhifaskAVVNAAIPAYHL--RDLIKSMLHDDPSRR 292
Cdd:cd14070 178 ARKKYGPKVDVWSIGVNMYAMLTG-TLPFTVEPFSLRALHQKMVD------KEMNPLPTDLSPgaISFLRSLLEPDPLKR 250
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
140-304 3.28e-08

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: 54.13  E-value: 3.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILW-SAENECFKLIDFGLSFKEGNQDVKYIQ--TDGYRAPEAELQNclaqaglqsd 216
Cdd:cd14107 105 QQVLEGIGYLHGMNILHLDIKPDNILMvSPTREDIKICDFGFAQEITPSEHQFSKygSPEFVAPEIVHQE---------- 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 tECTSAVDLWSLGIILLemfsgmkLKHTVRSQEWKANSSAIIDHIfaSKAVVNAAIP-AYHL----RDLIKSMLHDDPSR 291
Cdd:cd14107 175 -PVSAATDIWALGVIAY-------LSLTCHSPFAGENDRATLLNV--AEGVVSWDTPeITHLsedaKDFIKRVLQPDPEK 244
                       170
                ....*....|...
gi 28467003 292 RIPAEMALCSPFF 304
Cdd:cd14107 245 RPSASECLSHEWF 257
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
75-293 3.30e-08

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 54.27  E-value: 3.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFtihfspNVPSRcLLLELLDVSVSELLLYSSHQGcsmWMIQHCAR----DVLEALAFLH 150
Cdd:cd14075  50 REISSMEKLH-HPNIIRLYEVV------ETLSK-LHLVMEYASGGELYTKISTEG---KLSESEAKplfaQIVSAVKHMH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSAENeCFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTSA-VDLWS 227
Cdd:cd14075 119 ENNIIHRDLKAENVFYASNN-CVKVGDFGFSthAKRGETLNTFCGSPPYAAPE-----------LFKDEHYIGIyVDIWA 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 228 LGIILLEMFSGM---------KLKhtvrsqewkansSAIIDHIFaskavvnaAIPAY---HLRDLIKSMLHDDPSRRI 293
Cdd:cd14075 187 LGVLLYFMVTGVmpfraetvaKLK------------KCILEGTY--------TIPSYvsePCQELIRGILQPVPSDRY 244
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
73-282 3.41e-08

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: 54.64  E-value: 3.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGV----------FTIHFSPNVPSRCLLLELLD-VSVSELLLYSShqgcsmwmiQHCard 141
Cdd:cd14205  52 FEREIEILKSLQ-HDNIVKYKGVcysagrrnlrLIMEYLPYGSLRDYLQKHKErIDHIKLLQYTS---------QIC--- 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 vlEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfKEGNQDVKY--IQTDG-----YRAPEAelqnclaqaglQ 214
Cdd:cd14205 119 --KGMEYLGTKRYIHRDLATRNILVENENRV-KIGDFGLT-KVLPQDKEYykVKEPGespifWYAPES-----------L 183
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 215 SDTECTSAVDLWSLGIILLEMFSgmklkhtvRSQEWKANSSAIIDHIFASKavvNAAIPAYHLRDLIK 282
Cdd:cd14205 184 TESKFSVASDVWSFGVVLYELFT--------YIEKSKSPPAEFMRMIGNDK---QGQMIVFHLIELLK 240
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
74-238 3.71e-08

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: 54.19  E-value: 3.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELldVSVSELLLY-SSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14161  50 RREIEIMSSLN-HPHIISVYEVFE-----NSSKIVIVMEY--ASRGDLYDYiSERQRLSELEARHFFRQIVSAVHYCHAN 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAeNECFKLIDFGLSfKEGNQDvKYIQT----DGYRAPeaELQNCLAQAGLQsdtectsaVDLWSL 228
Cdd:cd14161 122 GIVHRDLKLENILLDA-NGNIKIADFGLS-NLYNQD-KFLQTycgsPLYASP--EIVNGRPYIGPE--------VDSWSL 188
                       170
                ....*....|
gi 28467003 229 GIILLEMFSG 238
Cdd:cd14161 189 GVLLYILVHG 198
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
30-237 4.25e-08

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 53.81  E-value: 4.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  30 GSGSSASVYRVRCCgnPGSPPGALKQFLPpgttgaaasaaeygFRKERAALEQLQgHRNIVTLYGVFTihfspNVPSRCL 109
Cdd:cd14060   2 GGGSFGSVYRAIWV--SQDKEVAVKKLLK--------------IEKEAEILSVLS-HRNIIQFYGAIL-----EAPNYGI 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 110 LLELLDV-SVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEG---YVHADLKPRNILWSAENeCFKLIDFGLS-FKE 184
Cdd:cd14060  60 VTEYASYgSLFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADG-VLKICDFGASrFHS 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 28467003 185 GNQDVKYIQTDGYRAPEaelqncLAQaGLQSDTECtsavDLWSLGIILLEMFS 237
Cdd:cd14060 139 HTTHMSLVGTFPWMAPE------VIQ-SLPVSETC----DTYSYGVVLWEMLT 180
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
75-238 4.35e-08

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: 54.07  E-value: 4.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELLDVSVSELLLYSSHQgcSMWMIQHCARDVLEALAFLHHEGY 154
Cdd:cd14112  49 REFESLRTLQ-HENVQRLIAAFK-----PSNFAYLVMEKLQEDVFTRFSSNDYY--SEEQVATTVRQILDALHYLHFKGI 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNILWSAENEC-FKLIDFGLSFKEGNQDVKYIQTD-GYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIIL 232
Cdd:cd14112 121 AHLDVQPDNIMFQSVRSWqVKLVDFGRAQKVSKLGKVPVDGDtDWASPEF----------HNPETPITVQSDIWGLGVLT 190

                ....*.
gi 28467003 233 LEMFSG 238
Cdd:cd14112 191 FCLLSG 196
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
139-293 4.55e-08

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: 54.18  E-value: 4.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfKEG----NQDVKYIQTDGYRAPEAeLQnclaqaGLQ 214
Cdd:cd05620 102 AAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH-IKIADFGMC-KENvfgdNRASTFCGTPDYIAPEI-LQ------GLK 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 SdtecTSAVDLWSLGIILLEMFSGMKLKHTVRSqewkanssaiiDHIFASKAVVNAAIPAYHL---RDLIKSMLHDDPSR 291
Cdd:cd05620 173 Y----TFSVDWWSFGVLLYEMLIGQSPFHGDDE-----------DELFESIRVDTPHYPRWITkesKDILEKLFERDPTR 237

                ..
gi 28467003 292 RI 293
Cdd:cd05620 238 RL 239
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
98-305 5.09e-08

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: 54.11  E-value: 5.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  98 IHFSPNVPSRcLLLELLDVSVSELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLI 176
Cdd:cd05585  59 LKFSFQSPEK-LYLVLAFINGGELFHHLQREGRfDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGH-IALC 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 177 DFGL---SFKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGMklkhtvrSQEWKAN 253
Cdd:cd05585 137 DFGLcklNMKDDDKTNTFCGTPEYLAPE-----------LLLGHGYTKAVDWWTLGVLLYEMLTGL-------PPFYDEN 198
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 254 SSAIIDHIFASKAVVNAAIPAyHLRDLIKSMLHDDPSRRIPAEMA---LCSPFFS 305
Cdd:cd05585 199 TNEMYRKILQEPLRFPDGFDR-DAKDLLIGLLNRDPTKRLGYNGAqeiKNHPFFD 252
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
19-258 5.56e-08

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 53.80  E-value: 5.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   19 FGRLWQVQSRLGSGSSASVYRVRCCGNPGSPPGALKQFLPPGTTGAAASAAEYGFRKERAALEQLQGHRNIVTL-----Y 93
Cdd:PHA02882  10 TGKEWKIDKLIGCGGFGCVYETQCASDHCINNQAVAKIENLENETIVMETLVYNNIYDIDKIALWKNIHNIDHLgipkyY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   94 GVFTIHFSpNVPSRCLLLELLDVSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECF 173
Cdd:PHA02882  90 GCGSFKRC-RMYYRFILLEKLVENTKEIF--KRIKCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  174 kLIDFGLS--FKEGNQDVKYiqtdgYRAPEAELQNCLAQAGLQSD--TECTSAVDLWSLGIILLEmFSGMKLKhtvrsqe 249
Cdd:PHA02882 167 -IIDYGIAshFIIHGKHIEY-----SKEQKDLHRGTLYYAGLDAHngACVTRRGDLESLGYCMLK-WAGIKLP------- 232
                        250
                 ....*....|.
gi 28467003  250 WK--ANSSAII 258
Cdd:PHA02882 233 WKgfGHNGNLI 243
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
132-293 6.03e-08

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: 54.16  E-value: 6.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 132 MWMIQHC-----------ARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVK---YIQTDGY 197
Cdd:cd05619  94 MFHIQSChkfdlpratfyAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH-IKIADFGMCKENMLGDAKtstFCGTPDY 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 198 RAPEAELqnclaqaGLQSDTectsAVDLWSLGIILLEMFSGMKLKHTVRSQEwkanssaiidhIFASKAVVNAAIPAY-- 275
Cdd:cd05619 173 IAPEILL-------GQKYNT----SVDWWSFGVLLYEMLIGQSPFHGQDEEE-----------LFQSIRMDNPFYPRWle 230
                       170
                ....*....|....*....
gi 28467003 276 -HLRDLIKSMLHDDPSRRI 293
Cdd:cd05619 231 kEAKDILVKLFVREPERRL 249
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
133-238 6.18e-08

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: 54.31  E-value: 6.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 WMIQHCARDVLeALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEG-NQDVK---YIQTDGYRAPEA-ELQNC 207
Cdd:cd05596 126 WARFYTAEVVL-ALDAIHSMGFVHRDVKPDNMLLDASGH-LKLADFGTCMKMDkDGLVRsdtAVGTPDYISPEVlKSQGG 203
                        90       100       110
                ....*....|....*....|....*....|.
gi 28467003 208 LAQAGlqsdTECtsavDLWSLGIILLEMFSG 238
Cdd:cd05596 204 DGVYG----REC----DWWSVGVFLYEMLVG 226
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
141-314 6.40e-08

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 53.90  E-value: 6.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfKE----GNQDVKYIQTDGYRAPEAELqnclaqaglqsD 216
Cdd:cd05571 103 EIVLALGYLHSQGIVYRDLKLENLLLDKDGH-IKITDFGLC-KEeisyGATTKTFCGTPEYLAPEVLE-----------D 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 TECTSAVDLWSLGIILLEMFSGmKLKHTVRSQEwkanssaIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRRI--- 293
Cdd:cd05571 170 NDYGRAVDWWGLGVVMYEMMCG-RLPFYNRDHE-------VLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLggg 241
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 28467003 294 --PAEMALCSPFF-SI------------PFAPHIED 314
Cdd:cd05571 242 prDAKEIMEHPFFaSInwddlyqkkippPFKPQVTS 277
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
134-304 6.49e-08

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: 53.39  E-value: 6.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLS--FKEGNQDvKYIQTDGYRAPEAELQnclaqa 211
Cdd:cd14005 108 LARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEVKLIDFGCGalLKDSVYT-DFDGTRVYSPPEWIRH------ 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 212 GLQSDTECTSavdlWSLGIILLEMFSGmKLKhTVRSQEWKANSSAIIDHIfaSKAVVnaaipayhlrDLIKSMLHDDPSR 291
Cdd:cd14005 181 GRYHGRPATV----WSLGILLYDMLCG-DIP-FENDEQILRGNVLFRPRL--SKECC----------DLISRCLQFDPSK 242
                       170
                ....*....|...
gi 28467003 292 RIPAEMALCSPFF 304
Cdd:cd14005 243 RPSLEQILSHPWF 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
140-238 6.81e-08

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 53.45  E-value: 6.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGlsFKEGN---QDVKYI--QT----DGYRAPEAelqnclaq 210
Cdd:cd14162 107 RQLVAGVEYCHSKGVVHRDLKCENLLLD-KNNNLKITDFG--FARGVmktKDGKPKlsETycgsYAYASPEI-------- 175
                        90       100
                ....*....|....*....|....*...
gi 28467003 211 agLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd14162 176 --LRGIPYDPFLSDIWSMGVVLYTMVYG 201
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
140-238 6.84e-08

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: 53.54  E-value: 6.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVK---YIQTDGYRAPEAELQNCLaqaglqsd 216
Cdd:cd06641 108 REILKGLDYLHSEKKIHRDIKAANVLLSEHGEV-KLADFGVAGQLTDTQIKrn*FVGTPFWMAPEVIKQSAY-------- 178
                        90       100
                ....*....|....*....|..
gi 28467003 217 tecTSAVDLWSLGIILLEMFSG 238
Cdd:cd06641 179 ---DSKADIWSLGITAIELARG 197
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
74-237 7.05e-08

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: 53.64  E-value: 7.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAAL-------EQLQGHRNIVTLYGVFTIHfSPN--VPSRCLLLELLDvsvseLLLYSSHQGCSMWMIQHCARDVLE 144
Cdd:cd05055  79 SSEREALmselkimSHLGNHENIVNLLGACTIG-GPIlvITEYCCYGDLLN-----FLRRKRESFLTLEDLLSFSYQVAK 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSfKEGNQDVKYIQTDGYR------APEAeLQNCLAqaglqsdte 218
Cdd:cd05055 153 GMAFLASKNCIHRDLAARNVLLT-HGKIVKICDFGLA-RDIMNDSNYVVKGNARlpvkwmAPES-IFNCVY--------- 220
                       170
                ....*....|....*....
gi 28467003 219 cTSAVDLWSLGIILLEMFS 237
Cdd:cd05055 221 -TFESDVWSYGILLWEIFS 238
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
75-293 8.17e-08

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: 53.41  E-value: 8.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFTihfSPNVPSRCLLLELLdvSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGY 154
Cdd:cd14200  72 QEIAILKKLD-HVNIVKLIEVLD---DPAEDNLYMVFDLL--RKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKI 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 155 VHADLKPRNILWSAENEcFKLIDFGLSFK-EGNqDVKYIQTDG---YRAPEAELQNCLAQAGlqsdtectSAVDLWSLGI 230
Cdd:cd14200 146 VHRDIKPSNLLLGDDGH-VKIADFGVSNQfEGN-DALLSSTAGtpaFMAPETLSDSGQSFSG--------KALDVWAMGV 215
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28467003 231 ILLEMFSGmklkhtvrsqewkaNSSAIIDHIFA------SKAVVNAAIP--AYHLRDLIKSMLHDDPSRRI 293
Cdd:cd14200 216 TLYCFVYG--------------KCPFIDEFILAlhnkikNKPVEFPEEPeiSEELKDLILKMLDKNPETRI 272
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
140-238 8.64e-08

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: 53.22  E-value: 8.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENE--CFKLIDFGLSfKEGNQD---VKYIQTDGYRAPEaelqnclaqagLQ 214
Cdd:cd13989 109 SDISSAISYLHENRIIHRDLKPENIVLQQGGGrvIYKLIDLGYA-KELDQGslcTSFVGTLQYLAPE-----------LF 176
                        90       100
                ....*....|....*....|....
gi 28467003 215 SDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd13989 177 ESKKYTCTVDYWSFGTLAFECITG 200
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
133-238 8.65e-08

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 53.73  E-value: 8.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 WMIQHCAR-----------DVLEALAFLHHEGYVHADLKPRNILWSAeNECFKLIDFGLS---FKEGNQDVKYIQTDGYR 198
Cdd:cd05586  85 WHLQKEGRfsedrakfyiaELVLALEHLHKNDIVYRDLKPENILLDA-NGHIALCDFGLSkadLTDNKTTNTFCGTTEYL 163
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 28467003 199 APEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd05586 164 APEV----------LLDEKGYTKMVDFWSLGVLVFEMCCG 193
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
145-305 8.89e-08

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: 53.47  E-value: 8.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfKEGNQDVK----YIQTDGYRAPEAELQNclaqaglqsdtECT 220
Cdd:cd05575 108 ALGYLHSLNIIYRDLKPENILLDSQGH-VVLTDFGLC-KEGIEPSDttstFCGTPEYLAPEVLRKQ-----------PYD 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 221 SAVDLWSLGIILLEMFSGMklkhtvrSQEWKANSSAIIDHIFASKAVV--NAAIPAyhlRDLIKSMLHDDPSRRIPA--- 295
Cdd:cd05575 175 RTVDWWCLGAVLYEMLYGL-------PPFYSRDTAEMYDNILHKPLRLrtNVSPSA---RDLLEGLLQKDRTKRLGSgnd 244
                       170
                ....*....|.
gi 28467003 296 -EMALCSPFFS 305
Cdd:cd05575 245 fLEIKNHSFFR 255
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
24-235 9.18e-08

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: 53.18  E-value: 9.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRCcgnPGSPPGALKQfLPPGTTGAAAsaaeygFRKERAALEQLQgHRNIVTLYGVftihfspn 103
Cdd:cd05068  11 KLLRKLGSGQFGEVWEGLW---NNTTPVAVKT-LKPGTMDPED------FLREAQIMKKLR-HPKLIQLYAV-------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 104 vpsrCLLLELLDVsVSELLLYSS------HQGCSMWMIQ--HCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKL 175
Cdd:cd05068  72 ----CTLEEPIYI-ITELMKHGSlleylqGKGRSLQLPQliDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNIC-KV 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 176 IDFGLSFKEGNQDVkYIQTDGYR------APEAELQNclaqaglqsdtECTSAVDLWSLGIILLEM 235
Cdd:cd05068 146 ADFGLARVIKVEDE-YEAREGAKfpikwtAPEAANYN-----------RFSIKSDVWSFGILLTEI 199
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
98-295 9.50e-08

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: 53.43  E-value: 9.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  98 IHFSPNVPSRclLLELLD-VSVSELLLYSSHQGC-SMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFkL 175
Cdd:cd05603  61 LHYSFQTSEK--LYFVLDyVNGGELFFHLQRERCfLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVV-L 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 176 IDFGLSfKEG----NQDVKYIQTDGYRAPEAELQNCLAQaglqsdtectsAVDLWSLGIILLEMFSGMKLKHTVRSQEWK 251
Cdd:cd05603 138 TDFGLC-KEGmepeETTSTFCGTPEYLAPEVLRKEPYDR-----------TVDWWCLGAVLYEMLYGLPPFYSRDVSQMY 205
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 28467003 252 ANSSAIIDHIFASKAVVNAaipayhlrDLIKSMLHDDPSRRIPA 295
Cdd:cd05603 206 DNILHKPLHLPGGKTVAAC--------DLLQGLLHKDQRRRLGA 241
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
73-240 1.01e-07

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 52.91  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTIHfspnvPSRCLLLELLDV-SVSELLLYSS-HQGCSMW----------------- 133
Cdd:cd05050  55 FQREAALMAEFD-HPNIVKLLGVCAVG-----KPMCLLFEYMAYgDLNEFLRHRSpRAQCSLShstssarkcglnplpls 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 -MIQHC-ARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSFKEGNQDvkYIQTDGYRA-------PEAEL 204
Cdd:cd05050 129 cTEQLCiAKQVAAGMAYLSERKFVHRDLATRNCL-VGENMVVKIADFGLSRNIYSAD--YYKASENDAipirwmpPESIF 205
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 28467003 205 QNclaqaglqsdtECTSAVDLWSLGIILLEMFS-GMK 240
Cdd:cd05050 206 YN-----------RYTTESDVWAYGVVLWEIFSyGMQ 231
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-292 1.20e-07

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: 52.89  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVRCCGNPGSPPgALKQ-FLPPGTTGAAASAAEYGFRK---ERAALEQLQGHRNIVTLYGVFTI 98
Cdd:cd08528   2 YAVLELLGSGAFGCVYKVRKKSNGQTLL-ALKEiNMTNPAFGRTEQERDKSVGDiisEVNIIKEQLRHPNIVRYYKTFLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  99 HfspnvpSRC-LLLELLD-VSVSELL--LYSSHQGCSMWMIQHCARDVLEALAFLHHE-GYVHADLKPRNILWSaENECF 173
Cdd:cd08528  81 N------DRLyIVMELIEgAPLGEHFssLKEKNEHFTEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIMLG-EDDKV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 174 KLIDFGLSFKEGNQDVKYIQTDG---YRAPEAeLQNclaqaglQSDTEctsAVDLWSLGIILLEMFSgmkLKHTVRSQEW 250
Cdd:cd08528 154 TITDFGLAKQKGPESSKMTSVVGtilYSCPEI-VQN-------EPYGE---KADIWALGCILYQMCT---LQPPFYSTNM 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 28467003 251 KANSSAIIDHIFASkavVNAAIPAYHLRDLIKSMLHDDPSRR 292
Cdd:cd08528 220 LTLATKIVEAEYEP---LPEGMYSDDITFVIRSCLTPDPEAR 258
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
135-303 1.38e-07

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: 52.34  E-value: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVK---YIQTDGYRAPEAelqnclaqA 211
Cdd:cd06646 108 IAYVCRETLQGLAYLHSKGKMHRDIKGANILLT-DNGDVKLADFGVAAKITATIAKrksFIGTPYWMAPEV--------A 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 212 GLQSDTECTSAVDLWSLGII---LLEMFSGMKLKHTVRSQEWKANSSaiidhiFASKAVVNAAIPAYHLRDLIKSMLHDD 288
Cdd:cd06646 179 AVEKNGGYNQLCDIWAVGITaieLAELQPPMFDLHPMRALFLMSKSN------FQPPKLKDKTKWSSTFHNFVKISLTKN 252
                       170
                ....*....|....*
gi 28467003 289 PSRRIPAEMALCSPF 303
Cdd:cd06646 253 PKKRPTAERLLTHLF 267
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
28-237 1.50e-07

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: 52.24  E-value: 1.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  28 RLGSGSSASVY--RVRCCGNPGSPPgALKQFLPPgttgaaasAAEYGFRKERAALEQLQgHRNIVTLYGVFT----IHfs 101
Cdd:cd05084   3 RIGRGNFGEVFsgRLRADNTPVAVK-SCRETLPP--------DLKAKFLQEARILKQYS-HPNIVRLIGVCTqkqpIY-- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 102 pnvpsrcLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENeCFKLIDFGLS 181
Cdd:cd05084  71 -------IVMELVQGGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKN-VLKISDFGMS 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 182 FKEgnQDVKYIQTDGYR-------APEAelqnclaqaglQSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05084 143 REE--EDGVYAATGGMKqipvkwtAPEA-----------LNYGRYSSESDVWSFGILLWETFS 192
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
142-239 1.64e-07

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: 52.19  E-value: 1.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVK-YIQTDGYRAPEAELQNclaQAGLQSDtect 220
Cdd:cd06619 104 VVKGLTYLWSLKILHRDVKPSNMLVNTRGQV-KLCDFGVSTQLVNSIAKtYVGTNAYMAPERISGE---QYGIHSD---- 175
                        90
                ....*....|....*....
gi 28467003 221 savdLWSLGIILLEMFSGM 239
Cdd:cd06619 176 ----VWSLGISFMELALGR 190
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
132-293 1.69e-07

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: 52.30  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 132 MWMIQHCarDVLEALAFLHHEGYVHADLKPRNILWSAENECFkLIDFGLSFK-----EGNQDVKYIQ-------TDGYRA 199
Cdd:cd13986 110 HIFLGIC--RGLKAMHEPELVPYAHRDIKPGNVLLSEDDEPI-LMDLGSMNParieiEGRREALALQdwaaehcTMPYRA 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 200 PeaELQNCLAQAGLqsdtecTSAVDLWSLGIILLEMfsgMKLKHTVRSQEWKANSSAIidhifaskAVVNAAI-----PA 274
Cdd:cd13986 187 P--ELFDVKSHCTI------DEKTDIWSLGCTLYAL---MYGESPFERIFQKGDSLAL--------AVLSGNYsfpdnSR 247
                       170       180
                ....*....|....*....|.
gi 28467003 275 Y--HLRDLIKSMLHDDPSRRI 293
Cdd:cd13986 248 YseELHQLVKSMLVVNPAERP 268
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
74-236 1.82e-07

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 52.01  E-value: 1.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQ--GHRNIVTLYGVFTihfspNVPSRCLLLELLDV-SVSELLLYSSHqgcSM-WMIQHC-ARDVLEALAF 148
Cdd:cd13992  41 RTILQELNQLKelVHDNLNKFIGICI-----NPPNIAVVTEYCTRgSLQDVLLNREI---KMdWMFKSSfIKDIVKGMNY 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LH-HEGYVHADLKPRNILWSAENECfKLIDFGL-SFKEGnQDVKYIQTDG------YRAPEAELQNCLAQAGLQsdtect 220
Cdd:cd13992 113 LHsSSIGYHGRLKSSNCLVDSRWVV-KLTDFGLrNLLEE-QTNHQLDEDAqhkkllWTAPELLRGSLLEVRGTQ------ 184
                       170
                ....*....|....*.
gi 28467003 221 sAVDLWSLGIILLEMF 236
Cdd:cd13992 185 -KGDVYSFAIILYEIL 199
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
86-292 1.95e-07

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: 51.80  E-value: 1.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGVFTIHF-----SPNVPSRCLLLelldvsvselLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLK 160
Cdd:cd05113  58 HEKLVQLYGVCTKQRpifiiTEYMANGCLLN----------YLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLA 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 161 PRNILWSaENECFKLIDFGLSfkegnqdvKYIQTDGY------------RAPEAELQnclaqaglqsdTECTSAVDLWSL 228
Cdd:cd05113 128 ARNCLVN-DQGVVKVSDFGLS--------RYVLDDEYtssvgskfpvrwSPPEVLMY-----------SKFSSKSDVWAF 187
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 229 GIILLEMFSGMKLKHTvrsqewKANSSAIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRR 292
Cdd:cd05113 188 GVLMWEVYSLGKMPYE------RFTNSETVEHVSQGLRLYRPHLASEKVYTIMYSCWHEKADER 245
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
79-305 1.99e-07

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: 51.86  E-value: 1.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  79 ALEQLQGHRNIVTLYGVFTIH-FSPNVPSRCLLLELLDvsvsellLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHA 157
Cdd:cd14187  59 AIHRSLAHQHVVGFHGFFEDNdFVYVVLELCRRRSLLE-------LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHR 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 158 DLKPRNILWSAENECfKLIDFGLSFK---EGNQDVKYIQTDGYRAPEAelqncLAQAGLQSDtectsaVDLWSLGIILLE 234
Cdd:cd14187 132 DLKLGNLFLNDDMEV-KIGDFGLATKveyDGERKKTLCGTPNYIAPEV-----LSKKGHSFE------VDIWSIGCIMYT 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 235 MFSGMKLKHTVRSQEW----KANSSAIIDHIFASKAvvnaaipayhlrDLIKSMLHDDPSRRIPAEMALCSPFFS 305
Cdd:cd14187 200 LLVGKPPFETSCLKETylriKKNEYSIPKHINPVAA------------SLIQKMLQTDPTARPTINELLNDEFFT 262
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
139-292 2.10e-07

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: 52.02  E-value: 2.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQNCLAqaglqsdte 218
Cdd:cd14209 107 AAQIVLAFEYLHSLDLIYRDLKPENLLID-QQGYIKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYN--------- 176
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 219 ctSAVDLWSLGIILLEMFSGmklkhtvRSQEWKANSSAIIDHIFASKavvnAAIPAY---HLRDLIKSMLHDDPSRR 292
Cdd:cd14209 177 --KAVDWWALGVLIYEMAAG-------YPPFFADQPIQIYEKIVSGK----VRFPSHfssDLKDLLRNLLQVDLTKR 240
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
137-333 2.16e-07

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: 52.73  E-value: 2.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 137 HCAR----DVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL-----------SFKEGNQDVK-YIQT------ 194
Cdd:cd05600 111 EHARfyiaEMFAAISSLHQLGYIHRDLKPENFLIDSSGH-IKLTDFGLasgtlspkkieSMKIRLEEVKnTAFLeltake 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 195 --DGYRAPEAELQNcLAQAGLQS----------DTECTSAVDLWSLGIILLEM------FSGMKLKHTVRS-QEWKanss 255
Cdd:cd05600 190 rrNIYRAMRKEDQN-YANSVVGSpdymapevlrGEGYDLTVDYWSLGCILFEClvgfppFSGSTPNETWANlYHWK---- 264
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 256 AIIDHIFASKAVVNAAIP--AYhlrDLIKSMLhDDPSRRipaemaLCSP--FFSIPFAPHI--EDLVMLPTP--VLRLLN 327
Cdd:cd05600 265 KTLQRPVYTDPDLEFNLSdeAW---DLITKLI-TDPQDR------LQSPeqIKNHPFFKNIdwDRLREGSKPpfIPELES 334

                ....*.
gi 28467003 328 VLDDDY 333
Cdd:cd05600 335 EIDTSY 340
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
140-237 2.30e-07

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: 51.79  E-value: 2.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLS-FKEGNQDVKYIQTDG-----YRAPEAelqnclaqagl 213
Cdd:cd05066 113 RGIASGMKYLSDMGYVHRDLAARNILVNSNLVC-KVSDFGLSrVLEDDPEAAYTTRGGkipirWTAPEA----------- 180
                        90       100
                ....*....|....*....|....
gi 28467003 214 QSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05066 181 IAYRKFTSASDVWSYGIVMWEVMS 204
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
140-304 2.45e-07

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: 51.54  E-value: 2.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILW-SAENECFKLIDFGLSFK-EGNQDVKYI-QTDGYRAPEAelqnclaqaglqSD 216
Cdd:cd14191 107 RQISEGVEYIHKQGIVHLDLKPENIMCvNKTGTKIKLIDFGLARRlENAGSLKVLfGTPEFVAPEV------------IN 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 TECTS-AVDLWSLGIILLEMFSGMKLKHTVRSQEWKAN-SSAIIDhiFASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIP 294
Cdd:cd14191 175 YEPIGyATDMWSIGVICYILVSGLSPFMGDNDNETLANvTSATWD--FDDEAFDEISDDA---KDFISNLLKKDMKARLT 249
                       170
                ....*....|
gi 28467003 295 AEMALCSPFF 304
Cdd:cd14191 250 CTQCLQHPWL 259
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
24-237 3.03e-07

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: 51.41  E-value: 3.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRCcgnpgSPPGALKQFLPPGT-TGAAASAAEYGFRKERAALEQLQgHRNIVTLYGVFTihfsP 102
Cdd:cd05065   7 KIEEVIGAGEFGEVCRGRL-----KLPGKREIFVAIKTlKSGYTEKQRRDFLSEASIMGQFD-HPNIIHLEGVVT----K 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 103 NVPSrCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLS- 181
Cdd:cd05065  77 SRPV-MIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVC-KVSDFGLSr 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 182 -FKEGNQDVKYIQTDG------YRAPEAelqnclaqaglQSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05065 155 fLEDDTSDPTYTSSLGgkipirWTAPEA-----------IAYRKFTSASDVWSYGIVMWEVMS 206
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
348-399 3.18e-07

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 47.28  E-value: 3.18e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 28467003 348 KEECQKYGPVVSLLVPKENPG--RGQVFVEYANAGDSKAAQKLLTGRMFDGKFV 399
Cdd:cd00590  16 RELFSKFGEVVSVRIVRDRDGksKGFAFVEFESPEDAEKALEALNGTELGGRPL 69
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
142-321 3.33e-07

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: 51.42  E-value: 3.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLS--FKEGNQDVK-YIQTDGYRAPEaelqnclaqagLQSDTE 218
Cdd:cd05608 114 IISGLEHLHQRRIIYRDLKPENVLLDDDGNV-RISDLGLAveLKDGQTKTKgYAGTPGFMAPE-----------LLLGEE 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 219 CTSAVDLWSLGIILLEMFSGmklKHTVRSQEWKANSSAIIDHIFaSKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMA 298
Cdd:cd05608 182 YDYSVDYFTLGVTLYEMIAA---RGPFRARGEKVENKELKQRIL-NDSVTYSEKFSPASKSICEALLAKDPEKRLGFRDG 257
                       170       180
                ....*....|....*....|....*..
gi 28467003 299 LCSPFFSIPFAPHIE----DLVMLPTP 321
Cdd:cd05608 258 NCDGLRTHPFFRDINwrklEAGILPPP 284
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
141-293 3.76e-07

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: 51.55  E-value: 3.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfKEGNQDVKYIQ----TDGYRAPEaelqnclaqagLQSD 216
Cdd:cd05595 103 EIVSALEYLHSRDVVYRDIKLENLMLDKDGH-IKITDFGLC-KEGITDGATMKtfcgTPEYLAPE-----------VLED 169
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 217 TECTSAVDLWSLGIILLEMFSGmklkhtvRSQEWKANSSAIIDHIFASKAVVNAAIPAyHLRDLIKSMLHDDPSRRI 293
Cdd:cd05595 170 NDYGRAVDWWGLGVVMYEMMCG-------RLPFYNQDHERLFELILMEEIRFPRTLSP-EAKSLLAGLLKKDPKQRL 238
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
29-179 4.19e-07

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: 48.98  E-value: 4.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRvrCCGNPGSPPGALKQflppgtTGAAASAAEYGFRKERAALEQLQGHR-NIVTLYgVFTIHFSPNVpsr 107
Cdd:cd13968   1 MGEGASAKVFW--AEGECTTIGVAVKI------GDDVNNEEGEDLESEMDILRRLKGLElNIPKVL-VTEDVDGPNI--- 68
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 108 cLLLELL-DVSVSELLLYSSHQGCSmwmIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFG 179
Cdd:cd13968  69 -LLMELVkGGTLIAYTQEEELDEKD---VESIMYQLAECMRLLHSFHLIHRDLNNDNILLS-EDGNVKLIDFG 136
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
142-310 4.27e-07

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: 51.19  E-value: 4.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSF---KEGNQDVKYIQTDGYRAPEaelqnclAQAGLQSDTE 218
Cdd:cd06658 127 VLRALSYLHNQGVIHRDIKSDSILLTSDGR-IKLSDFGFCAqvsKEVPKRKSLVGTPYWMAPE-------VISRLPYGTE 198
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 219 ctsaVDLWSLGIILLEMFSGMKLKHTVRS-QEWKANSSAIIDHIFASKAVVNAaipayhLRDLIKSMLHDDPSRRIPAEM 297
Cdd:cd06658 199 ----VDIWSLGIMVIEMIDGEPPYFNEPPlQAMRRIRDNLPPRVKDSHKVSSV------LRGFLDLMLVREPSQRATAQE 268
                       170
                ....*....|...
gi 28467003 298 ALCSPFFSIPFAP 310
Cdd:cd06658 269 LLQHPFLKLAGPP 281
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
142-239 4.29e-07

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: 51.28  E-value: 4.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHE-GYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVK-YIQTDGYRAPEaELQNclAQAGLQSDtec 219
Cdd:cd06615 108 VLRGLTYLREKhKIMHRDVKPSNILVNSRGEI-KLCDFGVSGQLIDSMANsFVGTRSYMSPE-RLQG--THYTVQSD--- 180
                        90       100
                ....*....|....*....|
gi 28467003 220 tsavdLWSLGIILLEMFSGM 239
Cdd:cd06615 181 -----IWSLGLSLVEMAIGR 195
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
133-299 4.44e-07

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: 50.74  E-value: 4.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 WMIQHCArdvleALAFLHHEGYVHADLKPRNILWSaENECFKLIDFG---LSFKEGNQDVKYIQTDGYRAPEaelqncla 209
Cdd:cd08219 105 WFVQMCL-----GVQHIHEKRVLHRDIKSKNIFLT-QNGKVKLGDFGsarLLTSPGAYACTYVGTPYYVPPE-------- 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 210 qagLQSDTECTSAVDLWSLGIILLEMFSgmkLKHTVRSQEWKanssAIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDP 289
Cdd:cd08219 171 ---IWENMPYNNKSDIWSLGCILYELCT---LKHPFQANSWK----NLILKVCQGSYKPLPSHYSYELRSLIKQMFKRNP 240
                       170
                ....*....|
gi 28467003 290 SRRIPAEMAL 299
Cdd:cd08219 241 RSRPSATTIL 250
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
73-292 4.62e-07

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 50.88  E-value: 4.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTIHFSPNVPSRCLLLEL---LDV-----SVSELLLYSShqgcsmwmiQHCardvlE 144
Cdd:cd05056  54 FLQEAYIMRQFD-HPHIVKLIGVITENPVWIVMELAPLGELrsyLQVnkyslDLASLILYAY---------QLS-----T 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkegnqdvKYIQTDGY------------RAPEAelqnclaqag 212
Cdd:cd05056 119 ALAYLESKRFVHRDIAARNVL-VSSPDCVKLGDFGLS--------RYMEDESYykaskgklpikwMAPES---------- 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 213 lQSDTECTSAVDLWSLGIILLEMFSgmklkHTVRSQEWKANSSaIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRR 292
Cdd:cd05056 180 -INFRRFTSASDVWMFGVCMWEILM-----LGVKPFQGVKNND-VIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSKR 252
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
139-293 4.74e-07

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: 51.13  E-value: 4.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFK--EGNQDVKYIQTDGYRAPEaelqnclaqagLQSD 216
Cdd:cd05632 110 AAEILCGLEDLHRENTVYRDLKPENILLDDYGH-IRISDLGLAVKipEGESIRGRVGTVGYMAPE-----------VLNN 177
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 217 TECTSAVDLWSLGIILLEMFSGmklKHTVRSQEWKANSSAIIDHIFASKAVVNAAIpAYHLRDLIKSMLHDDPSRRI 293
Cdd:cd05632 178 QRYTLSPDYWGLGCLIYEMIEG---QSPFRGRKEKVKREEVDRRVLETEEVYSAKF-SEEAKSICKMLLTKDPKQRL 250
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
75-260 4.87e-07

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: 51.19  E-value: 4.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVF-TIHFSPNVPSRCL--LLELLDVSVSELllysshQGCSMWMIQHCArdvLEALAFLHH 151
Cdd:cd06633  70 KEVKFLQQLK-HPNTIEYKGCYlKDHTAWLVMEYCLgsASDLLEVHKKPL------QEVEIAAITHGA---LQGLAYLHS 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDvKYIQTDGYRAPEAelqnCLAQAGLQSDTEctsaVDLWSLGII 231
Cdd:cd06633 140 HNMIHRDIKAGNILLTEPGQV-KLADFGSASIASPAN-SFVGTPYWMAPEV----ILAMDEGQYDGK----VDIWSLGIT 209
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 28467003 232 LLE----------MFSGMKLKH-------TVRSQEWKANSSAIIDH 260
Cdd:cd06633 210 CIElaerkpplfnMNAMSALYHiaqndspTLQSNEWTDSFRGFVDY 255
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
142-238 4.88e-07

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: 51.15  E-value: 4.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfKEG----NQDVKYIQTDGYRAPEaelqnclaqagLQSDT 217
Cdd:cd05589 110 VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV-KIADFGLC-KEGmgfgDRTSTFCGTPEFLAPE-----------VLTDT 176
                        90       100
                ....*....|....*....|.
gi 28467003 218 ECTSAVDLWSLGIILLEMFSG 238
Cdd:cd05589 177 SYTRAVDWWGLGVLIYEMLVG 197
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
74-297 5.33e-07

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 51.18  E-value: 5.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQGHRNIVTLYGVFtihfspNVPSRcLLLELLDVSVSELLLYSSHQgcSMWMIQHC---ARDVLEALAFLH 150
Cdd:cd05617  63 QTEKHVFEQASSNPFLVGLHSCF------QTTSR-LFLVIEYVNGGDLMFHMQRQ--RKLPEEHArfyAAEICIALNFLH 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSAENEcFKLIDFGL---SFKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWS 227
Cdd:cd05617 134 ERGIIYRDLKLDNVLLDADGH-IKLTDYGMckeGLGPGDTTSTFCGTPNYIAPE-----------ILRGEEYGFSVDWWA 201
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 228 LGIILLEMFSGmKLKHTVRSQEWKANSSAIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEM 297
Cdd:cd05617 202 LGVLMFEMMAG-RSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCQP 270
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
139-313 5.36e-07

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: 51.12  E-value: 5.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENECFkLIDFGLSfKEG--NQD--VKYIQTDGYRAPEAELQNclaqaglq 214
Cdd:cd05604 103 AAEIASALGYLHSINIVYRDLKPENILLDSQGHIV-LTDFGLC-KEGisNSDttTTFCGTPEYLAPEVIRKQ-------- 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 sdtECTSAVDLWSLGIILLEMFSGMklkhtvrSQEWKANSSAIIDHIFASKAVV--NAAIPAYhlrDLIKSMLHDDPSRR 292
Cdd:cd05604 173 ---PYDNTVDWWCLGSVLYEMLYGL-------PPFYCRDTAEMYENILHKPLVLrpGISLTAW---SILEELLEKDRQLR 239
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 28467003 293 IPAEMALCS----PFFSI-------------PFAPHIE 313
Cdd:cd05604 240 LGAKEDFLEiknhPFFESinwtdlvqkkippPFNPNVN 277
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
76-239 5.74e-07

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: 50.69  E-value: 5.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQgHRNIVTLYGVFtihfspNVPSRCLLL-------ELLDVSVSElllySSHQGCSMWMIqhCARDVLEALAF 148
Cdd:cd14190  51 EIQVMNQLN-HRNLIQLYEAI------ETPNEIVLFmeyveggELFERIVDE----DYHLTEVDAMV--FVRQICEGIQF 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILW-SAENECFKLIDFGLSFK-EGNQDVKY-IQTDGYRAPEaelqnclaqagLQSDTECTSAVDL 225
Cdd:cd14190 118 MHQMRVLHLDLKPENILCvNRTGHQVKIIDFGLARRyNPREKLKVnFGTPEFLSPE-----------VVNYDQVSFPTDM 186
                       170
                ....*....|....
gi 28467003 226 WSLGIILLEMFSGM 239
Cdd:cd14190 187 WSMGVITYMLLSGL 200
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
135-238 6.01e-07

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: 50.88  E-value: 6.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFK---EGNQDVKYIQTDGYRAPEAELQNCLAqa 211
Cdd:cd06655 117 IAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSV-KLTDFGFCAQitpEQSKRSTMVGTPYWMAPEVVTRKAYG-- 193
                        90       100
                ....*....|....*....|....*..
gi 28467003 212 glqsdtectSAVDLWSLGIILLEMFSG 238
Cdd:cd06655 194 ---------PKVDIWSLGIMAIEMVEG 211
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
140-238 6.49e-07

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: 50.44  E-value: 6.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVK---YIQTDGYRAPEAELQNCLaqaglqsd 216
Cdd:cd06640 108 KEILKGLDYLHSEKKIHRDIKAANVLLSEQGDV-KLADFGVAGQLTDTQIKrntFVGTPFWMAPEVIQQSAY-------- 178
                        90       100
                ....*....|....*....|..
gi 28467003 217 tecTSAVDLWSLGIILLEMFSG 238
Cdd:cd06640 179 ---DSKADIWSLGITAIELAKG 197
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
82-238 6.72e-07

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: 50.37  E-value: 6.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  82 QLQGHRNIVTLYGVF-TIHFSpnvpSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCA---RDVLEALAFLHHEGYVHA 157
Cdd:cd14172  52 RASGGPHIVHILDVYeNMHHG----KRCLLIIMECMEGGELFSRIQERGDQAFTEREASeimRDIGTAIQYLHSMNIAHR 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 158 DLKPRNILWSAENE--CFKLIDFGLSfKEGNQDvKYIQTDGYR----APEaelqnclAQAGLQSDTECtsavDLWSLGII 231
Cdd:cd14172 128 DVKPENLLYTSKEKdaVLKLTDFGFA-KETTVQ-NALQTPCYTpyyvAPE-------VLGPEKYDKSC----DMWSLGVI 194

                ....*..
gi 28467003 232 LLEMFSG 238
Cdd:cd14172 195 MYILLCG 201
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
132-238 6.87e-07

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: 50.85  E-value: 6.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 132 MWMIQHC-----------ARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfKEGNQDVK----YIQTDG 196
Cdd:cd05587  85 MYHIQQVgkfkepvavfyAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGH-IKIADFGMC-KEGIFGGKttrtFCGTPD 162
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 28467003 197 YRAPEAELQNCLAQAglqsdtectsaVDLWSLGIILLEMFSG 238
Cdd:cd05587 163 YIAPEIIAYQPYGKS-----------VDWWAYGVLLYEMLAG 193
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
135-238 6.88e-07

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: 50.49  E-value: 6.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFK---EGNQDVKYIQTDGYRAPEAELQNCLAqa 211
Cdd:cd06654 118 IAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSV-KLTDFGFCAQitpEQSKRSTMVGTPYWMAPEVVTRKAYG-- 194
                        90       100
                ....*....|....*....|....*..
gi 28467003 212 glqsdtectSAVDLWSLGIILLEMFSG 238
Cdd:cd06654 195 ---------PKVDIWSLGIMAIEMIEG 212
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
141-240 7.25e-07

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: 50.35  E-value: 7.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNI-LWSAENECF-KLIDFGLSfKEGNQD---VKYIQTDGYRAPEaelqnclaqagLQS 215
Cdd:cd14038 109 DISSALRYLHENRIIHRDLKPENIvLQQGEQRLIhKIIDLGYA-KELDQGslcTSFVGTLQYLAPE-----------LLE 176
                        90       100
                ....*....|....*....|....*
gi 28467003 216 DTECTSAVDLWSLGIILLEMFSGMK 240
Cdd:cd14038 177 QQKYTVTVDYWSFGTLAFECITGFR 201
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
142-237 7.26e-07

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: 50.75  E-value: 7.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSfKEGNQDVKYIQTDGYRAPeaelqncLAQAGLQS--DTEC 219
Cdd:cd05102 181 VARGMEFLASRKCIHRDLAARNILLS-ENNVVKICDFGLA-RDIYKDPDYVRKGSARLP-------LKWMAPESifDKVY 251
                        90
                ....*....|....*...
gi 28467003 220 TSAVDLWSLGIILLEMFS 237
Cdd:cd05102 252 TTQSDVWSFGVLLWEIFS 269
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
142-303 7.98e-07

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: 50.23  E-value: 7.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGlsfkEGN--QDVKYIQTDG---YRAPE-AELQNCLAQaglqs 215
Cdd:cd14101 117 VVEAVQHCHSKGVVHRDIKDENILVDLRTGDIKLIDFG----SGAtlKDSMYTDFDGtrvYSPPEwILYHQYHAL----- 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 216 dtectsAVDLWSLGIILLEMFSG-MKLKhtvRSQEwkanssaiidhIFASKAVVNAAIPAyHLRDLIKSMLHDDPSRRIP 294
Cdd:cd14101 188 ------PATVWSLGILLYDMVCGdIPFE---RDTD-----------ILKAKPSFNKRVSN-DCRSLIRSCLAYNPSDRPS 246

                ....*....
gi 28467003 295 AEMALCSPF 303
Cdd:cd14101 247 LEQILLHPW 255
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
108-238 8.30e-07

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: 50.29  E-value: 8.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYS-SHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLS--FKE 184
Cdd:cd05607  78 CLVMSLMNGGDLKYHIYNvGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNC-RLSDLGLAveVKE 156
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 28467003 185 GNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd05607 157 GKPITQRAGTNGYMAPE-----------ILKEESYSYPVDWFAMGCSIYEMVAG 199
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
98-296 8.39e-07

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: 50.40  E-value: 8.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  98 IHFSPNVPSRclLLELLD-VSVSELLLYSSHQGCSMW-MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFkL 175
Cdd:cd05602  73 LHFSFQTTDK--LYFVLDyINGGELFYHLQRERCFLEpRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIV-L 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 176 IDFGL---SFKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKA 252
Cdd:cd05602 150 TDFGLckeNIEPNGTTSTFCGTPEYLAPE-----------VLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYD 218
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 28467003 253 NssaIIDHIFASKA-VVNAAipayhlRDLIKSMLHDDPSRRIPAE 296
Cdd:cd05602 219 N---ILNKPLQLKPnITNSA------RHLLEGLLQKDRTKRLGAK 254
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
57-247 9.72e-07

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: 50.04  E-value: 9.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  57 LPPGTTGAAasaaeyGFRKERAALEQLQgHRNIVTLYGVFT----IHFSPNVPSRCLLLELLDVSVSELLLYSShqgcsm 132
Cdd:cd05072  39 LKPGTMSVQ------AFLEEANLMKTLQ-HDKLVRLYAVVTkeepIYIITEYMAKGSLLDFLKSDEGGKVLLPK------ 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 wMIQHCARdVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfkEGNQDVKYIQTDG------YRAPEAELQN 206
Cdd:cd05072 106 -LIDFSAQ-IAEGMAYIERKNYIHRDLRAANVLVSESLMC-KIADFGLA--RVIEDNEYTAREGakfpikWTAPEAINFG 180
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 28467003 207 CLaqaglqsdtecTSAVDLWSLGIILLEMFSGMKLKHTVRS 247
Cdd:cd05072 181 SF-----------TIKSDVWSFGILLYEIVTYGKIPYPGMS 210
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
142-303 9.79e-07

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: 50.23  E-value: 9.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHE-GYVHADLKPRNILWSAENECfKLIDFGLSfkeGNQDVKYIQTD----GYRAPEAelqncLAQAGLQSD 216
Cdd:cd06622 111 VVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQV-KLCDFGVS---GNLVASLAKTNigcqSYMAPER-----IKSGGPNQN 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 TECTSAVDLWSLGIILLEMFSGmklkhtvrSQEWKANSSaiiDHIFAS-KAVVNAAIPAY------HLRDLIKSMLHDDP 289
Cdd:cd06622 182 PTYTVQSDVWSLGLSILEMALG--------RYPYPPETY---ANIFAQlSAIVDGDPPTLpsgysdDAQDFVAKCLNKIP 250
                       170
                ....*....|....
gi 28467003 290 SRRIPAEMALCSPF 303
Cdd:cd06622 251 NRRPTYAQLLEHPW 264
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
138-237 1.05e-06

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 49.96  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 138 CARDVLEALAFLHHEGYVHADLKPRNILWSAENeCFKLIDFGLSfkEGNQDVKYIQ--TDG-----YRAPEAELqnclaq 210
Cdd:cd05099 139 CAYQVARGMEYLESRRCIHRDLAARNVLVTEDN-VMKIADFGLA--RGVHDIDYYKktSNGrlpvkWMAPEALF------ 209
                        90       100
                ....*....|....*....|....*..
gi 28467003 211 aglqsDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05099 210 -----DRVYTHQSDVWSFGILMWEIFT 231
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
138-237 1.06e-06

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 50.11  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 138 CARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVKYIQTDG-----YRAPEAelqnclaqag 212
Cdd:cd05053 138 FAYQVARGMEYLASKKCIHRDLAARNVLVT-EDNVMKIADFGLARDIHHIDYYRKTTNGrlpvkWMAPEA---------- 206
                        90       100
                ....*....|....*....|....*
gi 28467003 213 lQSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05053 207 -LFDRVYTHQSDVWSFGVLLWEIFT 230
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
99-183 1.17e-06

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 49.97  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  99 HFSPNVPSRCLLLELLDVSVSELLLYSSHQ---------GCSMwmiqhcardvLEALAFLHHEGYVHADLKPRNILWSAE 169
Cdd:cd14015  94 HEYKGEKYRFLVMPRFGRDLQKIFEKNGKRfpektvlqlALRI----------LDVLEYIHENGYVHADIKASNLLLGFG 163
                        90
                ....*....|....*.
gi 28467003 170 NECFK--LIDFGLSFK 183
Cdd:cd14015 164 KNKDQvyLVDYGLASR 179
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
142-292 1.18e-06

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 49.98  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSfKEGNQDVKYIQTDGYR------APEAELqnclaqaglqs 215
Cdd:cd05103 188 VAKGMEFLASRKCIHRDLAARNILLS-ENNVVKICDFGLA-RDIYKDPDYVRKGDARlplkwmAPETIF----------- 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 216 DTECTSAVDLWSLGIILLEMFS-GMKLKHTVRsqewkanssaiIDHIFAS--KAVVNAAIPAYHLRDLIKSML---HDDP 289
Cdd:cd05103 255 DRVYTIQSDVWSFGVLLWEIFSlGASPYPGVK-----------IDEEFCRrlKEGTRMRAPDYTTPEMYQTMLdcwHGEP 323

                ...
gi 28467003 290 SRR 292
Cdd:cd05103 324 SQR 326
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
135-238 1.21e-06

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: 49.72  E-value: 1.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFK---EGNQDVKYIQTDGYRAPEAELQNCLAqa 211
Cdd:cd06656 117 IAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSV-KLTDFGFCAQitpEQSKRSTMVGTPYWMAPEVVTRKAYG-- 193
                        90       100
                ....*....|....*....|....*..
gi 28467003 212 glqsdtectSAVDLWSLGIILLEMFSG 238
Cdd:cd06656 194 ---------PKVDIWSLGIMAIEMVEG 211
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
88-238 1.27e-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: 49.67  E-value: 1.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  88 NIVTLYGVFtihFSPNVPSRCLllELLDVSVSEL--LLYSSHQGC-SMWMIQHCARDVLEALAFLHHE-GYVHADLKPRN 163
Cdd:cd06616  66 YIVKFYGAL---FREGDCWICM--ELMDISLDKFykYVYEVLDSViPEEILGKIAVATVKALNYLKEElKIIHRDVKPSN 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 164 ILWSaENECFKLIDFGLSfkegNQDVKYI-QT-DG----YRAPEAELQNCLAQA-GLQSDtectsavdLWSLGIILLEMF 236
Cdd:cd06616 141 ILLD-RNGNIKLCDFGIS----GQLVDSIaKTrDAgcrpYMAPERIDPSASRDGyDVRSD--------VWSLGITLYEVA 207

                ..
gi 28467003 237 SG 238
Cdd:cd06616 208 TG 209
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
140-238 1.41e-06

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: 49.67  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVK---YIQTDGYRAPEAELQNCLaqaglqsd 216
Cdd:cd06642 108 REILKGLDYLHSERKIHRDIKAANVLLSEQGDV-KLADFGVAGQLTDTQIKrntFVGTPFWMAPEVIKQSAY-------- 178
                        90       100
                ....*....|....*....|..
gi 28467003 217 tecTSAVDLWSLGIILLEMFSG 238
Cdd:cd06642 179 ---DFKADIWSLGITAIELAKG 197
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
73-238 1.58e-06

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 49.31  E-value: 1.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKErAALEQLQGHRNIVTLYGVftihfSPNVPSRCLLLE--------------------LLDvsvselllysshqgcsm 132
Cdd:cd14061  40 VRQE-ARLFWMLRHPNIIALRGV-----CLQPPNLCLVMEyarggalnrvlagrkipphvLVD----------------- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 WMIQhcardVLEALAFLHHEGYV---HADLKPRNIL-------WSAENECFKLIDFGLSfKEGNQDVKYIQ--TDGYRAP 200
Cdd:cd14061  97 WAIQ-----IARGMNYLHNEAPVpiiHRDLKSSNILileaienEDLENKTLKITDFGLA-REWHKTTRMSAagTYAWMAP 170
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 28467003 201 EAELQNCLAQAGlqsdtectsavDLWSLGIILLEMFSG 238
Cdd:cd14061 171 EVIKSSTFSKAS-----------DVWSYGVLLWELLTG 197
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
76-237 1.77e-06

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: 49.24  E-value: 1.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQGHRNIVTLYGVFT----IHFSPNVPSRCLLLELLDVSVSELLLYSSHQGC------SMWMIQHCARDVLEA 145
Cdd:cd05098  68 EMEMMKMIGKHKNIINLLGACTqdgpLYVIVEYASKGNLREYLQARRPPGMEYCYNPSHnpeeqlSSKDLVSCAYQVARG 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 146 LAFLHHEGYVHADLKPRNILWSAENeCFKLIDFGLSFKEGNQDVKYIQTDG-----YRAPEAELqnclaqaglqsDTECT 220
Cdd:cd05098 148 MEYLASKKCIHRDLAARNVLVTEDN-VMKIADFGLARDIHHIDYYKKTTNGrlpvkWMAPEALF-----------DRIYT 215
                       170
                ....*....|....*..
gi 28467003 221 SAVDLWSLGIILLEMFS 237
Cdd:cd05098 216 HQSDVWSFGVLLWEIFT 232
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
86-321 1.81e-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: 49.29  E-value: 1.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGvftiHFSPNVPSRCLLLEL-----LDVSVSELLLYSSHQGCSMWMiqhcarDVLEALAFLHH--EGYVHAD 158
Cdd:cd14041  69 HPRIVKLYD----YFSLDTDSFCTVLEYcegndLDFYLKQHKLMSEKEARSIIM------QIVNALKYLNEikPPIIHYD 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 159 LKPRNILWSAENEC--FKLIDFGLSfkegnqdvKYIQTDGYRAPEA-ELQNCLAQAGLQSDTEC----------TSAVDL 225
Cdd:cd14041 139 LKPGNILLVNGTACgeIKITDFGLS--------KIMDDDSYNSVDGmELTSQGAGTYWYLPPECfvvgkeppkiSNKVDV 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 226 WSLGIILLEMFSGMKLKHTVRSQEWKANSSAIIDHI---FASKAVVNAAIPAYhlrdlIKSMLHDDPSRRIPAEMALCSP 302
Cdd:cd14041 211 WSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATevqFPPKPVVTPEAKAF-----IRRCLAYRKEDRIDVQQLACDP 285
                       250
                ....*....|....*....
gi 28467003 303 FfsipFAPHIEDLVMLPTP 321
Cdd:cd14041 286 Y----LLPHIRKSVSTSSP 300
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
135-305 1.85e-06

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: 49.27  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVK---YIQTDGYRAPEAelqnclaqA 211
Cdd:cd06645 110 IAYVSRETLQGLYYLHSKGKMHRDIKGANILLT-DNGHVKLADFGVSAQITATIAKrksFIGTPYWMAPEV--------A 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 212 GLQSDTECTSAVDLWSLGII---LLEMFSGMKLKHTVRSQEWKANSSaiidhiFASKAVVNAAIPAYHLRDLIKSMLHDD 288
Cdd:cd06645 181 AVERKGGYNQLCDIWAVGITaieLAELQPPMFDLHPMRALFLMTKSN------FQPPKLKDKMKWSNSFHHFVKMALTKN 254
                       170
                ....*....|....*..
gi 28467003 289 PSRRIPAEMALCSPFFS 305
Cdd:cd06645 255 PKKRPTAEKLLQHPFVT 271
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
135-308 1.88e-06

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: 49.08  E-value: 1.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFG-LSFKEGNQDVKYIQtDGYRAPEAelqnclaqAGL 213
Cdd:cd05576 115 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGH-IQLTYFSrWSEVEDSCDSDAIE-NMYCAPEV--------GGI 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 214 qsdTECTSAVDLWSLGIILLEMFSGMKLKhtvrsqewKANSSAIIDHIFASkavvnaaIPAY---HLRDLIKSMLHDDPS 290
Cdd:cd05576 185 ---SEETEACDWWSLGALLFELLTGKALV--------ECHPAGINTHTTLN-------IPEWvseEARSLLQQLLQFNPT 246
                       170
                ....*....|....*...
gi 28467003 291 RRIPAEMALCSPFFSIPF 308
Cdd:cd05576 247 ERLGAGVAGVEDIKSHPF 264
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
133-303 1.88e-06

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: 48.97  E-value: 1.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 WMIQhcardVLEALAFLHHEGYVHADLKPRNILWSAENeCFKLIDFGLS-FKEGNQDV--KYIQTDGYRAPEaelqncla 209
Cdd:cd08223 107 WFVQ-----IAMALQYMHERNILHRDLKTQNIFLTKSN-IIKVGDLGIArVLESSSDMatTLIGTPYYMSPE-------- 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 210 qagLQSDTECTSAVDLWSLGIILLEMFSgmkLKHTVRSQEWKANSSAIIdhifaskavvNAAIPAY------HLRDLIKS 283
Cdd:cd08223 173 ---LFSNKPYNHKSDVWALGCCVYEMAT---LKHAFNAKDMNSLVYKIL----------EGKLPPMpkqyspELGELIKA 236
                       170       180
                ....*....|....*....|
gi 28467003 284 MLHDDPSRRIPAEMALCSPF 303
Cdd:cd08223 237 MLHQDPEKRPSVKRILRQPY 256
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
74-239 1.89e-06

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: 48.74  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTihfspnvpSRCLLLELLDVSVSELLLYSSHQGCSMWM-IQHCARDVLEALAFLHHE 152
Cdd:cd14108  46 RRELALLAELD-HKSIVRFHDAFE--------KRRVVIIVTELCHEELLERITKRPTVCESeVRSYMRQLLEGIEYLHQN 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNIL-WSAENECFKLIDFGLSFKEGNQDVKYIQtdgYRAPEAELQNCLAQAGLQSDTectsavDLWSLGII 231
Cdd:cd14108 117 DVLHLDLKPENLLmADQKTDQVRICDFGNAQELTPNEPQYCK---YGTPEFVAPEIVNQSPVSKVT------DIWPVGVI 187

                ....*...
gi 28467003 232 LLEMFSGM 239
Cdd:cd14108 188 AYLCLTGI 195
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
348-399 2.03e-06

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 44.92  E-value: 2.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28467003   348 KEECQKYGPVVSLLVPKENPG--RGQVFVEYANAGDSKAAQKLLTGRMFDGKFV 399
Cdd:pfam00076  16 KDLFSKFGPIKSIRLVRDETGrsKGFAFVEFEDEEDAEKAIEALNGKELGGREL 69
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
23-238 2.07e-06

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 48.79  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVRCCGNPGS------PPGALKQFLppgttgaaasaaeygfRKERAALEQLQGHRNIVTLYGvf 96
Cdd:cd14017   2 WKVVKKIGGGGFGEIYKVRDVVDGEEvamkveSKSQPKQVL----------------KMEVAVLKKLQGKPHFCRLIG-- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  97 tihfSPNVPSRC-LLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILW----SAENE 171
Cdd:cd14017  64 ----CGRTERYNyIVMTLLGPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgpSDERT 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28467003 172 CFkLIDFGLS----FKEGNQDVKYIQTDGYRAPEaelQNCLAQAGLQSDTECTSavDLWSLGIILLEMFSG 238
Cdd:cd14017 140 VY-ILDFGLArqytNKDGEVERPPRNAAGFRGTV---RYASVNAHRNKEQGRRD--DLWSWFYMLIEFVTG 204
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
140-239 2.13e-06

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: 49.03  E-value: 2.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENE---CFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAelqncLAQAGLQ 214
Cdd:cd13988 103 RDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDgqsVYKLTDFGAAreLEDDEQFVSLYGTEEYLHPDM-----YERAVLR 177
                        90       100
                ....*....|....*....|....*..
gi 28467003 215 SDTE--CTSAVDLWSLGIILLEMFSGM 239
Cdd:cd13988 178 KDHQkkYGATVDLWSIGVTFYHAATGS 204
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
29-237 2.14e-06

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: 48.92  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCCGNPGSP---PGALKQfLPPGTTgaaaSAAEYGFRKERAALEQLQgHRNIVTLYGVftihfSPNVP 105
Cdd:cd05036  14 LGQGAFGEVYEGTVSGMPGDPsplQVAVKT-LPELCS----EQDEMDFLMEALIMSKFN-HPNIVRCIGV-----CFQRL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 106 SRCLLLELLDVSVSELLLYSSH------QGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAE--NECFKLID 177
Cdd:cd05036  83 PRFILLELMAGGDLKSFLRENRprpeqpSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKgpGRVAKIGD 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28467003 178 FGLS--------FKEGNQ---DVKYIqtdgyrAPEAELQNCLaqaglqsdtecTSAVDLWSLGIILLEMFS 237
Cdd:cd05036 163 FGMArdiyradyYRKGGKamlPVKWM------PPEAFLDGIF-----------TSKTDVWSFGVLLWEIFS 216
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
141-235 2.14e-06

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: 48.60  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFG-LSFKEGNQdvKYIQTDGYRAPEAelqnCLAQAGLQSDTEc 219
Cdd:cd06607 109 GALQGLAYLHSHNRIHRDVKAGNILLT-EPGTVKLADFGsASLVCPAN--SFVGTPYWMAPEV----ILAMDEGQYDGK- 180
                        90
                ....*....|....*.
gi 28467003 220 tsaVDLWSLGIILLEM 235
Cdd:cd06607 181 ---VDVWSLGITCIEL 193
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
142-297 2.22e-06

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: 48.54  E-value: 2.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAeNECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEA-ELQnclAQAGLQsdte 218
Cdd:cd14071 108 ILSAVEYCHKRHIVHRDLKAENLLLDA-NMNIKIADFGFSnfFKPGELLKTWCGSPPYAAPEVfEGK---EYEGPQ---- 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 219 ctsaVDLWSLGIILLEMFSGmklkhtvrSQEWKANSSAIIdhifasKAVVNAA---IPAYHLRD---LIKSMLHDDPSRR 292
Cdd:cd14071 180 ----LDIWSLGVVLYVLVCG--------ALPFDGSTLQTL------RDRVLSGrfrIPFFMSTDcehLIRRMLVLDPSKR 241

                ....*
gi 28467003 293 IPAEM 297
Cdd:cd14071 242 LTIEQ 246
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
138-237 2.25e-06

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: 49.25  E-value: 2.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 138 CARDVLEALAFLHHEGYVHADLKPRNILWSAENeCFKLIDFGLSFKEGNQDVKYIQTDG-----YRAPEAELqnclaqag 212
Cdd:cd05100 139 CAYQVARGMEYLASQKCIHRDLAARNVLVTEDN-VMKIADFGLARDVHNIDYYKKTTNGrlpvkWMAPEALF-------- 209
                        90       100
                ....*....|....*....|....*
gi 28467003 213 lqsDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05100 210 ---DRVYTHQSDVWSFGVLLWEIFT 231
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
28-304 2.27e-06

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 49.30  E-value: 2.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  28 RLGSGSSASVYRVRCCGNPGSPPGALKQFLPPGTTGAAAsaaeygfrKERAALEQLQgHRNIVTLYGVFTIHFSPNVpsr 107
Cdd:cd07867   9 KVGRGTYGHVYKAKRKDGKDEKEYALKQIEGTGISMSAC--------REIALLRELK-HPNVIALQKVFLSHSDRKV--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSM-------WMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENE---CFKLID 177
Cdd:cd07867  77 WLLFDYAEHDLWHIIKFHRASKANKkpmqlprSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPergRVKIAD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 178 FGLSfKEGNQDVK-------YIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGMKLKHtVRSQEW 250
Cdd:cd07867 157 MGFA-RLFNSPLKpladldpVVVTFWYRAPEL----------LLGARHYTKAIDIWAIGCIFAELLTSEPIFH-CRQEDI 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 251 KANSSAIIDHI------------------------------FASKAVVNAAIPAYHLRD----------LIKSMLHDDPS 290
Cdd:cd07867 225 KTSNPFHHDQLdrifsvmgfpadkdwedirkmpeyptlqkdFRRTTYANSSLIKYMEKHkvkpdskvflLLQKLLTMDPT 304
                       330
                ....*....|....
gi 28467003 291 RRIPAEMALCSPFF 304
Cdd:cd07867 305 KRITSEQALQDPYF 318
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
70-237 2.30e-06

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: 48.74  E-value: 2.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  70 EYGFRKERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFL 149
Cdd:cd05080  50 RSGWKQEIDILKTLY-HENIVKYKGCCS-----EQGGKSLQLIMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 150 HHEGYVHADLKPRNILWSAENeCFKLIDFGLS--FKEGNQDVKyIQTDG-----YRAPEaelqnCLaqaglqSDTECTSA 222
Cdd:cd05080 124 HSQHYIHRDLAARNVLLDNDR-LVKIGDFGLAkaVPEGHEYYR-VREDGdspvfWYAPE-----CL------KEYKFYYA 190
                       170
                ....*....|....*
gi 28467003 223 VDLWSLGIILLEMFS 237
Cdd:cd05080 191 SDVWSFGVTLYELLT 205
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
140-293 2.44e-06

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: 48.81  E-value: 2.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSFK-EGNQDV--KYIQTDGYRAPEAELQNCLAQAGlqsd 216
Cdd:cd14199 133 QDLIKGIEYLHYQKIIHRDVKPSNLL-VGEDGHIKIADFGVSNEfEGSDALltNTVGTPAFMAPETLSETRKIFSG---- 207
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 tectSAVDLWSLGIILLEMFSG---------MKLKHTVRSQEWKANSSAIIdhifaskavvnaaipAYHLRDLIKSMLHD 287
Cdd:cd14199 208 ----KALDVWAMGVTLYCFVFGqcpfmderiLSLHSKIKTQPLEFPDQPDI---------------SDDLKDLLFRMLDK 268

                ....*.
gi 28467003 288 DPSRRI 293
Cdd:cd14199 269 NPESRI 274
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
73-237 2.71e-06

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: 48.74  E-value: 2.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVftiHFSPNVPSRCLLLELL-DVSVSELLLYSSHQgcsmwmIQHC-----ARDVLEAL 146
Cdd:cd05081  52 FQREIQILKALH-SDFIVKYRGV---SYGPGRRSLRLVMEYLpSGCLRDFLQRHRAR------LDASrlllySSQICKGM 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 147 AFLHHEGYVHADLKPRNILWSAEnECFKLIDFGLSfKEGNQDVKY--IQTDG-----YRAPEAelqnclaqaglQSDTEC 219
Cdd:cd05081 122 EYLGSRRCVHRDLAARNILVESE-AHVKIADFGLA-KLLPLDKDYyvVREPGqspifWYAPES-----------LSDNIF 188
                       170
                ....*....|....*...
gi 28467003 220 TSAVDLWSLGIILLEMFS 237
Cdd:cd05081 189 SRQSDVWSFGVVLYELFT 206
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
145-293 3.54e-06

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: 48.88  E-value: 3.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL---SFKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTECTS 221
Cdd:cd05618 133 ALNYLHERGIIYRDLKLDNVLLDSEGH-IKLTDYGMckeGLRPGDTTSTFCGTPNYIAPE-----------ILRGEDYGF 200
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 222 AVDLWSLGIILLEMFSGMKLKHTVRSQEWKANSSAiiDHIFASKAVVNAAIP---AYHLRDLIKSMLHDDPSRRI 293
Cdd:cd05618 201 SVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTE--DYLFQVILEKQIRIPrslSVKAASVLKSFLNKDPKERL 273
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
145-238 3.57e-06

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 48.57  E-value: 3.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL---SFKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSDtECTS 221
Cdd:cd05588 108 ALNFLHEKGIIYRDLKLDNVLLDSEGH-IKLTDYGMckeGLRPGDTTSTFCGTPNYIAPEI----------LRGE-DYGF 175
                        90
                ....*....|....*..
gi 28467003 222 AVDLWSLGIILLEMFSG 238
Cdd:cd05588 176 SVDWWALGVLMFEMLAG 192
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
73-237 3.67e-06

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: 48.20  E-value: 3.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTIHfSPNVpsrcLLLELLDV-SVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHH 151
Cdd:cd05148  49 FQKEVQALKRLR-HKHLISLFAVCSVG-EPVY----IITELMEKgSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEE 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EGYVHADLKPRNILWSAENECfKLIDFGLS--FKEgnqDVkYIQTDG-----YRAPEAelqnclAQAGLQSdtectSAVD 224
Cdd:cd05148 123 QNSIHRDLAARNILVGEDLVC-KVADFGLArlIKE---DV-YLSSDKkipykWTAPEA------ASHGTFS-----TKSD 186
                       170
                ....*....|...
gi 28467003 225 LWSLGIILLEMFS 237
Cdd:cd05148 187 VWSFGILLYEMFT 199
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
139-183 3.80e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 47.20  E-value: 3.80e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 28467003   139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENECFklIDFGLSFK 183
Cdd:TIGR03724  96 AREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVYL--IDFGLGKY 138
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
136-303 4.26e-06

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: 47.93  E-value: 4.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 136 QHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKYIQ---TDGYRAPEAELQnclAQAG 212
Cdd:cd14186 105 RHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN-IKIADFGLATQLKMPHEKHFTmcgTPNYISPEIATR---SAHG 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 213 LQSDtectsavdLWSLGIILLEMFSGMKL--KHTVRSQewkANSSAIIDHIFAskavvnaAIPAYHLRDLIKSMLHDDPS 290
Cdd:cd14186 181 LESD--------VWSLGCMFYTLLVGRPPfdTDTVKNT---LNKVVLADYEMP-------AFLSREAQDLIHQLLRKNPA 242
                       170
                ....*....|...
gi 28467003 291 RRIPAEMALCSPF 303
Cdd:cd14186 243 DRLSLSSVLDHPF 255
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
75-237 4.31e-06

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: 47.99  E-value: 4.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLQgHRNIVTLYGVFtihfspnVPSRCLLL--------ELLDvSVSELLLYS-SHQGCSMWMIqhcardvLEA 145
Cdd:cd14110  48 REYQVLRRLS-HPRIAQLHSAY-------LSPRHLVLieelcsgpELLY-NLAERNSYSeAEVTDYLWQI-------LSA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 146 LAFLHHEGYVHADLKPRNILWSAENeCFKLIDFGlSFKEGNQDvKYIQTDGY------RAPEaelqnCLAQAGLQSDTec 219
Cdd:cd14110 112 VDYLHSRRILHLDLRSENMIITEKN-LLKIVDLG-NAQPFNQG-KVLMTDKKgdyvetMAPE-----LLEGQGAGPQT-- 181
                       170
                ....*....|....*...
gi 28467003 220 tsavDLWSLGIILLEMFS 237
Cdd:cd14110 182 ----DIWAIGVTAFIMLS 195
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
141-293 4.44e-06

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: 48.54  E-value: 4.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfKEGNQDVKYIQT----DGYRAPEaelqnclaqagLQSD 216
Cdd:cd05593 123 EIVSALDYLHSGKIVYRDLKLENLMLDKDGH-IKITDFGLC-KEGITDAATMKTfcgtPEYLAPE-----------VLED 189
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 217 TECTSAVDLWSLGIILLEMFSGmKLKHTVRSQEwKANSSAIIDHIFASKAVVNAAipayhlRDLIKSMLHDDPSRRI 293
Cdd:cd05593 190 NDYGRAVDWWGLGVVMYEMMCG-RLPFYNQDHE-KLFELILMEDIKFPRTLSADA------KSLLSGLLIKDPNKRL 258
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
142-305 4.75e-06

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: 48.10  E-value: 4.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSF---KEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDTE 218
Cdd:cd06657 125 VLKALSVLHAQGVIHRDIKSDSILLTHDGRV-KLSDFGFCAqvsKEVPRRKSLVGTPYWMAPE-----------LISRLP 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 219 CTSAVDLWSLGIILLEMFSGmklkHTVRSQEWKANSSAIIDHIFASKaVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMA 298
Cdd:cd06657 193 YGPEVDIWSLGIMVIEMVDG----EPPYFNEPPLKAMKMIRDNLPPK-LKNLHKVSPSLKGFLDRLLVRDPAQRATAAEL 267

                ....*..
gi 28467003 299 LCSPFFS 305
Cdd:cd06657 268 LKHPFLA 274
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
138-237 4.81e-06

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: 48.09  E-value: 4.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 138 CARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVKYIQTDG-----YRAPEAELqnclaqag 212
Cdd:cd05101 151 CTYQLARGMEYLASQKCIHRDLAARNVLVT-ENNVMKIADFGLARDINNIDYYKKTTNGrlpvkWMAPEALF-------- 221
                        90       100
                ....*....|....*....|....*
gi 28467003 213 lqsDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05101 222 ---DRVYTHQSDVWSFGVLMWEIFT 243
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
73-237 5.02e-06

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: 47.69  E-value: 5.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTiHFSPNVpsrcLLLELldVSVSELLLYSSHQGCSMWMIQ--HCARDVLEALAFLH 150
Cdd:cd05085  40 FLSEARILKQYD-HPNIVKLIGVCT-QRQPIY----IVMEL--VPGGDFLSFLRKKKDELKTKQlvKFSLDAAAGMAYLE 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILwSAENECFKLIDFGLSFKE-----GNQDVKYIQTDgYRAPEAelqnclaqaglQSDTECTSAVDL 225
Cdd:cd05085 112 SKNCIHRDLAARNCL-VGENNALKISDFGMSRQEddgvySSSGLKQIPIK-WTAPEA-----------LNYGRYSSESDV 178
                       170
                ....*....|..
gi 28467003 226 WSLGIILLEMFS 237
Cdd:cd05085 179 WSFGILLWETFS 190
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
142-238 5.22e-06

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: 47.80  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYV-HADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKYIQTDG--YRAPEAelqncLAQAGLQSDTE 218
Cdd:cd06617 112 IVKALEYLHSKLSViHRDVKPSNVLINRNGQ-VKLCDFGISGYLVDSVAKTIDAGCkpYMAPER-----INPELNQKGYD 185
                        90       100
                ....*....|....*....|
gi 28467003 219 CTSavDLWSLGIILLEMFSG 238
Cdd:cd06617 186 VKS--DVWSLGITMIELATG 203
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
73-235 5.28e-06

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: 47.57  E-value: 5.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd05067  49 FLAEANLMKQLQ-HQRLVRLYAVVT-----QEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEER 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILWSAENECfKLIDFGLSfkEGNQDVKYIQTDG------YRAPEAelqnclaqagLQSDTeCTSAVDLW 226
Cdd:cd05067 123 NYIHRDLRAANILVSDTLSC-KIADFGLA--RLIEDNEYTAREGakfpikWTAPEA----------INYGT-FTIKSDVW 188

                ....*....
gi 28467003 227 SLGIILLEM 235
Cdd:cd05067 189 SFGILLTEI 197
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
142-237 5.42e-06

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 48.08  E-value: 5.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSfkegnQDVkYIQTDGYRAPEAELQncLAQAGLQS--DTEC 219
Cdd:cd14207 189 VARGMEFLSSRKCIHRDLAARNILLS-ENNVVKICDFGLA-----RDI-YKNPDYVRKGDARLP--LKWMAPESifDKIY 259
                        90
                ....*....|....*...
gi 28467003 220 TSAVDLWSLGIILLEMFS 237
Cdd:cd14207 260 STKSDVWSYGVLLWEIFS 277
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
131-240 5.83e-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: 47.82  E-value: 5.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 131 SMWmiqHCARDVLEALAFLHHE---------GYVHADLKPRNILWSAENECFkLIDFGLSFK-EGNQDVKYIQTDG---- 196
Cdd:cd13998  93 SLC---RLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCC-IADFGLAVRlSPSTGEEDNANNGqvgt 168
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 28467003 197 --YRAPEAeLQNCLAQaglqSDTECTSAVDLWSLGIILLEMFSGMK 240
Cdd:cd13998 169 krYMAPEV-LEGAINL----RDFESFKRVDIYAMGLVLWEMASRCT 209
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
142-238 6.16e-06

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: 47.51  E-value: 6.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENeCFKLIDFG-------LSFKegnQDVKYIQTDGYRAPEAelqnclaqagLQ 214
Cdd:cd14111 108 ILQGLEYLHGRRVLHLDIKPDNIMVTNLN-AIKIVDFGsaqsfnpLSLR---QLGRRTGTLEYMAPEM----------VK 173
                        90       100
                ....*....|....*....|....
gi 28467003 215 SDTeCTSAVDLWSLGIILLEMFSG 238
Cdd:cd14111 174 GEP-VGPPADIWSIGVLTYIMLSG 196
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
115-285 6.61e-06

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: 48.10  E-value: 6.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 115 DVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWsAENECFKLIDFGLSfKEGNQDVKYIQT 194
Cdd:cd05105 219 DSEVKNLLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLL-AQGKIVKICDFGLA-RDIMHDSNYVSK 296
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 195 DG------YRAPEAELQNCLaqaglqsdtecTSAVDLWSLGIILLEMFS-------GMKLKHTVRSQEWKANSSAIIDHi 261
Cdd:cd05105 297 GStflpvkWMAPESIFDNLY-----------TTLSDVWSYGILLWEIFSlggtpypGMIVDSTFYNKIKSGYRMAKPDH- 364
                       170       180       190
                ....*....|....*....|....*....|....*
gi 28467003 262 fASKAVVNAAI----------PA-YHLRDLIKSML 285
Cdd:cd05105 365 -ATQEVYDIMVkcwnsepekrPSfLHLSDIVESLL 398
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
139-293 6.82e-06

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: 47.33  E-value: 6.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFK--EGNQDVKYIQTDGYRAPEaelqnclaqagLQSD 216
Cdd:cd05630 108 AAEICCGLEDLHRERIVYRDLKPENILLDDHGH-IRISDLGLAVHvpEGQTIKGRVGTVGYMAPE-----------VVKN 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 TECTSAVDLWSLGIILLEMFSG----MKLKHTVRSQEWKANSSAIIDHiFASKAVVNAaipayhlRDLIKSMLHDDPSRR 292
Cdd:cd05630 176 ERYTFSPDWWALGCLLYEMIAGqspfQQRKKKIKREEVERLVKEVPEE-YSEKFSPQA-------RSLCSMLLCKDPAER 247

                .
gi 28467003 293 I 293
Cdd:cd05630 248 L 248
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
134-235 7.21e-06

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: 47.34  E-value: 7.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCArDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkegnQDVKYiqTDGYR------------APE 201
Cdd:cd05032 121 FIQMAA-EIADGMAYLAAKKFVHRDLAARNCM-VAEDLTVKIGDFGMT-----RDIYE--TDYYRkggkgllpvrwmAPE 191
                        90       100       110
                ....*....|....*....|....*....|....
gi 28467003 202 AelqnclaqaglQSDTECTSAVDLWSLGIILLEM 235
Cdd:cd05032 192 S-----------LKDGVFTTKSDVWSFGVVLWEM 214
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
142-249 7.39e-06

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 47.33  E-value: 7.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfkEGNQDVKYIQTDG------YRAPEAELQNCLaqaglqs 215
Cdd:cd05073 116 IAEGMAFIEQRNYIHRDLRAANILVSASLVC-KIADFGLA--RVIEDNEYTAREGakfpikWTAPEAINFGSF------- 185
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 28467003 216 dtecTSAVDLWSLGIILLEMFS-------GMKLKHTVRSQE 249
Cdd:cd05073 186 ----TIKSDVWSFGILLMEIVTygripypGMSNPEVIRALE 222
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
141-292 7.62e-06

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: 47.22  E-value: 7.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSAENE--CFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSD 216
Cdd:cd14039 107 DIGSGIQYLHENKIIHRDLKPENIVLQEINGkiVHKIIDLGYAkdLDQGSLCTSFVGTLQYLAPE-----------LFEN 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 TECTSAVDLWSLGIILLEMFSGMK-LKHTVRSQEWKAN-SSAIIDHIFASKAV-----VNAAIPAYH---------LRDL 280
Cdd:cd14039 176 KSYTVTVDYWSFGTMVFECIAGFRpFLHNLQPFTWHEKiKKKDPKHIFAVEEMngevrFSTHLPQPNnlcslivepMEGW 255
                       170
                ....*....|..
gi 28467003 281 IKSMLHDDPSRR 292
Cdd:cd14039 256 LQLMLNWDPVQR 267
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
134-238 8.76e-06

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 47.34  E-value: 8.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAeNECFKLIDFGLSFKEGN----QDVKYIQTDGYRAPEAeLQNCLA 209
Cdd:cd05597 103 MARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDR-NGHIRLADFGSCLKLREdgtvQSSVAVGTPDYISPEI-LQAMED 180
                        90       100
                ....*....|....*....|....*....
gi 28467003 210 QAGlQSDTECtsavDLWSLGIILLEMFSG 238
Cdd:cd05597 181 GKG-RYGPEC----DWWSLGVCMYEMLYG 204
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
75-293 9.28e-06

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: 47.09  E-value: 9.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  75 KERAALEQLqGHRNIVTLYGVFTIHFSPNVpsrclLLELldVSVSELLLY-------SSHQGCSMWMiqhcarDVLEALA 147
Cdd:cd14076  55 REINILKGL-THPNIVRLLDVLKTKKYIGI-----VLEF--VSGGELFDYilarrrlKDSVACRLFA------QLISGVA 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 148 FLHHEGYVHADLKPRNILWSaENECFKLIDFGL--SFKEGNQDVkyIQTD----GYRAPEAELQNCLAQAglqsdtectS 221
Cdd:cd14076 121 YLHKKGVVHRDLKLENLLLD-KNRNLVITDFGFanTFDHFNGDL--MSTScgspCYAAPELVVSDSMYAG---------R 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 222 AVDLWSLGIILLEMFSGM----------KLKHTVRSQEWKANSSAIIDHIFASKAvvnaaipayhlRDLIKSMLHDDPSR 291
Cdd:cd14076 189 KADIWSCGVILYAMLAGYlpfdddphnpNGDNVPRLYRYICNTPLIFPEYVTPKA-----------RDLLRRILVPNPRK 257

                ..
gi 28467003 292 RI 293
Cdd:cd14076 258 RI 259
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
139-304 9.38e-06

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: 47.35  E-value: 9.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS--FKEGNQDVKyIQTDGYRAPEaelqncLAQAGLQSD 216
Cdd:cd14223 109 AAEIILGLEHMHSRFVVYRDLKPANILLD-EFGHVRISDLGLAcdFSKKKPHAS-VGTHGYMAPE------VLQKGVAYD 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 217 tectSAVDLWSLGIILLEMFSGmklkHTVRSQEwKANSSAIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRRI--- 293
Cdd:cd14223 181 ----SSADWFSLGCMLFKLLRG----HSPFRQH-KTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLgcm 251
                       170
                ....*....|...
gi 28467003 294 --PAEMALCSPFF 304
Cdd:cd14223 252 grGAQEVKEEPFF 264
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
93-237 9.77e-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: 47.31  E-value: 9.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  93 YGVFTIHFSPNVPSRCLLLELldVSVSELLLYSSHQGCSMwmiqhcarDVLEALAFLHHEGYVHADLKPRNILwSAENEC 172
Cdd:cd05107 209 YESPYDQYLPSAPERTRRDTL--INESPALSYMDLVGFSY--------QVANGMEFLASKNCVHRDLAARNVL-ICEGKL 277
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28467003 173 FKLIDFGLSfKEGNQDVKYIQTDG------YRAPEAELQNCLaqaglqsdtecTSAVDLWSLGIILLEMFS 237
Cdd:cd05107 278 VKICDFGLA-RDIMRDSNYISKGStflplkWMAPESIFNNLY-----------TTLSDVWSFGILLWEIFT 336
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
24-235 1.00e-05

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: 46.99  E-value: 1.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRCCGNPGSPPGALKqflpPGTTGAAasaaeyGFRKERAALEQLQgHRNIVTLYGVFT---IHF 100
Cdd:cd05071  12 RLEVKLGQGCFGEVWMGTWNGTTRVAIKTLK----PGTMSPE------AFLQEAQVMKKLR-HEKLVQLYAVVSeepIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 101 SPNVPSRCLLLELLDVSVSELLlysshqgcSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGL 180
Cdd:cd05071  81 VTEYMSKGSLLDFLKGEMGKYL--------RLPQLVDMAAQIASGMAYVERMNYVHRDLRAANIL-VGENLVCKVADFGL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28467003 181 SfkEGNQDVKYIQTDG------YRAPEAELQNclaqaglqsdtECTSAVDLWSLGIILLEM 235
Cdd:cd05071 152 A--RLIEDNEYTARQGakfpikWTAPEAALYG-----------RFTIKSDVWSFGILLTEL 199
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
135-251 1.03e-05

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: 46.91  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSAeNECFKLIDFGLSFKEGNQDVkYIQTDGYRAP----EAELQNCLAQ 210
Cdd:cd05087 104 LQRMACEVACGLLHLHRNNFVHSDLALRNCLLTA-DLTVKIGDYGLSHCKYKEDY-FVTADQLWVPlrwiAPELVDEVHG 181
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 28467003 211 AGLQSDTecTSAVDLWSLGIILLEMFS-GMK----------LKHTVRSQEWK 251
Cdd:cd05087 182 NLLVVDQ--TKQSNVWSLGVTIWELFElGNQpyrhysdrqvLTYTVREQQLK 231
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
140-178 1.07e-05

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 45.67  E-value: 1.07e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECFkLIDF 178
Cdd:COG0478  97 DKILEEIRRAHDAGIVHADLSEYNILVDDDGGVW-IIDW 134
RRM3_UHM_PUF60 cd12648
RNA recognition motif 3 (RRM3) found in UHM domain of poly(U)-binding-splicing factor PUF60 ...
349-409 1.12e-05

RNA recognition motif 3 (RRM3) found in UHM domain of poly(U)-binding-splicing factor PUF60 and similar proteins; This subgroup corresponds to the RRM3 of PUF60, also termed FUSE-binding protein-interacting repressor (FBP-interacting repressor or FIR), or Ro-binding protein 1 (RoBP1), or Siah-binding protein 1 (Siah-BP1), an essential splicing factor that functions as a poly-U RNA-binding protein required to reconstitute splicing in depleted nuclear extracts. Its function is enhanced through interaction with U2 auxiliary factor U2AF65. PUF60 also controls human c-myc gene expression by binding and inhibiting the transcription factor far upstream sequence element (FUSE)-binding-protein (FBP), an activator of c-myc promoters. PUF60 contains two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors another RRM and binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) in several nuclear proteins. The research indicates that PUF60 binds FUSE as a dimer, and only the first two RRM domains participate in the single-stranded DNA recognition.


Pssm-ID: 410052 [Multi-domain]  Cd Length: 98  Bit Score: 43.94  E-value: 1.12e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 349 EECQKYGPVVSLLVPKENPGRG-------QVFVEYANAGDSKAAQKLLTGRMFDGKFVVATFYPLSAY 409
Cdd:cd12648  25 EECGKFGAVNRVIIYQEKQGEEedaeiivKIFVEFSMPSEAEKAIQALNGRWFGGRKVVAELYDQTRF 92
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
140-238 1.17e-05

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: 46.50  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGlsfkEGN--QDVKYIQTDG---YRAPEaelqnclaqaGLQ 214
Cdd:cd14100 113 RQVLEAVRHCHNCGVLHRDIKDENILIDLNTGELKLIDFG----SGAllKDTVYTDFDGtrvYSPPE----------WIR 178
                        90       100
                ....*....|....*....|....
gi 28467003 215 SDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd14100 179 FHRYHGRSAAVWSLGILLYDMVCG 202
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
137-181 1.18e-05

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 47.58  E-value: 1.18e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 28467003  137 HCARDVLEALAFLHHEGYVHADLKPRNILWsAENECFkLIDFGLS 181
Cdd:PRK09605 432 ELVRKVGEIVAKLHKAGIVHGDLTTSNFIV-RDDRLY-LIDFGLG 474
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
140-238 1.24e-05

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: 46.95  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAE--NECFKLIDFGLSfKEG---NQDVKYIQTDGYRAPEaelqnclAQAGLQ 214
Cdd:cd14170 108 KSIGEAIQYLHSINIAHRDVKPENLLYTSKrpNAILKLTDFGFA-KETtshNSLTTPCYTPYYVAPE-------VLGPEK 179
                        90       100
                ....*....|....*....|....
gi 28467003 215 SDTECtsavDLWSLGIILLEMFSG 238
Cdd:cd14170 180 YDKSC----DMWSLGVIMYILLCG 199
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
142-237 1.33e-05

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 46.71  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSfKEGNQDVKYIQTDGYR------APEAELqnclaqaglqs 215
Cdd:cd05054 147 VARGMEFLASRKCIHRDLAARNILLS-ENNVVKICDFGLA-RDIYKDPDYVRKGDARlplkwmAPESIF----------- 213
                        90       100
                ....*....|....*....|..
gi 28467003 216 DTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05054 214 DKVYTTQSDVWSFGVLLWEIFS 235
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
145-238 1.45e-05

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: 46.93  E-value: 1.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAeNECFKLIDFGLSFK---EGN-QDVKYIQTDGYRAPE--AELQNCLAQAGlqsdTE 218
Cdd:cd05624 185 AIHSIHQLHYVHRDIKPDNVLLDM-NGHIRLADFGSCLKmndDGTvQSSVAVGTPDYISPEilQAMEDGMGKYG----PE 259
                        90       100
                ....*....|....*....|
gi 28467003 219 CtsavDLWSLGIILLEMFSG 238
Cdd:cd05624 260 C----DWWSLGVCMYEMLYG 275
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
108-293 1.47e-05

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: 46.59  E-value: 1.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLS--FKEG 185
Cdd:cd05633  84 CFILDLMNGGDLHYHL-SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHVRISDLGLAcdFSKK 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 186 NQDVKyIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGmklkHTVRSQEwKANSSAIIDHIfasK 265
Cdd:cd05633 162 KPHAS-VGTHGYMAPEV----------LQKGTAYDSSADWFSLGCMLFKLLRG----HSPFRQH-KTKDKHEIDRM---T 222
                       170       180       190
                ....*....|....*....|....*....|.
gi 28467003 266 AVVNAAIP---AYHLRDLIKSMLHDDPSRRI 293
Cdd:cd05633 223 LTVNVELPdsfSPELKSLLEGLLQRDVSKRL 253
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
134-236 1.48e-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: 46.43  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDvkYIQTDG-------YRAPE--AEL 204
Cdd:cd05042 101 TLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTV-KIGDYGLAHSRYKED--YIETDDklwfplrWTAPElvTEF 177
                        90       100       110
                ....*....|....*....|....*....|..
gi 28467003 205 QNCLAQAglqsdtECTSAVDLWSLGIILLEMF 236
Cdd:cd05042 178 HDRLLVV------DQTKYSNIWSLGVTLWELF 203
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
73-237 1.58e-05

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: 46.19  E-value: 1.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQGHRNIVTLYGV--------FTIHFSP--NVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDV 142
Cdd:cd05047  42 FAGELEVLCKLGHHPNIINLLGAcehrgylyLAIEYAPhgNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 143 LEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkeGNQDVkYIQTDGYRAPeaelQNCLAQAGLQSDTECTSA 222
Cdd:cd05047 122 ARGMDYLSQKQFIHRDLAARNIL-VGENYVAKIADFGLS---RGQEV-YVKKTMGRLP----VRWMAIESLNYSVYTTNS 192
                       170
                ....*....|....*
gi 28467003 223 vDLWSLGIILLEMFS 237
Cdd:cd05047 193 -DVWSYGVLLWEIVS 206
RRM_U2AF35_like cd12287
RNA recognition motif (RRM) found in U2 small nuclear ribonucleoprotein auxiliary factor U2AF ...
349-405 1.60e-05

RNA recognition motif (RRM) found in U2 small nuclear ribonucleoprotein auxiliary factor U2AF 35 kDa subunit (U2AF35) and similar proteins; This subfamily corresponds to the RRM in U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF) which has been implicated in the recruitment of U2 snRNP to pre-mRNAs. It is a highly conserved heterodimer composed of large and small subunits; this family includes the small subunit of U2AF (U2AF35 or U2AF1) and U2AF 35 kDa subunit B (U2AF35B or C3H60). U2AF35 directly binds to the 3' splice site of the conserved AG dinucleotide and performs multiple functions in the splicing process in a substrate-specific manner. It promotes U2 snRNP binding to the branch-point sequences of introns through association with the large subunit of U2AF (U2AF65 or U2AF2). Although the biological role of U2AF35B remains unclear, it shows high sequence homolgy to U2AF35, which contains two N-terminal zinc fingers, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal arginine/serine (SR) -rich segment interrupted by glycines. In contrast to U2AF35, U2AF35B has a plant-specific conserved C-terminal region containing SERE motif(s), which may have an important function specific to higher plants.


Pssm-ID: 409729 [Multi-domain]  Cd Length: 101  Bit Score: 43.41  E-value: 1.60e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 349 EECQKYGPVVSLLVpKENPG---RGQVFVEYANAGDSKAAQKLLTGRMFDGKFVVATFYP 405
Cdd:cd12287  43 LELSRFGEIEDLVV-CSNLNdhlLGNVYVKFESEEDAEAALQALNGRYYAGRPLYPELSP 101
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
133-238 1.62e-05

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 47.10  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  133 WMIQhcardVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGlsfkegnqdvkyI----------QTDG------ 196
Cdd:NF033483 112 IMIQ-----ILSALEHAHRNGIVHRDIKPQNILIT-KDGRVKVTDFG------------IaralssttmtQTNSvlgtvh 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 28467003  197 YRAPEaelqnclaQA-GLQSDTEctsaVDLWSLGIILLEMFSG 238
Cdd:NF033483 174 YLSPE--------QArGGTVDAR----SDIYSLGIVLYEMLTG 204
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
74-239 1.93e-05

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: 46.06  E-value: 1.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTihfspnvpSRC-LLLELLDVSVSEL---LLYSSHQGCSMWMIQHcARDVLEALAFL 149
Cdd:cd14193  49 KNEIEVMNQLN-HANLIQLYDAFE--------SRNdIVLVMEYVDGGELfdrIIDENYNLTELDTILF-IKQICEGIQYM 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 150 HHEGYVHADLKPRNILW-SAENECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAelqnclaqaglqSDTECTS-AVDL 225
Cdd:cd14193 119 HQMYILHLDLKPENILCvSREANQVKIIDFGLArrYKPREKLRVNFGTPEFLAPEV------------VNYEFVSfPTDM 186
                       170
                ....*....|....
gi 28467003 226 WSLGIILLEMFSGM 239
Cdd:cd14193 187 WSLGVIAYMLLSGL 200
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
141-238 2.10e-05

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: 46.18  E-value: 2.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHE-GYVHADLKPRNILWSAENEcFKLIDFGLSfKEGNQD----VKYIQTDGYRAPEaelqnclaqagLQS 215
Cdd:cd05594 133 EIVSALDYLHSEkNVVYRDLKLENLMLDKDGH-IKITDFGLC-KEGIKDgatmKTFCGTPEYLAPE-----------VLE 199
                        90       100
                ....*....|....*....|...
gi 28467003 216 DTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd05594 200 DNDYGRAVDWWGLGVVMYEMMCG 222
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
74-304 2.19e-05

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: 45.88  E-value: 2.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYG--VFTIHFSpnvpsrcLLLELL-DVSVSELLlySSHQGCSMWMIQHCARDVLEALAFLH 150
Cdd:cd06630  51 REEIRMMARLN-HPNIVRMLGatQHKSHFN-------IFVEWMaGGSVASLL--SKYGAFSENVIINYTLQILRGLAYLH 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 151 HEGYVHADLKPRNILWSAENECFKLIDFGLSFKEGNQDV-------KYIQTDGYRAPEAeLQnclaqaGLQSDTECtsav 223
Cdd:cd06630 121 DNQIIHRDLKGANLLVDSTGQRLRIADFGAAARLASKGTgagefqgQLLGTIAFMAPEV-LR------GEQYGRSC---- 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 224 DLWSLGIILLEMFSGmklkhtvrSQEWkaNSSAIIDH---IFA-SKAVVNAAIPAY---HLRDLIKSMLHDDPSRRIPAE 296
Cdd:cd06630 190 DVWSVGCVIIEMATA--------KPPW--NAEKISNHlalIFKiASATTPPPIPEHlspGLRDVTLRCLELQPEDRPPAR 259

                ....*...
gi 28467003 297 MALCSPFF 304
Cdd:cd06630 260 ELLKHPVF 267
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
139-238 2.25e-05

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: 45.81  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAeLQNclaqaglqsd 216
Cdd:cd05605 108 AAEITCGLEHLHSERIVYRDLKPENILLDDHGH-VRISDLGLAveIPEGETIRGRVGTVGYMAPEV-VKN---------- 175
                        90       100
                ....*....|....*....|..
gi 28467003 217 TECTSAVDLWSLGIILLEMFSG 238
Cdd:cd05605 176 ERYTFSPDWWGLGCLIYEMIEG 197
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
73-237 2.28e-05

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: 46.14  E-value: 2.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQGHRNIVTLYGV--------FTIHFSP--NVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDV 142
Cdd:cd05088  54 FAGELEVLCKLGHHPNIINLLGAcehrgylyLAIEYAPhgNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADV 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 143 LEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkeGNQDVkYIQTDGYRAPeaelQNCLAQAGLQSDTECTSA 222
Cdd:cd05088 134 ARGMDYLSQKQFIHRDLAARNIL-VGENYVAKIADFGLS---RGQEV-YVKKTMGRLP----VRWMAIESLNYSVYTTNS 204
                       170
                ....*....|....*
gi 28467003 223 vDLWSLGIILLEMFS 237
Cdd:cd05088 205 -DVWSYGVLLWEIVS 218
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
142-299 2.58e-05

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 45.47  E-value: 2.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLSFkEGNQD------VKYIQTD-GY----RAPEAELQNC--L 208
Cdd:cd14051 113 VAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSSEEEEEDF-EGEEDnpesneVTYKIGDlGHvtsiSNPQVEEGDCrfL 191
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 209 AQAGLQSDTECTSAVDLWSLGIILLEMFSGMKLKHTvrSQEW---KANSSAIIDHIFASkavvnaaipayhLRDLIKSML 285
Cdd:cd14051 192 ANEILQENYSHLPKADIFALALTVYEAAGGGPLPKN--GDEWheiRQGNLPPLPQCSPE------------FNELLRSMI 257
                       170
                ....*....|....
gi 28467003 286 HDDPSRRiPAEMAL 299
Cdd:cd14051 258 HPDPEKR-PSAAAL 270
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
86-280 2.75e-05

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: 45.82  E-value: 2.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  86 HRNIVTLYGvftiHFSPNVPSRCLLLEL-----LDVSVSELLLYSSHQGCSMWMiqhcarDVLEALAFLHH--EGYVHAD 158
Cdd:cd14040  69 HPRIVKLYD----YFSLDTDTFCTVLEYcegndLDFYLKQHKLMSEKEARSIVM------QIVNALRYLNEikPPIIHYD 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 159 LKPRNILWSAENEC--FKLIDFGLSfkegnqdvKYIQTDGYRAPEAELQNCLAQAGLQSDTEC----------TSAVDLW 226
Cdd:cd14040 139 LKPGNILLVDGTACgeIKITDFGLS--------KIMDDDSYGVDGMDLTSQGAGTYWYLPPECfvvgkeppkiSNKVDVW 210
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 227 SLGIILLEMFSGMKLKHTVRSQEWKANSSAIIDHI---FASKAVVNAAIPAYHLRDL 280
Cdd:cd14040 211 SVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATevqFPVKPVVSNEAKAFIRRCL 267
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
135-304 2.78e-05

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: 45.30  E-value: 2.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKE--GNQDVKYI-QTDGYRAPEAELQNclaQA 211
Cdd:cd14189 103 VRYYLKQIISGLKYLHLKGILHRDLKLGNFFIN-ENMELKVGDFGLAARLepPEQRKKTIcGTPNYLAPEVLLRQ---GH 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 212 GLQSdtectsavDLWSLGIILLEMFSG------MKLKHTVRSQEWkanssaiIDHIFASkavvNAAIPAYHlrdLIKSML 285
Cdd:cd14189 179 GPES--------DVWSLGCVMYTLLCGnppfetLDLKETYRCIKQ-------VKYTLPA----SLSLPARH---LLAGIL 236
                       170
                ....*....|....*....
gi 28467003 286 HDDPSRRIPAEMALCSPFF 304
Cdd:cd14189 237 KRNPGDRLTLDQILEHEFF 255
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
28-304 2.87e-05

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 45.82  E-value: 2.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  28 RLGSGSSASVYRVRCCGNPGSPPGALKQFLPPGTTGAAAsaaeygfrKERAALEQLQgHRNIVTLYGVFTIHFSPNVpsr 107
Cdd:cd07868  24 KVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSAC--------REIALLRELK-HPNVISLQKVFLSHADRKV--- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSM-------WMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENE---CFKLID 177
Cdd:cd07868  92 WLLFDYAEHDLWHIIKFHRASKANKkpvqlprGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPergRVKIAD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 178 FGLSfKEGNQDVK-------YIQTDGYRAPEAelqnclaqagLQSDTECTSAVDLWSLGIILLEMFSGMKLKHtVRSQEW 250
Cdd:cd07868 172 MGFA-RLFNSPLKpladldpVVVTFWYRAPEL----------LLGARHYTKAIDIWAIGCIFAELLTSEPIFH-CRQEDI 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 251 KANSSAIIDHI------------------------------FASKAVVNAAIPAYHLR----------DLIKSMLHDDPS 290
Cdd:cd07868 240 KTSNPYHHDQLdrifnvmgfpadkdwedikkmpehstlmkdFRRNTYTNCSLIKYMEKhkvkpdskafHLLQKLLTMDPI 319
                       330
                ....*....|....
gi 28467003 291 RRIPAEMALCSPFF 304
Cdd:cd07868 320 KRITSEQAMQDPYF 333
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
139-304 2.92e-05

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: 45.42  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfkegnqdvKYIQTdgyrapeaelqnCLAQAGLQSDT- 217
Cdd:cd06625 108 TRQILEGLAYLHSNMIVHRDIKGANILRDSNGNV-KLGDFGAS--------KRLQT------------ICSSTGMKSVTg 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 218 -------ECTSA------VDLWSLGIILLEMFsgmklkhTVRSQEWKANSSAIIDHIfaSKAVVNAAIPAY---HLRDLI 281
Cdd:cd06625 167 tpywmspEVINGegygrkADIWSVGCTVVEML-------TTKPPWAEFEPMAAIFKI--ATQPTNPQLPPHvseDARDFL 237
                       170       180
                ....*....|....*....|...
gi 28467003 282 KSMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd06625 238 SLIFVRNKKQRPSAEELLSHSFV 260
PRK14879 PRK14879
Kae1-associated kinase Bud32;
139-183 3.13e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 44.90  E-value: 3.13e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 28467003  139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENECFklIDFGLSFK 183
Cdd:PRK14879 101 SREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYL--IDFGLAEF 143
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
147-292 3.49e-05

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 405254 [Multi-domain]  Cd Length: 288  Bit Score: 45.18  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003   147 AFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKYIQTDGYRAPeaELQNCLAQAGLQSDTECTSAVDLW 226
Cdd:pfam14531 158 ANLQHYGLVHGQFTVDNFFLDQRGG-VFLGGFEHLVRDGTKVVASEVPRGFAPP--ELLGSRGGYTMKNTTLMTHAFDAW 234
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003   227 SLGIILLEMFSgMKLKHTVRSQEwkanssAIIDHIFasKAVVNAAIPayhLRDLIKSMLHDDPSRR 292
Cdd:pfam14531 235 QLGLVIYWIWC-LDLPNTLDAEE------GGIEWKF--RLCKNIPEP---VRALLKGFLNYSQEDR 288
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
24-237 3.71e-05

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: 45.06  E-value: 3.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRvrccgnpGSPPGALK---QFLPPGTTgaaasaAEYGFRKERAALEQLQgHRNIVTLYGVFT--- 97
Cdd:cd05069  15 RLDVKLGQGCFGEVWM-------GTWNGTTKvaiKTLKPGTM------MPEAFLQEAQIMKKLR-HDKLVPLYAVVSeep 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  98 IHFSPNVPSRCLLLELLDVSVSELLlysshqgcSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLID 177
Cdd:cd05069  81 IYIVTEFMGKGSLLDFLKEGDGKYL--------KLPQLVDMAAQIADGMAYIERMNYIHRDLRAANIL-VGDNLVCKIAD 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 178 FGLSfkEGNQDVKYIQTDG------YRAPEAELQNclaqaglqsdtECTSAVDLWSLGIILLEMFS 237
Cdd:cd05069 152 FGLA--RLIEDNEYTARQGakfpikWTAPEAALYG-----------RFTIKSDVWSFGILLTELVT 204
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
24-237 3.76e-05

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: 45.06  E-value: 3.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRCCGNPGSPPGALKqflpPGTTGAAasaaeyGFRKERAALEQLQgHRNIVTLYGVFT---IHF 100
Cdd:cd05070  12 QLIKRLGNGQFGEVWMGTWNGNTKVAIKTLK----PGTMSPE------SFLEEAQIMKKLK-HDKLVQLYAVVSeepIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 101 SPNVPSRCLLLELLDVSVSELLLYSShqgcsmwmIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGL 180
Cdd:cd05070  81 VTEYMSKGSLLDFLKDGEGRALKLPN--------LVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLIC-KIADFGL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 181 SfkEGNQDVKYIQTDG------YRAPEAELQNclaqaglqsdtECTSAVDLWSLGIILLEMFS 237
Cdd:cd05070 152 A--RLIEDNEYTARQGakfpikWTAPEAALYG-----------RFTIKSDVWSFGILLTELVT 201
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
29-284 3.77e-05

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: 45.14  E-value: 3.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCCGNPGSPpgALKqfLPPGTTGAAASAAEygFRKERAALEQLqGHRNIVTLYGVF--TIHFSpnvps 106
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMV--AIK--CLHSSPNCIEERKA--LLKEAEKMERA-RHSYVLPLLGVCveRRSLG----- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 107 rcLLLELLDVSVSELLLYSSHQ----GCSMWMIQHCArdvlEALAFLHH--EGYVHADLKPRNILWSAENEcFKLIDFGL 180
Cdd:cd13978  69 --LVMEYMENGSLKSLLEREIQdvpwSLRFRIIHEIA----LGMNFLHNmdPPLLHHDLKPENILLDNHFH-VKISDFGL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 181 S--------FKEGNQDVKYIQTDGYRAPEAeLQNCLAQAglqsdtecTSAVDLWSLGIILLEMFSGMKLKHTVRSQEwka 252
Cdd:cd13978 142 SklgmksisANRRRGTENLGGTPIYMAPEA-FDDFNKKP--------TSKSDVYSFAIVIWAVLTRKEPFENAINPL--- 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 28467003 253 nssaiidHIFASKA--------VVNAAIPAYHLRDLIKSM 284
Cdd:cd13978 210 -------LIMQIVSkgdrpsldDIGRLKQIENVQELISLM 242
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
127-237 4.02e-05

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 45.04  E-value: 4.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 127 HQGCSMWMiQHC--ARDVLEALAFLHHE---------GYVHADLKPRNILWSAENECFkLIDFGLSFK----------EG 185
Cdd:cd14054  86 RENTLDWM-SSCrmALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCV-ICDFGLAMVlrgsslvrgrPG 163
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 186 NQDVKYIQTDG---YRAPE-----AELQNClaQAGLQSdtectsaVDLWSLGIILLEMFS 237
Cdd:cd14054 164 AAENASISEVGtlrYMAPEvlegaVNLRDC--ESALKQ-------VDVYALGLVLWEIAM 214
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
141-239 4.15e-05

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: 45.26  E-value: 4.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVKYI-----------QTDGYRAPeAELQNCLA 209
Cdd:cd05610 112 EVALALDYLHRHGIIHRDLKPDNMLISNEGH-IKLTDFGLSKVTLNRELNMMdilttpsmakpKNDYSRTP-GQVLSLIS 189
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28467003 210 QAGLQSDTECTS-----------------------------------AVDLWSLGIILLEMFSGM 239
Cdd:cd05610 190 SLGFNTPTPYRTpksvrrgaarvegerilgtpdylapelllgkphgpAVDWWALGVCLFEFLTGI 254
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
109-303 4.21e-05

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: 45.04  E-value: 4.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 109 LLLELLDVSVSELLLYSSH--QGCSMWMIQHCArdvLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGlSFKEGN 186
Cdd:cd06635 102 LVMEYCLGSASDLLEVHKKplQEIEIAAITHGA---LQGLAYLHSHNMIHRDIKAGNILLTEPGQV-KLADFG-SASIAS 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 187 QDVKYIQTDGYRAPEAelqnCLAQAGLQSDTEctsaVDLWSLGIILLEMFSGmklkhtvRSQEWKANSSAIIDHIFASKA 266
Cdd:cd06635 177 PANSFVGTPYWMAPEV----ILAMDEGQYDGK----VDVWSLGITCIELAER-------KPPLFNMNAMSALYHIAQNES 241
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 28467003 267 -VVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd06635 242 pTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMF 279
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
139-238 4.60e-05

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: 44.99  E-value: 4.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL---SFKEGNQDVKYIQTDGYRAPEAELQNCLAQAglqs 215
Cdd:cd05616 107 AAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH-IKIADFGMckeNIWDGVTTKTFCGTPDYIAPEIIAYQPYGKS---- 181
                        90       100
                ....*....|....*....|...
gi 28467003 216 dtectsaVDLWSLGIILLEMFSG 238
Cdd:cd05616 182 -------VDWWAFGVLLYEMLAG 197
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
139-305 4.86e-05

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: 44.74  E-value: 4.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGL----SFKEGNQDVKyiqTDGYRAPEAelqnclaqagLQ 214
Cdd:cd05606 104 AAEVILGLEHMHNRFIVYRDLKPANILLD-EHGHVRISDLGLacdfSKKKPHASVG---THGYMAPEV----------LQ 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 215 SDTECTSAVDLWSLGIILLEMFSGmklkHTVRSQEwKANSSAIIDHIFASKAVVNAAIPAYHLRDLIKSMLHDDPSRRI- 293
Cdd:cd05606 170 KGVAYDSSADWFSLGCMLYKLLKG----HSPFRQH-KTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDVSKRLg 244
                       170
                ....*....|....*.
gi 28467003 294 ----PAEMALCSPFFS 305
Cdd:cd05606 245 clgrGATEVKEHPFFK 260
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
134-237 5.28e-05

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


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 44.57  E-value: 5.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCArDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkegnQDVkyIQTDGYRAPEAELQ--NCLAQA 211
Cdd:cd05061 121 MIQMAA-EIADGMAYLNAKKFVHRDLAARNCM-VAHDFTVKIGDFGMT-----RDI--YETDYYRKGGKGLLpvRWMAPE 191
                        90       100
                ....*....|....*....|....*.
gi 28467003 212 GLQsDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05061 192 SLK-DGVFTTSSDMWSFGVVLWEITS 216
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
149-249 6.14e-05

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: 44.60  E-value: 6.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 149 LHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFK--EGNQDVKYIQTDGYRAPEAeLQNclaqaglqsdTECTSAVDLW 226
Cdd:cd05631 118 LQRERIVYRDLKPENILLDDRGH-IRISDLGLAVQipEGETVRGRVGTVGYMAPEV-INN----------EKYTFSPDWW 185
                        90       100
                ....*....|....*....|....*..
gi 28467003 227 SLGIILLEMFSGM----KLKHTVRSQE 249
Cdd:cd05631 186 GLGCLIYEMIQGQspfrKRKERVKREE 212
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
73-235 6.30e-05

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: 44.61  E-value: 6.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGV-FTIHFSPNVPSRCLLLELLDV-SVSELLLYSSHQGCSMW----MIQHCARDVLEAL 146
Cdd:cd05075  48 FLSEAVCMKEFD-HPNVMRLIGVcLQNTESEGYPSPVVILPFMKHgDLHSFLLYSRLGDCPVYlptqMLVKFMTDIASGM 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 147 AFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGNQDVkYIQTDGYRAPeaelQNCLAQAGLqSDTECTSAVDLW 226
Cdd:cd05075 127 EYLSSKNFIHRDLAARNCMLN-ENMNVCVADFGLSKKIYNGDY-YRQGRISKMP----VKWIAIESL-ADRVYTTKSDVW 199

                ....*....
gi 28467003 227 SLGIILLEM 235
Cdd:cd05075 200 SFGVTMWEI 208
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
134-251 6.40e-05

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 44.47  E-value: 6.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDvkYIQTDG-------YRAPE--AEL 204
Cdd:cd05086 103 LLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTV-KVGDYGIGFSRYKED--YIETDDkkyaplrWTAPElvTSF 179
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 205 QNCLAQAglqsdtECTSAVDLWSLGIILLEMFSGMK-----------LKHTVRSQEWK 251
Cdd:cd05086 180 QDGLLAA------EQTKYSNIWSLGVTLWELFENAAqpysdlsdrevLNHVIKERQVK 231
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
142-237 6.84e-05

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


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 44.89  E-value: 6.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSfKEGNQDVKYIQTDGYRAPeaelqncLAQAGLQSDTEC-- 219
Cdd:cd05104 223 VAKGMEFLASKNCIHRDLAARNILLT-HGRITKICDFGLA-RDIRNDSNYVVKGNARLP-------VKWMAPESIFECvy 293
                        90
                ....*....|....*...
gi 28467003 220 TSAVDLWSLGIILLEMFS 237
Cdd:cd05104 294 TFESDVWSYGILLWEIFS 311
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
28-237 7.35e-05

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 44.14  E-value: 7.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  28 RLGSGSSASVYRVRCCGNPGSPPGALKqflpPGTTGAAasaaeyGFRKERAALEQLQgHRNIVTLYGVFT---IHFSPNV 104
Cdd:cd14203   2 KLGQGCFGEVWMGTWNGTTKVAIKTLK----PGTMSPE------AFLEEAQIMKKLR-HDKLVQLYAVVSeepIYIVTEF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 105 PSRCLLLELLDVSVSELLlysshqgcSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkE 184
Cdd:cd14203  71 MSKGSLLDFLKDGEGKYL--------KLPQLVDMAAQIASGMAYIERMNYIHRDLRAANIL-VGDNLVCKIADFGLA--R 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 185 GNQDVKYIQTDG------YRAPEAELQNclaqaglqsdtECTSAVDLWSLGIILLEMFS 237
Cdd:cd14203 140 LIEDNEYTARQGakfpikWTAPEAALYG-----------RFTIKSDVWSFGILLTELVT 187
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
133-235 7.56e-05

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 44.08  E-value: 7.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 133 WMIQHC-ARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSF---KEGNQDVKYIQTDG---YRAPEAELQ 205
Cdd:cd14045 102 WGFRFSfATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVC-KIADYGLTTyrkEDGSENASGYQQRLmqvYLPPENHSN 180
                        90       100       110
                ....*....|....*....|....*....|
gi 28467003 206 NclaqaglqsDTECTSAVDLWSLGIILLEM 235
Cdd:cd14045 181 T---------DTEPTQATDVYSYAIILLEI 201
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
140-238 7.85e-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: 44.18  E-value: 7.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGlsfkEGN--QDVKYIQTDG---YRAPEaelqnclaqaGLQ 214
Cdd:cd14102 112 RQVLEAVRHCYSCGVVHRDIKDENLLVDLRTGELKLIDFG----SGAllKDTVYTDFDGtrvYSPPE----------WIR 177
                        90       100
                ....*....|....*....|....
gi 28467003 215 SDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd14102 178 YHRYHGRSATVWSLGVLLYDMVCG 201
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
74-292 8.43e-05

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: 44.03  E-value: 8.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTihfspNVPSRCLLLELLD-------VSVSELLLYSSHQGCSmWMIQHCArdvleAL 146
Cdd:cd08218  47 RKEVAVLSKMK-HPNIVQYQESFE-----ENGNLYIVMDYCDggdlykrINAQRGVLFPEDQILD-WFVQLCL-----AL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 147 AFLHHEGYVHADLKPRNILWSAENeCFKLIDFGLSfKEGNQDVK----YIQTDGYRAPEaelqnclaqagLQSDTECTSA 222
Cdd:cd08218 115 KHVHDRKILHRDIKSQNIFLTKDG-IIKLGDFGIA-RVLNSTVElartCIGTPYYLSPE-----------ICENKPYNNK 181
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 223 VDLWSLGIILLEMFSgmkLKHTVRSQEWKANSSAIIDHIFaskavvnAAIP---AYHLRDLIKSMLHDDPSRR 292
Cdd:cd08218 182 SDIWALGCVLYEMCT---LKHAFEAGNMKNLVLKIIRGSY-------PPVPsrySYDLRSLVSQLFKRNPRDR 244
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
73-235 8.53e-05

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: 43.84  E-value: 8.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfSPNVPSRCLLLelldvsVSELLLYSSHQGCSMW-------MIQHCARDVLEA 145
Cdd:cd14033  47 FSEEVEMLKGLQ-HPNIVRFYDSWK---STVRGHKCIIL------VTELMTSGTLKTYLKRfremklkLLQRWSRQILKG 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 146 LAFLHHEG--YVHADLKPRNILWSAENECFKLIDFGL-SFKEGNQDVKYIQTDGYRAPEaelqnclaqaglQSDTECTSA 222
Cdd:cd14033 117 LHFLHSRCppILHRDLKCDNIFITGPTGSVKIGDLGLaTLKRASFAKSVIGTPEFMAPE------------MYEEKYDEA 184
                       170
                ....*....|...
gi 28467003 223 VDLWSLGIILLEM 235
Cdd:cd14033 185 VDVYAFGMCILEM 197
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
141-292 8.57e-05

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 44.03  E-value: 8.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGL-SFK--------EGNQDVKYIQTDG-------YRAPEAel 204
Cdd:cd14027  98 EIIEGMAYLHGKGVIHKDLKPENILVD-NDFHIKIADLGLaSFKmwskltkeEHNEQREVDGTAKknagtlyYMAPEH-- 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 205 qnclaqagLQS-DTECTSAVDLWSLGIILLEMFSGMKLKHTVRSQEwkanssAIIDHIFASKAVVNAAIPAY---HLRDL 280
Cdd:cd14027 175 --------LNDvNAKPTEKSDVYSFAIVLWAIFANKEPYENAINED------QIIMCIKSGNRPDVDDITEYcprEIIDL 240
                       170
                ....*....|..
gi 28467003 281 IKSMLHDDPSRR 292
Cdd:cd14027 241 MKLCWEANPEAR 252
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
132-237 9.18e-05

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 44.45  E-value: 9.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 132 MWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSfKEGNQDVKYIQTDGYRAPeaelqncLAQA 211
Cdd:cd05106 211 LDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLT-DGRVAKICDFGLA-RDIMNDSNYVVKGNARLP-------VKWM 281
                        90       100
                ....*....|....*....|....*...
gi 28467003 212 GLQSDTECTSAV--DLWSLGIILLEMFS 237
Cdd:cd05106 282 APESIFDCVYTVqsDVWSYGILLWEIFS 309
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
140-239 9.44e-05

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: 43.80  E-value: 9.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILW-SAENECFKLIDFGLSFKEGNQDVKYIQ--TDGYRAPEAelqnclaqaglqSD 216
Cdd:cd14192 109 RQICEGVHYLHQHYILHLDLKPENILCvNSTGNQIKIIDFGLARRYKPREKLKVNfgTPEFLAPEV------------VN 176
                        90       100
                ....*....|....*....|....
gi 28467003 217 TECTS-AVDLWSLGIILLEMFSGM 239
Cdd:cd14192 177 YDFVSfPTDMWSVGVITYMLLSGL 200
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
141-303 9.65e-05

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: 43.87  E-value: 9.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNIL---WSAENECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEaelqnCLAQAGLqsdt 217
Cdd:cd14184 107 NLASALKYLHGLCIVHRDIKPENLLvceYPDGTKSLKLGDFGLATVVEGPLYTVCGTPTYVAPE-----IIAETGY---- 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 218 ecTSAVDLWSLGIILLEMFSGMKLKHTVRSQEWKANSSAIIDHI-FASKAVVNAAIPAyhlRDLIKSMLHDDPSRRIPAE 296
Cdd:cd14184 178 --GLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILLGKLeFPSPYWDNITDSA---KELISHMLQVNVEARYTAE 252

                ....*..
gi 28467003 297 MALCSPF 303
Cdd:cd14184 253 QILSHPW 259
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
142-238 1.02e-04

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: 43.89  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYV-HADLKPRNILWSAENEcFKLIDFGLSFKEGNQDVK-YIQTDGYRAPEaELQNclaqaglqsdTEC 219
Cdd:cd06650 112 VIKGLTYLREKHKImHRDVKPSNILVNSRGE-IKLCDFGVSGQLIDSMANsFVGTRSYMSPE-RLQG----------THY 179
                        90
                ....*....|....*....
gi 28467003 220 TSAVDLWSLGIILLEMFSG 238
Cdd:cd06650 180 SVQSDIWSMGLSLVEMAVG 198
RRM_snRNP70 cd12236
RNA recognition motif (RRM) found in U1 small nuclear ribonucleoprotein 70 kDa (U1-70K) and ...
348-400 1.02e-04

RNA recognition motif (RRM) found in U1 small nuclear ribonucleoprotein 70 kDa (U1-70K) and similar proteins; This subfamily corresponds to the RRM of U1-70K, also termed snRNP70, a key component of the U1 snRNP complex, which is one of the key factors facilitating the splicing of pre-mRNA via interaction at the 5' splice site, and is involved in regulation of polyadenylation of some viral and cellular genes, enhancing or inhibiting efficient poly(A) site usage. U1-70K plays an essential role in targeting the U1 snRNP to the 5' splice site through protein-protein interactions with regulatory RNA-binding splicing factors, such as the RS protein ASF/SF2. Moreover, U1-70K protein can specifically bind to stem-loop I of the U1 small nuclear RNA (U1 snRNA) contained in the U1 snRNP complex. It also mediates the binding of U1C, another U1-specific protein, to the U1 snRNP complex. U1-70K contains a conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by an adjacent glycine-rich region at the N-terminal half, and two serine/arginine-rich (SR) domains at the C-terminal half. The RRM is responsible for the binding of stem-loop I of U1 snRNA molecule. Additionally, the most prominent immunodominant region that can be recognized by auto-antibodies from autoimmune patients may be located within the RRM. The SR domains are involved in protein-protein interaction with SR proteins that mediate 5' splice site recognition. For instance, the first SR domain is necessary and sufficient for ASF/SF2 Binding. The family also includes Drosophila U1-70K that is an essential splicing factor required for viability in flies, but its SR domain is dispensable. The yeast U1-70k doesn't contain easily recognizable SR domains and shows low sequence similarity in the RRM region with other U1-70k proteins and therefore not included in this family. The RRM domain is dispensable for yeast U1-70K function.


Pssm-ID: 409682 [Multi-domain]  Cd Length: 91  Bit Score: 40.68  E-value: 1.02e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 348 KEECQKYGPVVSLLV---PKENPGRGQVFVEYANAGDSKAAQKLLTGRMFDGKFVV 400
Cdd:cd12236  19 RREFEKYGPIKRVRLvrdKKTGKSRGYAFIEFEHERDMKAAYKHADGKKIDGRRVL 74
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-235 1.13e-04

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: 43.48  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRVRCCGNpgSPPGALKQFlppGTTGAAASAAEYGFRKERAALEQLQgHRNIVTLYGVFTIHFSP 102
Cdd:cd08228   4 FQIEKKIGRGQFSEVYRATCLLD--RKPVALKKV---QIFEMMDAKARQDCVKEIDLLKQLN-HPNVIKYLDSFIEDNEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 103 NVpsrclLLELLDV-SVSELLLYSSHQGC-----SMW--MIQHCArdvleALAFLHHEGYVHADLKPRNILWSAENECfK 174
Cdd:cd08228  78 NI-----VLELADAgDLSQMIKYFKKQKRliperTVWkyFVQLCS-----AVEHMHSRRVMHRDIKPANVFITATGVV-K 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003 175 LIDFGLS---FKEGNQDVKYIQTDGYRAPEAELQNclaqaGLQSDTectsavDLWSLGIILLEM 235
Cdd:cd08228 147 LGDLGLGrffSSKTTAAHSLVGTPYYMSPERIHEN-----GYNFKS------DIWSLGCLLYEM 199
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
47-236 1.14e-04

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: 43.44  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  47 GSPPGALKQFLPpgttgaaasaaeygfrKERAALEQLQgHRNIVTLYGVFtihfSPNVPSRCLLLELLDVSvsELLLYSS 126
Cdd:cd14163  37 GGPEEFIQRFLP----------------RELQIVERLD-HKNIIHVYEML----ESADGKIYLVMELAEDG--DVFDCVL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 127 HQGCsmwMIQHCA----RDVLEALAFLHHEGYVHADLKPRNILWSAENecFKLIDFGLS--FKEGNQDVK--YIQTDGYR 198
Cdd:cd14163  94 HGGP---LPEHRAkalfRQLVEAIRYCHGCGVAHRDLKCENALLQGFT--LKLTDFGFAkqLPKGGRELSqtFCGSTAYA 168
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 28467003 199 APEAeLQnclaqaGLQSDTEctsAVDLWSLGIILLEMF 236
Cdd:cd14163 169 APEV-LQ------GVPHDSR---KGDIWSMGVVLYVML 196
RRM_RBMX_like cd12382
RNA recognition motif (RRM) found in heterogeneous nuclear ribonucleoprotein G (hnRNP G), Y ...
348-397 1.14e-04

RNA recognition motif (RRM) found in heterogeneous nuclear ribonucleoprotein G (hnRNP G), Y chromosome RNA recognition motif 1 (hRBMY), testis-specific heterogeneous nuclear ribonucleoprotein G-T (hnRNP G-T) and similar proteins; This subfamily corresponds to the RRM domain of hnRNP G, also termed glycoprotein p43 or RBMX, an RNA-binding motif protein located on the X chromosome. It is expressed ubiquitously and has been implicated in the splicing control of several pre-mRNAs. Moreover, hnRNP G may function as a regulator of transcription for SREBP-1c and GnRH1. Research has shown that hnRNP G may also act as a tumor-suppressor since it upregulates the Txnip gene and promotes the fidelity of DNA end-joining activity. In addition, hnRNP G appears to play a critical role in proper neural development of zebrafish and frog embryos. The family also includes several paralogs of hnRNP G, such as hRBMY and hnRNP G-T (also termed RNA-binding motif protein, X-linked-like-2). Both, hRBMY and hnRNP G-T, are exclusively expressed in testis and critical for male fertility. Like hnRNP G, hRBMY and hnRNP G-T interact with factors implicated in the regulation of pre-mRNA splicing, such as hTra2-beta1 and T-STAR. Although members in this family share a high conserved N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), they appear to recognize different RNA targets. For instance, hRBMY interacts specifically with a stem-loop structure in which the loop is formed by the sequence CA/UCAA. In contrast, hnRNP G associates with single stranded RNA sequences containing a CCA/C motif. In addition to the RRM, hnRNP G contains a nascent transcripts targeting domain (NTD) in the middle region and a novel auxiliary RNA-binding domain (RBD) in its C-terminal region. The C-terminal RBD exhibits distinct RNA binding specificity, and would play a critical role in the regulation of alternative splicing by hnRNP G.


Pssm-ID: 409816 [Multi-domain]  Cd Length: 80  Bit Score: 40.47  E-value: 1.14e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 28467003 348 KEECQKYGPVVSLLVPKE---NPGRGQVFVEYANAGDSKAAQKLLTGRMFDGK 397
Cdd:cd12382  19 EAVFGKYGRIVEVLLMKDretNKSRGFAFVTFESPADAKDAARDMNGKELDGK 71
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
141-238 1.20e-04

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: 44.23  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSFKEGNQDV----KYIQTDGYRAPEAelqnCLAQAGlqsD 216
Cdd:cd05622 180 EVVLALDAIHSMGFIHRDVKPDNMLLDKSGH-LKLADFGTCMKMNKEGMvrcdTAVGTPDYISPEV----LKSQGG---D 251
                        90       100
                ....*....|....*....|..
gi 28467003 217 TECTSAVDLWSLGIILLEMFSG 238
Cdd:cd05622 252 GYYGRECDWWSVGVFLYEMLVG 273
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
108-165 1.24e-04

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


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 43.85  E-value: 1.24e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE-GYVHADLKPRNIL 165
Cdd:cd14218  94 CMVLEVLGHQLLKWIIKSNYQGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENIL 152
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
130-236 1.29e-04

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 43.40  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 130 CSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEnECFKLIDFGLSFKEGNQDVkYIQTDG------YRAPE-- 201
Cdd:cd14206 104 RDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSD-LTVRIGDYGLSHNNYKEDY-YLTPDRlwiplrWVAPEll 181
                        90       100       110
                ....*....|....*....|....*....|....*
gi 28467003 202 AELQNCLAQaglqsdTECTSAVDLWSLGIILLEMF 236
Cdd:cd14206 182 DELHGNLIV------VDQSKESNVWSLGVTIWELF 210
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
109-303 1.36e-04

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: 43.47  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 109 LLLELLDVSVSELLLYSSH--QGCSMWMIQHCArdvLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKEGN 186
Cdd:cd06634  92 LVMEYCLGSASDLLEVHKKplQEVEIAAITHGA---LQGLAYLHSHNMIHRDVKAGNILLT-EPGLVKLGDFGSASIMAP 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 187 QDvKYIQTDGYRAPEAelqnCLAQAGLQSDTEctsaVDLWSLGIILLEMFSGmklkhtvRSQEWKANSSAIIDHIFASKA 266
Cdd:cd06634 168 AN-SFVGTPYWMAPEV----ILAMDEGQYDGK----VDVWSLGITCIELAER-------KPPLFNMNAMSALYHIAQNES 231
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 28467003 267 -VVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPF 303
Cdd:cd06634 232 pALQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRF 269
PTZ00284 PTZ00284
protein kinase; Provisional
136-323 1.47e-04

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 43.80  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  136 QHCARDVLE---ALAFLHHEGYV-HADLKPRNILWSAENE--------------C-FKLIDFGLSFKEGNQDVKYIQTDG 196
Cdd:PTZ00284 231 RHLAQIIFQtgvALDYFHTELHLmHTDLKPENILMETSDTvvdpvtnralppdpCrVRICDLGGCCDERHSRTAIVSTRH 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  197 YRAPEAELqnclaQAGLQSDTectsavDLWSLGIILLEMFSGMKLKHTVRS---------------QEWKA--------- 252
Cdd:PTZ00284 311 YRSPEVVL-----GLGWMYST------DMWSMGCIIYELYTGKLLYDTHDNlehlhlmektlgrlpSEWAGrcgteearl 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  253 --NSSAII------DHI--FASKAVVNAAIPAYHLRDLIKSMLHDDPSRRIPAEMALCSPFFSIPF-----AP-HIEDLV 316
Cdd:PTZ00284 380 lyNSAGQLrpctdpKHLarIARARPVREVIRDDLLCDLIYGLLHYDRQKRLNARQMTTHPYVLKYYpecrqHPnYPDNRS 459

                 ....*...
gi 28467003  317 ML-PTPVL 323
Cdd:PTZ00284 460 MLrPTPIM 467
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
132-305 1.56e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 43.91  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  132 MWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFkLIDFG--LSFKEGNQDVKY--IQTDGYRAPEAelqnc 207
Cdd:PHA03210 266 LKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIV-LGDFGtaMPFEKEREAFDYgwVGTVATNSPEI----- 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  208 laqagLQSDTECtSAVDLWSLGIILLEMFS-------------GMKLKHTVRS-----QEWKANSSAIIDHIFASK---- 265
Cdd:PHA03210 340 -----LAGDGYC-EITDIWSCGLILLDMLShdfcpigdgggkpGKQLLKIIDSlsvcdEEFPDPPCKLFDYIDSAEidha 413
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 28467003  266 ------AVVNAAIPAYHLRDLIKsMLHDDPSRRIPAEMALCSPFFS 305
Cdd:PHA03210 414 ghsvppLIRNLGLPADFEYPLVK-MLTFDWHLRPGAAELLALPLFS 458
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
139-238 1.60e-04

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: 43.45  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGL---SFKEGNQDVKYIQTDGYRAPEaelqnclaqagLQS 215
Cdd:cd05615 117 AAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH-IKIADFGMckeHMVEGVTTRTFCGTPDYIAPE-----------IIA 184
                        90       100
                ....*....|....*....|...
gi 28467003 216 DTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd05615 185 YQPYGRSVDWWAYGVLLYEMLAG 207
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
145-235 1.63e-04

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: 43.31  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENE--CFKLIDFGLS--------FKEGNQDV-KY-----IQTDGYRAPEAELQNCL 208
Cdd:cd13977 146 ALAFLHRNQIVHRDLKPDNILISHKRGepILKVADFGLSkvcsgsglNPEEPANVnKHflssaCGSDFYMAPEVWEGHYT 225
                        90       100
                ....*....|....*....|....*..
gi 28467003 209 AQAglqsdtectsavDLWSLGIILLEM 235
Cdd:cd13977 226 AKA------------DIFALGIIIWAM 240
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
130-237 1.75e-04

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 43.13  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 130 CSMwmiqhcARDVLEALAFLHHEGY---------VHADLKPRNILWSAENECFkLIDFGLSFKEGNQ-DVKYIQTDG--- 196
Cdd:cd14055 101 CKM------AGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILVKNDGTCV-LADFGLALRLDPSlSVDELANSGqvg 173
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 28467003 197 ---YRAPEAeLQnclAQAGLQsDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd14055 174 tarYMAPEA-LE---SRVNLE-DLESFKQIDVYSMALVLWEMAS 212
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
140-238 1.80e-04

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: 43.09  E-value: 1.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLI--DFGLSFKEGNQDVKYIQTDGYRAPEAelqnclaqAGLQsdt 217
Cdd:cd14088 106 RQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVisDFHLAKLENGLIKEPCGTPEYLAPEV--------VGRQ--- 174
                        90       100
                ....*....|....*....|.
gi 28467003 218 ECTSAVDLWSLGIILLEMFSG 238
Cdd:cd14088 175 RYGRPVDCWAIGVIMYILLSG 195
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
142-238 1.82e-04

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: 42.88  E-value: 1.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLSFK---EGNQDVKYIQ-----TDGYRAPEAELQNclaqagl 213
Cdd:cd13991 107 ALEGLEYLHSRKILHGDVKADNVLLSSDGSDAFLCDFGHAECldpDGLGKSLFTGdyipgTETHMAPEVVLGK------- 179
                        90       100
                ....*....|....*....|....*
gi 28467003 214 qsdtECTSAVDLWSLGIILLEMFSG 238
Cdd:cd13991 180 ----PCDAKVDVWSSCCMMLHMLNG 200
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
108-169 1.85e-04

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


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 43.48  E-value: 1.85e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE-GYVHADLKPRNILWSAE 169
Cdd:cd14216  94 CMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLSVN 156
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
146-240 1.94e-04

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: 42.64  E-value: 1.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 146 LAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfKEGNQDVKYIQTDG-------YRAPEaelqnCLAQAGLQSDTe 218
Cdd:cd05116 108 MKYLEESNFVHRDLAARNVLLVTQHYA-KISDFGLS-KALRADENYYKAQThgkwpvkWYAPE-----CMNYYKFSSKS- 179
                        90       100
                ....*....|....*....|....*....
gi 28467003 219 ctsavDLWSLGIILLEMFS-------GMK 240
Cdd:cd05116 180 -----DVWSFGVLMWEAFSygqkpykGMK 203
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
130-237 1.96e-04

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: 43.09  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 130 CSMWMIQHCARdVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSfKEGNQDVKYIQTDGYRAPeaelqncLA 209
Cdd:cd05108 107 GSQYLLNWCVQ-IAKGMNYLEDRRLVHRDLAARNVLVKTPQHV-KITDFGLA-KLLGAEEKEYHAEGGKVP-------IK 176
                        90       100       110
                ....*....|....*....|....*....|
gi 28467003 210 QAGLQSDTE--CTSAVDLWSLGIILLEMFS 237
Cdd:cd05108 177 WMALESILHriYTHQSDVWSYGVTVWELMT 206
RRM1_U1A_like cd12246
RNA recognition motif 1 (RRM1) found in the U1A/U2B"/SNF protein family; This subfamily ...
351-397 2.00e-04

RNA recognition motif 1 (RRM1) found in the U1A/U2B"/SNF protein family; This subfamily corresponds to the RRM1 of U1A/U2B"/SNF protein family which contains Drosophila sex determination protein SNF and its two mammalian counterparts, U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A or U1A) and U2 small nuclear ribonucleoprotein B" (U2 snRNP B" or U2B"), all of which consist of two RNA recognition motifs (RRMs), connected by a variable, flexible linker. SNF is an RNA-binding protein found in the U1 and U2 snRNPs of Drosophila where it is essential in sex determination and possesses a novel dual RNA binding specificity. SNF binds with high affinity to both Drosophila U1 snRNA stem-loop II (SLII) and U2 snRNA stem-loop IV (SLIV). It can also bind to poly(U) RNA tracts flanking the alternatively spliced Sex-lethal (Sxl) exon, as does Drosophila Sex-lethal protein (SXL). U1A is an RNA-binding protein associated with the U1 snRNP, a small RNA-protein complex involved in pre-mRNA splicing. U1A binds with high affinity and specificity to stem-loop II (SLII) of U1 snRNA. It is predominantly a nuclear protein that shuttles between the nucleus and the cytoplasm independently of interactions with U1 snRNA. Moreover, U1A may be involved in RNA 3'-end processing, specifically cleavage, splicing and polyadenylation, through interacting with a large number of non-snRNP proteins. U2B", initially identified to bind to stem-loop IV (SLIV) at the 3' end of U2 snRNA, is a unique protein that comprises of the U2 snRNP. Additional research indicates U2B" binds to U1 snRNA stem-loop II (SLII) as well and shows no preference for SLIV or SLII on the basis of binding affinity. Moreover, U2B" does not require an auxiliary protein for binding to RNA, and its nuclear transport is independent of U2 snRNA binding.


Pssm-ID: 409692 [Multi-domain]  Cd Length: 78  Bit Score: 39.82  E-value: 2.00e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 28467003 351 CQKYGPVVSLLVPKENPGRGQVFVEYANAGDSKAAQKLLTGRMFDGK 397
Cdd:cd12246  24 FSQFGPVLDIVASKSLKMRGQAFVVFKDVESATNALRALQGFPFYGK 70
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
139-181 2.21e-04

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 42.49  E-value: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 28467003   139 ARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLIDFGLS 181
Cdd:pfam01636 154 LAALLALLPAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDA 196
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
145-238 2.42e-04

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: 43.08  E-value: 2.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAeNECFKLIDFGLSFK---EGN-QDVKYIQTDGYRAPEAeLQNCLAQAGlQSDTECt 220
Cdd:cd05623 185 AIDSVHQLHYVHRDIKPDNILMDM-NGHIRLADFGSCLKlmeDGTvQSSVAVGTPDYISPEI-LQAMEDGKG-KYGPEC- 260
                        90
                ....*....|....*...
gi 28467003 221 savDLWSLGIILLEMFSG 238
Cdd:cd05623 261 ---DWWSLGVCMYEMLYG 275
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
73-238 2.66e-04

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: 42.25  E-value: 2.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLygvftihFSPNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14068  34 LRQELVVLSHLH-HPSLVAL-------LAAGTAPRMLVMELAPKGSLDALLQQDNASLTRTLQHRIALHVADGLRYLHSA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNI-LWSAENEC---FKLIDFGLSFKEGNQDVKYIQ-TDGYRAPEAELQNCLAQaglqsdtectSAVDLWS 227
Cdd:cd14068 106 MIIYRDLKPHNVlLFTLYPNCaiiAKIADYGIAQYCCRMGIKTSEgTPGFRAPEVARGNVIYN----------QQADVYS 175
                       170
                ....*....|.
gi 28467003 228 LGIILLEMFSG 238
Cdd:cd14068 176 FGLLLYDILTC 186
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
74-304 2.69e-04

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: 42.25  E-value: 2.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  74 RKERAALEQLQgHRNIVTLYGVFTIHfspnvPSRCLLLELLD-------VSVSELLLYSSHQGCSmWMIQhcardVLEAL 146
Cdd:cd08225  47 KKEVILLAKMK-HPNIVTFFASFQEN-----GRLFIVMEYCDggdlmkrINRQRGVLFSEDQILS-WFVQ-----ISLGL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 147 AFLHHEGYVHADLKPRNILWSAENECFKLIDFGLSfKEGNQDVKYIQ----TDGYRAPEaelqnclaqagLQSDTECTSA 222
Cdd:cd08225 115 KHIHDRKILHRDIKSQNIFLSKNGMVAKLGDFGIA-RQLNDSMELAYtcvgTPYYLSPE-----------ICQNRPYNNK 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 223 VDLWSLGIILLEMFSgmkLKHTVRSQEWKANSSAIIDHIFASKAvvnaaiP--AYHLRDLIKSMLHDDPSRRIPAEMALC 300
Cdd:cd08225 183 TDIWSLGCVLYELCT---LKHPFEGNNLHQLVLKICQGYFAPIS------PnfSRDLRSLISQLFKVSPRDRPSITSILK 253

                ....
gi 28467003 301 SPFF 304
Cdd:cd08225 254 RPFL 257
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
140-304 2.92e-04

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: 42.34  E-value: 2.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWSAENEC------------FKLIDFGLSFKEGnqdvkyiqTDGYRAPEaelqnC 207
Cdd:cd14023  91 KQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTqlrlesledthiMKGEDDALSDKHG--------CPAYVSPE-----I 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 208 LAQAGlqsdTECTSAVDLWSLGIILLEMFSGMKLKHtvrsqewKANSSAIIDHIFASKAVVNAAIPAyHLRDLIKSMLHD 287
Cdd:cd14023 158 LNTTG----TYSGKSADVWSLGVMLYTLLVGRYPFH-------DSDPSALFSKIRRGQFCIPDHVSP-KARCLIRSLLRR 225
                       170
                ....*....|....*..
gi 28467003 288 DPSRRIPAEMALCSPFF 304
Cdd:cd14023 226 EPSERLTAPEILLHPWF 242
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
24-239 2.94e-04

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: 42.31  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  24 QVQSRLGSGSSASVYRVRCCGNPgsppgALKQFLPPGTTGAAASaaeyGFRKERAALEQLQgHRNIVTLYGVFTihfspn 103
Cdd:cd14150   3 SMLKRIGTGSFGTVFRGKWHGDV-----AVKILKVTEPTPEQLQ----AFKNEMQVLRKTR-HVNILLFMGFMT------ 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 104 VPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFK 183
Cdd:cd14150  67 RPNFAIITQWCEGSSLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLH-EGLTVKIGDFGLATV 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28467003 184 E----GNQDVKyiQTDG---YRAPEAelqnclaqAGLQSDTECTSAVDLWSLGIILLEMFSGM 239
Cdd:cd14150 146 KtrwsGSQQVE--QPSGsilWMAPEV--------IRMQDTNPYSFQSDVYAYGVVLYELMSGT 198
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
27-238 2.95e-04

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: 42.33  E-value: 2.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  27 SRLGSGSSASVYRVRCCGNPgsppgALKQFLPPGTTGAAASaaeyGFRKERAALEQLQgHRNIVTLYGVFTIHFSPNVPS 106
Cdd:cd14149  18 TRIGSGSFGTVYKGKWHGDV-----AVKILKVVDPTPEQFQ----AFRNEVAVLRKTR-HVNILLFMGYMTKDNLAIVTQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 107 RClllellDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKE-- 184
Cdd:cd14149  88 WC------EGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH-EGLTVKIGDFGLATVKsr 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 185 --GNQDVKyiQTDG---YRAPEAelqnclaqAGLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd14149 161 wsGSQQVE--QPTGsilWMAPEV--------IRMQDNNPFSFQSDVYSYGIVLYELMTG 209
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
142-238 3.32e-04

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: 42.34  E-value: 3.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 142 VLEALAFLHHEGYV-HADLKPRNILWSAENEcFKLIDFGLSFKE-GNQDVKYIQTDGYRAPEaELQNclaqaglqsdTEC 219
Cdd:cd06649 112 VLRGLAYLREKHQImHRDVKPSNILVNSRGE-IKLCDFGVSGQLiDSMANSFVGTRSYMSPE-RLQG----------THY 179
                        90
                ....*....|....*....
gi 28467003 220 TSAVDLWSLGIILLEMFSG 238
Cdd:cd06649 180 SVQSDIWSMGLSLVELAIG 198
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
82-170 3.32e-04

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: 42.28  E-value: 3.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  82 QLQgHRNIVTLYGVFTIHfspnvPSRCLLLELLDVSVSELLLySSH--QGCSMWMIQHCARDVLEALAFLHHEGYVHADL 159
Cdd:cd08216  55 QLQ-HPNILPYVTSFVVD-----NDLYVVTPLMAYGSCRDLL-KTHfpEGLPELAIAFILRDVLNALEYIHSKGYIHRSV 127
                        90
                ....*....|.
gi 28467003 160 KPRNILWSAEN 170
Cdd:cd08216 128 KASHILISGDG 138
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
73-235 3.49e-04

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: 42.02  E-value: 3.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFT--------IHFSPNvpsRCLLLELLDVSVSEL----LLYSSHQgcsmwmiqhcar 140
Cdd:cd05052  49 FLKEAAVMKEIK-HPNLVQLLGVCTreppfyiiTEFMPY---GNLLDYLRECNREELnavvLLYMATQ------------ 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 dVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSfkegnqdvKYIQTDGYRAPE-AELQ-NCLAQAGLQSDTE 218
Cdd:cd05052 113 -IASAMEYLEKKNFIHRDLAARNCLVG-ENHLVKVADFGLS--------RLMTGDTYTAHAgAKFPiKWTAPESLAYNKF 182
                       170
                ....*....|....*..
gi 28467003 219 CTSAvDLWSLGIILLEM 235
Cdd:cd05052 183 SIKS-DVWAFGVLLWEI 198
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
70-181 3.57e-04

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


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 40.75  E-value: 3.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  70 EYGFRKERAALEQLQGHRNIV--TLYGVFTIHFSPNvpsrcLLLELLD-VSVSELLLYSSHQgcsmwMIQHCARDVLEAL 146
Cdd:cd05120  33 KKDLEKEAAMLQLLAGKLSLPvpKVYGFGESDGWEY-----LLMERIEgETLSEVWPRLSEE-----EKEKIADQLAEIL 102
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 28467003 147 AFLH-HEGYV--HADLKPRNILWSAENECFKLIDFGLS 181
Cdd:cd05120 103 AALHrIDSSVltHGDLHPGNILVKPDGKLSGIIDWEFA 140
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
73-260 3.73e-04

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


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 41.96  E-value: 3.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQGHRNIVTLYGVftihfSPNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14129  42 LKMEVAVLKKLQGKDHVCRFIGC-----GRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNILW----SAENECFkLIDFGLS--FKEGNQDVKYIQ-TDGYRAPEAelqncLAQAGLQSDTECTSAVDL 225
Cdd:cd14129 117 GFLHRDIKPSNFAMgrfpSTCRKCY-MLDFGLArqFTNSCGDVRPPRaVAGFRGTVR-----YASINAHRNREMGRHDDL 190
                       170       180       190
                ....*....|....*....|....*....|....*
gi 28467003 226 WSLGIILLEMFSGMKLKHTVRSQEWKANSSAIIDH 260
Cdd:cd14129 191 WSLFYMLVEFVVGQLPWRKIKDKEQVGSIKERYEH 225
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
131-237 4.00e-04

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 41.87  E-value: 4.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 131 SMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfKEGNQDVKYIQTDGYRAPeaelQNCLAQ 210
Cdd:cd05045 125 TMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVL-VAEGRKMKISDFGLS-RDVYEEDSYVKRSKGRIP----VKWMAI 198
                        90       100
                ....*....|....*....|....*..
gi 28467003 211 AGLqSDTECTSAVDLWSLGIILLEMFS 237
Cdd:cd05045 199 ESL-FDHIYTTQSDVWSFGVLLWEIVT 224
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
76-241 4.38e-04

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 41.77  E-value: 4.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  76 ERAALEQLQGHRNIVTLYGVFT----IHFSPNVPSRCLLLELLDVSVSELllysshqgcSMWMIQHCARDVLEALAFLHH 151
Cdd:cd05114  48 EEAKVMMKLTHPKLVQLYGVCTqqkpIYIVTEFMENGCLLNYLRQRRGKL---------SRDMLLSMCQDVCEGMEYLER 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EGYVHADLKPRNILWSAENeCFKLIDFGLSfkEGNQDVKYIQTDGYRAPeaeLQNCLAQAGLQSdtECTSAVDLWSLGII 231
Cdd:cd05114 119 NNFIHRDLAARNCLVNDTG-VVKVSDFGMT--RYVLDDQYTSSSGAKFP---VKWSPPEVFNYS--KFSSKSDVWSFGVL 190
                       170
                ....*....|
gi 28467003 232 LLEMFSGMKL 241
Cdd:cd05114 191 MWEVFTEGKM 200
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
88-238 4.90e-04

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: 41.59  E-value: 4.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  88 NIVTLYGVFTIHFSPNVpsrCLllELLDVSVsELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE-GYVHADLKPRNILW 166
Cdd:cd06618  75 YIVKCYGYFITDSDVFI---CM--ELMSTCL-DKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILL 148
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 167 SaENECFKLIDFGLSFK--EGNQDVKYIQTDGYRAPEAelqnclaqagLQSDTECTSAV--DLWSLGIILLEMFSG 238
Cdd:cd06618 149 D-ESGNVKLCDFGISGRlvDSKAKTRSAGCAAYMAPER----------IDPPDNPKYDIraDVWSLGISLVELATG 213
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
25-238 5.03e-04

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 41.59  E-value: 5.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  25 VQSRLGSGSSASVYRVRCCGNPgsppgALKQFLPPGTTGAAASaaeyGFRKERAALEQLQgHRNIVTLYGVFTihfspnV 104
Cdd:cd14151  12 VGQRIGSGSFGTVYKGKWHGDV-----AVKMLNVTAPTPQQLQ----AFKNEVGVLRKTR-HVNILLFMGYST------K 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 105 PSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFKE 184
Cdd:cd14151  76 PQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH-EDLTVKIGDFGLATVK 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 185 G--NQDVKYIQTDG---YRAPEAelqnclaqAGLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd14151 155 SrwSGSHQFEQLSGsilWMAPEV--------IRMQDKNPYSFQSDVYAFGIVLYELMTG 205
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
57-237 5.53e-04

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 41.45  E-value: 5.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  57 LPPGTTGAAASaaeyGFRKERAALEQLQgHRNIVTLYGVFTIHFSPNVPsrcLLLELLDVSVSELLLYSSHQGCSMWMIQ 136
Cdd:cd05079  41 LKPESGGNHIA----DLKKEIEILRNLY-HENIVKYKGICTEDGGNGIK---LIMEFLPSGSLKEYLPRNKNKINLKQQL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 137 HCARDVLEALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLSfkegnqdvKYIQTD-GYRAPEAELQN--------C 207
Cdd:cd05079 113 KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ-VKIGDFGLT--------KAIETDkEYYTVKDDLDSpvfwyapeC 183
                       170       180       190
                ....*....|....*....|....*....|
gi 28467003 208 LAQAGLQsdtectSAVDLWSLGIILLEMFS 237
Cdd:cd05079 184 LIQSKFY------IASDVWSFGVTLYELLT 207
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
140-237 5.59e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 41.79  E-value: 5.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  140 RDVLEALAFLHHEGYVHADLKPRNILWSAENE-CfkLIDFGLSFKEGNQDVKY-----IQTDgyrAPEAelqncLAQAGL 213
Cdd:PHA03209 164 KQILEGLRYLHAQRIIHRDVKTENIFINDVDQvC--IGDLGAAQFPVVAPAFLglagtVETN---APEV-----LARDKY 233
                         90       100
                 ....*....|....*....|....
gi 28467003  214 QSDtectsaVDLWSLGIILLEMFS 237
Cdd:PHA03209 234 NSK------ADIWSAGIVLFEMLA 251
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
139-237 5.61e-04

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: 41.52  E-value: 5.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSFKEGnqdvKYIQTDGYRAPeaelQNCLAQAGLQSDTE 218
Cdd:cd05089 125 ASDVAKGMQYLSEKQFIHRDLAARNVL-VGENLVSKIADFGLSRGEE----VYVKKTMGRLP----VRWMAIESLNYSVY 195
                        90
                ....*....|....*....
gi 28467003 219 CTSAvDLWSLGIILLEMFS 237
Cdd:cd05089 196 TTKS-DVWSFGVLLWEIVS 213
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
139-238 6.09e-04

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


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 41.22  E-value: 6.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 139 ARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGL----SFKEGNQDVKyiQTDG---YRAPEAelqnclaqA 211
Cdd:cd14062  95 ARQTAQGMDYLHAKNIIHRDLKSNNIFLH-EDLTVKIGDFGLatvkTRWSGSQQFE--QPTGsilWMAPEV--------I 163
                        90       100
                ....*....|....*....|....*..
gi 28467003 212 GLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd14062 164 RMQDENPYSFQSDVYAFGIVLYELLTG 190
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
135-238 6.18e-04

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 41.18  E-value: 6.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWsaENECFKLIDFGLS-----FKEGNQDVKYIQTDG---YRAPEAeLQN 206
Cdd:cd14063  99 TVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL--ENGRVVITDFGLFslsglLQPGRREDTLVIPNGwlcYLAPEI-IRA 175
                        90       100       110
                ....*....|....*....|....*....|..
gi 28467003 207 CLAQAGLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd14063 176 LSPDLDFEESLPFTKASDVYAFGTVWYELLAG 207
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
73-235 6.58e-04

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 41.19  E-value: 6.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfSPNVPSRCLLLELLDVSVSELLLY-SSHQGCSMWMIQHCARDVLEALAFLHH 151
Cdd:cd14030  71 FKEEAGMLKGLQ-HPNIVRFYDSWE---STVKGKKCIVLVTELMTSGTLKTYlKRFKVMKIKVLRSWCRQILKGLQFLHT 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EG--YVHADLKPRNILWSAENECFKLIDFGL-SFKEGNQDVKYIQTDGYRAPEaelqnclaqaglQSDTECTSAVDLWSL 228
Cdd:cd14030 147 RTppIIHRDLKCDNIFITGPTGSVKIGDLGLaTLKRASFAKSVIGTPEFMAPE------------MYEEKYDESVDVYAF 214

                ....*..
gi 28467003 229 GIILLEM 235
Cdd:cd14030 215 GMCMLEM 221
RRM2_TatSF1_like cd12282
RNA recognition motif 2 (RRM2) found in HIV Tat-specific factor 1 (Tat-SF1) and similar ...
348-404 7.49e-04

RNA recognition motif 2 (RRM2) found in HIV Tat-specific factor 1 (Tat-SF1) and similar proteins; This subfamily corresponds to the RRM2 of Tat-SF1 and CUS2. Tat-SF1 is the cofactor for stimulation of transcriptional elongation by human immunodeficiency virus-type 1 (HIV-1) Tat. It is a substrate of an associated cellular kinase. Tat-SF1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a highly acidic carboxyl-terminal half. The family also includes CUS2, a yeast homolog of human Tat-SF1. CUS2 interacts with U2 RNA in splicing extracts and functions as a splicing factor that aids assembly of the splicing-competent U2 snRNP in vivo. CUS2 also associates with PRP11 that is a subunit of the conserved splicing factor SF3a. Like Tat-SF1, CUS2 contains two RRMs as well.


Pssm-ID: 409724 [Multi-domain]  Cd Length: 91  Bit Score: 38.37  E-value: 7.49e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 348 KEECQKYGPVVSLLVPKENPgRGQVFVEYANAGDSKAAQKLLTGRMFDGKFVVATFY 404
Cdd:cd12282  30 REECEKFGQVKKVVVFDRHP-DGVASVKFKEPEEADKCIQALNGRWFAGRKLEAETW 85
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
29-237 7.69e-04

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: 40.86  E-value: 7.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  29 LGSGSSASVYRVRCCGNPGSPPGALK---QFLPPGTTGAAASAaeygFRKERAALEQLQgHRNIVTLYGVfTIHFSPNVp 105
Cdd:cd05044   3 LGSGAFGEVFEGTAKDILGDGSGETKvavKTLRKGATDQEKAE----FLKEAHLMSNFK-HPNILKLLGV-CLDNDPQY- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 106 srcLLLELLDVSvsELLLY------SSHQGCS---MWMIQHCArDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLI 176
Cdd:cd05044  76 ---IILELMEGG--DLLSYlraarpTAFTPPLltlKDLLSICV-DVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRERVV 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28467003 177 ---DFGLSfkegnQDVkYiQTDGYR------------APEAELQNCLaqaglqsdtecTSAVDLWSLGIILLEMFS 237
Cdd:cd05044 150 kigDFGLA-----RDI-Y-KNDYYRkegegllpvrwmAPESLVDGVF-----------TTQSDVWAFGVLMWEILT 207
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
23-237 7.72e-04

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: 41.18  E-value: 7.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  23 WQVQSRLGSGSSASVYRvrCCGNPGSPPGALKQ--FLP--PGTTgaaasaaeygfrKERAALE---QLQG---HRNIVTL 92
Cdd:cd06652   4 WRLGKLLGQGAFGRVYL--CYDADTGRELAVKQvqFDPesPETS------------KEVNALEceiQLLKnllHERIVQY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  93 YGVFTihfSPNVPSRCLLLELL-DVSVSELLlySSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENE 171
Cdd:cd06652  70 YGCLR---DPQERTLSIFMEYMpGGSIKDQL--KSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGN 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 172 cFKLIDFGLSfkegnqdvKYIQTDgyrapeaelqnCLAQAGLQSDT--------ECTSA------VDLWSLGIILLEMFS 237
Cdd:cd06652 145 -VKLGDFGAS--------KRLQTI-----------CLSGTGMKSVTgtpywmspEVISGegygrkADIWSVGCTVVEMLT 204
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
137-237 8.33e-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: 41.18  E-value: 8.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 137 HCARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkegnQDVkyIQTDGYRA------------PEAEL 204
Cdd:cd05093 124 HIAQQIAAGMVYLASQHFVHRDLATRNCL-VGENLLVKIGDFGMS-----RDV--YSTDYYRVgghtmlpirwmpPESIM 195
                        90       100       110
                ....*....|....*....|....*....|...
gi 28467003 205 QNclaqaglqsdtECTSAVDLWSLGIILLEMFS 237
Cdd:cd05093 196 YR-----------KFTTESDVWSLGVVLWEIFT 217
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
135-304 8.91e-04

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: 40.77  E-value: 8.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWSaENECFKLIDFGLSFK---EGNQDVKYIQTDGYRAPEAelqncLAQA 211
Cdd:cd14188 103 VRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN-ENMELKVGDFGLAARlepLEHRRRTICGTPNYLSPEV-----LNKQ 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 212 GlqsdTECTSavDLWSLGIILLEM------FSGMKLKHT---VRSQEWKANSSAIidhifaskavvnaaIPAYHlrdLIK 282
Cdd:cd14188 177 G----HGCES--DIWALGCVMYTMllgrppFETTNLKETyrcIREARYSLPSSLL--------------APAKH---LIA 233
                       170       180
                ....*....|....*....|..
gi 28467003 283 SMLHDDPSRRIPAEMALCSPFF 304
Cdd:cd14188 234 SMLSKNPEDRPSLDEIIRHDFF 255
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
348-404 1.02e-03

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 41.21  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28467003   348 KEECQKYGPVVSLLVPKENPGRGQ-------VFVEYANAGDSKAAQKLLTGRMFDGKFVVATFY 404
Cdd:TIGR01645 537 REECGKFGVVDRVIINFEKQGEEEdaeiivkIFVEFSDSMEVDRAKAALDGRFFGGRTVVAEAY 600
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
73-249 1.20e-03

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


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 40.40  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQGHRNIVTLYGVftihfSPNVPSRCLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE 152
Cdd:cd14130  42 LKMEVAVLKKLQGKDHVCRFIGC-----GRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 153 GYVHADLKPRNI----LWSAENECFkLIDFGLSfkegnqdVKYIQTDG-YRAPE--AELQNCLAQAGLQS--DTECTSAV 223
Cdd:cd14130 117 GFLHRDIKPSNFamgrLPSTYRKCY-MLDFGLA-------RQYTNTTGeVRPPRnvAGFRGTVRYASVNAhkNREMGRHD 188
                       170       180
                ....*....|....*....|....*.
gi 28467003 224 DLWSLGIILLEMFSGMKLKHTVRSQE 249
Cdd:cd14130 189 DLWSLFYMLVEFAVGQLPWRKIKDKE 214
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
73-257 1.28e-03

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 40.33  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFT------------IHFSPNV------PSRCLLLELLDVSVSELLLYSshqgcsmwm 134
Cdd:cd05092  54 FQREAELLTVLQ-HQHIVRFYGVCTegeplimvfeymRHGDLNRflrshgPDAKILDGGEGQAPGQLTLGQ--------- 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkegnQDVkyIQTDGYRA------------PEA 202
Cdd:cd05092 124 MLQIASQIASGMVYLASLHFVHRDLATRNCL-VGQGLVVKIGDFGMS-----RDI--YSTDYYRVggrtmlpirwmpPES 195
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 203 ELQNclaqaglqsdtECTSAVDLWSLGIILLEMFsgmklkhTVRSQEWK--ANSSAI 257
Cdd:cd05092 196 ILYR-----------KFTTESDIWSFGVVLWEIF-------TYGKQPWYqlSNTEAI 234
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
73-235 1.32e-03

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: 40.45  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTihfSPNVPSRCLLLELLDVSVSELLLY-SSHQGCSMWMIQHCARDVLEALAFLHH 151
Cdd:cd14032  47 FKEEAEMLKGLQ-HPNIVRFYDFWE---SCAKGKRCIVLVTELMTSGTLKTYlKRFKVMKPKVLRSWCRQILKGLLFLHT 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EG--YVHADLKPRNILWSAENECFKLIDFGL-SFKEGNQDVKYIQTDGYRAPEaelqnclaqaglQSDTECTSAVDLWSL 228
Cdd:cd14032 123 RTppIIHRDLKCDNIFITGPTGSVKIGDLGLaTLKRASFAKSVIGTPEFMAPE------------MYEEHYDESVDVYAF 190

                ....*..
gi 28467003 229 GIILLEM 235
Cdd:cd14032 191 GMCMLEM 197
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
73-261 1.37e-03

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 40.14  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTIHFSPnvpsrCLLLELLDV-SVSELLlySSHQGCSMWMIQ--------------H 137
Cdd:cd05049  55 FEREAELLTNLQ-HENIVKFYGVCTEGDPL-----LMVFEYMEHgDLNKFL--RSHGPDAAFLASedsapgeltlsqllH 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 138 CARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkegnQDVkyIQTDGYR------------APEAELQ 205
Cdd:cd05049 127 IAVQIASGMVYLASQHFVHRDLATRNCL-VGTNLVVKIGDFGMS-----RDI--YSTDYYRvgghtmlpirwmPPESILY 198
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28467003 206 NclaqaglqsdtECTSAVDLWSLGIILLEMFSGMKlkhtvrsQEWKANS-SAIIDHI 261
Cdd:cd05049 199 R-----------KFTTESDVWSFGVVLWEIFTYGK-------QPWFQLSnTEVIECI 237
pknD PRK13184
serine/threonine-protein kinase PknD;
146-237 1.37e-03

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 40.91  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  146 LAFLHHEGYVHADLKPRNILWSAENECFkLIDFGLS-FKEGNQDV--------------------KYIQTDGYRAPEAEL 204
Cdd:PRK13184 126 IEYVHSKGVLHRDLKPDNILLGLFGEVV-ILDWGAAiFKKLEEEDlldidvdernicyssmtipgKIVGTPDYMAPERLL 204
                         90       100       110
                 ....*....|....*....|....*....|...
gi 28467003  205 QNclaqaglqsdtECTSAVDLWSLGIILLEMFS 237
Cdd:PRK13184 205 GV-----------PASESTDIYALGVILYQMLT 226
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
140-238 1.45e-03

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: 40.11  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 140 RDVLEALAFLHHEGYVHADLKPRNILWsAENECFKLIDFG--------LSFKEGNQDVKYIQ-TDGYRAPEaelqnclaq 210
Cdd:cd06631 110 KQILEGVAYLHNNNVIHRDIKGNNIML-MPNGVIKLIDFGcakrlcinLSSGSQSQLLKSMRgTPYWMAPE--------- 179
                        90       100
                ....*....|....*....|....*...
gi 28467003 211 agLQSDTECTSAVDLWSLGIILLEMFSG 238
Cdd:cd06631 180 --VINETGHGRKSDIWSIGCTVFEMATG 205
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
117-238 1.72e-03

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


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 40.31  E-value: 1.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 117 SVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENEC--------FKLIDFGLSFKEGNQD 188
Cdd:cd08227  85 SAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVylsglrsnLSMINHGQRLRVVHDF 164
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 28467003 189 VKY-IQTDGYRAPEAELQNclaqagLQSdteCTSAVDLWSLGIILLEMFSG 238
Cdd:cd08227 165 PKYsVKVLPWLSPEVLQQN------LQG---YDAKSDIYSVGITACELANG 206
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
135-235 1.80e-03

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 39.95  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 135 IQHCARDVLEALAFLHHEGYVHADLKPRNILWsaENECFKLIDFGL-----SFKEGNQDVKYIQTDG---YRAPEaelqn 206
Cdd:cd14152  99 TRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY--DNGKVVITDFGLfgisgVVQEGRRENELKLPHDwlcYLAPE----- 171
                        90       100       110
                ....*....|....*....|....*....|..
gi 28467003 207 CLAQAGLQSDTEC---TSAVDLWSLGIILLEM 235
Cdd:cd14152 172 IVREMTPGKDEDClpfSKAADVYAFGTIWYEL 203
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
141-305 1.94e-03

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: 39.98  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 141 DVLEALAFLHHEGYVHADLKPRNILWSAENE---CFKLIDFGLSFKEGNQDVKYIQTDGYRAPEaelqnclaqagLQSDT 217
Cdd:cd14183 112 NLASAIKYLHSLNIVHRDIKPENLLVYEHQDgskSLKLGDFGLATVVDGPLYTVCGTPTYVAPE-----------IIAET 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 218 ECTSAVDLWSLGIILLEMFSGM-KLKHTVRSQEwkanssAIIDHIFASKavVNAAIPAY-----HLRDLIKSMLHDDPSR 291
Cdd:cd14183 181 GYGLKVDIWAAGVITYILLCGFpPFRGSGDDQE------VLFDQILMGQ--VDFPSPYWdnvsdSAKELITMMLQVDVDQ 252
                       170
                ....*....|....
gi 28467003 292 RIPAEMALCSPFFS 305
Cdd:cd14183 253 RYSALQVLEHPWVN 266
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
131-237 2.04e-03

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: 39.92  E-value: 2.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 131 SMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQNCLAQ 210
Cdd:cd05096 136 SYSSLLHVALQIASGMKYLSSLNFVHRDLATRNCL-VGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILM 214
                        90       100
                ....*....|....*....|....*..
gi 28467003 211 AGLqsdtecTSAVDLWSLGIILLEMFS 237
Cdd:cd05096 215 GKF------TTASDVWAFGVTLWEILM 235
RRM_U2AF35B cd12539
RNA recognition motif (RRM) found in splicing factor U2AF 35 kDa subunit B (U2AF35B); This ...
349-405 2.29e-03

RNA recognition motif (RRM) found in splicing factor U2AF 35 kDa subunit B (U2AF35B); This subgroup corresponds to the RRM of U2AF35B, also termed zinc finger CCCH domain-containing protein 60 (C3H60), which is one of the small subunits of U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF). It has been implicated in the recruitment of U2 snRNP to pre-mRNAs and is a highly conserved heterodimer composed of large and small subunits. Members in this family are mainly found in plant. They show high sequence homology to vertebrates U2AF35 that directly binds to the 3' splice site of the conserved AG dinucleotide and performs multiple functions in the splicing process in a substrate-specific manner. U2AF35B contains two N-terminal zinc fingers, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal arginine/serine (SR)-rich domain. In contrast to U2AF35, U2AF35B has a plant-specific conserved C-terminal region containing SERE motif(s), which may have an important function specific to higher plants.


Pssm-ID: 409955 [Multi-domain]  Cd Length: 102  Bit Score: 37.38  E-value: 2.29e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 349 EECQKYGPVVSLLVPkENPGR---GQVFVEYANAGDSKAAQKLLTGRMFDGKFVVATFYP 405
Cdd:cd12539  44 EELSKFGEVEALNVC-DNLGDhmvGNVYVKFRDEEHAAAALKALQGRFYAGRPIIVEFSP 102
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
145-181 2.30e-03

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: 39.83  E-value: 2.30e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 28467003 145 ALAFLHHEGYVHADLKPRNILWSAENEcFKLIDFGLS 181
Cdd:cd05629 113 AIEAVHKLGFIHRDIKPDNILIDRGGH-IKLSDFGLS 148
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
108-165 2.44e-03

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 40.01  E-value: 2.44e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28467003 108 CLLLELLDVSVSELLLYSSHQGCSMWMIQHCARDVLEALAFLHHE-GYVHADLKPRNIL 165
Cdd:cd14217  96 CMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 154
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
146-237 2.80e-03

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: 39.16  E-value: 2.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 146 LAFLHHEGYVHADLKPRNILWSAENECfKLIDFGLSFKEGNQDVKYIQTDG------YRAPEaelqnCLAQAGLQSDTec 219
Cdd:cd05115 117 MKYLEEKNFVHRDLAARNVLLVNQHYA-KISDFGLSKALGADDSYYKARSAgkwplkWYAPE-----CINFRKFSSRS-- 188
                        90
                ....*....|....*...
gi 28467003 220 tsavDLWSLGIILLEMFS 237
Cdd:cd05115 189 ----DVWSYGVTMWEAFS 202
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
137-235 3.49e-03

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: 39.00  E-value: 3.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 137 HCARDVLEALAFLHHEGYVHADLKPRNILWSAENECFKLI--DFGL-----SFKEGNQDVKYIQTDGYRAPEaelqnCLa 209
Cdd:cd14155  92 KLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVvgDFGLaekipDYSDGKEKLAVVGSPYWMAPE-----VL- 165
                        90       100
                ....*....|....*....|....*.
gi 28467003 210 qaglqSDTECTSAVDLWSLGIILLEM 235
Cdd:cd14155 166 -----RGEPYNEKADVFSYGIILCEI 186
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
73-235 3.86e-03

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: 38.63  E-value: 3.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003  73 FRKERAALEQLQgHRNIVTLYGVFTIHFSPNvpsrcLLLELLDVSVSELLLySSHQGCSMWMIQ-HCARDVLEALAFLHH 151
Cdd:cd14065  35 FLKEVKLMRRLS-HPNILRFIGVCVKDNKLN-----FITEYVNGGTLEELL-KSMDEQLPWSQRvSLAKDIASGMAYLHS 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 152 EGYVHADLKPRNILWSAENECFKLI--DFGLS-------FKEGNQDVKY--IQTDGYRAPE---AELQNclaqaglqsdt 217
Cdd:cd14065 108 KNIIHRDLNSKNCLVREANRGRNAVvaDFGLArempdekTKKPDRKKRLtvVGSPYWMAPEmlrGESYD----------- 176
                       170
                ....*....|....*...
gi 28467003 218 ectSAVDLWSLGIILLEM 235
Cdd:cd14065 177 ---EKVDVFSFGIVLCEI 191
RRM_ALKBH8 cd12431
RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and ...
349-406 3.96e-03

RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and similar proteins; This subfamily corresponds to the RRM of ALKBH8, also termed alpha-ketoglutarate-dependent dioxygenase ABH8, or S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8, expressed in various types of human cancers. It is essential in urothelial carcinoma cell survival mediated by NOX-1-dependent ROS signals. ALKBH8 has also been identified as a tRNA methyltransferase that catalyzes methylation of tRNA to yield 5-methylcarboxymethyl uridine (mcm5U) at the wobble position of the anticodon loop. Thus, ALKBH8 plays a crucial role in the DNA damage survival pathway through a distinct mechanism involving the regulation of tRNA modification. ALKBH8 localizes to the cytoplasm. It contains the characteristic AlkB domain that is composed of a tRNA methyltransferase motif, a motif homologous to the bacterial AlkB DNA/RNA repair enzyme, and a dioxygenase catalytic core domain encompassing cofactor-binding sites for iron and 2-oxoglutarate. In addition, unlike other AlkB homologs, ALKBH8 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal S-adenosylmethionine (SAM)-dependent methyltransferase (MT) domain.


Pssm-ID: 409865 [Multi-domain]  Cd Length: 80  Bit Score: 36.02  E-value: 3.96e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28467003 349 EECQKYGPVVSLLVPkenPGRGQVFVEYANAGDSKAAQKLLTGRMFDGKFVVATFYPL 406
Cdd:cd12431  22 EVFEKYGTVEDIVML---PGKPYSFVSFKSVEEAAKAYNALNGKELELPQQNVPLYLS 76
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
134-179 5.62e-03

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 38.90  E-value: 5.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 28467003  134 MIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAENECfKLIDFG 179
Cdd:PLN03224 310 VIKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQV-KIIDFG 354
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
134-235 5.80e-03

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (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, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R 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: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 38.48  E-value: 5.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28467003 134 MIQhCARDVLEALAFLHHEGYVHADLKPRNILwSAENECFKLIDFGLSfkegnQDVkyIQTDGYRAPEAELQ--NCLAQA 211
Cdd:cd05062 121 MIQ-MAGEIADGMAYLNANKFVHRDLAARNCM-VAEDFTVKIGDFGMT-----RDI--YETDYYRKGGKGLLpvRWMSPE 191
                        90       100
                ....*....|....*....|....
gi 28467003 212 GLQsDTECTSAVDLWSLGIILLEM 235
Cdd:cd05062 192 SLK-DGVFTTYSDVWSFGVVLWEI 214
 
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